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Reviewed, UniProtKB/Swiss-Prot P35998 (PRS7_HUMAN)

Last modified February 9, 2010. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    26S protease regulatory subunit 7
Alternative name(s):
    Proteasome 26S subunit ATPase 2
    Protein MSS1
Gene names
Name: PSMC2
Synonyms: MSS1
OrganismHomo sapiens (Human) [Complete 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. Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleus.

Sequence similarities

Belongs to the AAA ATPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.13
Chain2 – 43343226S protease regulatory subunit 7
PRO_0000084709

Regions

Nucleotide binding216 – 2238ATP Potential

Amino acid modifications

Modified residue1161N6-acetyllysine Ref.15
Modified residue4221N6-acetyllysine Ref.15

Experimental info

Sequence conflict151D → V in BAE45763. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35998-1 [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: 1377363] [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: 12880961] [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: 12690205] [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: 15489334] [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: 8500623] [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: 12665801] [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, 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: 9295362] [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: 10409732] [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: 15340068] [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: 15831487] [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: 17323924] [Abstract]
Cited for: CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]"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-116 AND LYS-422, MASS SPECTROMETRY.
+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.
IPIIPI00021435.
PIRS24353.
RefSeqNP_002794.1.
UniGeneHs.437366

3D structure databases

SMRP35998. Positions 167-414.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-27554N.
IntActP35998. 22 interactions.
STRINGP35998.

PTM databases

PhosphoSiteP35998.

2-D gel databases

OGPP35998.
REPRODUCTION-2DPAGEIPI00021435.
P35998.

Proteomic databases

PeptideAtlasP35998.
PRIDEP35998.

Genome annotation databases

EnsemblENST00000292644; ENSP00000292644; ENSG00000161057; Homo sapiens. [Genome view]
ENST00000435765; ENSP00000391211; ENSG00000161057; Homo sapiens. [Genome view]
GeneID5701.
KEGGhsa:5701.
UCSCuc003vbs.1. human.

Organism-specific databases

CTD5701.
GeneCardsGC07P102775.
H-InvDBHIX0006971.
HGNCHGNC:9548. PSMC2.
HPAHPA019238.
MIM154365. gene.
PharmGKBPA33893.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG724153.
HOVERGENP35998.
InParanoidP35998.
OMAKACIIFF.
OrthoDBEOG9GMXH6.
PhylomeDBP35998.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressP35998.
BgeeP35998.
CleanExHS_PSMC2.
GenevestigatorP35998.
GermOnlineENSG00000161057. Homo sapiens.

Family and domain databases

InterProIPR005937. 26S_Psome_P45.
IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01242. 26Sp45. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio22150.
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: February 9, 2010
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents