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C102A_HUMAN
ID   C102A_HUMAN             Reviewed;         550 AA.
AC   Q96A19; Q9BT74;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Coiled-coil domain-containing protein 102A;
GN   Name=CCDC102A;
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=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Placenta, 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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-28, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-28, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-28, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
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DR   EMBL; AC004382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004307; AAH04307.1; -; mRNA.
DR   EMBL; BC008285; AAH08285.1; -; mRNA.
DR   EMBL; BC009941; AAH09941.1; -; mRNA.
DR   CCDS; CCDS10784.1; -.
DR   RefSeq; NP_149989.2; NM_033212.3.
DR   RefSeq; XP_011521771.1; XM_011523469.2.
DR   AlphaFoldDB; Q96A19; -.
DR   SMR; Q96A19; -.
DR   BioGRID; 124987; 56.
DR   IntAct; Q96A19; 23.
DR   STRING; 9606.ENSP00000258214; -.
DR   iPTMnet; Q96A19; -.
DR   PhosphoSitePlus; Q96A19; -.
DR   BioMuta; CCDC102A; -.
DR   DMDM; 296434412; -.
DR   EPD; Q96A19; -.
DR   jPOST; Q96A19; -.
DR   MassIVE; Q96A19; -.
DR   MaxQB; Q96A19; -.
DR   PaxDb; Q96A19; -.
DR   PeptideAtlas; Q96A19; -.
DR   PRIDE; Q96A19; -.
DR   ProteomicsDB; 75892; -.
DR   Antibodypedia; 48917; 110 antibodies from 24 providers.
DR   DNASU; 92922; -.
DR   Ensembl; ENST00000258214.3; ENSP00000258214.2; ENSG00000135736.6.
DR   GeneID; 92922; -.
DR   KEGG; hsa:92922; -.
DR   MANE-Select; ENST00000258214.3; ENSP00000258214.2; NM_033212.4; NP_149989.2.
DR   UCSC; uc002elw.4; human.
DR   CTD; 92922; -.
DR   DisGeNET; 92922; -.
DR   GeneCards; CCDC102A; -.
DR   HGNC; HGNC:28097; CCDC102A.
DR   HPA; ENSG00000135736; Low tissue specificity.
DR   neXtProt; NX_Q96A19; -.
DR   OpenTargets; ENSG00000135736; -.
DR   PharmGKB; PA144596469; -.
DR   VEuPathDB; HostDB:ENSG00000135736; -.
DR   eggNOG; ENOG502QSJ6; Eukaryota.
DR   GeneTree; ENSGT00730000110960; -.
DR   HOGENOM; CLU_033486_1_0_1; -.
DR   InParanoid; Q96A19; -.
DR   OMA; CWEVRSV; -.
DR   OrthoDB; 1304833at2759; -.
DR   PhylomeDB; Q96A19; -.
DR   TreeFam; TF320856; -.
DR   PathwayCommons; Q96A19; -.
DR   SignaLink; Q96A19; -.
DR   BioGRID-ORCS; 92922; 20 hits in 1076 CRISPR screens.
DR   ChiTaRS; CCDC102A; human.
DR   GenomeRNAi; 92922; -.
DR   Pharos; Q96A19; Tdark.
DR   PRO; PR:Q96A19; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q96A19; protein.
DR   Bgee; ENSG00000135736; Expressed in right coronary artery and 97 other tissues.
DR   Genevisible; Q96A19; HS.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   InterPro; IPR002928; Myosin_tail.
DR   Pfam; PF01576; Myosin_tail_1; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein; Reference proteome.
FT   CHAIN           1..550
FT                   /note="Coiled-coil domain-containing protein 102A"
FT                   /id="PRO_0000274400"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          72..161
FT                   /evidence="ECO:0000255"
FT   COILED          263..396
FT                   /evidence="ECO:0000255"
FT   COILED          427..518
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        7..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..550
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CONFLICT        96
FT                   /note="R -> W (in Ref. 2; AAH08285/AAH09941)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  62596 MW;  FB8D693B4B7E580A CRC64;
     MSHGPSPRLA ESPQLSKGSL LTILGSPSPE RMGPADSLPP TPPSGTPSPG PPPALPLPPA
     PALLADGDWE SREELRLREL EEARARAAQM EKTMRRWSDC TANWREKWSK VRAERNRARE
     EVRQLRQRLD ALTKELAGAR RERQEAQGEC EARGRELARL RGARGVADQT RDGPEPEAER
     EPVRDVGSER PPGSQELELV ESLLKSMPEE SEDCWEARSL GAGGPRGSSG RQERSRLPWE
     DTAATEEEAS KLTALRLRLD ESQKVLLKER EDKLALSRNI EKLEGELSQW KIKYEELSKT
     KQEMLKQLSI LKEAHQDELG RMSEDLEDEL GARSSMDRKM AELRGEMERL QAENAAEWGR
     RERLETEKLG LERENKKLRA QVGDLEEALA RRRRQTASAL DCDLRASQAA LFEKNKELAD
     LKHVHGKLKK QFQEKVAELA HANRRVEQHE AEVKKLRLRV EELKKELAQA EDELDEAHNQ
     ARKLQRSLDE QTEQSENLQV QLEHLQSRLR RQQQNAPLFG KIRSARFGTE EAEDGTSDLD
     EDEDLQIQVA
 
 
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