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Q14155 (ARHG7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho guanine nucleotide exchange factor 7
Alternative name(s):
Beta-Pix
COOL-1
PAK-interacting exchange factor beta
p85
Gene names
Name:ARHGEF7
Synonyms:COOL1, KIAA0142, P85SPR, PAK3BP, PIXB
ORF Names:Nbla10314
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length803 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions By similarity. May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons. Ref.10 Ref.11 Ref.13

Subunit structure

Interacts with PAK kinases through the SH3 domain. Interacts with GIT1 and TGFB1I1. Interacts with PTK2/FAK1 and RAC1. Interacts with ITCH and PARVB By similarity. Interacts with unphosphorylated PAK1. Interacts with SCRIB; interaction is direct and may play a role in regulation of apoptosis. Interacts with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with BIN2. Isoform 1 and isoform 5 interact with SNX27. Ref.9 Ref.10 Ref.12 Ref.13 Ref.17 Ref.19

Subcellular location

Cell junctionfocal adhesion By similarity. Cell projectionruffle By similarity. Cytoplasmcell cortex By similarity. Cell projectionlamellipodium By similarity. Note: Detected at cell adhesions. A small proportion is detected at focal adhesions.

Post-translational modification

Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1 By similarity. Phosphorylated on Ser-694 by CaMK1; enhancement of GEF activity and downstream activation of RAC1. Ref.13

Sequence similarities

Contains 1 CH (calponin-homology) domain.

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAH50521.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA09763.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAD38906.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentCell junction
Cell projection
Cytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3 domain
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic signaling pathway

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of GTPase activity

Inferred from direct assay PubMed 21048939. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of Rho GTPase activity

Inferred from electronic annotation. Source: GOC

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from direct assay PubMed 21048939. Source: BHF-UCL

neuronal cell body

Inferred from direct assay PubMed 21048939. Source: BHF-UCL

protein complex

Inferred from direct assay PubMed 11864573. Source: UniProtKB

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

guanyl-nucleotide exchange factor activity

Inferred from direct assay PubMed 21048939. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: Q14155-4)

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 1 (identifier: Q14155-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-178: Missing.
     733-803: TWQGTDLMHN...SCCSYISHQN → SSRKESAPQV...NDPAWDETNL
Note: Contains a phosphoserine at position 560. Contains a phosphoserine at position 579.
Isoform 2 (identifier: Q14155-2)

The sequence of this isoform differs from the canonical sequence as follows:
     56-105: Missing.
Isoform 3 (identifier: Q14155-3)

The sequence of this isoform differs from the canonical sequence as follows:
     85-105: Missing.
Isoform 5 (identifier: Q14155-5)

The sequence of this isoform differs from the canonical sequence as follows:
     85-177: Missing.
     733-803: TWQGTDLMHN...SCCSYISHQN → SSRKESAPQV...NDPAWDETNL
Note: Contains a phosphoserine at position 645. Contains a phosphoserine at position 664.
Isoform 6 (identifier: Q14155-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-178: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 803803Rho guanine nucleotide exchange factor 7
PRO_0000080921

Regions

Domain1 – 132132CH
Domain184 – 24360SH3
Domain271 – 451181DH
Domain473 – 578106PH

Amino acid modifications

Modified residue1761Phosphoserine By similarity
Modified residue2491Phosphoserine Ref.18
Modified residue5181Phosphoserine Ref.15
Modified residue6941Phosphoserine; by CaMK1 Ref.13 Ref.14 Ref.18

Natural variations

Alternative sequence1 – 178178Missing in isoform 1 and isoform 6.
VSP_011032
Alternative sequence56 – 10550Missing in isoform 2.
VSP_011033
Alternative sequence85 – 17793Missing in isoform 5.
VSP_034639
Alternative sequence85 – 10521Missing in isoform 3.
VSP_011034
Alternative sequence733 – 80371TWQGT…ISHQN → SSRKESAPQVLLPEEEKIIV EETKSNGQTVIEEKSLVDTV YALKDEVQELRQDNKKMKKS LEEEQRARKDLEKLVRKVLK NMNDPAWDETNL in isoform 1 and isoform 5.
VSP_011035
Natural variant7901T → A Found in a clear cell renal carcinoma case; somatic mutation. Ref.24
VAR_064694

Experimental info

Sequence conflict52 – 554TIEK → EEKR in BAD66827. Ref.7
Sequence conflict3431Q → K in AAH33905. Ref.6
Sequence conflict5521M → V in AAH33905. Ref.6
Sequence conflict5951H → D in BAD66827. Ref.7
Sequence conflict6361I → T in AAH50521. Ref.6
Sequence conflict7401M → L in AAH33905. Ref.6

Secondary structure

.............................................. 803
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 613EBA839E6FDBFD

FASTA80390,012
        10         20         30         40         50         60 
MNSAEQTVTW LITLGVLESP KKTISDPEGF LQASLKDGVV LCRLLERLLP GTIEKVYPEP 

        70         80         90        100        110        120 
RSESECLSNI REFLRGCGAS LRLELLFPPS QPPQHLVTTI LLSASTFDAN DLYQGQNFNK 

       130        140        150        160        170        180 
VLSSLVTLNK VTADIGLGSD SVCARPSSHR IKSFDSLGSQ SLHTRTSKLF QGQYRSLDMT 

       190        200        210        220        230        240 
DNSNNQLVVR AKFNFQQTNE DELSFSKGDV IHVTRVEEGG WWEGTLNGRT GWFPSNYVRE 

       250        260        270        280        290        300 
VKASEKPVSP KSGTLKSPPK GFDTTAINKS YYNVVLQNIL ETENEYSKEL QTVLSTYLRP 

       310        320        330        340        350        360 
LQTSEKLSSA NISYLMGNLE EICSFQQMLV QSLEECTKLP EAQQRVGGCF LNLMPQMKTL 

       370        380        390        400        410        420 
YLTYCANHPS AVNVLTEHSE ELGEFMETKG ASSPGILVLT TGLSKPFMRL DKYPTLLKEL 

       430        440        450        460        470        480 
ERHMEDYHTD RQDIQKSMAA FKNLSAQCQE VRKRKELELQ ILTEAIRNWE GDDIKTLGNV 

       490        500        510        520        530        540 
TYMSQVLIQC AGSEEKNERY LLLFPNVLLM LSASPRMSGF IYQGKLPTTG MTITKLEDSE 

       550        560        570        580        590        600 
NHRNAFEISG SMIERILVSC NNQQDLQEWV EHLQKQTKVT SVGNPTIKPH SVPSHTLPSH 

       610        620        630        640        650        660 
PVTPSSKHAD SKPAPLTPAY HTLPHPSHHG TPHTTINWGP LEPPKTPKPW SLSCLRPAPP 

       670        680        690        700        710        720 
LRPSAALCYK EDLSKSPKTM KKLLPKRKPE RKPSDEEFAS RKSTAALEED AQILKVIEAY 

       730        740        750        760        770        780 
CTSAKTRQTL NSTWQGTDLM HNHVLADDDQ PSLDSLGRRS SLSRLEPSDL SEDSDYDSIW 

       790        800 
TAHSYRMGST SRKSCCSYIS HQN 

« Hide

Isoform 1 [UniParc].

Checksum: B5B5A83F0EBC28D2
Show »

FASTA64673,140
Isoform 2 [UniParc].

Checksum: 04178E64ACF43846
Show »

FASTA75384,477
Isoform 3 [UniParc].

Checksum: 9C602026D90A6D01
Show »

FASTA78287,770
Isoform 5 [UniParc].

Checksum: E82D55E6187DADB2
Show »

FASTA73182,571
Isoform 6 [UniParc].

Checksum: 25DAD75DD4B0AC2E
Show »

