Full text data of PSMF1
PSMF1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Proteasome inhibitor PI31 subunit; hPI31
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome inhibitor PI31 subunit; hPI31
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00009949
IPI00009949 Proteasome inhibitor PI31 subunit Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00009949 Proteasome inhibitor PI31 subunit Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q92530
ID PSMF1_HUMAN Reviewed; 271 AA.
AC Q92530; A0AVQ9; D3DVW3; Q9H4I1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-MAR-2007, sequence version 2.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Proteasome inhibitor PI31 subunit;
DE Short=hPI31;
GN Name=PSMF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-36.
RX PubMed=10764772; DOI=10.1074/jbc.M001697200;
RA McCutchen-Maloney S.L., Matsuda K., Shimbara N., Binns D.D.,
RA Tanaka K., Slaughter C.A., DeMartino G.N.;
RT "cDNA cloning, expression, and functional characterization of PI31, a
RT proline-rich inhibitor of the proteasome.";
RL J. Biol. Chem. 275:18557-18565(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT CYS-36.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-36.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Plays an important role in control of proteasome
CC function. Inhibits the hydrolysis of protein and peptide
CC substrates by the 20S proteasome. Also inhibits the activation of
CC the proteasome by the proteasome regulatory proteins PA700 and
CC PA28.
CC -!- SUBUNIT: Monomer (Probable).
CC -!- INTERACTION:
CC Q9NWB1:RBFOX1; NbExp=2; IntAct=EBI-945916, EBI-945906;
CC -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D88378; BAA13603.1; -; mRNA.
DR EMBL; AL031665; CAC10383.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10650.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10651.1; -; Genomic_DNA.
DR EMBL; BC126462; AAI26463.1; -; mRNA.
DR RefSeq; NP_006805.2; NM_006814.3.
DR RefSeq; NP_848693.2; NM_178578.2.
DR UniGene; Hs.471917; -.
DR PDB; 2VT8; X-ray; 2.60 A; A/B=1-151.
DR PDBsum; 2VT8; -.
DR ProteinModelPortal; Q92530; -.
DR SMR; Q92530; 1-142.
DR IntAct; Q92530; 12.
DR MINT; MINT-1633308; -.
DR STRING; 9606.ENSP00000327704; -.
DR PhosphoSite; Q92530; -.
DR DMDM; 134047876; -.
DR PaxDb; Q92530; -.
DR PRIDE; Q92530; -.
DR DNASU; 9491; -.
DR Ensembl; ENST00000333082; ENSP00000327704; ENSG00000125818.
DR Ensembl; ENST00000335877; ENSP00000338039; ENSG00000125818.
DR GeneID; 9491; -.
DR KEGG; hsa:9491; -.
DR UCSC; uc002wel.4; human.
DR CTD; 9491; -.
DR GeneCards; GC20P001041; -.
DR HGNC; HGNC:9571; PSMF1.
DR HPA; HPA041122; -.
DR HPA; HPA041300; -.
DR neXtProt; NX_Q92530; -.
DR PharmGKB; PA33917; -.
DR eggNOG; NOG255866; -.
DR HOGENOM; HOG000231957; -.
DR HOVERGEN; HBG053746; -.
DR InParanoid; Q92530; -.
DR KO; K06700; -.
DR OMA; DFHRTYK; -.
DR PhylomeDB; Q92530; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMF1; human.
DR EvolutionaryTrace; Q92530; -.
DR GeneWiki; PSMF1; -.
DR GenomeRNAi; 9491; -.
DR NextBio; 35560; -.
DR PRO; PR:Q92530; -.
DR ArrayExpress; Q92530; -.
DR Bgee; Q92530; -.
DR CleanEx; HS_PSMF1; -.
DR Genevestigator; Q92530; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; NAS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR021625; FP_dom.
DR InterPro; IPR013886; PI31_Prot_Reg.
DR Pfam; PF08577; PI31_Prot_C; 1.
DR Pfam; PF11566; PI31_Prot_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Polymorphism;
KW Proteasome; Reference proteome.
FT CHAIN 1 271 Proteasome inhibitor PI31 subunit.
FT /FTId=PRO_0000220920.
FT COMPBIAS 154 271 Pro-rich.
FT MOD_RES 252 252 Phosphoserine.
FT VARIANT 36 36 F -> C (in dbSNP:rs1803415).
FT /FTId=VAR_024564.
FT VARIANT 174 174 H -> R (in dbSNP:rs2235587).
FT /FTId=VAR_022153.
FT HELIX 4 11
FT HELIX 12 14
FT HELIX 18 31
FT TURN 32 34
FT STRAND 35 43
FT STRAND 51 53
FT TURN 56 59
FT STRAND 62 72
FT STRAND 77 85
FT STRAND 88 95
FT TURN 96 99
FT STRAND 100 107
FT HELIX 108 111
FT HELIX 120 123
FT HELIX 127 137
SQ SEQUENCE 271 AA; 29817 MW; C669F8210AFAD727 CRC64;
MAGLEVLFAS AAPAITCRQD ALVCFLHWEV VTHGYFGLGV GDQPGPNDKK SELLPAGWNN
NKDLYVLRYE YKDGSRKLLV KAITVESSMI LNVLEYGSQQ VADLTLNLDD YIDAEHLGDF
HRTYKNSEEL RSRIVSGIIT PIHEQWEKAN VSSPHREFPP ATAREVDPLR IPPHHPHTSR
QPPWCDPLGP FVVGGEDLDP FGPRRGGMIV DPLRSGFPRA LIDPSSGLPN RLPPGAVPPG
ARFDPFGPIG TSPPGPNPDH LPPPGYDDMY L
//
ID PSMF1_HUMAN Reviewed; 271 AA.
