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CSTP1_RAT
ID   CSTP1_RAT               Reviewed;         331 AA.
AC   Q5M9F0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Centriolar satellite-associated tubulin polyglutamylase complex regulator 1;
GN   Name=Cstpp1;
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-319, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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   -!- FUNCTION: Regulator of the tubulin polyglutamylase complex (TPGC) that
CC       controls cytoskeletal organization, nuclear shape, and cilium
CC       disassembly by balancing microtubule and actin assembly. Regulates the
CC       assembly and stability of the TPGC and thereby modulates
CC       polyglutamylation of the microtubule, which antagonizes MAP4 binding.
CC       {ECO:0000250|UniProtKB:Q9H6J7}.
CC   -!- SUBUNIT: Interacts with PCM1. Interacts with TTLL1, TPGS1, TPGS2 and
CC       LRRC49; the interactions link CSTPP1 to the complex TPGC. Binds to
CC       alpha-tubulin. {ECO:0000250|UniProtKB:Q9H6J7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriolar satellite
CC       {ECO:0000250|UniProtKB:Q9H6J7}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9H6J7}. Note=Associated with microtubules.
CC       {ECO:0000250|UniProtKB:Q9H6J7}.
CC   -!- SIMILARITY: Belongs to the CSTPP1 family. {ECO:0000305}.
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DR   EMBL; BC087159; AAH87159.1; -; mRNA.
DR   RefSeq; NP_001013940.1; NM_001013918.1.
DR   AlphaFoldDB; Q5M9F0; -.
DR   STRING; 10116.ENSRNOP00000039464; -.
DR   iPTMnet; Q5M9F0; -.
DR   PhosphoSitePlus; Q5M9F0; -.
DR   PaxDb; Q5M9F0; -.
DR   PRIDE; Q5M9F0; -.
DR   Ensembl; ENSRNOT00000095774; ENSRNOP00000088632; ENSRNOG00000014798.
DR   GeneID; 295930; -.
DR   KEGG; rno:295930; -.
DR   UCSC; RGD:1309540; rat.
DR   CTD; 79096; -.
DR   RGD; 1309540; RGD1309540.
DR   eggNOG; ENOG502QRVN; Eukaryota.
DR   GeneTree; ENSGT00390000012935; -.
DR   HOGENOM; CLU_064579_0_0_1; -.
DR   InParanoid; Q5M9F0; -.
DR   OMA; NIHHRRK; -.
DR   OrthoDB; 1103030at2759; -.
DR   PhylomeDB; Q5M9F0; -.
DR   TreeFam; TF329168; -.
DR   PRO; PR:Q5M9F0; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000014798; Expressed in frontal cortex and 20 other tissues.
DR   Genevisible; Q5M9F0; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   InterPro; IPR038968; C11orf49.
DR   PANTHER; PTHR34252; PTHR34252; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome.
FT   CHAIN           1..331
FT                   /note="Centriolar satellite-associated tubulin
FT                   polyglutamylase complex regulator 1"
FT                   /id="PRO_0000281429"
FT   REGION          1..225
FT                   /note="Required for interaction with TPGS1, LRRC49, and
FT                   TTLL1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6J7"
FT   REGION          1..111
FT                   /note="Required for interaction with PCM1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6J7"
FT   REGION          112..331
FT                   /note="Required for interaction with TPGS2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6J7"
FT   REGION          292..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   331 AA;  37476 MW;  64CCA6B1EA9A8B37 CRC64;
     MLSPERLALP DYEYLAQRHV LTYMEDAVCQ LLENKEDISQ YGIARFFTEY FNSVCQGTHI
     LFREFSFIQA TPHNRASFLR AFWRCFRTVG KNGDLLTMRE YHCLLQLLCP DFPLELTQKA
     ARIVLMDDAM DCLMSFSDFL FAFQIQFYYS EFLESVAAIY QDLLSGKNPN TVIVPTSSSG
     QHRQRPALGD AGMLDGVEAS LFCQRLENLC DRHKYSCPPP ALVKEILSNV QRLTFYGFLV
     ALSKHHGINQ ALGALPDKGD LMHDPAMDEE LERLLVQVPG LVNSITATSE ASCLPSRTPP
     RVGSPWKPLH RSRKLDAESD GSTEETDESE T
 
 
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