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Entry: CCS_MOUSE
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ID   CCS_MOUSE               Reviewed;         274 AA.
AC   Q9WU84; Q9CRJ9;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   13-FEB-2019, entry version 157.
DE   RecName: Full=Copper chaperone for superoxide dismutase;
DE   AltName: Full=Superoxide dismutase copper chaperone;
GN   Name=Ccs; Synonyms=Ccsd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10694572; DOI=10.1073/pnas.040461197;
RA   Wong P.C., Waggoner D., Subramaniam J.R., Tessarollo L.,
RA   Bartnikas T.B., Culotta V.C., Price D.L., Rothstein J., Gitlin J.D.;
RT   "Copper chaperone for superoxide dismutase is essential to activate
RT   mammalian Cu/Zn superoxide dismutase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:2886-2891(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NOD; TISSUE=Brain;
RX   PubMed=10773661;
RA   Moore S.D., Chen M.M., Cox D.W.;
RT   "Cloning and mapping of murine superoxide dismutase copper chaperone
RT   (Ccsd) and mapping of the human ortholog.";
RL   Cytogenet. Cell Genet. 88:35-37(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-274.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Delivers copper to copper zinc superoxide dismutase
CC       (SOD1).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:O14618};
CC       Note=Binds 2 copper ions per subunit.
CC       {ECO:0000250|UniProtKB:O14618};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O14618};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O14618};
CC   -!- SUBUNIT: Homodimer, and heterodimer with SOD1. Interacts with
CC       COMMD1 (By similarity). Interacts with XIAP/BIRC4 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Ubiquitinion by XIAP/BIRC4 leads to enhancement of its
CC       chaperone activity toward its physiologic target, SOD1, rather
CC       than proteasomal degradation. XIAP/BIRC4 preferentially
CC       ubiquitinates at Lys-241 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn
CC       superoxide dismutase family. {ECO:0000305}.
DR   EMBL; AF121906; AAD23832.1; -; mRNA.
DR   EMBL; AF173379; AAF70242.1; -; mRNA.
DR   EMBL; AK010264; BAB26806.1; -; mRNA.
DR   EMBL; BC026938; AAH26938.1; -; mRNA.
DR   CCDS; CCDS29438.1; -.
DR   RefSeq; NP_058588.1; NM_016892.3.
DR   UniGene; Mm.434411; -.
DR   ProteinModelPortal; Q9WU84; -.
DR   SMR; Q9WU84; -.
DR   BioGrid; 198563; 2.
DR   DIP; DIP-48692N; -.
DR   IntAct; Q9WU84; 2.
DR   STRING; 10090.ENSMUSP00000035486; -.
DR   iPTMnet; Q9WU84; -.
DR   PhosphoSitePlus; Q9WU84; -.
DR   SwissPalm; Q9WU84; -.
DR   EPD; Q9WU84; -.
DR   jPOST; Q9WU84; -.
DR   MaxQB; Q9WU84; -.
DR   PaxDb; Q9WU84; -.
DR   PRIDE; Q9WU84; -.
DR   Ensembl; ENSMUST00000037246; ENSMUSP00000035486; ENSMUSG00000034108.
DR   GeneID; 12460; -.
DR   KEGG; mmu:12460; -.
DR   UCSC; uc008gba.1; mouse.
DR   CTD; 9973; -.
DR   MGI; MGI:1333783; Ccs.
DR   eggNOG; ENOG410IPMW; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00940000159785; -.
DR   HOGENOM; HOG000263450; -.
DR   HOVERGEN; HBG018933; -.
DR   InParanoid; Q9WU84; -.
DR   KO; K04569; -.
DR   OMA; QDSDRHR; -.
DR   OrthoDB; 1527306at2759; -.
DR   PhylomeDB; Q9WU84; -.
DR   TreeFam; TF105184; -.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:Q9WU84; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000034108; Expressed in 265 organ(s), highest expression level in membranous labyrinth.
DR   ExpressionAtlas; Q9WU84; baseline and differential.
DR   Genevisible; Q9WU84; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   GO; GO:0051353; P:positive regulation of oxidoreductase activity; IMP:MGI.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   PROSITE; PS50846; HMA_2; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome;
KW   Ubl conjugation; Zinc.
FT   CHAIN         1    274       Copper chaperone for superoxide
FT                                dismutase.
FT                                /FTId=PRO_0000213544.
FT   DOMAIN       12     75       HMA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   REGION       88    234       Superoxide dismutase-like.
FT   METAL        22     22       Copper 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL        25     25       Copper 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       147    147       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       155    155       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       164    164       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       167    167       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       244    244       Copper 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       246    246       Copper 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   MOD_RES     267    267       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   DISULFID    141    227       {ECO:0000250}.
FT   CROSSLNK     76     76       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:O14618}.
FT   CROSSLNK    189    189       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:O14618}.
FT   CROSSLNK    216    216       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:O14618}.
FT   CROSSLNK    241    241       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:O14618}.
SQ   SEQUENCE   274 AA;  28912 MW;  19DCE48376C9D5A2 CRC64;
     MASKSGDGGT VCALEFAVQM SCQSCVDAVH KTLKGVAGVQ NVDVQLENQM VLVQTTLPSQ
     EVQALLESTG RQAVLKGMGS SQLQNLGAAV AILEGCGSIQ GVVRFLQLSS ELCLIEGTID
     GLEPGLHGLH VHQYGDLTRD CNSCGDHFNP DGASHGGPQD TDRHRGDLGN VRAEAGGRAT
     FRIEDKQLKV WDVIGRSLVI DEGEDDLGRG GHPLSKITGN SGKRLACGII ARSAGLFQNP
     KQICSCDGLT IWEERGRPIA GQGRKDSAQP PAHL
//
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