ID BORG2_HUMAN Reviewed; 254 AA. AC Q9UKI2; B2R8S0; O95353; Q9UQJ0; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 165. DE RecName: Full=Cdc42 effector protein 3; DE AltName: Full=Binder of Rho GTPases 2; DE AltName: Full=MSE55-related Cdc42-binding protein; GN Name=CDC42EP3; Synonyms=BORG2, CEP3; 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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION RP WITH RHOQ AND CDC42. RC TISSUE=Heart; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Uterus; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Alberts A.S.; RT "MSE55-related Cdc42-binding protein."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). 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 (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 [10] 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; 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). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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. {ECO:0000269|PubMed:10490598, CC 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:11584266}. CC -!- INTERACTION: CC Q9UKI2; O14579: COPE; NbExp=3; IntAct=EBI-723480, EBI-711301; CC Q9UKI2; Q5S007: LRRK2; NbExp=2; IntAct=EBI-723480, EBI-5323863; 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 and weakly in the CC brain. {ECO:0000269|PubMed:10490598}. 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; AF164118; AAD48815.1; -; mRNA. DR EMBL; AF104857; AAD16888.1; -; mRNA. DR EMBL; AF094521; AAC71773.1; -; mRNA. DR EMBL; AL136842; CAB66776.1; -; mRNA. DR EMBL; BT007190; AAP35854.1; -; mRNA. DR EMBL; AK313483; BAG36267.1; -; mRNA. DR EMBL; AC006369; AAX93072.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00390.1; -; Genomic_DNA. DR EMBL; BC019270; AAH19270.1; -; mRNA. DR CCDS; CCDS1791.1; -. DR PIR; T46465; T46465. DR RefSeq; NP_001257365.1; NM_001270436.1. DR RefSeq; NP_001257366.1; NM_001270437.1. DR RefSeq; NP_001257367.1; NM_001270438.1. DR RefSeq; NP_006440.2; NM_006449.4. DR RefSeq; XP_011530784.1; XM_011532482.2. DR AlphaFoldDB; Q9UKI2; -. DR BioGRID; 115849; 20. DR IntAct; Q9UKI2; 9. DR STRING; 9606.ENSP00000480549; -. DR GlyGen; Q9UKI2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UKI2; -. DR PhosphoSitePlus; Q9UKI2; -. DR BioMuta; CDC42EP3; -. DR DMDM; 71152340; -. DR CPTAC; CPTAC-961; -. DR EPD; Q9UKI2; -. DR jPOST; Q9UKI2; -. DR MassIVE; Q9UKI2; -. DR MaxQB; Q9UKI2; -. DR PaxDb; 9606-ENSP00000295324; -. DR PeptideAtlas; Q9UKI2; -. DR ProteomicsDB; 84789; -. DR Pumba; Q9UKI2; -. DR Antibodypedia; 29451; 240 antibodies from 27 providers. DR DNASU; 10602; -. DR Ensembl; ENST00000295324.4; ENSP00000295324.3; ENSG00000163171.8. DR Ensembl; ENST00000611976.1; ENSP00000480549.1; ENSG00000163171.8. DR GeneID; 10602; -. DR KEGG; hsa:10602; -. DR MANE-Select; ENST00000295324.4; ENSP00000295324.3; NM_006449.5; NP_006440.2. DR UCSC; uc002rqi.3; human. DR AGR; HGNC:16943; -. DR CTD; 10602; -. DR DisGeNET; 10602; -. DR GeneCards; CDC42EP3; -. DR HGNC; HGNC:16943; CDC42EP3. DR HPA; ENSG00000163171; Low tissue specificity. DR MIM; 606133; gene. DR neXtProt; NX_Q9UKI2; -. DR OpenTargets; ENSG00000163171; -. DR PharmGKB; PA38429; -. DR VEuPathDB; HostDB:ENSG00000163171; -. DR eggNOG; ENOG502RKYM; Eukaryota. DR GeneTree; ENSGT00940000157736; -. DR HOGENOM; CLU_073229_0_0_1; -. DR InParanoid; Q9UKI2; -. DR OMA; LPTIGGC; -. DR OrthoDB; 5317319at2759; -. DR PhylomeDB; Q9UKI2; -. DR TreeFam; TF331725; -. DR PathwayCommons; Q9UKI2; -. 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; Q9UKI2; -. DR BioGRID-ORCS; 10602; 11 hits in 1155 CRISPR screens. DR ChiTaRS; CDC42EP3; human. DR GeneWiki; CDC42EP3; -. DR GenomeRNAi; 10602; -. DR Pharos; Q9UKI2; Tbio. DR PRO; PR:Q9UKI2; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9UKI2; Protein. DR Bgee; ENSG00000163171; Expressed in tibia and 199 other cell types or tissues. DR ExpressionAtlas; Q9UKI2; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; TAS:ProtInc. DR GO; GO:0031267; F:small GTPase binding; 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; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central. DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR029273; Cdc42_effect-like. DR InterPro; IPR000095; CRIB_dom. DR PANTHER; PTHR15344:SF3; CDC42 EFFECTOR PROTEIN 3; 1. DR PANTHER; PTHR15344; CDC42 EFFECTOR PROTEIN BORG; 1. DR Pfam; PF14957; BORG_CEP; 1. DR Pfam; PF00786; PBD; 1. DR SMART; SM00285; PBD; 1. DR PROSITE; PS50108; CRIB; 1. DR Genevisible; Q9UKI2; HS. PE 1: Evidence at protein level; KW Cell shape; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; KW Reference proteome. FT CHAIN 1..254 FT /note="Cdc42 effector protein 3" FT /id="PRO_0000212651" FT DOMAIN 31..45 FT /note="CRIB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057" FT REGION 164..225 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 164..196 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 208..222 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 63 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9CQC5" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 108 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CQC5" FT MOD_RES 144 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CQC5" FT CONFLICT 56 FT /note="I -> N (in Ref. 2; AAD16888)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="S -> F (in Ref. 3; AAC71773)" FT /evidence="ECO:0000305" SQ SEQUENCE 254 AA; 27678 MW; C31CDBE151C161ED CRC64; MPAKTPIYLK AANNKKGKKF KLRDILSPDM ISPPLGDFRH TIHIGKEGQH DVFGDISFLQ GNYELLPGNQ EKAHLGQFPG HNEFFRANST SDSVFTETPS PVLKNAISLP TIGGSQALML PLLSPVTFNS KQESFGPAKL PRLSCEPVME EKAQEKSSLL ENGTVHQGDT SWGSSGSASQ SSQGRDSHSS SLSEQYPDWP AEDMFDHPTP CELIKGKTKS EESLSDLTGS LLSLQLDLGP SLLDEVLNVM DKNK //