AC Q92530; A0AVQ9; D3DVW3; Q9H4I1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-MAR-2007, sequence version 2.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Proteasome inhibitor PI31 subunit;
DE Short=hPI31;
GN Name=PSMF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-36.
RX PubMed=10764772; DOI=10.1074/jbc.M001697200;
RA McCutchen-Maloney S.L., Matsuda K., Shimbara N., Binns D.D.,
RA Tanaka K., Slaughter C.A., DeMartino G.N.;
RT "cDNA cloning, expression, and functional characterization of PI31, a
RT proline-rich inhibitor of the proteasome.";
RL J. Biol. Chem. 275:18557-18565(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT CYS-36.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-36.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Plays an important role in control of proteasome
CC function. Inhibits the hydrolysis of protein and peptide
CC substrates by the 20S proteasome. Also inhibits the activation of
CC the proteasome by the proteasome regulatory proteins PA700 and
CC PA28.
CC -!- SUBUNIT: Monomer (Probable).
CC -!- INTERACTION:
CC Q9NWB1:RBFOX1; NbExp=2; IntAct=EBI-945916, EBI-945906;
CC -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D88378; BAA13603.1; -; mRNA.
DR EMBL; AL031665; CAC10383.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10650.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10651.1; -; Genomic_DNA.
DR EMBL; BC126462; AAI26463.1; -; mRNA.
DR RefSeq; NP_006805.2; NM_006814.3.
DR RefSeq; NP_848693.2; NM_178578.2.
DR UniGene; Hs.471917; -.
DR PDB; 2VT8; X-ray; 2.60 A; A/B=1-151.
DR PDBsum; 2VT8; -.
DR ProteinModelPortal; Q92530; -.
DR SMR; Q92530; 1-142.
DR IntAct; Q92530; 12.
DR MINT; MINT-1633308; -.
DR STRING; 9606.ENSP00000327704; -.
DR PhosphoSite; Q92530; -.
DR DMDM; 134047876; -.
DR PaxDb; Q92530; -.
DR PRIDE; Q92530; -.
DR DNASU; 9491; -.
DR Ensembl; ENST00000333082; ENSP00000327704; ENSG00000125818.
DR Ensembl; ENST00000335877; ENSP00000338039; ENSG00000125818.
DR GeneID; 9491; -.
DR KEGG; hsa:9491; -.
DR UCSC; uc002wel.4; human.
DR CTD; 9491; -.
DR GeneCards; GC20P001041; -.
DR HGNC; HGNC:9571; PSMF1.
DR HPA; HPA041122; -.
DR HPA; HPA041300; -.
DR neXtProt; NX_Q92530; -.
DR PharmGKB; PA33917; -.
DR eggNOG; NOG255866; -.
DR HOGENOM; HOG000231957; -.
DR HOVERGEN; HBG053746; -.
DR InParanoid; Q92530; -.
DR KO; K06700; -.
DR OMA; DFHRTYK; -.
DR PhylomeDB; Q92530; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PSMF1; human.
DR EvolutionaryTrace; Q92530; -.
DR GeneWiki; PSMF1; -.
DR GenomeRNAi; 9491; -.
DR NextBio; 35560; -.
DR PRO; PR:Q92530; -.
DR ArrayExpress; Q92530; -.
DR Bgee; Q92530; -.
DR CleanEx; HS_PSMF1; -.
DR Genevestigator; Q92530; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005839; C:proteasome core complex; NAS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR021625; FP_dom.
DR InterPro; IPR013886; PI31_Prot_Reg.
DR Pfam; PF08577; PI31_Prot_C; 1.
DR Pfam; PF11566; PI31_Prot_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Polymorphism;
KW Proteasome; Reference proteome.
FT CHAIN 1 271 Proteasome inhibitor PI31 subunit.
FT /FTId=PRO_0000220920.
FT COMPBIAS 154 271 Pro-rich.
FT MOD_RES 252 252 Phosphoserine.
FT VARIANT 36 36 F -> C (in dbSNP:rs1803415).
FT /FTId=VAR_024564.
FT VARIANT 174 174 H -> R (in dbSNP:rs2235587).
FT /FTId=VAR_022153.
FT HELIX 4 11
FT HELIX 12 14
FT HELIX 18 31
FT TURN 32 34
FT STRAND 35 43
FT STRAND 51 53
FT TURN 56 59
FT STRAND 62 72
FT STRAND 77 85
FT STRAND 88 95
FT TURN 96 99
FT STRAND 100 107
FT HELIX 108 111
FT HELIX 120 123
FT HELIX 127 137
SQ SEQUENCE 271 AA; 29817 MW; C669F8210AFAD727 CRC64;
MAGLEVLFAS AAPAITCRQD ALVCFLHWEV VTHGYFGLGV GDQPGPNDKK SELLPAGWNN
NKDLYVLRYE YKDGSRKLLV KAITVESSMI LNVLEYGSQQ VADLTLNLDD YIDAEHLGDF
HRTYKNSEEL RSRIVSGIIT PIHEQWEKAN VSSPHREFPP ATAREVDPLR IPPHHPHTSR
QPPWCDPLGP FVVGGEDLDP FGPRRGGMIV DPLRSGFPRA LIDPSSGLPN RLPPGAVPPG
ARFDPFGPIG TSPPGPNPDH LPPPGYDDMY L
//