位置:首页 > 蛋白库 > PSMG3_HUMAN
PSMG3_HUMAN
ID   PSMG3_HUMAN             Reviewed;         122 AA.
AC   Q9BT73; A4D216; A8MPW2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Proteasome assembly chaperone 3;
DE            Short=PAC-3;
DE            Short=hPAC3;
GN   Name=PSMG3; Synonyms=C7orf48, PAC3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   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., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., 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., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adrenal cortex, and Uterus;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION, FUNCTION, AND INTERACTION WITH THE PROTEASOME.
RX   PubMed=17189198; DOI=10.1016/j.molcel.2006.11.015;
RA   Hirano Y., Hayashi H., Iemura S., Hendil K.B., Niwa S., Kishimoto T.,
RA   Kasahara M., Natsume T., Tanaka K., Murata S.;
RT   "Cooperation of multiple chaperones required for the assembly of mammalian
RT   20S proteasomes.";
RL   Mol. Cell 24:977-984(2006).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
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., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX   PubMed=18278057; DOI=10.1038/nsmb.1386;
RA   Yashiroda H., Mizushima T., Okamoto K., Kameyama T., Hayashi H.,
RA   Kishimoto T., Niwa S., Kasahara M., Kurimoto E., Sakata E., Takagi K.,
RA   Suzuki A., Hirano Y., Murata S., Kato K., Yamane T., Tanaka K.;
RT   "Crystal structure of a chaperone complex that contributes to the assembly
RT   of yeast 20S proteasomes.";
RL   Nat. Struct. Mol. Biol. 15:228-236(2008).
CC   -!- FUNCTION: Chaperone protein which promotes assembly of the 20S
CC       proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate
CC       the correct assembly of proteasomes. {ECO:0000269|PubMed:17189198}.
CC   -!- SUBUNIT: Homodimer. Interacts with PSMG4. Interacts directly with alpha
CC       and beta subunits of the 20S proteasome but dissociates before the
CC       formation of half-proteasomes, probably upon recruitment of POMP.
CC       {ECO:0000269|PubMed:17189198, ECO:0000269|PubMed:18278057}.
CC   -!- SIMILARITY: Belongs to the PSMG3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC093734; AAP21867.1; -; Genomic_DNA.
DR   EMBL; CH236953; EAL23945.1; -; Genomic_DNA.
DR   EMBL; CH471144; EAW87212.1; -; Genomic_DNA.
DR   EMBL; BC004308; AAH04308.1; -; mRNA.
DR   EMBL; BC027171; AAH27171.1; -; mRNA.
DR   EMBL; BR000337; FAA00325.1; -; mRNA.
DR   CCDS; CCDS5327.1; -.
DR   RefSeq; NP_001127812.1; NM_001134340.1.
DR   RefSeq; NP_115678.1; NM_032302.3.
DR   PDB; 2Z5E; X-ray; 2.00 A; A/B=1-122.
DR   PDB; 6JPT; X-ray; 0.96 A; A=1-122.
DR   PDBsum; 2Z5E; -.
DR   PDBsum; 6JPT; -.
DR   AlphaFoldDB; Q9BT73; -.
DR   SMR; Q9BT73; -.
DR   BioGRID; 123989; 108.
DR   CORUM; Q9BT73; -.
DR   IntAct; Q9BT73; 34.
DR   MINT; Q9BT73; -.
DR   STRING; 9606.ENSP00000288607; -.
DR   BindingDB; Q9BT73; -.
DR   ChEMBL; CHEMBL1075137; -.
DR   GlyGen; Q9BT73; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BT73; -.
DR   PhosphoSitePlus; Q9BT73; -.
DR   BioMuta; PSMG3; -.
DR   DMDM; 74733099; -.
DR   EPD; Q9BT73; -.
DR   jPOST; Q9BT73; -.
DR   MassIVE; Q9BT73; -.
DR   MaxQB; Q9BT73; -.
DR   PaxDb; Q9BT73; -.
DR   PeptideAtlas; Q9BT73; -.
DR   PRIDE; Q9BT73; -.
DR   ProteomicsDB; 78955; -.
