P51665 (PSD7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
26S proteasome non-ATPase regulatory subunit 7

Alternative name(s):
26S proteasome regulatory subunit RPN8
26S proteasome regulatory subunit S12
Mov34 protein homolog
Proteasome subunit p40

Gene names

Name:	PSMD7
Synonyms:	MOV34L

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Subunit structure	Homodimer. Ref.8
Miscellaneous	Does not bind a metal ion.
Sequence similarities	Belongs to the peptidase M67A family. Contains 1 MPN (JAB/Mov34) domain.
Sequence caution	The sequence AAH00338.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Proteasome
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
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 peptide antigen via MHC class I Traceable author statement. Source: Reactome apoptotic process 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 viral reproduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome regulatory particle Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 324

323

26S proteasome non-ATPase regulatory subunit 7

PRO_0000213943

Regions

Domain

4 – 118

115

MPN

Compositional bias

286 – 324

39

Glu/Lys-rich

Amino acid modifications

Modified residue

186

1

Phosphothreonine Ref.4

Modified residue

204

1

N6-acetyllysine Ref.6

Modified residue

214

1

N6-acetyllysine Ref.6

Cross-link

180

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Experimental info

Sequence conflict

27

1

G → V in BAA08780. Ref.1

Sequence conflict

144 – 145

2

VH → DQ in BAA08780. Ref.1

Sequence conflict

216

1

A → G in BAA08780. Ref.1

Secondary structure

1

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324

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

13 – 28

16

Beta strand

36 – 56

21

Beta strand

58 – 60

3

Beta strand

67 – 70

4

Helix

72 – 83

12

Beta strand

86 – 88

3

Beta strand

90 – 96

7

Helix

105 – 112

8

Turn

113 – 115

3

Beta strand

120 – 124

5

Beta strand

134 – 143

10

Beta strand

152 – 164

13

Helix

166 – 178

13

Sequences

	Sequence		Length	Mass (Da)
	P51665 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: 3F7B343996B102B7	FASTA	324	37,025
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and a homolog of the Mov-34 gene product." Tsurumi C., DeMartino G.N., Slaughter C., Shimbara N., Tanaka K. Biochem. Biophys. Res. Commun. 210:600-608(1995) [PubMed: 7755639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	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].
[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: Lung and Skin.
[4]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[5]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-180, MASS SPECTROMETRY.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-214, MASS SPECTROMETRY.
[7]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer." Sanches M., Alves B.S.C., Zanchin N.I.T., Guimaraes B.G. J. Mol. Biol. 370:846-855(2007) [PubMed: 17559875] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-186, SUBUNIT, LACK OF METAL-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D50063 mRNA. Translation: BAA08780.1.
CH471166 Genomic DNA. Translation: EAW59162.1.
CH471166 Genomic DNA. Translation: EAW59163.1.
BC000338 mRNA. Translation: AAH00338.1. Sequence problems.
BC012606 mRNA. Translation: AAH12606.1.

IPI

IPI00019927.

PIR

JC4154.
S65491.

RefSeq

NP_002802.2. NM_002811.4.

UniGene

Hs.440604.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O95	X-ray	1.95	A/B	1-186	[»]
2O96	X-ray	3.00	A/B	1-177	[»]

ProteinModelPortal

P51665.

SMR

P51665. Positions 1-184.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27572N.

IntAct

P51665. 27 interactions.

MINT

MINT-5002613.

STRING

P51665.

Protein family/group databases

MEROPS

M67.973.

PTM databases

PhosphoSite

P51665.

Polymorphism databases

DMDM

20532412.

Proteomic databases

PeptideAtlas

P51665.

PRIDE

P51665.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000219313; ENSP00000219313; ENSG00000103035.

GeneID

5713.

KEGG

hsa:5713.

UCSC

uc002fcq.1. human.

Organism-specific databases

CTD

5713.

GeneCards

GC16P074330.

H-InvDB

HIX0013230.

HGNC

HGNC:9565. PSMD7.

HPA

CAB019379.

MIM

157970. gene.

neXtProt

NX_P51665.

PharmGKB

PA33911.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11217.

GeneTree

ENSGT00530000063075.

HOGENOM

HBG524656.

HOVERGEN

HBG035951.

InParanoid

P51665.

OMA

RSIIALH.

OrthoDB

EOG441QC3.

PhylomeDB

P51665.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
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_6900. Immune System.

Gene expression databases

ArrayExpress

P51665.

Bgee

P51665.

CleanEx

HS_PSMD7.

Genevestigator

P51665.

GermOnline

ENSG00000103035. Homo sapiens.

Family and domain databases

InterPro

IPR000555. Mov34_MPN_PAD1.
[Graphical view]

KO

K03038.

Pfam

PF01398. Mov34. 1 hit.
[Graphical view]

SMART

SM00232. JAB_MPN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

22194.

SOURCE

Search...

Entry information

Entry name

PSD7_HUMAN

Accession

Primary (citable) accession number: P51665
Secondary accession number(s): D3DWS9, Q6PKI2, Q96E97

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 10, 2002
Last modified:	January 25, 2012
This is version 108 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.