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Q9H3Q1 (BORG4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cdc42 effector protein 4
Alternative name(s):
Binder of Rho GTPases 4
Gene names
Name:CDC42EP4
Synonyms:BORG4, CEP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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, when overexpressed in fibroblasts.

Subunit structure

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

Subcellular location

Endomembrane system; Peripheral membrane protein. Cytoplasmcytoskeleton.

Tissue specificity

Not detected in any of the adult tissues tested. May be expressed only in fetal or embryonic tissues.

Sequence similarities

Belongs to the BORG/CEP family.

Contains 1 CRIB domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Cdc42 effector protein 4
PRO_0000212655

Regions

Domain27 – 4115CRIB
Compositional bias70 – 745Poly-Ser

Amino acid modifications

Modified residue641Phosphoserine Ref.5 Ref.8
Modified residue1181Phosphoserine Ref.8
Modified residue1381Phosphoserine Ref.5
Modified residue1401Phosphoserine Ref.8
Modified residue1421Phosphoserine Ref.8
Modified residue1741Phosphoserine Ref.4 Ref.5 Ref.8
Modified residue2921Phosphoserine Ref.4 Ref.5
Modified residue2951Phosphoserine Ref.4 Ref.5 Ref.8

Experimental info

Sequence conflict21P → L in AAH10451. Ref.3
Sequence conflict331D → T in AAD16299. Ref.2
Sequence conflict2881A → T in AAD16299. Ref.2
Sequence conflict2961A → T in AAD16299. Ref.2
Sequence conflict3391P → PP in AAD16299. Ref.2
Sequence conflict3551Missing in AAD16299. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9H3Q1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 2CF677C60C6EF1B5

FASTA35637,980
        10         20         30         40         50         60 
MPILKQLVSS SVHSKRRSRA DLTAEMISAP LGDFRHTMHV GRAGDAFGDT SFLNSKAGEP 

        70         80         90        100        110        120 
DGESLDEQPS SSSSKRSLLS RKFRGSKRSQ SVTRGEREQR DMLGSLRDSA LFVKNAMSLP 

       130        140        150        160        170        180 
QLNEKEAAEK GTSKLPKSLS SSPVKKANDG EGGDEEAGTE EAVPRRNGAA GPHSPDPLLD 

       190        200        210        220        230        240 
EQAFGDLTDL PVVPKATYGL KHAESIMSFH IDLGPSMLGD VLSIMDKEEW DPEEGEGGYH 

       250        260        270        280        290        300 
GDEGAAGTIT QAPPYAVAAP PLARQEGKAG PDLPSLPSHA LEDEGWAAAA PSPGSARSMG 

       310        320        330        340        350 
SHTTRDSSSL SSCTSGILEE RSPAFRGPDR ARAAVSRQPD KEFSFMDEEE EDEIRV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis, gene expression, and chromosomal assignment of mouse Borg4 gene and its human orthologue."
Osada N., Kusuda J., Suzuki Y., Sugano S., Hashimoto K.
J. Hum. Genet. 45:374-377(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ileal mucosa.
[2]"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], CHARACTERIZATION.
Tissue: Eye.
[3]"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: Brain and Skin.
[4]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-292 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"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-64; SER-138; SER-174; SER-292 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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-64; SER-118; SER-140; SER-142; SER-174 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB042237 mRNA. Translation: BAB17272.1.
AF099664 mRNA. Translation: AAD16299.1.
BC002774 mRNA. Translation: AAH02774.1.
BC010451 mRNA. Translation: AAH10451.1.
RefSeqNP_036253.2. NM_012121.4.
XP_005257239.1. XM_005257182.2.
UniGeneHs.3903.

3D structure databases

ProteinModelPortalQ9H3Q1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117115. 10 interactions.
IntActQ9H3Q1. 5 interactions.
MINTMINT-1464445.
STRING9606.ENSP00000338258.

PTM databases

PhosphoSiteQ9H3Q1.

Polymorphism databases

DMDM21362403.

Proteomic databases

PaxDbQ9H3Q1.
PeptideAtlasQ9H3Q1.
PRIDEQ9H3Q1.

Protocols and materials databases

DNASU23580.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335793; ENSP00000338258; ENSG00000179604.
GeneID23580.
KEGGhsa:23580.
UCSCuc002jjn.3. human.

Organism-specific databases

CTD23580.
GeneCardsGC17M071279.
HGNCHGNC:17147. CDC42EP4.
HPAHPA023335.
HPA024797.
MIM605468. gene.
neXtProtNX_Q9H3Q1.
PharmGKBPA38439.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44582.
HOGENOMHOG000231054.
HOVERGENHBG052803.
InParanoidQ9H3Q1.
OMAKEFSFMD.
PhylomeDBQ9H3Q1.
TreeFamTF331725.

Gene expression databases

ArrayExpressQ9H3Q1.
BgeeQ9H3Q1.
CleanExHS_CDC42EP4.
GenevestigatorQ9H3Q1.

Family and domain databases

InterProIPR000095. CRIB_dom.
[Graphical view]
PfamPF00786. PBD. 1 hit.
[Graphical view]
PROSITEPS50108. CRIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDC42EP4. human.
GeneWikiCDC42EP4.
GenomeRNAi23580.
NextBio46182.
PROQ9H3Q1.
SOURCESearch...

Entry information

Entry nameBORG4_HUMAN
AccessionPrimary (citable) accession number: Q9H3Q1
Secondary accession number(s): O95828, Q96FT3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM