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CCD86_MOUSE
ID   CCD86_MOUSE             Reviewed;         426 AA.
AC   Q9JJ89; Q8BGH9; Q8C2F2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Coiled-coil domain-containing protein 86;
DE   AltName: Full=Cytokine-induced protein with coiled-coil domain;
DE            Short=mCyclon;
GN   Name=Ccdc86; Synonyms=Cyclon, D19Ertd678e; ORFNames=MNCb-4327;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=17300783; DOI=10.1016/j.febslet.2007.01.083;
RA   Hoshino A., Fujii H.;
RT   "Redundant promoter elements mediate IL-3-induced expression of a novel
RT   cytokine-inducible gene, cyclon.";
RL   FEBS Lett. 581:975-980(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT   oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Wolffian duct;
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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-194; SER-225;
RP   SER-252; SER-253 AND SER-283, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Pancreas, and Spleen;
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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   CITRULLINATION AT ARG-408.
RX   PubMed=24463520; DOI=10.1038/nature12942;
RA   Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA   Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA   Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT   "Citrullination regulates pluripotency and histone H1 binding to
RT   chromatin.";
RL   Nature 507:104-108(2014).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17300783}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
CC       heart, liver, kidney. {ECO:0000269|PubMed:17300783}.
CC   -!- INDUCTION: By interleukin-3 (IL3). {ECO:0000269|PubMed:17300783}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
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DR   EMBL; DQ501252; ABF68613.1; -; mRNA.
DR   EMBL; AB041663; BAA95108.1; -; mRNA.
DR   EMBL; AK078407; BAC37260.1; -; mRNA.
DR   EMBL; AK078455; BAC37282.1; -; mRNA.
DR   EMBL; AK088727; BAC40530.1; -; mRNA.
DR   EMBL; BC043326; AAH43326.1; -; mRNA.
DR   CCDS; CCDS29593.1; -.
DR   RefSeq; NP_076220.2; NM_023731.3.
DR   AlphaFoldDB; Q9JJ89; -.
DR   SMR; Q9JJ89; -.
DR   BioGRID; 224366; 1.
DR   IntAct; Q9JJ89; 1.
DR   MINT; Q9JJ89; -.
DR   STRING; 10090.ENSMUSP00000025639; -.
DR   iPTMnet; Q9JJ89; -.
DR   PhosphoSitePlus; Q9JJ89; -.
DR   EPD; Q9JJ89; -.
DR   jPOST; Q9JJ89; -.
DR   MaxQB; Q9JJ89; -.
DR   PaxDb; Q9JJ89; -.
DR   PeptideAtlas; Q9JJ89; -.
DR   PRIDE; Q9JJ89; -.
DR   ProteomicsDB; 265600; -.
DR   Antibodypedia; 43508; 53 antibodies from 19 providers.
DR   DNASU; 108673; -.
DR   Ensembl; ENSMUST00000025639; ENSMUSP00000025639; ENSMUSG00000024732.
DR   GeneID; 108673; -.
DR   KEGG; mmu:108673; -.
DR   UCSC; uc008grj.2; mouse.
DR   CTD; 79080; -.
DR   MGI; MGI:1277220; Ccdc86.
DR   VEuPathDB; HostDB:ENSMUSG00000024732; -.
DR   eggNOG; KOG4538; Eukaryota.
DR   GeneTree; ENSGT00390000017281; -.
DR   HOGENOM; CLU_065828_0_0_1; -.
DR   InParanoid; Q9JJ89; -.
DR   OMA; FSQMLQD; -.
DR   OrthoDB; 1470010at2759; -.
DR   PhylomeDB; Q9JJ89; -.
DR   TreeFam; TF325663; -.
DR   BioGRID-ORCS; 108673; 24 hits in 76 CRISPR screens.
DR   ChiTaRS; Ccdc86; mouse.
DR   PRO; PR:Q9JJ89; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q9JJ89; protein.
DR   Bgee; ENSMUSG00000024732; Expressed in primitive streak and 242 other tissues.
DR   Genevisible; Q9JJ89; MM.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   InterPro; IPR026570; CCDC86.
DR   InterPro; IPR005579; Cgr1-like.
DR   PANTHER; PTHR13557; PTHR13557; 1.
DR   Pfam; PF03879; Cgr1; 1.
PE   1: Evidence at protein level;
KW   Citrullination; Coiled coil; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..426
FT                   /note="Coiled-coil domain-containing protein 86"
FT                   /id="PRO_0000286093"
FT   REGION          1..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          346..389
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        31..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..149
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6F5"
FT   MOD_RES         66
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6F5"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6F5"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6F5"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6F5"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6F5"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6F5"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6F5"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         408
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000269|PubMed:24463520"
FT   CONFLICT        1
FT                   /note="M -> L (in Ref. 2; BAA95108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="C -> F (in Ref. 3; BAC37282/BAC37260)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  46487 MW;  63A4014176E1F1B7 CRC64;
     MDTPLRRSRR LEGLKPLSPE NLPVPEVSRA KRALVDFKSN SEETGELKST RVPPLSLPSP
     GPQPETSPGS PCPPLSLPSP GPQPETSPGS PCPPLSLPSP GPQPETSPGS PCPPLSLPSP
     GPQPETSPGS PCPPLSLPSP GPQPEASPGS PGPRQDADDG SPQRQPEPHP GSLQPHQDLG
     LESPAGQTES SPESPQREQP SKLPPPQGEL DSEAAHAKEE VIPGSPEPCP GQQAPGPEPS
     QPAQELTVQA PSSPERQLEP GKLPPAGETV TESLNLKKRV IASPQAPASK KLKEKEELPV
     IPKGKPKSGR VWKDRSKKRF SQMVQDKPLR TSWQRKMKER QERKLAKDFA RHLEEEKQRR
     RQEKKERRAE NLRRRLENER KAEIVQVIRN PAKLKKAKKK QLRSIEKRDT LALLQKQPPQ
     RPVAKV
 
 
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