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Reviewed, UniProtKB/Swiss-Prot Q14155 (ARHG7_HUMAN)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length803 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling By similarity.

Subunit structure

Interacts with PAK kinases through the SH3 domain. Interacts with GIT1 and TGFB1I1. Interacts with ITCH By similarity. Interacts with unphosphorylated PAK1.

Sequence similarities

Contains 1 CH (calponin-homology) domain.

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainSH3 domain
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processintracellular signaling cascade

Inferred from electronic annotation. Source: InterPro

regulation of Rho protein signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

nucleolus

Inferred from direct assay. Source: HPA

   Molecular functionRho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

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
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
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.9
Modified residue5181Phosphoserine Ref.9
Modified residue6941Phosphoserine Ref.10

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

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.

Checksum: B5B5A83F0EBC28D2
Show »

FASTA64673,140
Isoform 2.

Checksum: 04178E64ACF43846
Show »

FASTA75384,477
Isoform 3.

Checksum: 9C602026D90A6D01
Show »

FASTA78287,770
Isoform 5.

Checksum: E82D55E6187DADB2
Show »

FASTA73182,571
Isoform 6.

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: 8590280] [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: 9726964] [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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [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: 15057823] [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: 15489334] [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: 15491607] [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: 12880961] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-803.
Tissue: Neuroblastoma.
[9]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-518, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, MASS SPECTROMETRY.
[11]"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: 9846881] [Abstract]
Cited for: STRUCTURE BY NMR OF 260-467.
[12]"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: 16101281] [Abstract]
Cited for: STRUCTURE BY NMR OF 179-243 OF COMPLEX WITH UNPHOSPHORYLATED PAK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00449906.
IPI00449907.
IPI00449908.
IPI00449909.
IPI00900260.
IPI00900378.
RefSeqNP_001106983.1.
NP_001106984.1.
NP_001106985.1.
NP_003890.1.
NP_663788.1.
UniGeneHs.508738

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BY1NMR-A260-467[»]
1ZSGNMR-A179-243[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ14155. 3 interactions.

PTM databases

PhosphoSiteQ14155.

Proteomic databases

PRIDEQ14155.

Genome annotation databases

EnsemblENSG00000102606. Homo sapiens. [Contig view]
GeneID8874.
KEGGhsa:8874.

Organism-specific databases

GeneCardsGC13P110565.
H-InvDBHIX0011460.
HIX0037536.
HGNCHGNC:15607. ARHGEF7.
HPAHPA004744.
MIM605477. gene.
PharmGKBPA24977.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ14155.
HOVERGENQ14155.
OMAQ14155. TLPSHPI.

Enzyme and pathway databases

Pathway_Interaction_DBaurora_a_pathway. Aurora A signaling.
pi3kcipathway. Class I PI3K signaling events.
ReactomeREACT_11044. Signaling by Rho GTPases.
REACT_9417. Signaling by EGFR.

Gene expression databases

ArrayExpressQ14155.
BgeeQ14155.
GermOnlineENSG00000102606. Homo sapiens.

Family and domain databases

InterProIPR001715. Calponin_act_bd.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
[Graphical view]
Gene3DG3DSA:1.10.418.10. Calponin-homology. 1 hit.
G3DSA:1.20.900.10. RhoGEF. 1 hit.
PfamPF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
ProDomPD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
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 Resources

NextBio33313.
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: June 16, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 13

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents