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BORG5_RAT
ID   BORG5_RAT               Reviewed;         388 AA.
AC   A1A5P0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cdc42 effector protein 1;
DE   AltName: Full=Binder of Rho GTPases 5;
GN   Name=Cdc42ep1 {ECO:0000312|EMBL:AAI28745.1};
GN   Synonyms=Borg5 {ECO:0000250|UniProtKB:Q00587};
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] {ECO:0000312|EMBL:AAI28745.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung {ECO:0000312|EMBL:AAI28745.1};
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-121; SER-207; SER-209;
RP   SER-298; SER-318; SER-347 AND SER-350, AND IDENTIFICATION BY MASS
RP   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: Probably involved in the organization of the actin
CC       cytoskeleton. Induced membrane extensions in fibroblasts (By
CC       similarity). {ECO:0000250|UniProtKB:Q00587}.
CC   -!- SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner.
CC       {ECO:0000250|UniProtKB:Q00587}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- DOMAIN: The CRIB domain mediates interaction with CDC42.
CC       {ECO:0000250|UniProtKB:Q00587}.
CC   -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000255}.
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DR   EMBL; BC128744; AAI28745.1; -; mRNA.
DR   RefSeq; NP_001073168.1; NM_001079700.1.
DR   RefSeq; XP_017450354.1; XM_017594865.1.
DR   RefSeq; XP_017450355.1; XM_017594866.1.
DR   RefSeq; XP_017450356.1; XM_017594867.1.
DR   RefSeq; XP_017450357.1; XM_017594868.1.
DR   AlphaFoldDB; A1A5P0; -.
DR   IntAct; A1A5P0; 2.
DR   STRING; 10116.ENSRNOP00000011269; -.
DR   iPTMnet; A1A5P0; -.
DR   PhosphoSitePlus; A1A5P0; -.
DR   PaxDb; A1A5P0; -.
DR   PeptideAtlas; A1A5P0; -.
DR   PRIDE; A1A5P0; -.
DR   Ensembl; ENSRNOT00000011270; ENSRNOP00000011269; ENSRNOG00000008517.
DR   GeneID; 315121; -.
DR   KEGG; rno:315121; -.
DR   CTD; 11135; -.
DR   RGD; 1311131; Cdc42ep1.
DR   eggNOG; ENOG502RZ2H; Eukaryota.
DR   GeneTree; ENSGT00940000160068; -.
DR   HOGENOM; CLU_787446_0_0_1; -.
DR   InParanoid; A1A5P0; -.
DR   OMA; PRGHCPN; -.
DR   OrthoDB; 1244464at2759; -.
DR   PhylomeDB; A1A5P0; -.
DR   TreeFam; TF331725; -.
DR   Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR   Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR   Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR   Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR   Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR   Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR   Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR   PRO; PR:A1A5P0; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000008517; Expressed in stomach and 20 other tissues.
DR   Genevisible; A1A5P0; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:RGD.
DR   GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR   InterPro; IPR029273; Cdc42_effect.
DR   InterPro; IPR000095; CRIB_dom.
DR   Pfam; PF14957; BORG_CEP; 1.
DR   Pfam; PF00786; PBD; 1.
DR   SMART; SM00285; PBD; 1.
DR   PROSITE; PS50108; CRIB; 1.
PE   1: Evidence at protein level;
KW   Cell shape; Cytoplasm; Cytoskeleton; Membrane; Methylation; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..388
FT                   /note="Cdc42 effector protein 1"
FT                   /id="PRO_0000278120"
FT   DOMAIN          38..52
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   REPEAT          237..243
FT                   /note="1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          250..256
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..270
FT                   /note="2 X 7 AA tandem repeats of [PT]-[AT]-A-[ENT]-[PT]-
FT                   [PTS]-[AG]"
FT                   /evidence="ECO:0000255"
FT   REGION          237..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         34
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91W92"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91W92"
FT   MOD_RES         53
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91W92"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00587"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   388 AA;  41029 MW;  62D900F6AEDBEC3E CRC64;
     MPGPQGGTGA PSMSLGKLSP VGWVPSSHGK RRLTADMISP PLGDFRHTMH VGRGGDVFGD
     TSFLSNHGGR SGNTHRSPRS FLARKLQQVR RVGVPPRRMA SPAATSPAPP PISPIIKNAI
     SLPQLNQATY DSLVVSKLSF DSTPASSTDG RSGYGLESGF CTISRLPRVE KHSSRDRDHD
     RDPDHSQDRE QSSSPSEPNP NPELRRSDSL LSFRFDLDLG PSLLSELLGV MSLSEAPAAN
     PPAPAANPAP TAKPPADAVT TLDTVTSLPA PTASSPSSGR FPNGVTAVLG PVAEVKASPV
     GEGPQVPSKM AFDRRGASWG AIRASRHYTE MDARRELAGV LPQVHGSWES LNEEWSAPPA
     SSRAPVPSTV QANAFEFADA DEDDEVKV
 
 
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