DR   TopDownProteomics; Q9BT73; -.
DR   Antibodypedia; 10998; 69 antibodies from 18 providers.
DR   DNASU; 84262; -.
DR   Ensembl; ENST00000252329.3; ENSP00000252329.3; ENSG00000157778.9.
DR   Ensembl; ENST00000288607.3; ENSP00000288607.2; ENSG00000157778.9.
DR   Ensembl; ENST00000404674.7; ENSP00000384799.3; ENSG00000157778.9.
DR   GeneID; 84262; -.
DR   KEGG; hsa:84262; -.
DR   MANE-Select; ENST00000288607.3; ENSP00000288607.2; NM_032302.4; NP_115678.1.
DR   UCSC; uc003skx.3; human.
DR   CTD; 84262; -.
DR   DisGeNET; 84262; -.
DR   GeneCards; PSMG3; -.
DR   HGNC; HGNC:22420; PSMG3.
DR   HPA; ENSG00000157778; Low tissue specificity.
DR   MIM; 617528; gene.
DR   neXtProt; NX_Q9BT73; -.
DR   OpenTargets; ENSG00000157778; -.
DR   PharmGKB; PA162400247; -.
DR   VEuPathDB; HostDB:ENSG00000157778; -.
DR   eggNOG; KOG4828; Eukaryota.
DR   GeneTree; ENSGT00390000000324; -.
DR   HOGENOM; CLU_133503_1_0_1; -.
DR   InParanoid; Q9BT73; -.
DR   OMA; IRTCQVW; -.
DR   OrthoDB; 1469039at2759; -.
DR   PhylomeDB; Q9BT73; -.
DR   TreeFam; TF300294; -.
DR   PathwayCommons; Q9BT73; -.
DR   SignaLink; Q9BT73; -.
DR   BioGRID-ORCS; 84262; 733 hits in 1079 CRISPR screens.
DR   ChiTaRS; PSMG3; human.
DR   EvolutionaryTrace; Q9BT73; -.
DR   GenomeRNAi; 84262; -.
DR   Pharos; Q9BT73; Tchem.
DR   PRO; PR:Q9BT73; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9BT73; protein.
DR   Bgee; ENSG00000157778; Expressed in mucosa of transverse colon and 177 other tissues.
DR   ExpressionAtlas; Q9BT73; baseline and differential.
DR   Genevisible; Q9BT73; HS.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0060090; F:molecular adaptor activity; IMP:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:UniProtKB.
DR   GO; GO:0043248; P:proteasome assembly; IEA:InterPro.
DR   InterPro; IPR018788; Proteasome_assmbl_chp_3.
DR   PANTHER; PTHR31051; PTHR31051; 1.
DR   Pfam; PF10178; PAC3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chaperone; Reference proteome.
FT   CHAIN           1..122
FT                   /note="Proteasome assembly chaperone 3"
FT                   /id="PRO_0000271358"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   STRAND          6..16
FT                   /evidence="ECO:0007829|PDB:6JPT"
FT   STRAND          19..27
FT                   /evidence="ECO:0007829|PDB:6JPT"
FT   STRAND          29..38
FT                   /evidence="ECO:0007829|PDB:6JPT"
FT   STRAND          44..51
FT                   /evidence="ECO:0007829|PDB:6JPT"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:2Z5E"
FT   STRAND          61..69
FT                   /evidence="ECO:0007829|PDB:6JPT"
FT   HELIX           73..89
FT                   /evidence="ECO:0007829|PDB:6JPT"
FT   STRAND          94..100
FT                   /evidence="ECO:0007829|PDB:6JPT"
FT   HELIX           106..118
FT                   /evidence="ECO:0007829|PDB:6JPT"
SQ   SEQUENCE   122 AA;  13104 MW;  FA3D42A2CF4B88B7 CRC64;
     MEDTPLVISK QKTEVVCGVP TQVVCTAFSS HILVVVTQFG KMGTLVSLEP SSVASDVSKP
     VLTTKVLLGQ DEPLIHVFAK NLVAFVSQEA GNRAVLLAVA VKDKSMEGLK ALREVIRVCQ
     VW
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024