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 25-JAN-2012, entry version 122. DE RecName: Full=26S protease regulatory subunit 7; DE AltName: Full=26S proteasome AAA-ATPase subunit RPT1; 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. RC TISSUE=Embryonic kidney; 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 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). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). 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 P62191:PSMC1; NbExp=2; IntAct=EBI-359710, EBI-357598; CC Q16401:PSMD5; NbExp=4; IntAct=EBI-359710, EBI-752143; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- SIMILARITY: Belongs to the AAA ATPase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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_001191382.1; NM_001204453.1. DR RefSeq; NP_002794.1; NM_002803.3. DR UniGene; Hs.437366; -. DR ProteinModelPortal; P35998; -. DR SMR; P35998; 3-420. DR DIP; DIP-27554N; -. DR IntAct; P35998; 15. DR MINT; MINT-1163662; -. DR STRING; P35998; -. DR PhosphoSite; P35998; -. DR DMDM; 547930; -. DR OGP; P35998; -. DR REPRODUCTION-2DPAGE; IPI00021435; -. DR REPRODUCTION-2DPAGE; P35998; -. DR PeptideAtlas; P35998; -. DR PRIDE; P35998; -. DR Ensembl; ENSRNOT00000016450; ENSRNOP00000016450; ENSRNOG00000012026. DR Ensembl; ENST00000292644; ENSP00000292644; ENSG00000161057. DR Ensembl; ENST00000435765; ENSP00000391211; ENSG00000161057. DR GeneID; 5701; -. DR KEGG; hsa:5701; -. DR UCSC; uc003vbs.1; human. DR CTD; 5701; -. DR GeneCards; GC07P102984; -. DR H-InvDB; HIX0006971; -. DR HGNC; HGNC:9548; PSMC2. DR HPA; HPA019238; -. DR MIM; 154365; gene. DR neXtProt; NX_P35998; -. DR PharmGKB; PA33893; -. DR HOGENOM; HBG724153; -. DR HOVERGEN; HBG000109; -. DR InParanoid; P35998; -. DR OMA; DIRWELI; -. DR PhylomeDB; P35998; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34. 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_6900; Immune System. DR NextBio; 22150; -. DR ArrayExpress; P35998; -. DR Bgee; P35998; -. DR CleanEx; HS_PSMC2; -. DR Genevestigator; P35998; -. DR GermOnline; ENSG00000161057; Homo sapiens. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. 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 proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW. DR GO; GO:0000216; P:M/G1 transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome. DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome. DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome. DR GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome. DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome. DR GO; GO:0000084; P:S phase of mitotic cell cycle; TAS:Reactome. DR GO; GO:0016032; P:viral reproduction; TAS: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 KO; K03061; -. 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; Reference proteome. 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 //