FASTA62570,450

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[2]"A novel regulator of p21-activated kinases."
Bagrodia S., Taylor S.J., Jordon K.A., Van Aelst L., Cerione R.A.
J. Biol. Chem. 273:23633-23636(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Amygdala.
[4]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [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. expand/collapse author list , 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] (ISOFORMS 1; 2 AND 4).
Tissue: Brain and Testis.
[7]"Alternative splice variants encoding unstable protein domains exist in the human brain."
Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.
J. Mol. Biol. 343:1207-1220(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-803 (ISOFORM 5).
[8]"Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
Cancer Lett. 197:63-68(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-803.
Tissue: Neuroblastoma.
[9]"Mammalian Scribble forms a tight complex with the betaPIX exchange factor."
Audebert S., Navarro C., Nourry C., Chasserot-Golaz S., Lecine P., Bellaiche Y., Dupont J.-L., Premont R.T., Sempere C., Strub J.-M., Van Dorsselaer A., Vitale N., Borg J.-P.
Curr. Biol. 14:987-995(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCRIB.
[10]"Deregulation of scribble promotes mammary tumorigenesis and reveals a role for cell polarity in carcinoma."
Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C., Muthuswamy S.K.
Cell 135:865-878(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SCRIB.
[11]"Scrib regulates PAK activity during the cell migration process."
Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S., Navarro C., Rachel R., Montcouquiol M., Sans N., Etienne-Manneville S., Borg J.-P., Santoni M.-J.
Hum. Mol. Genet. 17:3552-3565(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
[12]"Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis."
Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B., Eom S.H., Kim H., Kim E.
J. Neurosci. 28:14546-14556(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FRMPD4.
[13]"Activity-dependent synaptogenesis: regulation by a CaM-kinase kinase/CaM-kinase I/betaPIX signaling complex."
Saneyoshi T., Wayman G., Fortin D., Davare M., Hoshi N., Nozaki N., Natsume T., Soderling T.R.
Neuron 57:94-107(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-694, INTERACTION WITH CAMK1.
[14]"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-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Sorting nexin 27 protein regulates trafficking of a p21-activated kinase (PAK) interacting exchange factor (beta-Pix)-G protein-coupled receptor kinase interacting protein (GIT) complex via a PDZ domain interaction."
Valdes J.L., Tang J., McDermott M.I., Kuo J.C., Zimmerman S.P., Wincovitch S.M., Waterman C.M., Milgram S.L., Playford M.P.
J. Biol. Chem. 286:39403-39416(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX27.
[18]"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-249 AND SER-694, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-579 (ISOFORM 1), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-664 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Bin2 is a membrane sculpting N-BAR protein that influences leucocyte podosomes, motility and phagocytosis."
Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J., Veprintsev D.B., Evans P.R., McMahon H.T.
PLoS ONE 7:E52401-E52401(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIN2.
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Structure and mutagenesis of the Dbl homology domain."
Aghazadeh B., Zhu K., Kubiseski T.J., Liu G.A., Pawson T., Zheng Y., Rosen M.K.
Nat. Struct. Biol. 5:1098-1107(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 260-467.
[22]"Structural analysis of the SH3 domain of beta-PIX and its interaction with alpha-p21 activated kinase (PAK)."
Mott H.R., Nietlispach D., Evetts K.A., Owen D.
Biochemistry 44:10977-10983(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 179-243 OF COMPLEX WITH UNPHOSPHORYLATED PAK1.
[23]"Northeast structural genomics consortium target HR4495E."
Northeast structural genomics consortium (NESG)
Submitted (DEC-2010) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-137.
[24]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-790.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63476 mRNA. Translation: BAA09763.2. Different initiation.
AL834228 mRNA. Translation: CAD38906.1. Different initiation.
AL390754, AL139086 Genomic DNA. Translation: CAI12461.1.
AL139086, AL390754 Genomic DNA. Translation: CAI14671.1.
AL390754, AL139086 Genomic DNA. Translation: CAM13628.1.
AL139086, AL390754 Genomic DNA. Translation: CAM20788.1.
CH471085 Genomic DNA. Translation: EAX09143.1.
BC033905 mRNA. Translation: AAH33905.1.
BC050521 mRNA. Translation: AAH50521.1. Different initiation.
BC060776 mRNA. Translation: AAH60776.1.
AB177849 mRNA. Translation: BAD66827.1.
AB075521 mRNA. Translation: BAE45764.1.
RefSeqNP_001106983.1. NM_001113511.1.
NP_001106984.1. NM_001113512.1.
NP_001106985.1. NM_001113513.1.
NP_003890.1. NM_003899.3.
NP_663788.1. NM_145735.2.
XP_005254147.1. XM_005254090.1.
XP_005254152.1. XM_005254095.1.
UniGeneHs.508738.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BY1NMR-A260-467[»]
1ZSGNMR-A179-243[»]
2L3GNMR-A1-137[»]
ProteinModelPortalQ14155.
SMRQ14155. Positions 1-137, 151-578.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114393. 25 interactions.
IntActQ14155. 19 interactions.
MINTMINT-92779.

PTM databases

PhosphoSiteQ14155.

Polymorphism databases

DMDM50403776.

Proteomic databases

PaxDbQ14155.
PRIDEQ14155.

Protocols and materials databases

DNASU8874.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317133; ENSP00000325994; ENSG00000102606. [Q14155-3]
ENST00000370623; ENSP00000359657; ENSG00000102606. [Q14155-5]
ENST00000375723; ENSP00000364875; ENSG00000102606. [Q14155-6]
ENST00000375736; ENSP00000364888; ENSG00000102606. [Q14155-1]
ENST00000375739; ENSP00000364891; ENSG00000102606. [Q14155-2]
ENST00000375741; ENSP00000364893; ENSG00000102606. [Q14155-4]
ENST00000426073; ENSP00000397068; ENSG00000102606. [Q14155-1]
GeneID8874.
KEGGhsa:8874.
UCSCuc001vrr.2. human. [Q14155-3]
uc001vrs.2. human. [Q14155-4]
uc001vrt.2. human. [Q14155-2]
uc001vrv.4. human. [Q14155-1]

Organism-specific databases

CTD8874.
GeneCardsGC13P111766.
H-InvDBHIX0037536.
HGNCHGNC:15607. ARHGEF7.
HPAHPA004744.
MIM605477. gene.
neXtProtNX_Q14155.
PharmGKBPA24977.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314429.
HOVERGENHBG050569.
InParanoidQ14155.
KOK13710.
OrthoDBEOG708W04.
TreeFamTF316105.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkQ14155.

Gene expression databases

ArrayExpressQ14155.
BgeeQ14155.
GenevestigatorQ14155.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGEF7. human.
EvolutionaryTraceQ14155.
GeneWikiARHGEF7.
GenomeRNAi8874.
NextBio33313.
PROQ14155.
SOURCESearch...

Entry information

Entry nameARHG7_HUMAN
AccessionPrimary (citable) accession number: Q14155
Secondary accession number(s): B1ALK6 expand/collapse secondary AC list , B1ALK8, Q3LIA4, Q5W9H0, Q6P9G3, Q6PII2, Q86W63, Q8N3M1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2004
Last modified: March 19, 2014
This is version 154 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM