26S protease regulatory subunit 4 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P62191 (PRS4_HUMAN)

Last modified June 16, 2009. Version 61. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    26S protease regulatory subunit 4
Alternative name(s):
    P26s4
    Proteasome 26S subunit ATPase 1

Gene names

Name:

PSMC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Ligand	ATP-binding Nucleotide-binding
PTM	Isopeptide bond Lipoprotein Myristate Phosphoprotein Ubl conjugation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA proteasome complex Non-traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
PAAF1	Q9BRP4	1	EBI-357598,EBI-1056358
PSMC4	P43686	1	EBI-357598,EBI-743997
PSMD10	O75832	1	EBI-357598,EBI-752185
PSMD6	Q15008	1	EBI-357598,EBI-359701

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 440

439

26S protease regulatory subunit 4

PRO_0000084677

Regions

Nucleotide binding

226 – 233

ATP Potential

Amino acid modifications

Modified residue

439

Phosphotyrosine Ref.5

Lipidation

N-myristoyl glycine

Cross-link

237

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Experimental info

Sequence conflict

K → E in AAA35484. Ref.1

Sequence conflict

120

H → R in AAH16368. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P62191-1 [UniParc].

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

440

49,185

        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

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References

	« Hide 'large scale' referencesShow '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: 1429620] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow, 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: 11734547] [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: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, MASS SPECTROMETRY. Tissue: 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: 15358861] [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: 15831487] [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: 17323924] [Abstract] Cited for: MYRISTOYLATION [LARGE SCALE ANALYSIS] AT GLY-2, MASS SPECTROMETRY.
[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: 17370265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	L02426 mRNA. Translation: AAA35484.1. CR457044 mRNA. Translation: CAG33325.1. BC000512 mRNA. Translation: AAH00512.1. BC016368 mRNA. Translation: AAH16368.1. BC073818 mRNA. Translation: AAH73818.1.
IPI	IPI00011126.
PIR	A44468.
RefSeq	NP_002793.2.
UniGene	Hs.356654
3D structure databases
HSSP	HSSP built from PDB template 1OFI based on UniProtKB P43773.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62191. 15 interactions.
PTM databases
PhosphoSite	P62191.
Proteomic databases
PeptideAtlas	P62191.
PRIDE	P62191.
Genome annotation databases
Ensembl	ENSG00000100764. Homo sapiens. [Contig view]
GeneID	5700.
KEGG	hsa:5700.
Organism-specific databases
GeneCards	GC14P089792.
H-InvDB	HIX0011881. HIX0030744.
HGNC	HGNC:9547. PSMC1.
HPA	HPA000872.
MIM	602706. gene.
PharmGKB	PA33892.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P62191.
HOVERGEN	P62191.
OMA	P62191. PKYEPPV.
Enzyme and pathway databases
Reactome	REACT_11045. Signaling by Wnt. REACT_13. Metabolism of amino acids. REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	P62191.
Bgee	P62191.
CleanEx	HS_PSMC1.
GermOnline	ENSG00000100764. Homo sapiens.
Family and domain databases
InterPro	IPR005937. 26S_Psome_P45. IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. [Graphical view]
Pfam	PF00004. AAA. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
TIGRFAMs	TIGR01242. 26Sp45. 1 hit.
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	22146.
SOURCE	Search...

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Entry information

Entry name

PRS4_HUMAN

Accession

Primary (citable) accession number: P62191
Secondary accession number(s): P49014

Q96AZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 14

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Recent format changes

Overview of recent format changes

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents