Full text data of CDC42EP3
CDC42EP3
(BORG2, CEP3)
[Confidence: low (only semi-automatic identification from reviews)]
Cdc42 effector protein 3 (Binder of Rho GTPases 2; MSE55-related Cdc42-binding protein)
Cdc42 effector protein 3 (Binder of Rho GTPases 2; MSE55-related Cdc42-binding protein)
UniProt
Q9UKI2
ID BORG2_HUMAN Reviewed; 254 AA.
AC Q9UKI2; B2R8S0; O95353; Q9UQJ0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 103.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH RHOQ AND CDC42.
RC TISSUE=Heart;
RX PubMed=10490598;
RA Joberty G., Perlungher R.R., Macara I.G.;
RT "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
RT 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
RT and 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT regulated by 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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
CC formation in fibroblasts.
CC -!- SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner,
CC and with SEPT7.
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC protein. Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Highly expressed in the heart and weakly in
CC the brain.
CC -!- SIMILARITY: Belongs to the BORG/CEP family.
CC -!- SIMILARITY: Contains 1 CRIB domain.
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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 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 UniGene; Hs.369574; -.
DR ProteinModelPortal; Q9UKI2; -.
DR IntAct; Q9UKI2; 4.
DR MINT; MINT-1397043; -.
DR STRING; 9606.ENSP00000295324; -.
DR PhosphoSite; Q9UKI2; -.
DR DMDM; 71152340; -.
DR PaxDb; Q9UKI2; -.
DR PRIDE; Q9UKI2; -.
DR DNASU; 10602; -.
DR Ensembl; ENST00000295324; ENSP00000295324; ENSG00000163171.
DR GeneID; 10602; -.
DR KEGG; hsa:10602; -.
DR UCSC; uc002rqi.2; human.
DR CTD; 10602; -.
DR GeneCards; GC02M037782; -.
DR HGNC; HGNC:16943; CDC42EP3.
DR HPA; HPA034986; -.
DR MIM; 606133; gene.
DR neXtProt; NX_Q9UKI2; -.
DR PharmGKB; PA38429; -.
DR eggNOG; NOG46217; -.
DR HOGENOM; HOG000233908; -.
DR HOVERGEN; HBG052803; -.
DR InParanoid; Q9UKI2; -.
DR OMA; SMFTETP; -.
DR OrthoDB; EOG7V1FSH; -.
DR SignaLink; Q9UKI2; -.
DR ChiTaRS; CDC42EP3; human.
DR GeneWiki; CDC42EP3; -.
DR GenomeRNAi; 10602; -.
DR NextBio; 40262; -.
DR PRO; PR:Q9UKI2; -.
DR ArrayExpress; Q9UKI2; -.
DR Bgee; Q9UKI2; -.
DR CleanEx; HS_CDC42EP3; -.
DR Genevestigator; Q9UKI2; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; TAS:ProtInc.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR000095; CRIB_dom.
DR Pfam; PF00786; PBD; 1.
DR SMART; SM00285; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cell shape; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 254 Cdc42 effector protein 3.
FT /FTId=PRO_0000212651.
FT DOMAIN 31 45 CRIB.
FT MOD_RES 63 63 Phosphotyrosine (By similarity).
FT MOD_RES 108 108 Phosphoserine (By similarity).
FT CONFLICT 56 56 I -> N (in Ref. 2; AAD16888).
FT CONFLICT 233 233 S -> F (in Ref. 3; AAC71773).
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
//
ID BORG2_HUMAN Reviewed; 254 AA.
AC Q9UKI2; B2R8S0; O95353; Q9UQJ0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 103.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH RHOQ AND CDC42.
RC TISSUE=Heart;
RX PubMed=10490598;
RA Joberty G., Perlungher R.R., Macara I.G.;
RT "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
RT 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
RT and 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT regulated by 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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
CC formation in fibroblasts.
CC -!- SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner,
CC and with SEPT7.
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC protein. Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Highly expressed in the heart and weakly in
CC the brain.
CC -!- SIMILARITY: Belongs to the BORG/CEP family.
CC -!- SIMILARITY: Contains 1 CRIB domain.
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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 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 UniGene; Hs.369574; -.
DR ProteinModelPortal; Q9UKI2; -.
DR IntAct; Q9UKI2; 4.
DR MINT; MINT-1397043; -.
DR STRING; 9606.ENSP00000295324; -.
DR PhosphoSite; Q9UKI2; -.
DR DMDM; 71152340; -.
DR PaxDb; Q9UKI2; -.
DR PRIDE; Q9UKI2; -.
DR DNASU; 10602; -.
DR Ensembl; ENST00000295324; ENSP00000295324; ENSG00000163171.
DR GeneID; 10602; -.
DR KEGG; hsa:10602; -.
DR UCSC; uc002rqi.2; human.
DR CTD; 10602; -.
DR GeneCards; GC02M037782; -.
DR HGNC; HGNC:16943; CDC42EP3.
DR HPA; HPA034986; -.
DR MIM; 606133; gene.
DR neXtProt; NX_Q9UKI2; -.
DR PharmGKB; PA38429; -.
DR eggNOG; NOG46217; -.
DR HOGENOM; HOG000233908; -.
DR HOVERGEN; HBG052803; -.
DR InParanoid; Q9UKI2; -.
DR OMA; SMFTETP; -.
DR OrthoDB; EOG7V1FSH; -.
DR SignaLink; Q9UKI2; -.
DR ChiTaRS; CDC42EP3; human.
DR GeneWiki; CDC42EP3; -.
DR GenomeRNAi; 10602; -.
DR NextBio; 40262; -.
DR PRO; PR:Q9UKI2; -.
DR ArrayExpress; Q9UKI2; -.
DR Bgee; Q9UKI2; -.
DR CleanEx; HS_CDC42EP3; -.
DR Genevestigator; Q9UKI2; -.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; TAS:ProtInc.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR000095; CRIB_dom.
DR Pfam; PF00786; PBD; 1.
DR SMART; SM00285; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cell shape; Complete proteome; Cytoplasm; Cytoskeleton; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 254 Cdc42 effector protein 3.
FT /FTId=PRO_0000212651.
FT DOMAIN 31 45 CRIB.
FT MOD_RES 63 63 Phosphotyrosine (By similarity).
FT MOD_RES 108 108 Phosphoserine (By similarity).
FT CONFLICT 56 56 I -> N (in Ref. 2; AAD16888).
FT CONFLICT 233 233 S -> F (in Ref. 3; AAC71773).
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
//
MIM
606133
*RECORD*
*FIELD* NO
606133
*FIELD* TI
*606133 CDC42 EFFECTOR PROTEIN 3; CDC42EP3
;;CEP3;;
BINDER OF RHO GTPases 2; BORG2
read more*FIELD* TX
DESCRIPTION
CDC42 (116952), a small RHO GTPase, regulates the formation of
F-actin-containing structures through its interaction with several
downstream effector proteins. These effectors include the CEPs, also
called the BORGs, all of which contain a CDC42/RAC (602048) interactive
binding (CRIB) motif (Joberty et al., 1999; Hirsch et al., 2001).
CLONING
Using a yeast 2-hybrid screen on a mouse embryo cDNA library with TC10
(605857) as the bait, followed by EST database searching, Joberty et al.
(1999) identified cDNAs encoding human and mouse BORG1 (CEP2; 606132),
BORG2 (CEP3), BORG3 (CEP5), BORG4 (CEP4; 605468), and BORG5 (CEP1).
Sequence analysis predicted that the 254-amino acid BORG2 protein
contains a CRIB motif followed by a conserved 12-residue BORG homology-1
(BH1) domain in its N terminus; an 11-amino acid BH2 domain in its
central region; and a 22-residue BH3 domain in its C terminus. Northern
blot analysis revealed ubiquitous but variable expression of 4 BORG2
transcripts ranging from 2.0 to 5.5 kb, with high levels in heart and
low levels in brain; liver lacked the largest transcript.
By EST database searching with CEP1 as the probe, Hirsch et al. (2001)
identified cDNAs encoding several CEPs, including CEP3. They referred to
the BH2 and BH3 domains as CI and CII, respectively, and considered the
BH1 domain to be part of an extended CRIB motif. Hirsch et al. (2001)
proposed that these motifs are potential signaling domains.
GENE FUNCTION
By binding analysis, Joberty et al. (1999) confirmed that BORG2
interacts with TC10 and CDC42. Immunofluorescence microscopy
demonstrated cytoplasmic expression of BORG2. BORG2 expression caused no
dramatic changes in cell shape and a reduced abundance of stress fibers.
Coexpression of BORG2 with CDC42 resulted in cells showing a 'porcupine'
phenotype characterized by an abundance of actin-filled spikes.
Alberts et al. (1998) found that CEP3 interacted with CDC42 but not with
activated ARHA (165390) in a yeast 2-hybrid screen.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CEP3
gene to chromosome 2 (TMAP WI-13652).
*FIELD* RF
1. Alberts, A. S.; Bouquin, N.; Johnston, L. H.; Treisman, R.: Analysis
of RhoA-binding proteins reveals an interaction domain conserved in
heterotrimeric G protein beta subunits and the yeast response regulator
protein Skn7. J. Biol. Chem. 273: 8616-8622, 1998.
2. Hirsch, D. S.; Pirone, D. M.; Burbelo, P. D.: A new family of
Cdc42 effector proteins, CEPs, function in fibroblast and epithelial
cell shape changes. J. Biol. Chem. 276: 875-883, 2001.
3. Joberty, G.; Perlungher, R. R.; Macara, I. G.: The Borgs, a new
family of Cdc42 and TC10 GTPase-interacting proteins. Molec. Cell.
Biol. 19: 6585-6597, 1999.
*FIELD* CD
Paul J. Converse: 7/20/2001
*FIELD* ED
carol: 11/02/2010
mgross: 8/30/2002
mgross: 7/20/2001
*RECORD*
*FIELD* NO
606133
*FIELD* TI
*606133 CDC42 EFFECTOR PROTEIN 3; CDC42EP3
;;CEP3;;
BINDER OF RHO GTPases 2; BORG2
read more*FIELD* TX
DESCRIPTION
CDC42 (116952), a small RHO GTPase, regulates the formation of
F-actin-containing structures through its interaction with several
downstream effector proteins. These effectors include the CEPs, also
called the BORGs, all of which contain a CDC42/RAC (602048) interactive
binding (CRIB) motif (Joberty et al., 1999; Hirsch et al., 2001).
CLONING
Using a yeast 2-hybrid screen on a mouse embryo cDNA library with TC10
(605857) as the bait, followed by EST database searching, Joberty et al.
(1999) identified cDNAs encoding human and mouse BORG1 (CEP2; 606132),
BORG2 (CEP3), BORG3 (CEP5), BORG4 (CEP4; 605468), and BORG5 (CEP1).
Sequence analysis predicted that the 254-amino acid BORG2 protein
contains a CRIB motif followed by a conserved 12-residue BORG homology-1
(BH1) domain in its N terminus; an 11-amino acid BH2 domain in its
central region; and a 22-residue BH3 domain in its C terminus. Northern
blot analysis revealed ubiquitous but variable expression of 4 BORG2
transcripts ranging from 2.0 to 5.5 kb, with high levels in heart and
low levels in brain; liver lacked the largest transcript.
By EST database searching with CEP1 as the probe, Hirsch et al. (2001)
identified cDNAs encoding several CEPs, including CEP3. They referred to
the BH2 and BH3 domains as CI and CII, respectively, and considered the
BH1 domain to be part of an extended CRIB motif. Hirsch et al. (2001)
proposed that these motifs are potential signaling domains.
GENE FUNCTION
By binding analysis, Joberty et al. (1999) confirmed that BORG2
interacts with TC10 and CDC42. Immunofluorescence microscopy
demonstrated cytoplasmic expression of BORG2. BORG2 expression caused no
dramatic changes in cell shape and a reduced abundance of stress fibers.
Coexpression of BORG2 with CDC42 resulted in cells showing a 'porcupine'
phenotype characterized by an abundance of actin-filled spikes.
Alberts et al. (1998) found that CEP3 interacted with CDC42 but not with
activated ARHA (165390) in a yeast 2-hybrid screen.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CEP3
gene to chromosome 2 (TMAP WI-13652).
*FIELD* RF
1. Alberts, A. S.; Bouquin, N.; Johnston, L. H.; Treisman, R.: Analysis
of RhoA-binding proteins reveals an interaction domain conserved in
heterotrimeric G protein beta subunits and the yeast response regulator
protein Skn7. J. Biol. Chem. 273: 8616-8622, 1998.
2. Hirsch, D. S.; Pirone, D. M.; Burbelo, P. D.: A new family of
Cdc42 effector proteins, CEPs, function in fibroblast and epithelial
cell shape changes. J. Biol. Chem. 276: 875-883, 2001.
3. Joberty, G.; Perlungher, R. R.; Macara, I. G.: The Borgs, a new
family of Cdc42 and TC10 GTPase-interacting proteins. Molec. Cell.
Biol. 19: 6585-6597, 1999.
*FIELD* CD
Paul J. Converse: 7/20/2001
*FIELD* ED
carol: 11/02/2010
mgross: 8/30/2002
mgross: 7/20/2001