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Protein

Cdc42 effector protein 3

Gene

Cdc42ep3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell shape

Enzyme and pathway databases

ReactomeiR-MMU-5687128. MAPK6/MAPK4 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Cdc42 effector protein 3
Alternative name(s):
Binder of Rho GTPases 2
Gene namesi
Name:Cdc42ep3
Synonyms:Borg2, Cep3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2384718. Cdc42ep3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254Cdc42 effector protein 3PRO_0000212652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631PhosphotyrosineCombined sources
Modified residuei89 – 891PhosphoserineCombined sources
Modified residuei108 – 1081PhosphoserineCombined sources
Modified residuei144 – 1441PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9CQC5.
PaxDbiQ9CQC5.
PRIDEiQ9CQC5.

PTM databases

iPTMnetiQ9CQC5.
PhosphoSiteiQ9CQC5.

Expressioni

Gene expression databases

BgeeiQ9CQC5.
CleanExiMM_CDC42EP3.
GenevisibleiQ9CQC5. MM.

Interactioni

Subunit structurei

Interacts with RHOQ and CDC42, in a GTP-dependent manner, and with SEPT7.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000067217.

Structurei

3D structure databases

ProteinModelPortaliQ9CQC5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 4515CRIBPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi171 – 19727Ser-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IHT2. Eukaryota.
ENOG410Y5G0. LUCA.
GeneTreeiENSGT00730000110928.
HOGENOMiHOG000233908.
HOVERGENiHBG052803.
InParanoidiQ9CQC5.
OMAiSMFTETP.
OrthoDBiEOG7V1FSH.
PhylomeDBiQ9CQC5.
TreeFamiTF331725.

Family and domain databases

InterProiIPR029273. Cdc42_effect.
IPR000095. CRIB_dom.
[Graphical view]
PfamiPF14957. BORG_CEP. 1 hit.
PF00786. PBD. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CQC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAKTPIYLK AANNKKGKKF KLRDILSPDM ISPPLGDFRH TIHIGKEGQH
60 70 80 90 100
DVFGDISFLQ GNYELLPGNQ EKAHSGQFPG HNDFFRANST SDSMFTETPS
110 120 130 140 150
PVLKNAISLP TIGGSQALML PLLSPVTFHS KQESFGRPKL PRLSCEPVME
160 170 180 190 200
EKVQEQSSLL ENGAVHQGDT SWGSSGSGSQ SSQGRDSHSS SLSEQSSDWP
210 220 230 240 250
ADDMFEHPAS CELVKSKTKS EESFSDLTGS LLSLQLDLGP SLLDEVLNVM

DKNK
Length:254
Mass (Da):27,686
Last modified:June 1, 2001 - v1
Checksum:i9EB9991CF1EB678F
GO

Sequence cautioni

The sequence BAC36479.1 differs from that shown. Reason: Frameshift at positions 167 and 205. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012309 mRNA. Translation: BAB28155.1.
AK014281 mRNA. Translation: BAB29241.1.
AK019447 mRNA. Translation: BAB31723.1.
AK076782 mRNA. Translation: BAC36479.1. Frameshift.
AK150214 mRNA. Translation: BAE29384.1.
BC021409 mRNA. Translation: AAH21409.1.
BC034714 mRNA. Translation: AAH34714.1.
BC092297 mRNA. Translation: AAH92297.1.
CCDSiCCDS28984.1.
RefSeqiNP_080790.1. NM_026514.2.
XP_006524358.1. XM_006524295.2.
UniGeneiMm.140601.

Genome annotation databases

EnsembliENSMUST00000068958; ENSMUSP00000067217; ENSMUSG00000036533.
GeneIDi260409.
KEGGimmu:260409.
UCSCiuc008dpx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012309 mRNA. Translation: BAB28155.1.
AK014281 mRNA. Translation: BAB29241.1.
AK019447 mRNA. Translation: BAB31723.1.
AK076782 mRNA. Translation: BAC36479.1. Frameshift.
AK150214 mRNA. Translation: BAE29384.1.
BC021409 mRNA. Translation: AAH21409.1.
BC034714 mRNA. Translation: AAH34714.1.
BC092297 mRNA. Translation: AAH92297.1.
CCDSiCCDS28984.1.
RefSeqiNP_080790.1. NM_026514.2.
XP_006524358.1. XM_006524295.2.
UniGeneiMm.140601.

3D structure databases

ProteinModelPortaliQ9CQC5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000067217.

PTM databases

iPTMnetiQ9CQC5.
PhosphoSiteiQ9CQC5.

Proteomic databases

MaxQBiQ9CQC5.
PaxDbiQ9CQC5.
PRIDEiQ9CQC5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068958; ENSMUSP00000067217; ENSMUSG00000036533.
GeneIDi260409.
KEGGimmu:260409.
UCSCiuc008dpx.1. mouse.

Organism-specific databases

CTDi10602.
MGIiMGI:2384718. Cdc42ep3.

Phylogenomic databases

eggNOGiENOG410IHT2. Eukaryota.
ENOG410Y5G0. LUCA.
GeneTreeiENSGT00730000110928.
HOGENOMiHOG000233908.
HOVERGENiHBG052803.
InParanoidiQ9CQC5.
OMAiSMFTETP.
OrthoDBiEOG7V1FSH.
PhylomeDBiQ9CQC5.
TreeFamiTF331725.

Enzyme and pathway databases

ReactomeiR-MMU-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

NextBioi392110.
PROiQ9CQC5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQC5.
CleanExiMM_CDC42EP3.
GenevisibleiQ9CQC5. MM.

Family and domain databases

InterProiIPR029273. Cdc42_effect.
IPR000095. CRIB_dom.
[Graphical view]
PfamiPF14957. BORG_CEP. 1 hit.
PF00786. PBD. 1 hit.
[Graphical view]
SMARTiSM00285. PBD. 1 hit.
[Graphical view]
PROSITEiPS50108. CRIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Embryo and Head.
  2. "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].
    Strain: 129, FVB/N and FVB/N-3.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Lung.

Entry informationi

Entry nameiBORG2_MOUSE
AccessioniPrimary (citable) accession number: Q9CQC5
Secondary accession number(s): Q3UD77, Q8BVR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.