BORG1_HUMAN
ID BORG1_HUMAN Reviewed; 210 AA.
AC O14613; B2RD85; Q9UNS0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cdc42 effector protein 2;
DE AltName: Full=Binder of Rho GTPases 1;
GN Name=CDC42EP2; Synonyms=BORG1, CEP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9253601; DOI=10.1101/gr.7.7.725;
RA Guru S.C., Agarwal S.K., Manickam P., Olufemi S.-E., Crabtree J.S.,
RA Weisemann J.M., Kester M.B., Kim Y.S., Wang Y., Emmert-Buck M.R.,
RA Liotta L.A., Spiegel A.M., Boguski M.S., Roe B.A., Collins F.S.,
RA Burns A.L., Marx S.J., Chandrasekharappa S.C.;
RT "A transcript map for the 2.8-Mb region containing the multiple endocrine
RT neoplasia type 1 locus.";
RL Genome Res. 7:725-735(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RHOQ AND CDC42, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=10490598; DOI=10.1128/mcb.19.10.6585;
RA Joberty G., Perlungher R.R., Macara I.G.;
RT "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins.";
RL Mol. Cell. Biol. 19:6585-6597(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDC42, MUTAGENESIS
RP OF 39-HIS--HIS-42, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=11035016; DOI=10.1074/jbc.m007039200;
RA Hirsch D.S., Pirone D.M., Burbelo P.D.;
RT "A new family of Cdc42 effector proteins, CEPs, function in fibroblast and
RT epithelial cell shape changes.";
RL J. Biol. Chem. 276:875-883(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-176 AND PHE-191.
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Pancreas;
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 [8]
RP INTERACTION WITH SEPT7.
RX PubMed=11584266; DOI=10.1038/ncb1001-861;
RA Joberty G., Perlungher R.R., Sheffield P.J., Kinoshita M., Noda M.,
RA Haystead T., Macara I.G.;
RT "Borg proteins control septin organization and are negatively regulated by
RT Cdc42.";
RL Nat. Cell Biol. 3:861-866(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-141, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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.
CC {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016}.
CC -!- SUBUNIT: Interacts with RHOQ and CDC42 in a GTP-dependent manner, and
CC with SEPT7. {ECO:0000269|PubMed:10490598, ECO:0000269|PubMed:11035016,
CC ECO:0000269|PubMed:11584266}.
CC -!- INTERACTION:
CC O14613; Q9UNA1: ARHGAP26; NbExp=3; IntAct=EBI-3438291, EBI-1390913;
CC O14613; Q9UNA1-2: ARHGAP26; NbExp=3; IntAct=EBI-3438291, EBI-16430964;
CC O14613; Q9NQ75-2: CASS4; NbExp=4; IntAct=EBI-3438291, EBI-12270182;
CC O14613; P60953: CDC42; NbExp=10; IntAct=EBI-3438291, EBI-81752;
CC O14613; P10606: COX5B; NbExp=3; IntAct=EBI-3438291, EBI-1053725;
CC O14613; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-3438291, EBI-11746523;
CC O14613; Q9Y5B8: NME7; NbExp=6; IntAct=EBI-3438291, EBI-744782;
CC O14613; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3438291, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:11035016}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11035016}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11035016}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the heart. Weakly expressed in
CC the pancreas and liver. {ECO:0000269|PubMed:10490598}.
CC -!- DOMAIN: The CRIB domain mediates interaction with CDC42.
CC -!- SIMILARITY: Belongs to the BORG/CEP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc42ep2/";
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DR EMBL; AF001436; AAB81206.1; -; mRNA.
DR EMBL; AF163840; AAD48784.1; -; mRNA.
DR EMBL; AF098290; AAD16185.1; -; mRNA.
DR EMBL; AK315444; BAG37832.1; -; mRNA.
DR EMBL; BT020004; AAV38807.1; -; mRNA.
DR EMBL; AF548903; AAN39381.1; -; Genomic_DNA.
DR EMBL; BC022337; AAH22337.1; -; mRNA.
DR EMBL; BC075834; AAH75834.1; -; mRNA.
DR CCDS; CCDS8099.1; -.
