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CCD81_RAT
ID   CCD81_RAT               Reviewed;         651 AA.
AC   Q5XIN9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Coiled-coil domain-containing protein 81;
GN   Name=Ccdc81;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-273; SER-275;
RP   SER-294 AND SER-416, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q6ZN84}.
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DR   EMBL; BC083639; AAH83639.1; -; mRNA.
DR   RefSeq; NP_001014043.1; NM_001014021.1.
DR   AlphaFoldDB; Q5XIN9; -.
DR   SMR; Q5XIN9; -.
DR   iPTMnet; Q5XIN9; -.
DR   PhosphoSitePlus; Q5XIN9; -.
DR   Ensembl; ENSRNOT00000102115; ENSRNOP00000080187; ENSRNOG00000033733.
DR   GeneID; 308810; -.
DR   KEGG; rno:308810; -.
DR   UCSC; RGD:1306766; rat.
DR   CTD; 60494; -.
DR   RGD; 1306766; Ccdc81.
DR   GeneTree; ENSGT00390000011985; -.
DR   InParanoid; Q5XIN9; -.
DR   OrthoDB; 759717at2759; -.
DR   PhylomeDB; Q5XIN9; -.
DR   PRO; PR:Q5XIN9; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   InterPro; IPR040673; CCDC81_HU_dom_2.
DR   InterPro; IPR026295; Coiled-coil_dom_cont_p_81.
DR   InterPro; IPR028034; HU-CCDC81.
DR   InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR   PANTHER; PTHR14362; PTHR14362; 1.
DR   Pfam; PF14908; HU-CCDC81_euk_1; 1.
DR   Pfam; PF18289; HU-CCDC81_euk_2; 1.
DR   SUPFAM; SSF47729; SSF47729; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..651
FT                   /note="Coiled-coil domain-containing protein 81"
FT                   /id="PRO_0000288879"
FT   REGION          194..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          428..465
FT                   /evidence="ECO:0000255"
FT   COILED          539..566
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        209..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   651 AA;  75314 MW;  23A752432A730B66 CRC64;
     MLDRIGPGFQ DLCRQVLPTL PSLSQEEVST IWGNVSDFVE RQLTMHKGVQ ISGLGTFTFT
     RQQLEMGNKK FVLVQRPVFI MSEKLVQTHG LKQNKVFSPG DIPVVPLNFV MISLEGPFNR
     DTIEGCVRET LLFLSRSISI KQNVEFTFKG IGVLSIRDNK VKMRFYKDFL SSVDGSGTLT
     KALANRPGTM DSVLSSRESF GKRPNSALAF PRIEHKETEN KPPVEVFGEE GGENRPRKSK
     LKDQSDKEEG AWEISSAKKH RDRQSISPAK VTSGSLLDKF ERSGNGGKIT ENLSPGGQRN
     DNEKPKTSPA PACQDHNKAG QEMCYVCLQR AQRNFALYYG DEKRRREIED ERLMQQYQIA
     KDQEAFFKSQ MKSMATREQN QKNAAYNLGV AEAIRSHKNE KPDFYKSFLF DKRPLSPEIN
     AFKQEEYSQS LLKQMESKRE KEIKQRQNRE LMDRLEQVQL TEELAAQRAQ YLKEKMEETQ
     YYKRALDAQV KNKPSQLPMF EPDSAEPIFG KNEGEMEMEK RKREQSCMKH QMEAAANLKR
     NTILNQLVDQ RRDLQMLQRT KREHLADRAA EVDRVNRLNQ CLQEDWDRSL AMKKQRDLEE
     KAFERASDKL FLLDQCEKYR RCRQCQRRTS NTGESNVWPL NKFLQGSRLL V
 
 
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