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Protein

Cdc42 effector protein 2

Gene

CDC42EP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner.2 Publications

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB
  • GTP-Rho binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • actin filament organization Source: UniProtKB
  • positive regulation of actin filament polymerization Source: UniProtKB
  • positive regulation of GTPase activity Source: GOC
  • positive regulation of protein complex assembly Source: UniProtKB
  • positive regulation of pseudopodium assembly Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • Rho protein signal transduction Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Cell shape

Enzyme and pathway databases

ReactomeiR-HSA-5687128. MAPK6/MAPK4 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Cdc42 effector protein 2
Alternative name(s):
Binder of Rho GTPases 1
Gene namesi
Name:CDC42EP2
Synonyms:BORG1, CEP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:16263. CDC42EP2.

Subcellular locationi

  • Endomembrane system 1 Publication; Peripheral membrane protein 1 Publication
  • Cytoplasmcytoskeleton 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • endomembrane system Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • microtubule cytoskeleton Source: HPA
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 424HTIH → ATIA: No binding with CDC42; no induced pseudopodia formation. 1 Publication

Organism-specific databases

PharmGKBiPA38396.

Polymorphism and mutation databases

BioMutaiCDC42EP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 210209Cdc42 effector protein 2PRO_0000212648Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineBy similarity
Modified residuei141 – 1411PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO14613.
MaxQBiO14613.
PaxDbiO14613.
PRIDEiO14613.

PTM databases

iPTMnetiO14613.
PhosphoSiteiO14613.

Expressioni

Tissue specificityi

Highly expressed in the heart. Weakly expressed in the pancreas and liver.1 Publication

Gene expression databases

BgeeiO14613.
CleanExiHS_CDC42EP2.
GenevisibleiO14613. HS.

Organism-specific databases

HPAiHPA038562.

Interactioni

Subunit structurei

Interacts with RHOQ and CDC42 in a GTP-dependent manner, and with SEPT7.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGAP26Q9UNA13EBI-3438291,EBI-1390913
CDC42P609535EBI-3438291,EBI-81752
NME7Q9Y5B83EBI-3438291,EBI-744782

GO - Molecular functioni

  • GTP-Rho binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115702. 7 interactions.
IntActiO14613. 3 interactions.
STRINGi9606.ENSP00000279249.

Structurei

3D structure databases

ProteinModelPortaliO14613.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 4415CRIBPROSITE-ProRule annotationAdd
BLAST

Domaini

The CRIB domain mediates interaction with CDC42.

Sequence similaritiesi

Belongs to the BORG/CEP family.Curated
Contains 1 CRIB domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IZS0. Eukaryota.
ENOG4111X3X. LUCA.
GeneTreeiENSGT00730000110928.
HOGENOMiHOG000233908.
HOVERGENiHBG052803.
InParanoidiO14613.
OMAiIMDQDLG.
OrthoDBiEOG7V1FSH.
PhylomeDBiO14613.
TreeFamiTF331725.

Family and domain databases

InterProiIPR029273. Cdc42_effect.
IPR017363. Cdc42_effector_prot_2.
IPR000095. CRIB_dom.
[Graphical view]
PANTHERiPTHR15344:SF4. PTHR15344:SF4. 1 hit.
PfamiPF14957. BORG_CEP. 1 hit.
PF00786. PBD. 1 hit.
[Graphical view]
PIRSFiPIRSF038036. Cdc42_effector_p2. 1 hit.
SMARTiSM00285. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O14613-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKVPIYLK RGSRKGKKEK LRDLLSSDMI SPPLGDFRHT IHIGSGGGSD
60 70 80 90 100
MFGDISFLQG KFHLLPGTMV EGPEEDGTFD LPFQFTRTAT VCGRELPDGP
110 120 130 140 150
SPLLKNAISL PVIGGPQALT LPTAQAPPKP PRLHLETPQP SPQEGGSVDI
160 170 180 190 200
WRIPETGSPN SGLTPESGAE EPFLSNASSL LSLHVDLGPS ILDDVLQIMD
210
QDLDSMQIPT
Length:210
Mass (Da):22,484
Last modified:January 1, 1998 - v1
Checksum:i7755100672FFB69C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921C → V in AAD16185 (PubMed:11035016).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761N → S.1 Publication
Corresponds to variant rs4149839 [ dbSNP | Ensembl ].
VAR_023001
Natural varianti191 – 1911I → F.1 Publication
Corresponds to variant rs7120634 [ dbSNP | Ensembl ].
VAR_023002

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001436 mRNA. Translation: AAB81206.1.
AF163840 mRNA. Translation: AAD48784.1.
AF098290 mRNA. Translation: AAD16185.1.
AK315444 mRNA. Translation: BAG37832.1.
BT020004 mRNA. Translation: AAV38807.1.
AF548903 Genomic DNA. Translation: AAN39381.1.
BC022337 mRNA. Translation: AAH22337.1.
BC075834 mRNA. Translation: AAH75834.1.
CCDSiCCDS8099.1.
RefSeqiNP_006770.1. NM_006779.3.
UniGeneiHs.343380.

