[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1006/bbrc.1995.1701; PubMed=7755639 [NCBI, ExPASy, EBI, Israel, Japan] Tsurumi C., DeMartino G.N., Slaughter C., Shimbara N., Tanaka K.; "cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and a homolog of the Mov-34 gene product."; Biochem. Biophys. Res. Commun. 210:600-608(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung, and Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, CLEAVAGE OF INITIATOR METHIONINE, AND MASS SPECTROMETRY. DOI=10.1021/bi061994u; PubMed=17323924 [NCBI, ExPASy, EBI, Israel, Japan] Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."; Biochemistry 46:3553-3565(2007).

Comments

FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
INTERACTION:
Q9BRP4:PAAF1; NbExp=1; IntAct=EBI-357659, EBI-1056358;
P43686:PSMC4; NbExp=1; IntAct=EBI-357659, EBI-743997;
O75832:PSMD10; NbExp=1; IntAct=EBI-357659, EBI-752185;
Q15008:PSMD6; NbExp=1; IntAct=EBI-357659, EBI-359701;
SIMILARITY: Belongs to the peptidase M67A family [view classification].
SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
SEQUENCE CAUTION:
- Sequence=AAH00338.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D50063; BAA08780.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000338; AAH00338.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012606; AAH12606.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC4154; JC4154.
S65491; S65491.

RefSeq

NP_002802.2; -.

UniGene

Hs.440604

3D structure databases

PDB

2O95; X-ray; 1.95 A; A/B=1-186.	[ExPASy / RCSB / EBI]
2O96; X-ray; 3.00 A; A/B=1-177.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2O95; -.
2O96; -.

ModBase

P51665.

Protein-protein interaction databases

DIP

DIP:27572N; -.

IntAct

P51665; 10.

Protein family/group databases

MEROPS

M67.973; -.

PTM databases

PhosphoSite

P51665; -.

Enzyme and pathway databases

Reactome

REACT_11045; Signaling by Wnt.
REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
REACT_6185; HIV Infection.
REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.

Organism-specific databases

GC16P072888; -.

HIX0013230; -.

HGNC:9565; PSMD7.

157970; gene. [NCBI / EBI]

PharmGKB

PA33911; -.

GeneCards

P51665.

Gene expression databases

ArrayExpress

P51665; -.

CleanEx

HS_PSMD7; -.

GermOnline

ENSG00000103035; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from electronic annotation from UniProtKB-KW).
GO:0005838;	Cellular component: proteasome regulatory particle (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031145;	Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0051436;	Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0051437;	Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.

Family and domain databases

InterPro

IPR000555; Mov34_MPN_PAD1.
Graphical view of domain structure.

Pfam

PF01398; Mov34; 1.
Pfam graphical view of domain structure.

ProDom

PD363422; Mov34-1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00232; JAB_MPN; 1.
SMART graphical view of domain structure.

Proteomic databases

PeptideAtlas

P51665; -.

Proteomics databases

PRIDE

P51665; -.

Genome annotation databases

Ensembl

ENSG00000103035; Homo sapiens. [Contig view]

GeneID

5713; -.

KEGG

hsa:5713; -.

Phylogenomic databases

HOGENOM

P51665; -.

HOVERGEN

P51665; -.

Other

P51665; -.

22194; -.

PSMD7; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Phosphoprotein; Proteasome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 324`	`323`	`26S proteasome non-ATPase regulatory subunit 7.`	`PRO_0000213943`
`DOMAIN`	`4 118`	`115`	`MPN.`
`COMPBIAS`	`286 324`	`39`	`Glu/Lys-rich.`
`MOD_RES`	`186 186`		`Phosphothreonine.`
`CONFLICT`	`27 27`		`G -> V (in Ref. 1; BAA08780).`
`CONFLICT`	`144 145`		`VH -> DQ (in Ref. 1; BAA08780).`
`CONFLICT`	`216 216`		`A -> G (in Ref. 1; BAA08780).`
`STRAND`	`7 11`	`5`
`HELIX`	`13 28`	`16`
`STRAND`	`36 56`	`21`
`STRAND`	`58 60`	`3`
`STRAND`	`67 70`	`4`
`HELIX`	`72 83`	`12`
`STRAND`	`86 88`	`3`
`STRAND`	`90 96`	`7`
`HELIX`	`105 112`	`8`
`TURN`	`113 115`	`3`
`STRAND`	`120 124`	`5`
`STRAND`	`134 143`	`10`
`STRAND`	`152 164`	`13`
`HELIX`	`166 178`	`13`

Sequence information

Length: 324 AA [This is the length of the unprocessed precursor]

Molecular weight: 37025 Da [This is the MW of the unprocessed precursor]

CRC64: 3F7B343996B102B7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV SNSFAVPFDE 

        70         80         90        100        110        120 
DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK LHKNDIAINE LMKRYCPNSV 

       130        140        150        160        170        180 
LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK 

       190        200        210        220        230        240 
DTTVGTLSQR ITNQVHGLKG LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV 

       250        260        270        280        290        300 
SLQEFVKAFY LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR 

       310        320 
KEDKEKDKDK EKSDVKKEEK KEKK

P51665 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools