Microprotein - Revision history

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	~~{{for\|a similar (if not identical) concept\|Micropeptide}}~~
	A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>		A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>

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2026-10-01T02:48:38Z

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	{{for\|a similar (if not identical) concept\|Micropeptide}}		{{for\|a similar (if not identical) concept\|Micropeptide}}
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	A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>		A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>

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2026-10-01T02:47:36Z

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	~~{{short description\|Small protein encoded from a small open reading frame (sORF)}}~~
	{{for\|a similar (if not identical) concept\|Micropeptide}}		{{for\|a similar (if not identical) concept\|Micropeptide}}
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2026-10-01T02:44:57Z

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wikipedia>Fences and windows: Nominated for merging; see :Wikipedia:Articles for deletion/Microprotein.

2026-09-30T22:03:09Z

Nominated for merging; see Wikipedia:Articles for deletion/Microprotein.

← Older revision		Revision as of 22:03, 30 September 2026
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	{{short description\|Small protein encoded from a small open reading frame (sORF)}}		{{short description\|Small protein encoded from a small open reading frame (sORF)}}
	{{for\|a similar (if not identical) concept\|Micropeptide}}		{{for\|a similar (if not identical) concept\|Micropeptide}}
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	A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>		A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>

~2026-50447-01: Added "of" that was missing.

2026-09-19T03:14:45Z

Added "of" that was missing.

← Older revision		Revision as of 03:14, 19 September 2026
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	{{short description\|Small protein encoded from a small open reading frame (sORF)}}		{{short description\|Small protein encoded from a small open reading frame (sORF)}}
	{{for\|a similar (if not identical) concept\|Micropeptide}}		{{for\|a similar (if not identical) concept\|Micropeptide}}
	A '''microprotein''' (miP) is a small [[protein]] about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>		A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>

	== History ==		== History ==

wikipedia>Rkott: Cleaning up articles listed under Category:Post-translational modification

2026-08-16T02:44:24Z

Cleaning up articles listed under Category:Post-translational modification

← Older revision		Revision as of 02:44, 16 August 2026
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	[[Category:Protein classification]]		[[Category:Protein classification]]
	~~[[Category:Post-translational modification]]~~

wikipedia>Nexian123: /* growthexperiments-addlink-summary-summary:1|0|0 */

2026-08-12T12:54:53Z

growthexperiments-addlink-summary-summary:1|0|0

← Older revision		Revision as of 12:54, 12 August 2026
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	== Function ==		== Function ==
	Microproteins function as [[Post-translational regulation\|post-translational regulators]].<ref name=":1" /> Microproteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes.<ref name=":2" /> Furthermore, microproteins can interact with any protein that requires functional dimers to function normally.<ref name=":1" /> The primary targets are transcription factors that bind to DNA as dimers.<ref>{{Cite journal\|last1=de Klein\|first1=Niek\|last2=Magnani\|first2=Enrico\|last3=Banf\|first3=Michael\|last4=Rhee\|first4=Seung Yon\|date=2015\|title=microProtein Prediction Program (miP3): A Software for Predicting microProteins and Their Target Transcription Factors\|journal=International Journal of Genomics\|volume=2015\|article-number=734147\|doi=10.1155/2015/734147\|pmid=26060811\|pmc=4427850\|issn=2314-436X\|doi-access=free}}</ref><ref name=":1" /> Microproteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function.<ref name=":1" /> The two types of miP inhibitions are: homotypic miP inhibition and heterotypic miP inhibition.<ref name=":2" /> In homotypic miP inhibition, microproteins interact with proteins with similar protein-protein interaction (PPI) domain.<ref name=":2" /> In heterotypic miP inhibition, microproteins interact with proteins with different but compatible PPI domain.<ref name=":2" /> In both types of inhibition, microproteins interfere and prevent the PPI domains from interacting with their normal proteins.<ref name=":2" /> Microproteins plays roles in biological process such as immunity and inflammation, cancer and cell cycle regulation, cellular transport, muscle and heart functions, gene expression and genome maintenance, proteostasis, and metabolic homeostasis.<ref name=":4" />		Microproteins function as [[Post-translational regulation\|post-translational regulators]].<ref name=":1" /> Microproteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes.<ref name=":2" /> Furthermore, microproteins can interact with any protein that requires functional dimers to function normally.<ref name=":1" /> The primary targets are transcription factors that bind to DNA as dimers.<ref>{{Cite journal\|last1=de Klein\|first1=Niek\|last2=Magnani\|first2=Enrico\|last3=Banf\|first3=Michael\|last4=Rhee\|first4=Seung Yon\|date=2015\|title=microProtein Prediction Program (miP3): A Software for Predicting microProteins and Their Target Transcription Factors\|journal=International Journal of Genomics\|volume=2015\|article-number=734147\|doi=10.1155/2015/734147\|pmid=26060811\|pmc=4427850\|issn=2314-436X\|doi-access=free}}</ref><ref name=":1" /> Microproteins regulate these complexes by creating homotypic dimers with the targets and inhibit [[protein complex]] function.<ref name=":1" /> The two types of miP inhibitions are: homotypic miP inhibition and heterotypic miP inhibition.<ref name=":2" /> In homotypic miP inhibition, microproteins interact with proteins with similar protein-protein interaction (PPI) domain.<ref name=":2" /> In heterotypic miP inhibition, microproteins interact with proteins with different but compatible PPI domain.<ref name=":2" /> In both types of inhibition, microproteins interfere and prevent the PPI domains from interacting with their normal proteins.<ref name=":2" /> Microproteins plays roles in biological process such as immunity and inflammation, cancer and cell cycle regulation, cellular transport, muscle and heart functions, gene expression and genome maintenance, proteostasis, and metabolic homeostasis.<ref name=":4" />

	== References ==		== References ==

wikipedia>Idk20042: Edited a couple typos.

2026-08-03T22:08:04Z

Edited a couple typos.

← Older revision		Revision as of 22:08, 3 August 2026
Line 1:		Line 1:
	{{short description\|Small protein encoded from a small open reading frame (sORF)}}		{{short description\|Small protein encoded from a small open reading frame (sORF)}}
	{{for\|a similar (if not identical) concept\|Micropeptide}}		{{for\|a similar (if not identical) concept\|Micropeptide}}
	A '''microprotein''' (miP) is a small [[protein]] about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several ~~method~~ for microprotein study such as ribosome profiling, mass spectrometry, and genetic ~~screen~~.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>		A '''microprotein''' (miP) is a small [[protein]] about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>

	== History ==		== History ==

wikipedia>Ateofen: Add 0.1146/annurev-biochem-080124-012840

2026-07-20T19:50:53Z

Add 0.1146/annurev-biochem-080124-012840

← Older revision		Revision as of 19:50, 20 July 2026
Line 1:		Line 1:
	{{short description\|Small protein encoded from a small open reading frame (sORF)}}		{{short description\|Small protein encoded from a small open reading frame (sORF)}}
	{{for\|a similar (if not identical) concept\|Micropeptide}}		{{for\|a similar (if not identical) concept\|Micropeptide}}
	A '''microprotein''' (miP) is a small [[protein]] encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>		A '''microprotein''' (miP) is a small [[protein]] about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several method for microprotein study such as ribosome profiling, mass spectrometry, and genetic screen.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>

	== History ==		== History ==
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	== Function ==		== Function ==
	Microproteins function as [[Post-translational regulation\|post-translational regulators]].<ref name=":1" /> Microproteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes.<ref name=":2" /> Furthermore, microproteins can interact with any protein that requires functional dimers to function normally.<ref name=":1" /> The primary targets are transcription factors that bind to DNA as dimers.<ref>{{Cite journal\|last1=de Klein\|first1=Niek\|last2=Magnani\|first2=Enrico\|last3=Banf\|first3=Michael\|last4=Rhee\|first4=Seung Yon\|date=2015\|title=microProtein Prediction Program (miP3): A Software for Predicting microProteins and Their Target Transcription Factors\|journal=International Journal of Genomics\|volume=2015\|article-number=734147\|doi=10.1155/2015/734147\|pmid=26060811\|pmc=4427850\|issn=2314-436X\|doi-access=free}}</ref><ref name=":1" /> Microproteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function.<ref name=":1" /> The two types of miP inhibitions are: homotypic miP inhibition and heterotypic miP inhibition.<ref name=":2" /> In homotypic miP inhibition, microproteins interact with proteins with similar protein-protein interaction (PPI) domain.<ref name=":2" /> In heterotypic miP inhibition, microproteins interact with proteins with different but compatible PPI domain.<ref name=":2" /> In both types of inhibition, microproteins interfere and prevent the PPI domains from interacting with their normal proteins.<ref name=":2" />		Microproteins function as [[Post-translational regulation\|post-translational regulators]].<ref name=":1" /> Microproteins disrupt the formation of heterodimeric, homodimeric, or multimeric complexes.<ref name=":2" /> Furthermore, microproteins can interact with any protein that requires functional dimers to function normally.<ref name=":1" /> The primary targets are transcription factors that bind to DNA as dimers.<ref>{{Cite journal\|last1=de Klein\|first1=Niek\|last2=Magnani\|first2=Enrico\|last3=Banf\|first3=Michael\|last4=Rhee\|first4=Seung Yon\|date=2015\|title=microProtein Prediction Program (miP3): A Software for Predicting microProteins and Their Target Transcription Factors\|journal=International Journal of Genomics\|volume=2015\|article-number=734147\|doi=10.1155/2015/734147\|pmid=26060811\|pmc=4427850\|issn=2314-436X\|doi-access=free}}</ref><ref name=":1" /> Microproteins regulate these complexes by creating homotypic dimers with the targets and inhibit protein complex function.<ref name=":1" /> The two types of miP inhibitions are: homotypic miP inhibition and heterotypic miP inhibition.<ref name=":2" /> In homotypic miP inhibition, microproteins interact with proteins with similar protein-protein interaction (PPI) domain.<ref name=":2" /> In heterotypic miP inhibition, microproteins interact with proteins with different but compatible PPI domain.<ref name=":2" /> In both types of inhibition, microproteins interfere and prevent the PPI domains from interacting with their normal proteins.<ref name=":2" /> Microproteins plays roles in biological process such as immunity and inflammation, cancer and cell cycle regulation, cellular transport, muscle and heart functions, gene expression and genome maintenance, proteostasis, and metabolic homeostasis.<ref name=":4" />

	== References ==		== References ==

← Older revision		Revision as of 22:03, 30 September 2026
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	{{short description\|Small protein encoded from a small open reading frame (sORF)}}		{{short description\|Small protein encoded from a small open reading frame (sORF)}}
	{{for\|a similar (if not identical) concept\|Micropeptide}}		{{for\|a similar (if not identical) concept\|Micropeptide}}
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			{{Article for deletion/dated\|page=Microprotein\|timestamp=20260930220309\|year=2026\|month=September\|day=30\|substed=yes\|help=off\|outcome=merging\|target=Micropeptide}}
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	A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>		A '''microprotein''' (miP) is a small [[protein]] of about 100–150 amino acids or fewer encoded from a [[small open reading frame]] (sORF),<ref name=":3">{{Cite web\|url=https://www.the-scientist.com/features/the-dark-matter-of-the-human-proteome-65628\|title=The Dark Matter of the Human Proteome\|website=The Scientist Magazine®\|language=en\|access-date=2019-04-25}}</ref><ref name=":4">{{Cite journal \|last=Jaunbocus \|first=Nadiya \|last2=Ebenki \|first2=Valerie \|last3=Su \|first3=Haomiao \|last4=Slavoff \|first4=Sarah A. \|date=2025-06-20 \|title=Eukaryotic Microproteins \|url=https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-080124-012840 \|journal=Annual Review of Biochemistry \|language=en \|volume=94 \|issue=1 \|pages=1–28 \|doi=10.1146/annurev-biochem-080124-012840 \|issn=0066-4154 \|pmc=12207985 \|pmid=40245354}}</ref> also known as '''sORF-encoded protein''' ('''SEP'''). They are a class of protein with a single [[protein domain]]. They are related to multidomain proteins.<ref name=":0">{{Cite journal\|last1=Bhati\|first1=Kaushal Kumar\|last2=Blaakmeer\|first2=Anko\|last3=Paredes\|first3=Esther Botterweg\|last4=Dolde\|first4=Ulla\|last5=Eguen\|first5=Tenai\|last6=Hong\|first6=Shin-Young\|last7=Rodrigues\|first7=Vandasue\|last8=Straub\|first8=Daniel\|last9=Sun\|first9=Bin\|date=2018-04-18\|title=Approaches to identify and characterize microProteins and their potential uses in biotechnology\|journal=Cellular and Molecular Life Sciences\|volume=75\|issue=14\|pages=2529–2536\|doi=10.1007/s00018-018-2818-8\|pmid=29670998\|pmc=6003976\|issn=1420-682X}}</ref> Microproteins regulate larger multidomain proteins at the post-translational level.<ref name=":1">{{Cite journal\|last1=Staudt\|first1=Annica-Carolin\|last2=Wenkel\|first2=Stephan\|date=2010-12-10\|title=Regulation of protein function by 'microProteins'\|journal=EMBO Reports\|volume=12\|issue=1\|pages=35–42\|doi=10.1038/embor.2010.196\|pmid=21151039\|pmc=3024132\|issn=1469-221X}}</ref> Microproteins are analogous to [[MicroRNA\|microRNAs]] (miRNAs) and [[Protein dimer\|heterodimerize]] with their targets causing dominant and negative effects.<ref name=":2">{{Cite journal\|last1=Eguen\|first1=T\|last2=Straub\|first2=D\|last3=Graeff\|first3=M\|last4=Wenkel\|first4=S\|date=August 2015\|title=MicroProteins: small size-big impact\|journal=Trends in Plant Science\|volume=20\|issue=8\|pages=477–482\|doi=10.1016/j.tplants.2015.05.011\|pmid=26115780\|bibcode=2015TPS....20..477E}}</ref> In animals and plants, microproteins influence many biological processes.<ref name=":0" /> Because of their dominant effects on their targets, microproteins are currently under study for use in biotechnology.<ref name=":0" /> There are several methods for microprotein study, such as ribosome profiling, mass spectrometry, and genetic screening.<ref name=":4" /> In humans, they are associated with genetic diseases and cancers, and are called [[Peptidein\|peptideins]].<ref name=":02">{{Cite journal \|last=Callaway\|first=Ewen\|date=2026-05-06\|title=Revealed: the mysterious ‘dark’ proteins that might play a big role in biology\|url=https://www.nature.com/articles/d41586-026-01492-x\|journal=Nature\|language=en\|doi=10.1038/d41586-026-01492-x\|issn=1476-4687\|url-access=subscription}}</ref>