Genome annotation databases

EnsembliENST00000279249; ENSP00000279249; ENSG00000149798.
ENST00000533419; ENSP00000431660; ENSG00000149798.
GeneIDi10435.
KEGGihsa:10435.
UCSCiuc001odl.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF001436 mRNA. Translation: AAB81206.1.
AF163840 mRNA. Translation: AAD48784.1.
AF098290 mRNA. Translation: AAD16185.1.
AK315444 mRNA. Translation: BAG37832.1.
BT020004 mRNA. Translation: AAV38807.1.
AF548903 Genomic DNA. Translation: AAN39381.1.
BC022337 mRNA. Translation: AAH22337.1.
BC075834 mRNA. Translation: AAH75834.1.
CCDSiCCDS8099.1.
RefSeqiNP_006770.1. NM_006779.3.
UniGeneiHs.343380.

3D structure databases

ProteinModelPortaliO14613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115702. 7 interactions.
IntActiO14613. 3 interactions.
STRINGi9606.ENSP00000279249.

PTM databases

iPTMnetiO14613.
PhosphoSiteiO14613.

Polymorphism and mutation databases

BioMutaiCDC42EP2.

Proteomic databases

EPDiO14613.
MaxQBiO14613.
PaxDbiO14613.
PRIDEiO14613.

Protocols and materials databases

DNASUi10435.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279249; ENSP00000279249; ENSG00000149798.
ENST00000533419; ENSP00000431660; ENSG00000149798.
GeneIDi10435.
KEGGihsa:10435.
UCSCiuc001odl.3. human.

Organism-specific databases

CTDi10435.
GeneCardsiCDC42EP2.
HGNCiHGNC:16263. CDC42EP2.
HPAiHPA038562.
MIMi606132. gene.
neXtProtiNX_O14613.
PharmGKBiPA38396.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZS0. Eukaryota.
ENOG4111X3X. LUCA.
GeneTreeiENSGT00730000110928.
HOGENOMiHOG000233908.
HOVERGENiHBG052803.
InParanoidiO14613.
OMAiIMDQDLG.
OrthoDBiEOG7V1FSH.
PhylomeDBiO14613.
TreeFamiTF331725.

Enzyme and pathway databases

ReactomeiR-HSA-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

GeneWikiiCDC42EP2.
GenomeRNAii10435.
PROiO14613.
SOURCEiSearch...

Gene expression databases

BgeeiO14613.
CleanExiHS_CDC42EP2.
GenevisibleiO14613. HS.

Family and domain databases

InterProiIPR029273. Cdc42_effect.
IPR017363. Cdc42_effector_prot_2.
IPR000095. CRIB_dom.
[Graphical view]
PANTHERiPTHR15344:SF4. PTHR15344:SF4. 1 hit.
PfamiPF14957. BORG_CEP. 1 hit.
PF00786. PBD. 1 hit.
[Graphical view]
PIRSFiPIRSF038036. Cdc42_effector_p2. 1 hit.
SMARTiSM00285. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A transcript map for the 2.8-Mb region containing the multiple endocrine neoplasia type 1 locus."
    Guru S.C., Agarwal S.K., Manickam P., Olufemi S.-E., Crabtree J.S., Weisemann J.M., Kester M.B., Kim Y.S., Wang Y., Emmert-Buck M.R., Liotta L.A., Spiegel A.M., Boguski M.S., Roe B.A., Collins F.S., Burns A.L., Marx S.J., Chandrasekharappa S.C.
    Genome Res. 7:725-735(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RHOQ AND CDC42, TISSUE SPECIFICITY.
    Tissue: Embryo.
  3. "A new family of Cdc42 effector proteins, CEPs, function in fibroblast and epithelial cell shape changes."
    Hirsch D.S., Pirone D.M., Burbelo P.D.
    J. Biol. Chem. 276:875-883(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDC42, MUTAGENESIS OF 39-HIS--HIS-42, SUBCELLULAR LOCATION.
    Tissue: Brain.
  4. "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].
    Tissue: Heart.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. NIEHS SNPs program
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-176 AND PHE-191.
  7. "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].
    Tissue: Lung and Pancreas.
  8. "Borg proteins control septin organization and are negatively regulated by Cdc42."
    Joberty G., Perlungher R.R., Sheffield P.J., Kinoshita M., Noda M., Haystead T., Macara I.G.
    Nat. Cell Biol. 3:861-866(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEPT7.
  9. "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-31 AND SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBORG1_HUMAN
AccessioniPrimary (citable) accession number: O14613
Secondary accession number(s): B2RD85, Q9UNS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.