Q00587 (BORG5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cdc42 effector protein 1

Alternative name(s):
Binder of Rho GTPases 5
Serum protein MSE55

Gene names

Name:	CDC42EP1
Synonyms:	BORG5, CEP1, MSE55

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts. Ref.9
Subunit structure	Interacts with RHOQ and CDC42, in a GTP-dependent manner. Ref.8 Ref.9
Subcellular location	Endomembrane system; Peripheral membrane protein. Cytoplasm › cytoskeleton Ref.9.
Tissue specificity	Endothelial and bone marrow stromal cells.
Domain	The CRIB domain mediates interaction with CDC42.
Sequence similarities	Belongs to the BORG/CEP family. Contains 1 CRIB domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred from electronic annotation. Source: Compara positive regulation of pseudopodium assembly Inferred from direct assay PubMed 11035016. Source: UniProtKB regulation of cell shape Inferred from direct assay PubMed 11035016. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA actin cytoskeleton Inferred from direct assay. Source: HPA endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: HPA
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC42	P60953	3	EBI-744130,EBI-81752

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q00587-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q00587-2)

The sequence of this isoform differs from the canonical sequence as follows:
     258-264: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 391	391	Cdc42 effector protein 1		PRO_0000212657
Regions
	Domain	38 – 52	15	CRIB
	Repeat	220 – 226	7	1
	Repeat	227 – 233	7	2
	Repeat	234 – 240	7	3
	Repeat	241 – 247	7	4
	Repeat	248 – 254	7	5
	Repeat	255 – 261	7	6
	Repeat	262 – 268	7	7
	Repeat	269 – 275	7	8
	Region	220 – 275	56	8 X 7 AA tandem repeats of [PT]-[AT]-A-[ENT]-[PT]-[PTS]-[AG]
Amino acid modifications
	Modified residue	19	1	Phosphoserine Ref.12
	Modified residue	101	1	Phosphoserine Ref.12 Ref.14
	Modified residue	113	1	Phosphoserine Ref.12 Ref.14
	Modified residue	121	1	Phosphoserine Ref.12 Ref.13 Ref.14
	Modified residue	190	1	Phosphoserine Ref.13
	Modified residue	192	1	Phosphoserine Ref.13 Ref.14 Ref.15
	Modified residue	195	1	Phosphoserine Ref.13
	Modified residue	350	1	Phosphoserine Ref.12 Ref.13 Ref.14
	Modified residue	353	1	Phosphoserine Ref.13 Ref.14
Natural variations
	Alternative sequence	258 – 264	7	Missing in isoform 2.		VSP_004325
Experimental info
	Mutagenesis	36 – 47	12	DMISH…GDFRH → AMISHALGDFRA: No binding with CDC42. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 625EA3C71F20CF2B	FASTA	391	40,295
	10 20 30 40 50 60 MPGPQGGRGA ATMSLGKLSP VGWVSSSQGK RRLTADMISH PLGDFRHTMH VGRGGDVFGD 70 80 90 100 110 120 TSFLSNHGGS SGSTHRSPRS FLAKKLQLVR RVGAPPRRMA SPPAPSPAPP AISPIIKNAI 130 140 150 160 170 180 SLPQLNQAAY DSLVVGKLSF DSSPTSSTDG HSSYGLDSGF CTISRLPRSE KPHDRDRDGS 190 200 210 220 230 240 FPSEPGLRRS DSLLSFRLDL DLGPSLLSEL LGVMSLPEAP AAETPAPAAN PPAPTANPTG 250 260 270 280 290 300 PAANPPATTA NPPAPAANPS APAATPTGPA ANPPAPAASS TPHGHCPNGV TAGLGPVAEV 310 320 330 340 350 360 KSSPVGGGPR GPAGPALGRH WGAGWDGGHH YPEMDARQER VEVLPQARAS WESLDEEWRA 370 380 390 PQAGSRTPVP STVQANTFEF ADAEEDDEVK V
	Isoform 2 [UniParc]. Checksum: 3D056D62399AE422	FASTA	384	39,686
	10 20 30 40 50 60 MPGPQGGRGA ATMSLGKLSP VGWVSSSQGK RRLTADMISH PLGDFRHTMH VGRGGDVFGD 70 80 90 100 110 120 TSFLSNHGGS SGSTHRSPRS FLAKKLQLVR RVGAPPRRMA SPPAPSPAPP AISPIIKNAI 130 140 150 160 170 180 SLPQLNQAAY DSLVVGKLSF DSSPTSSTDG HSSYGLDSGF CTISRLPRSE KPHDRDRDGS 190 200 210 220 230 240 FPSEPGLRRS DSLLSFRLDL DLGPSLLSEL LGVMSLPEAP AAETPAPAAN PPAPTANPTG 250 260 270 280 290 300 PAANPPATTA NPPAPAATPT GPAANPPAPA ASSTPHGHCP NGVTAGLGPV AEVKSSPVGG 310 320 330 340 350 360 GPRGPAGPAL GRHWGAGWDG GHHYPEMDAR QERVEVLPQA RASWESLDEE WRAPQAGSRT 370 380 PVPSTVQANT FEFADAEEDD EVKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and molecular characterization of MSE55, a novel human serum constituent protein that displays bone marrow stromal/endothelial cell-specific expression." Bahou W.F., Campbell A.D., Wicha M.S. J. Biol. Chem. 267:13986-13992(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Mammary gland.
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Pancreas.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 166-175. Tissue: Platelet.
[8]	"The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins." Joberty G., Perlungher R.R., Macara I.G. Mol. Cell. Biol. 19:6585-6597(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RHOQ AND CDC42. Tissue: Embryo.
[9]	"MSE55, a Cdc42 effector protein, induces long cellular extensions in fibroblasts." Burbelo P.D., Snow D.M., Bahou W., Spiegel S. Proc. Natl. Acad. Sci. U.S.A. 96:9083-9088(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDC42, SUBCELLULAR LOCATION, MUTAGENESIS OF 36-ASP--HIS-47.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-101; SER-113; SER-121 AND SER-350, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-190; SER-192; SER-195; SER-350 AND SER-353, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-113; SER-121; SER-192; SER-350 AND SER-353, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M88338 mRNA. Translation: AAA36606.1. CR456524 mRNA. Translation: CAG30410.1. AK292190 mRNA. Translation: BAF84879.1. AL022315 Genomic DNA. Translation: CAB42833.1. CH471095 Genomic DNA. Translation: EAW60164.1. BC009356 mRNA. Translation: AAH09356.1.
IPI	IPI00023605. IPI00220243.
PIR	A42973.
RefSeq	NP_689449.1. NM_152243.2.
UniGene	Hs.225356.
3D structure databases
ProteinModelPortal	Q00587.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q00587. 10 interactions.
MINT	MINT-1454089.
STRING	9606.ENSP00000249014.
PTM databases
PhosphoSite	Q00587.
Polymorphism databases
DMDM	462623.
Proteomic databases
PaxDb	Q00587.
PRIDE	Q00587.
Protocols and materials databases
DNASU	11135.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000249014; ENSP00000249014; ENSG00000128283.
GeneID	11135.
KEGG	hsa:11135.
UCSC	uc003asz.4. human.
Organism-specific databases
CTD	11135.
GeneCards	GC22P037956.
H-InvDB	HIX0016445.
HGNC	HGNC:17014. CDC42EP1.
HPA	HPA006379.
MIM	606084. gene.
neXtProt	NX_Q00587.
PharmGKB	PA38430.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG45247.
HOGENOM	HOG000095252.
HOVERGEN	HBG080906.
InParanoid	Q00587.
OMA	FEFADAE.
OrthoDB	EOG4M65K3.
PhylomeDB	Q00587.
Gene expression databases
ArrayExpress	Q00587.
Bgee	Q00587.
CleanEx	HS_CDC42EP1.
Genevestigator	Q00587.
GermOnline	ENSG00000128283. Homo sapiens.
Family and domain databases
InterPro	IPR000095. PAK_box_Rho-bd. [Graphical view]
Pfam	PF00786. PBD. 1 hit. [Graphical view]
SMART	SM00285. PBD. 1 hit. [Graphical view]
PROSITE	PS50108. CRIB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	11135.
NextBio	42326.
SOURCE	Search...

Entry information

Entry name

BORG5_HUMAN

Accession

Primary (citable) accession number: Q00587
Secondary accession number(s): A8K825, Q96GN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.