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CSTOS_HUMAN
ID   CSTOS_HUMAN             Reviewed;         262 AA.
AC   Q96C57; Q53HF0; Q9H9Z7;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protein CUSTOS {ECO:0000250|UniProtKB:A9C3N6};
GN   Name=CUSTOS {ECO:0000250|UniProtKB:A9C3N6}; Synonyms=C12orf43;
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 MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211, AND IDENTIFICATION BY
RP   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   [6]
RP   IDENTIFICATION BY MASS 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP   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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; THR-79; THR-182 AND
RP   THR-211, AND 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).
CC   -!- FUNCTION: Plays a role in the regulation of Wnt signaling pathway
CC       during early development. {ECO:0000250|UniProtKB:A9C3N6}.
CC   -!- INTERACTION:
CC       Q96C57; P54274: TERF1; NbExp=2; IntAct=EBI-11305571, EBI-710997;
CC   -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:A9C3N6}.
CC   -!- SIMILARITY: Belongs to the CUSTOS family. {ECO:0000305}.
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DR   EMBL; AK022510; BAB14068.1; -; mRNA.
DR   EMBL; AK222630; BAD96350.1; -; mRNA.
DR   EMBL; BC014661; AAH14661.1; -; mRNA.
DR   CCDS; CCDS9210.1; -.
DR   RefSeq; NP_001273120.1; NM_001286191.1.
DR   RefSeq; NP_001273121.1; NM_001286192.1.
DR   RefSeq; NP_001273124.1; NM_001286195.1.
DR   RefSeq; NP_001273125.1; NM_001286196.1.
DR   RefSeq; NP_001273126.1; NM_001286197.1.
DR   RefSeq; NP_001273127.1; NM_001286198.1.
DR   RefSeq; NP_075046.1; NM_022895.2.
DR   AlphaFoldDB; Q96C57; -.
DR   BioGRID; 122339; 62.
DR   IntAct; Q96C57; 18.
DR   STRING; 9606.ENSP00000437803; -.
DR   GlyGen; Q96C57; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96C57; -.
DR   MetOSite; Q96C57; -.
DR   PhosphoSitePlus; Q96C57; -.
DR   BioMuta; C12orf43; -.
DR   DMDM; 125863775; -.
DR   EPD; Q96C57; -.
DR   jPOST; Q96C57; -.
DR   MassIVE; Q96C57; -.
DR   MaxQB; Q96C57; -.
DR   PaxDb; Q96C57; -.
DR   PeptideAtlas; Q96C57; -.
DR   PRIDE; Q96C57; -.
DR   ProteomicsDB; 76161; -.
DR   Antibodypedia; 51084; 40 antibodies from 11 providers.
DR   DNASU; 64897; -.
DR   Ensembl; ENST00000288757.7; ENSP00000288757.5; ENSG00000157895.11.
DR   GeneID; 64897; -.
DR   KEGG; hsa:64897; -.
DR   MANE-Select; ENST00000288757.7; ENSP00000288757.5; NM_022895.3; NP_075046.1.
DR   UCSC; uc001tzh.3; human.
DR   CTD; 64897; -.
DR   DisGeNET; 64897; -.
DR   GeneCards; C12orf43; -.
DR   HGNC; HGNC:25719; C12orf43.
DR   HPA; ENSG00000157895; Low tissue specificity.
DR   MalaCards; C12orf43; -.
DR   neXtProt; NX_Q96C57; -.
DR   OpenTargets; ENSG00000157895; -.
DR   PharmGKB; PA143485373; -.
DR   VEuPathDB; HostDB:ENSG00000157895; -.
DR   eggNOG; ENOG502S3AI; Eukaryota.
DR   GeneTree; ENSGT00390000010771; -.
DR   InParanoid; Q96C57; -.
DR   OMA; RPCRKRQ; -.
DR   OrthoDB; 1545516at2759; -.
DR   PhylomeDB; Q96C57; -.
DR   TreeFam; TF336221; -.
DR   PathwayCommons; Q96C57; -.
DR   SignaLink; Q96C57; -.
DR   BioGRID-ORCS; 64897; 17 hits in 1019 CRISPR screens.
DR   GeneWiki; C12orf43; -.
DR   GenomeRNAi; 64897; -.
DR   Pharos; Q96C57; Tdark.
DR   PRO; PR:Q96C57; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q96C57; protein.
DR   Bgee; ENSG00000157895; Expressed in secondary oocyte and 178 other tissues.
DR   ExpressionAtlas; Q96C57; baseline and differential.
DR   Genevisible; Q96C57; HS.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0060061; P:Spemann organizer formation; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR026694; CUSTOS.
DR   PANTHER; PTHR14482; PTHR14482; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Nucleus; Phosphoprotein; Reference proteome;
KW   Wnt signaling pathway.
FT   CHAIN           1..262
FT                   /note="Protein CUSTOS"
FT                   /id="PRO_0000276850"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           236..241
FT                   /note="Nucleolar localization signal (NLS)"
FT                   /evidence="ECO:0000250|UniProtKB:A9C3N6"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         79
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         182
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         211
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         44
FT                   /note="G -> R (in dbSNP:rs11537857)"
FT                   /id="VAR_030491"
FT   CONFLICT        106
FT                   /note="E -> A (in Ref. 2; BAD96350)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="S -> SS (in Ref. 3; AAH14661)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   262 AA;  28171 MW;  443F91BC023F0DC1 CRC64;
     MAAPSGTVSD SESSNSSSDA EELERCREAA MPAWGLEQRP HVAGKPRAGA ANSQLSTSQP
     SLRHKVNEHE QDGNELQTTP EFRAHVAKKL GALLDSFITI SEAAKEPAKA KVQKVALEDD
     GFRLFFTSVP GGREKEESPQ PRRKRQPSSS SEDSDEEWRR CREAAVSASD ILQESAIHSP
     GTVEKEAKKK RKLKKKAKKV ASVDSAVAAT TPTSMATVQK QKSGELNGDQ VSLGTKKKKK
     AKKASETSPF PPAKSATAIP AN
 
 
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