BORG1_MOUSE
ID BORG1_MOUSE Reviewed; 214 AA.
AC Q8JZX9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cdc42 effector protein 2;
DE AltName: Full=Binder of Rho GTPases 1;
GN Name=Cdc42ep2; Synonyms=Borg1, Cep2;
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 MRNA].
RC STRAIN=Czech II; TISSUE=Lung;
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-137; SER-141 AND SER-145, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
CC -!- FUNCTION: Probably involved in the organization of the actin
CC cytoskeleton. May act downstream of CDC42 to induce actin filament
CC assembly leading to cell shape changes. Induces pseudopodia formation
CC in fibroblasts in a CDC42-dependent manner (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC42 and RHOQ in a GTP-dependent manner, and
CC with SEPT7. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000305}.
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; BC034884; AAH34884.1; -; mRNA.
DR CCDS; CCDS29484.1; -.
DR RefSeq; NP_081048.1; NM_026772.2.
DR AlphaFoldDB; Q8JZX9; -.
DR BioGRID; 222493; 1.
DR STRING; 10090.ENSMUSP00000059883; -.
DR iPTMnet; Q8JZX9; -.
DR PhosphoSitePlus; Q8JZX9; -.
DR jPOST; Q8JZX9; -.
DR MaxQB; Q8JZX9; -.
DR PaxDb; Q8JZX9; -.
DR PRIDE; Q8JZX9; -.
DR ProteomicsDB; 265225; -.
DR Antibodypedia; 29752; 223 antibodies from 30 providers.
DR DNASU; 104252; -.
DR Ensembl; ENSMUST00000055458; ENSMUSP00000059883; ENSMUSG00000045664.
DR GeneID; 104252; -.
DR KEGG; mmu:104252; -.
DR UCSC; uc008gfz.2; mouse.
DR CTD; 10435; -.
DR MGI; MGI:1929744; Cdc42ep2.
DR VEuPathDB; HostDB:ENSMUSG00000045664; -.
DR eggNOG; ENOG502RY28; Eukaryota.
DR GeneTree; ENSGT00940000161776; -.
DR HOGENOM; CLU_073229_0_0_1; -.
DR InParanoid; Q8JZX9; -.
DR OMA; DQDLGHM; -.
DR OrthoDB; 1244464at2759; -.
DR PhylomeDB; Q8JZX9; -.
DR TreeFam; TF331725; -.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR BioGRID-ORCS; 104252; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Cdc42ep2; mouse.
DR PRO; PR:Q8JZX9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8JZX9; protein.
DR Bgee; ENSMUSG00000045664; Expressed in tarsal region and 177 other tissues.
DR Genevisible; Q8JZX9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0001515; F:opioid peptide activity; IPI:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR InterPro; IPR029273; Cdc42_effect.
DR InterPro; IPR017363; Cdc42_effector_prot_2.
DR InterPro; IPR000095; CRIB_dom.
DR Pfam; PF14957; BORG_CEP; 2.
DR Pfam; PF00786; PBD; 1.
DR PIRSF; PIRSF038036; Cdc42_effector_p2; 1.
DR SMART; SM00285; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell shape; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O14613"
FT CHAIN 2..214
FT /note="Cdc42 effector protein 2"
FT /id="PRO_0000212649"
FT DOMAIN 30..44
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 119..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O14613"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14613"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQP4"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 214 AA; 22997 MW; 24AD498747C2A6D5 CRC64;
MSTKVPIYLK RGSRKGKKEK LRDLLSSDMI SPPLGDFRHT IHIGSGGGDD MFGDISFLQG
KFHLLPGTAV EEAEEDGSFD LPFQFTRTTT VCGRELPDGL SPLLKNAISL PVIGGPQALT
LPTAQAPPKP PRLHLESPQP SPQPSPQGAG NVDVWRIPEA GSPHNGMSPE PEAEEPFLSH
ASSLLSLHVD LGPSILDDVL QIMDHDLGRV QIPT
