26S protease regulatory subunit 7 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P35998 (PRS7_HUMAN)

Last modified June 16, 2009. Version 95. 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 7
Alternative name(s):
    Proteasome 26S subunit ATPase 2
    Protein MSS1

Gene names

Name:	PSMC2
Synonyms:	MSS1

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	433 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. In case of HIV-1 infection, positive modulator of Tat-mediated transactivation. Ref.5
Subunit structure	Interacts with NDC80 and SQSTM1. Interacts with PAAF1. Interacts with HIV-1 Tat. Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the AAA ATPase family.

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Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus Proteasome
Ligand	ATP-binding Nucleotide-binding
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 interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW 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 electronic annotation. Source: UniProtKB-SubCell proteasome complex Ref.5 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Ref.5 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
NDRG1	Q92597	1	EBI-359710,EBI-716486
PAAF1	Q9BRP4	1	EBI-359710,EBI-1056358
PSMC4	P43686	1	EBI-359710,EBI-743997
PSMD10	O75832	1	EBI-359710,EBI-752185
PSMD6	Q15008	1	EBI-359710,EBI-359701

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3 Ref.9

Chain

2 – 433

432

26S protease regulatory subunit 7

PRO_0000084709

Regions

Nucleotide binding

216 – 223

ATP Potential

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Sequences

Sequence

Length

Mass (Da)

Tools

P35998-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 85FD95F6DF7A3E84
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FASTA

433

48,634

        10         20         30         40         50         60 
MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED DIQQLLKKIN 

        70         80         90        100        110        120 
ELTGIKESDT GLAPPALWDL AADKQTLQSE QPLQVARCTK IINADSEDPK YIINVKQFAK 

       130        140        150        160        170        180 
FVVDLSDQVA PTDIEEGMRV GVDRNKYQIH IPLPPKIDPT VTMMQVEEKP DVTYSDVGGC 

       190        200        210        220        230        240 
KEQIEKLREV VETPLLHPER FVNLGIEPPK GVLLFGPPGT GKTLCARAVA NRTDACFIRV 

       250        260        270        280        290        300 
IGSELVQKYV GEGARMVREL FEMARTKKAC LIFFDEIDAI GGARFDDGAG GDNEVQRTML 

       310        320        330        340        350        360 
ELINQLDGFD PRGNIKVLMA TNRPDTLDPA LMRPGRLDRK IEFSLPDLEG RTHIFKIHAR 

       370        380        390        400        410        420 
SMSVERDIRF ELLARLCPNS TGAEIRSVCT EAGMFAIRAR RKIATEKDFL EAVNKVIKSY 

       430 
AKFSATPRYM TYN

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"New human gene encoding a positive modulator of HIV Tat-mediated transactivation." Shibuya H., Irie K., Ninomiya-Tsuji J., Goebl M., Taniguchi T., Matsumoto K. Nature 357:700-702(1992) [PubMed: 1377363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: Brain.
[3]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10. Tissue: Platelet.
[4]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 85-97; 101-110; 201-210; 269-284 AND 298-312, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[5]	"HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins." Chen Y., Sharp Z.D., Lee W.-H. J. Biol. Chem. 272:24081-24087(1997) [PubMed: 9295362] [Abstract] Cited for: FUNCTION, INTERACTION WITH NDC80.
[6]	"Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins." Zheng L., Chen Y., Lee W.-H. Mol. Cell. Biol. 19:5417-5428(1999) [PubMed: 10409732] [Abstract] Cited for: INTERACTION WITH NDC80.
[7]	"Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation." Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., Wooten M.W. Mol. Cell. Biol. 24:8055-8068(2004) [PubMed: 15340068] [Abstract] Cited for: INTERACTION WITH SQSTM1.
[8]	"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.
[9]	"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: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

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Cross-references

Sequence databases
	D11094 mRNA. Translation: BAA01868.1. BC002589 mRNA. Translation: AAH02589.1.
IPI	IPI00021435.
PIR	S24353.
RefSeq	NP_002794.1.
UniGene	Hs.437366
3D structure databases
HSSP	HSSP built from PDB template 1IXZ based on UniProtKB Q9LCZ4.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:27554N.
IntAct	P35998. 13 interactions.
PTM databases
PhosphoSite	P35998.
2-D gel databases
OGP	P35998.
REPRODUCTION-2DPAGE	IPI00021435. P35998.
Proteomic databases
PeptideAtlas	P35998.
PRIDE	P35998.
Genome annotation databases
Ensembl	ENSG00000161057. Homo sapiens. [Contig view]
GeneID	5701.
KEGG	hsa:5701.
Organism-specific databases
GeneCards	GC07P102775.
H-InvDB	HIX0006971.
HGNC	HGNC:9548. PSMC2.
MIM	154365. gene.
PharmGKB	PA33893.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P35998.
HOVERGEN	P35998.
OMA	P35998. KACIIFF.
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	P35998.
Bgee	P35998.
CleanEx	HS_PSMC2.
GermOnline	ENSG00000161057. 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	22150.
SOURCE	Search...

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Entry information

Entry name

PRS7_HUMAN

Accession

Primary (citable) accession number: P35998

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 95 of the entry and version 3 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 7

Human chromosome 7: 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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel 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