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P62191 (PRS4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
26S protease regulatory subunit 4

Short name=P26s4
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT2
Proteasome 26S subunit ATPase 1
Gene names
Name:PSMC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.

Subunit structure

Interacts with SCA7. Interacts with NGLY1. Interacts with PAAF1. Ref.4 Ref.6 Ref.7

Subcellular location

Cytoplasm. Nucleus.

Sequence similarities

Belongs to the AAA ATPase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Proteasome
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Isopeptide bond
Lipoprotein
Myristate
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity Ref.1. Source: GOC

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

RNA metabolic process

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

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic 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

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

proteasome accessory complex

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome complex

Non-traceable author statement PubMed 8811196. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16189514PubMed 19060904PubMed 19490896PubMed 22901813PubMed 23455924. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 44043926S protease regulatory subunit 4
PRO_0000084677

Regions

Nucleotide binding226 – 2338ATP Potential

Amino acid modifications

Modified residue41Phosphoserine Ref.10
Modified residue2581N6-acetyllysine Ref.11
Modified residue4391Phosphotyrosine Ref.5
Lipidation21N-myristoyl glycine By similarity
Cross-link237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Experimental info

Sequence conflict191K → E in AAA35484. Ref.1
Sequence conflict701D → G in AAH67741. Ref.3
Sequence conflict1201H → R in AAH16368. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P62191 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: ACA80782F4F96F49

FASTA44049,185
        10         20         30         40         50         60 
MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP LVTPHTQCRL 

        70         80         90        100        110        120 
KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD DLRGTPMSVG TLEEIIDDNH 

       130        140        150        160        170        180 
AIVSTSVGSE HYVSILSFVD KDLLEPGCSV LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP 

       190        200        210        220        230        240 
QETYADIGGL DNQIQEIKES VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA 

       250        260        270        280        290        300 
NQTSATFLRV VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG 

       310        320        330        340        350        360 
GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK IEFPLPDEKT 

       370        380        390        400        410        420 
KKRIFQIHTS RMTLADDVTL DDLIMAKDDL SGADIKAICT EAGLMALRER RMKVTNEDFK 

       430        440 
KSKENVLYKK QEGTPEGLYL 

« Hide

References

« Hide 'large scale' references
[1]"Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase family."
Dubiel W., Ferrell K., Pratt G., Rechsteiner M.C.
J. Biol. Chem. 267:22699-22702(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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].
Tissue: Bone marrow, Brain, Lung and Prostate.
[4]"Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex."
Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A., van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H.
Hum. Mol. Genet. 10:2821-2831(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCA7.
[5]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[6]"A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins."
Katiyar S., Li G., Lennarz W.J.
Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGLY1.
[7]"Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases."
Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.
Mol. Cell. Biol. 25:3842-3853(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAAF1.
[8]"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237.
Tissue: Mammary cancer.
[10]"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-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02426 mRNA. Translation: AAA35484.1.
CR457044 mRNA. Translation: CAG33325.1.
BC000512 mRNA. Translation: AAH00512.1.
BC016368 mRNA. Translation: AAH16368.1.
BC067741 mRNA. Translation: AAH67741.1.
BC073818 mRNA. Translation: AAH73818.1.
CCDSCCDS32139.1.
PIRA44468.
RefSeqNP_002793.2. NM_002802.2.
UniGeneHs.356654.

3D structure databases

ProteinModelPortalP62191.
SMRP62191. Positions 78-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111673. 86 interactions.
IntActP62191. 29 interactions.
MINTMINT-1141832.
STRING9606.ENSP00000261303.

PTM databases

PhosphoSiteP62191.

Polymorphism databases

DMDM49065817.

Proteomic databases

MaxQBP62191.
PaxDbP62191.
PeptideAtlasP62191.
PRIDEP62191.

Protocols and materials databases

DNASU5700.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261303; ENSP00000261303; ENSG00000100764.
GeneID5700.
KEGGhsa:5700.
UCSCuc001xyf.3. human.

Organism-specific databases

CTD5700.
GeneCardsGC14P090722.
H-InvDBHIX0030744.
HGNCHGNC:9547. PSMC1.
HPAHPA000872.
MIM602706. gene.
neXtProtNX_P62191.
PharmGKBPA33892.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1222.
HOGENOMHOG000225143.
HOVERGENHBG000109.
InParanoidP62191.
KOK03062.
OMAMCTEAGL.
OrthoDBEOG7F24ST.
PhylomeDBP62191.
TreeFamTF106226.

Enzyme and pathway databases

ReactomeREACT_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

BgeeP62191.
CleanExHS_PSMC1.
GenevestigatorP62191.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01242. 26Sp45. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPSMC1.
GenomeRNAi5700.
NextBio22146.
PROP62191.
SOURCESearch...

Entry information

Entry namePRS4_HUMAN
AccessionPrimary (citable) accession number: P62191
Secondary accession number(s): P49014 expand/collapse secondary AC list , Q03527, Q6IAW0, Q6NW36, Q96AZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM