Q92530 (PSMF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome inhibitor PI31 subunit
Short name=hPI31

Gene names

Name:

PSMF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Monomer Probable.
Sequence similarities	Belongs to the proteasome inhibitor PI31 family.

Ontologies

Keywords
Cellular component	Proteasome
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein polyubiquitination Traceable author statement. Source: Reactome regulation of apoptotic process Traceable author statement. Source: Reactome regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome core complex Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	endopeptidase inhibitor activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RBFOX1	Q9NWB1	2	EBI-945916,EBI-945906

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 271

271

Proteasome inhibitor PI31 subunit

PRO_0000220920

Regions

Compositional bias

154 – 271

118

Pro-rich

Amino acid modifications

Modified residue

153

1

Phosphoserine By similarity

Modified residue

252

1

Phosphoserine Ref.5 Ref.6

Natural variations

Natural variant

36

1

F → C. Ref.1 Ref.3 Ref.4
Corresponds to variant rs1803415 [ dbSNP | Ensembl ].

VAR_024564

Natural variant

174

1

H → R.
Corresponds to variant rs2235587 [ dbSNP | Ensembl ].

VAR_022153

Secondary structure

1

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271

Helix Strand Turn

Details...

Helix

4 – 11

8

Helix

12 – 14

3

Helix

18 – 31

14

Turn

32 – 34

3

Beta strand

35 – 43

9

Beta strand

51 – 53

3

Turn

56 – 59

4

Beta strand

62 – 72

11

Beta strand

77 – 85

9

Beta strand

88 – 95

8

Turn

96 – 99

4

Beta strand

100 – 107

8

Helix

108 – 111

4

Helix

120 – 123

4

Helix

127 – 137

11

Sequences

	Sequence		Length	Mass (Da)
	Q92530 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: C669F8210AFAD727	FASTA	271	29,817
	10 20 30 40 50 60 MAGLEVLFAS AAPAITCRQD ALVCFLHWEV VTHGYFGLGV GDQPGPNDKK SELLPAGWNN 70 80 90 100 110 120 NKDLYVLRYE YKDGSRKLLV KAITVESSMI LNVLEYGSQQ VADLTLNLDD YIDAEHLGDF 130 140 150 160 170 180 HRTYKNSEEL RSRIVSGIIT PIHEQWEKAN VSSPHREFPP ATAREVDPLR IPPHHPHTSR 190 200 210 220 230 240 QPPWCDPLGP FVVGGEDLDP FGPRRGGMIV DPLRSGFPRA LIDPSSGLPN RLPPGAVPPG 250 260 270 ARFDPFGPIG TSPPGPNPDH LPPPGYDDMY L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome." McCutchen-Maloney S.L., Matsuda K., Shimbara N., Binns D.D., Tanaka K., Slaughter C.A., DeMartino G.N. J. Biol. Chem. 275:18557-18565(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-36.
[2]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT CYS-36.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CYS-36.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D88378 mRNA. Translation: BAA13603.1.
AL031665 Genomic DNA. Translation: CAC10383.1.
CH471133 Genomic DNA. Translation: EAX10650.1.
CH471133 Genomic DNA. Translation: EAX10651.1.
BC126462 mRNA. Translation: AAI26463.1.

IPI

IPI00009949.

RefSeq

NP_006805.2. NM_006814.3.
NP_848693.2. NM_178578.2.

UniGene

Hs.471917.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VT8	X-ray	2.60	A/B	1-151	[»]

ProteinModelPortal

Q92530.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92530. 11 interactions.

MINT

MINT-1633308.

STRING

9606.ENSP00000327704.

PTM databases

PhosphoSite

Q92530.

Polymorphism databases

DMDM

134047876.

Proteomic databases

PaxDb

Q92530.

PRIDE

Q92530.

Protocols and materials databases

DNASU

9491.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000333082; ENSP00000327704; ENSG00000125818.
ENST00000335877; ENSP00000338039; ENSG00000125818.

GeneID

9491.

KEGG

hsa:9491.

UCSC

uc002wel.4. human.

Organism-specific databases

CTD

9491.

GeneCards

GC20P001041.

HGNC

HGNC:9571. PSMF1.

HPA

HPA041122.
HPA041300.

neXtProt

NX_Q92530.

PharmGKB

PA33917.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG255866.

HOGENOM

HOG000231957.

HOVERGEN

HBG053746.

InParanoid

Q92530.

KO

K06700.

OMA

DFHRTYK.

PhylomeDB

Q92530.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q92530.

Bgee

Q92530.

CleanEx

HS_PSMF1.

Genevestigator

Q92530.

GermOnline

ENSG00000125818. Homo sapiens.

Family and domain databases

InterPro

IPR021625. Inhibitor_PI31.
IPR013886. PI31_Prot_Reg.
[Graphical view]

Pfam

PF08577. PI31_Prot_C. 1 hit.
PF11566. PI31_Prot_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PSMF1. human.

EvolutionaryTrace

Q92530.

GenomeRNAi

9491.

NextBio

35560.

Entry information

Entry name

PSMF1_HUMAN

Accession

Primary (citable) accession number: Q92530
Secondary accession number(s): A0AVQ9, D3DVW3, Q9H4I1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.