ID   PRS7_HUMAN              Reviewed;         433 AA.
AC   P35998; A4D0Q1; Q3LIA5; Q9UDI3;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   09-FEB-2010, entry version 104.
DE   RecName: Full=26S protease regulatory subunit 7;
DE   AltName: Full=Proteasome 26S subunit ATPase 2;
DE   AltName: Full=Protein MSS1;
GN   Name=PSMC2; Synonyms=MSS1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92310549; PubMed=1377363; DOI=10.1038/357700a0;
RA   Shibuya H., Irie K., Ninomiya-Tsuji J., Goebl M., Taniguchi T.,
RA   Matsumoto K.;
RT   "New human gene encoding a positive modulator of HIV Tat-mediated
RT   transactivation.";
RL   Nature 357:700-702(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neuroblastoma;
RX   PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
RA   Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA   Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA   Hirato J., Nakagawara A.;
RT   "Neuroblastoma oligo-capping cDNA project: toward the understanding of
RT   the genesis and biology of neuroblastoma.";
RL   Cancer Lett. 197:63-68(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22616434; PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA   Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA   Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA   Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA   Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA   Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA   Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA   Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA   Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA   Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA   Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA   Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA   Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA   Mural R.J., Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-23; 139-158 AND 320-331.
RC   TISSUE=Blood;
RX   MEDLINE=93272970; PubMed=8500623; DOI=10.1016/0014-5793(93)81356-5;
RA   Dubiel W., Ferrell K., Rechsteiner M.;
RT   "Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated
RT   transactivation, as subunit 7 of the 26 S protease.";
RL   FEBS Lett. 323:276-278(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-10.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   PROTEIN SEQUENCE OF 85-97; 101-110; 201-210; 269-284 AND 298-312, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [9]
RP   FUNCTION, AND INTERACTION WITH NDC80.
RX   PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
RA   Chen Y., Sharp Z.D., Lee W.-H.;
RT   "HEC binds to the seventh regulatory subunit of the 26 S proteasome
RT   and modulates the proteolysis of mitotic cyclins.";
RL   J. Biol. Chem. 272:24081-24087(1997).
RN   [10]
RP   INTERACTION WITH NDC80.
RX   PubMed=10409732;
RA   Zheng L., Chen Y., Lee W.-H.;
RT   "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT   chromosome segregation through interaction with SMC proteins.";
RL   Mol. Cell. Biol. 19:5417-5428(1999).
RN   [11]
RP   INTERACTION WITH SQSTM1.
RX   PubMed=15340068; DOI=10.1128/MCB.24.18.8055-8068.2004;
RA   Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R.,
RA   Wooten M.W.;
RT   "Sequestosome 1/p62 is a polyubiquitin chain binding protein involved
RT   in ubiquitin proteasome degradation.";
RL   Mol. Cell. Biol. 24:8055-8068(2004).
RN   [12]
RP   INTERACTION WITH PAAF1.
RX   PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
RA   Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT   "Proteasomal ATPase-associated factor 1 negatively regulates
RT   proteasome activity by interacting with proteasomal ATPases.";
RL   Mol. Cell. Biol. 25:3842-3853(2005).
RN   [13]
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND MASS
RP   SPECTROMETRY.
RX   PubMed=17323924; DOI=10.1021/bi061994u;
RA   Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT   "Mass spectrometric characterization of the affinity-purified human
RT   26S proteasome complex.";
RL   Biochemistry 46:3553-3565(2007).
RN   [14]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-422, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
CC   -!- FUNCTION: The 26S protease is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC       complex confers ATP dependency and substrate specificity to the
CC       26S complex. In case of HIV-1 infection, positive modulator of
CC       Tat-mediated transactivation.
CC   -!- SUBUNIT: Interacts with NDC80 and SQSTM1. Interacts with PAAF1.
CC       Interacts with HIV-1 Tat.
CC   -!- INTERACTION:
CC       Q92597:NDRG1; NbExp=1; IntAct=EBI-359710, EBI-716486;
CC       Q9BRP4:PAAF1; NbExp=1; IntAct=EBI-359710, EBI-1056358;
CC       P62191:PSMC1; NbExp=1; IntAct=EBI-359710, EBI-357598;
CC       P43686:PSMC4; NbExp=1; IntAct=EBI-359710, EBI-743997;
CC       O75832:PSMD10; NbExp=1; IntAct=EBI-359710, EBI-752185;
CC       Q16401:PSMD5; NbExp=1; IntAct=EBI-359710, EBI-752143;
CC       Q15008:PSMD6; NbExp=1; IntAct=EBI-359710, EBI-359701;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR   EMBL; D11094; BAA01868.1; -; mRNA.
