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P35998 (PRS7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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 7
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT1
Proteasome 26S subunit ATPase 2
Protein MSS1
Gene names
Name:PSMC2
Synonyms:MSS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length433 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. In case of HIV-1 infection, positive modulator of Tat-mediated transactivation. Ref.9

Subunit structure

Interacts with NDC80 and SQSTM1. Interacts with PAAF1. Interacts with HIV-1 Tat. Interacts with TRIM5. Ref.9 Ref.10 Ref.11 Ref.12 Ref.16

Subcellular location

Cytoplasm. Nucleus. CytoplasmP-body By similarity. Note: Colocalizes with TRIM5 in the cytoplasmic bodies By similarity.

Sequence similarities

Belongs to the AAA ATPase family.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Nucleus
Proteasome
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.9. 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

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

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

ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

cytoplasmic mRNA processing body

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

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

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7
Chain2 – 43343226S protease regulatory subunit 7
PRO_0000084709

Regions

Nucleotide binding216 – 2238ATP Potential

Amino acid modifications

Modified residue1161N6-acetyllysine Ref.14
Modified residue4221N6-acetyllysine Ref.14

Experimental info

Sequence conflict151D → V in BAE45763. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35998 [UniParc].

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

FASTA43348,634
        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 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Neuroblastoma.
[3]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Brain.
[6]"Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease."
Dubiel W., Ferrell K., Rechsteiner M.
FEBS Lett. 323:276-278(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-23; 139-158 AND 320-331.
Tissue: Blood.
[7]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10.
Tissue: Platelet.
[8]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NDC80.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NDC80.
[11]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1.
[12]"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.
[13]"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.
[14]"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-116 AND LYS-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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].
[16]"TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM5.
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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
D11094 mRNA. Translation: BAA01868.1.
AB075520 mRNA. Translation: BAE45763.1.
CH236947 Genomic DNA. Translation: EAL24412.1.
CH471070 Genomic DNA. Translation: EAW83332.1.
BC002589 mRNA. Translation: AAH02589.1.
CCDSCCDS5731.1.
PIRS24353.
RefSeqNP_001191382.1. NM_001204453.1.
NP_002794.1. NM_002803.3.
UniGeneHs.437366.

3D structure databases

ProteinModelPortalP35998.
SMRP35998. Positions 45-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111674. 109 interactions.
DIPDIP-27554N.
IntActP35998. 31 interactions.
MINTMINT-1163662.
STRING9606.ENSP00000292644.

PTM databases

PhosphoSiteP35998.

Polymorphism databases

DMDM547930.

2D gel databases

OGPP35998.
REPRODUCTION-2DPAGEIPI00021435.
P35998.

Proteomic databases

MaxQBP35998.
PaxDbP35998.
PeptideAtlasP35998.
PRIDEP35998.

Protocols and materials databases

DNASU5701.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292644; ENSP00000292644; ENSG00000161057.
ENST00000435765; ENSP00000391211; ENSG00000161057.
GeneID5701.
KEGGhsa:5701.
UCSCuc003vbs.3. human.

Organism-specific databases

CTD5701.
GeneCardsGC07P102984.
HGNCHGNC:9548. PSMC2.
HPAHPA019238.
MIM154365. gene.
neXtProtNX_P35998.
PharmGKBPA33893.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1222.
HOGENOMHOG000225143.
HOVERGENHBG000109.
InParanoidP35998.
KOK03061.
OMARDIRYDL.
OrthoDBEOG7TF78Z.
PhylomeDBP35998.
TreeFamTF105661.

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

ArrayExpressP35998.
BgeeP35998.
CleanExHS_PSMC2.
GenevestigatorP35998.

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

ChiTaRSPSMC2. human.
GeneWikiPSMC2.
GenomeRNAi5701.
NextBio22150.
PROP35998.
SOURCESearch...

Entry information

Entry namePRS7_HUMAN
AccessionPrimary (citable) accession number: P35998
Secondary accession number(s): A4D0Q1, Q3LIA5, Q9UDI3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 148 of the entry and version 3 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 7

Human chromosome 7: entries, gene names and cross-references to MIM