DR RefSeq; NP_006770.1; NM_006779.3.
DR RefSeq; XP_016872583.1; XM_017017094.1.
DR AlphaFoldDB; O14613; -.
DR BioGRID; 115702; 13.
DR IntAct; O14613; 8.
DR STRING; 9606.ENSP00000279249; -.
DR iPTMnet; O14613; -.
DR PhosphoSitePlus; O14613; -.
DR BioMuta; CDC42EP2; -.
DR EPD; O14613; -.
DR jPOST; O14613; -.
DR MassIVE; O14613; -.
DR MaxQB; O14613; -.
DR PaxDb; O14613; -.
DR PeptideAtlas; O14613; -.
DR PRIDE; O14613; -.
DR ProteomicsDB; 48116; -.
DR Antibodypedia; 29752; 223 antibodies from 30 providers.
DR DNASU; 10435; -.
DR Ensembl; ENST00000279249.3; ENSP00000279249.2; ENSG00000149798.5.
DR Ensembl; ENST00000533419.1; ENSP00000431660.1; ENSG00000149798.5.
DR GeneID; 10435; -.
DR KEGG; hsa:10435; -.
DR MANE-Select; ENST00000279249.3; ENSP00000279249.2; NM_006779.4; NP_006770.1.
DR UCSC; uc001odl.3; human.
DR CTD; 10435; -.
DR DisGeNET; 10435; -.
DR GeneCards; CDC42EP2; -.
DR HGNC; HGNC:16263; CDC42EP2.
DR HPA; ENSG00000149798; Low tissue specificity.
DR MIM; 606132; gene.
DR neXtProt; NX_O14613; -.
DR OpenTargets; ENSG00000149798; -.
DR PharmGKB; PA38396; -.
DR VEuPathDB; HostDB:ENSG00000149798; -.
DR eggNOG; ENOG502RY28; Eukaryota.
DR GeneTree; ENSGT00940000161776; -.
DR HOGENOM; CLU_073229_0_0_1; -.
DR InParanoid; O14613; -.
DR OMA; DQDLGHM; -.
DR OrthoDB; 1244464at2759; -.
DR PhylomeDB; O14613; -.
DR TreeFam; TF331725; -.
DR PathwayCommons; O14613; -.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR SignaLink; O14613; -.
DR SIGNOR; O14613; -.
DR BioGRID-ORCS; 10435; 21 hits in 1077 CRISPR screens.
DR ChiTaRS; CDC42EP2; human.
DR GeneWiki; CDC42EP2; -.
DR GenomeRNAi; 10435; -.
DR Pharos; O14613; Tbio.
DR PRO; PR:O14613; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O14613; protein.
DR Bgee; ENSG00000149798; Expressed in apex of heart and 93 other tissues.
DR Genevisible; O14613; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0001515; F:opioid peptide activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; NAS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; TAS:UniProtKB.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
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:0007744|PubMed:22814378"
FT CHAIN 2..210
FT /note="Cdc42 effector protein 2"
FT /id="PRO_0000212648"
FT DOMAIN 30..44
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 122..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQP4"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 176
FT /note="N -> S (in dbSNP:rs4149839)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_023001"
FT VARIANT 191
FT /note="I -> F (in dbSNP:rs7120634)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_023002"
FT MUTAGEN 39..42
FT /note="HTIH->ATIA: No binding with CDC42; no induced
FT pseudopodia formation."
FT /evidence="ECO:0000269|PubMed:11035016"
FT CONFLICT 92
FT /note="C -> V (in Ref. 3; AAD16185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 22484 MW; 7755100672FFB69C CRC64;
MSTKVPIYLK RGSRKGKKEK LRDLLSSDMI SPPLGDFRHT IHIGSGGGSD MFGDISFLQG
KFHLLPGTMV EGPEEDGTFD LPFQFTRTAT VCGRELPDGP SPLLKNAISL PVIGGPQALT
LPTAQAPPKP PRLHLETPQP SPQEGGSVDI WRIPETGSPN SGLTPESGAE EPFLSNASSL
LSLHVDLGPS ILDDVLQIMD QDLDSMQIPT
