位置:首页 > 蛋白库 > CCDC6_MOUSE
CCDC6_MOUSE
ID   CCDC6_MOUSE             Reviewed;         469 AA.
AC   D3YZP9;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Coiled-coil domain-containing protein 6;
GN   Name=Ccdc6;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233 AND SER-237, AND
RP   IDENTIFICATION BY 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-233; SER-237 AND
RP   SER-316, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-380, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Note=May be a cytoskeletal protein. {ECO:0000250}.
CC   -!- DOMAIN: The protein has mostly an alpha helical conformation similar to
CC       myosin heavy-chain tail that might adopt a coiled-coil conformation.
CC       {ECO:0000250}.
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; AC132435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466553; EDL31982.1; -; Genomic_DNA.
DR   CCDS; CCDS48591.1; -.
DR   RefSeq; NP_001104591.1; NM_001111121.1.
DR   AlphaFoldDB; D3YZP9; -.
DR   SMR; D3YZP9; -.
DR   BioGRID; 218173; 10.
DR   IntAct; D3YZP9; 1.
DR   STRING; 10090.ENSMUSP00000123374; -.
DR   iPTMnet; D3YZP9; -.
DR   PhosphoSitePlus; D3YZP9; -.
DR   EPD; D3YZP9; -.
DR   jPOST; D3YZP9; -.
DR   MaxQB; D3YZP9; -.
DR   PaxDb; D3YZP9; -.
DR   PeptideAtlas; D3YZP9; -.
DR   PRIDE; D3YZP9; -.
DR   ProteomicsDB; 265369; -.
DR   Antibodypedia; 14268; 230 antibodies from 29 providers.
DR   Ensembl; ENSMUST00000147545; ENSMUSP00000123374; ENSMUSG00000048701.
DR   GeneID; 76551; -.
DR   KEGG; mmu:76551; -.
DR   UCSC; uc011xfv.1; mouse.
DR   CTD; 8030; -.
DR   MGI; MGI:1923801; Ccdc6.
DR   VEuPathDB; HostDB:ENSMUSG00000048701; -.
DR   eggNOG; KOG2129; Eukaryota.
DR   GeneTree; ENSGT00390000013594; -.
DR   HOGENOM; CLU_033433_2_0_1; -.
DR   InParanoid; D3YZP9; -.
DR   OMA; NLSAHIQ; -.
DR   OrthoDB; 1142037at2759; -.
DR   PhylomeDB; D3YZP9; -.
DR   TreeFam; TF321211; -.
DR   BioGRID-ORCS; 76551; 8 hits in 75 CRISPR screens.
DR   ChiTaRS; Ccdc6; mouse.
DR   PRO; PR:D3YZP9; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; D3YZP9; protein.
DR   Bgee; ENSMUSG00000048701; Expressed in animal zygote and 255 other tissues.
DR   ExpressionAtlas; D3YZP9; baseline and differential.
DR   Genevisible; D3YZP9; MM.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   InterPro; IPR019152; DUF2046.
DR   PANTHER; PTHR15276; PTHR15276; 1.
DR   Pfam; PF09755; DUF2046; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosomal rearrangement; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW   SH3-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   CHAIN           2..469
FT                   /note="Coiled-coil domain-containing protein 6"
FT                   /id="PRO_0000415808"
FT   REPEAT          99..127
FT                   /note="1"
FT   REPEAT          128..156
FT                   /note="2"
FT   REPEAT          157..185
FT                   /note="3"
FT   REPEAT          186..199
FT                   /note="4; approximate"
FT   REPEAT          200..228
FT                   /note="5"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..228
FT                   /note="5 X 29 AA tandem repeats"
FT   REGION          335..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          47..320
FT                   /evidence="ECO:0000255"
FT   MOTIF           435..444
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        337..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..463
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   MOD_RES         277
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         342
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   MOD_RES         380
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16204"
SQ   SEQUENCE   469 AA;  52939 MW;  708882EB2F131354 CRC64;
     MADSASESDT DAAGGGPAAM QSSCSATSGG SGGGGGGKSG GIVISPFRLE ELTNRLASLQ
     QENKVLKIEL ETYKLKCKAL QEENRDLRKA SVTIQARAEQ EEEFISNTLF KKIQALQKEK
     ETLAVNYEKE EEFLTNELSR KLMQLQHEKA ELEQHLEQEQ EFQVNKLMKK IKKLENDTIS
     KQLTLEQLRR EKIDLENTLE QEQEALVNRL WKRMDKLEAE KRILQEKLDQ PVSAPPSPRD
     ISMEIDSPEN MMRHIRFLKN EVERLKKQLR AAQLQHSEKM AQYLEEERHM REENLRLQRK
     LQREMERREA LCRQLSESES SLEMDDERYF NEMSAQGLRP RTVSSPIPYT PSPSSSRPIS
     PGLSYASHTV GFTPPTSLTR AGMSYYNSPG LHVQHMGASH GITRPSPRRS SSPDKFKRPT
     PPPSPNTQSP VQPPPPPPPP PMQPAVPSAA PTQPAPTQPQ HPVHPSSQP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024