DR   EMBL; AB075520; BAE45763.1; -; mRNA.
DR   EMBL; CH236947; EAL24412.1; -; Genomic_DNA.
DR   EMBL; CH471070; EAW83332.1; -; Genomic_DNA.
DR   EMBL; BC002589; AAH02589.1; -; mRNA.
DR   IPI; IPI00021435; -.
DR   PIR; S24353; S24353.
DR   RefSeq; NP_002794.1; -.
DR   UniGene; Hs.437366; -.
DR   SMR; P35998; 167-414.
DR   DIP; DIP-27554N; -.
DR   IntAct; P35998; 22.
DR   STRING; P35998; -.
DR   PhosphoSite; P35998; -.
DR   OGP; P35998; -.
DR   REPRODUCTION-2DPAGE; IPI00021435; -.
DR   REPRODUCTION-2DPAGE; P35998; -.
DR   PeptideAtlas; P35998; -.
DR   PRIDE; P35998; -.
DR   Ensembl; ENST00000292644; ENSP00000292644; ENSG00000161057; Homo sapiens.
DR   Ensembl; ENST00000435765; ENSP00000391211; ENSG00000161057; Homo sapiens.
DR   GeneID; 5701; -.
DR   KEGG; hsa:5701; -.
DR   UCSC; uc003vbs.1; human.
DR   CTD; 5701; -.
DR   GeneCards; GC07P102775; -.
DR   H-InvDB; HIX0006971; -.
DR   HGNC; HGNC:9548; PSMC2.
DR   HPA; HPA019238; -.
DR   MIM; 154365; gene.
DR   PharmGKB; PA33893; -.
DR   HOGENOM; HBG724153; -.
DR   HOVERGEN; P35998; -.
DR   InParanoid; P35998; -.
DR   OMA; KACIIFF; -.
DR   OrthoDB; EOG9GMXH6; -.
DR   PhylomeDB; P35998; -.
DR   Reactome; REACT_11045; Signaling by Wnt.
DR   Reactome; REACT_13; Metabolism of amino acids.
DR   Reactome; REACT_13635; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   Reactome; REACT_383; DNA Replication.
DR   Reactome; REACT_578; Apoptosis.
DR   Reactome; REACT_6185; HIV Infection.
DR   Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
DR   NextBio; 22150; -.
DR   ArrayExpress; P35998; -.
DR   Bgee; P35998; -.
DR   CleanEx; HS_PSMC2; -.
DR   Genevestigator; P35998; -.
DR   GermOnline; ENSG00000161057; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent protea...; EXP:Reactome.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0051436; P:negative regulation of ubiquitin-protein li...; EXP:Reactome.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein li...; EXP:Reactome.
DR   InterPro; IPR005937; 26S_Psome_P45.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Host-virus interaction; Nucleotide-binding;
KW   Nucleus; Proteasome.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    433       26S protease regulatory subunit 7.
FT                                /FTId=PRO_0000084709.
FT   NP_BIND     216    223       ATP (Potential).
FT   MOD_RES     116    116       N6-acetyllysine.
FT   MOD_RES     422    422       N6-acetyllysine.
FT   CONFLICT     15     15       D -> V (in Ref. 2; BAE45763).
SQ   SEQUENCE   433 AA;  48634 MW;  85FD95F6DF7A3E84 CRC64;
     MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED DIQQLLKKIN
     ELTGIKESDT GLAPPALWDL AADKQTLQSE QPLQVARCTK IINADSEDPK YIINVKQFAK
     FVVDLSDQVA PTDIEEGMRV GVDRNKYQIH IPLPPKIDPT VTMMQVEEKP DVTYSDVGGC
     KEQIEKLREV VETPLLHPER FVNLGIEPPK GVLLFGPPGT GKTLCARAVA NRTDACFIRV
     IGSELVQKYV GEGARMVREL FEMARTKKAC LIFFDEIDAI GGARFDDGAG GDNEVQRTML
     ELINQLDGFD PRGNIKVLMA TNRPDTLDPA LMRPGRLDRK IEFSLPDLEG RTHIFKIHAR
     SMSVERDIRF ELLARLCPNS TGAEIRSVCT EAGMFAIRAR RKIATEKDFL EAVNKVIKSY
     AKFSATPRYM TYN
//