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Q15052 (ARHG6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. 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 6
Alternative name(s):
Alpha-Pix
COOL-2
PAK-interacting exchange factor alpha
Rac/Cdc42 guanine nucleotide exchange factor 6
Gene names
Name:ARHGEF6
Synonyms:COOL2, KIAA0006, PIXA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length776 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a RAC1 guanine nucleotide exchange factor (GEF).

Subunit structure

Interacts with PAK kinases through the SH3 domain. Interacts with GIT1. Component of cytoplasmic complexes, which also contain PXN, GIT1 and PAK1 By similarity. Interacts with PARVB. Interacts with BIN2. Identified in a complex with BIN2 and GIT2. Ref.10 Ref.12

Subcellular location

Cell projectionlamellipodium By similarity.

Tissue specificity

Ubiquitous.

Involvement in disease

Mental retardation, X-linked 46 (MRX46) [MIM:300436]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

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 BAA02796.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell projection
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   DomainSH3 domain
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Non-traceable author statement PubMed 11564864. Source: UniProtKB

apoptotic process

Non-traceable author statement PubMed 11564864. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of GTPase activity

Non-traceable author statement PubMed 9582122. Source: GOC

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of Rho GTPase activity

Non-traceable author statement Ref.6. Source: GOC

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

intracellular

Inferred by curator Ref.6. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGTPase activator activity

Non-traceable author statement PubMed 9582122. Source: UniProtKB

Rho guanyl-nucleotide exchange factor activity

Non-traceable author statement Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11864573. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15052-1)

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 2 (identifier: Q15052-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-154: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 776776Rho guanine nucleotide exchange factor 6
PRO_0000080917

Regions

Domain1 – 110110CH
Domain160 – 21960SH3
Domain241 – 421181DH
Domain443 – 548106PH

Amino acid modifications

Modified residue1261Phosphoserine Ref.11
Modified residue1441Phosphoserine Ref.11
Modified residue1501Phosphoserine Ref.9 Ref.11
Modified residue4881Phosphoserine By similarity
Modified residue6401Phosphoserine Ref.11
Modified residue6841Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 154154Missing in isoform 2.
VSP_015782
Natural variant2971Q → H.
Corresponds to variant rs5974620 [ dbSNP | Ensembl ].
VAR_051981

Experimental info

Sequence conflict1991E → G in CAD97632. Ref.2

Secondary structure

............................ 776
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 5D2622314E46341B

FASTA77687,499
        10         20         30         40         50         60 
MNPEEQIVTW LISLGVLESP KKTICDPEEF LKSSLKNGVV LCKLINRLMP GSVEKFCLDP 

        70         80         90        100        110        120 
QTEADCINNI NDFLKGCATL QVEIFDPDDL YSGVNFSKVL STLLAVNKAT EDQLSERPCG 

       130        140        150        160        170        180 
RSSSLSAANT SQTNPQGAVS STVSGLQRQS KTVEMTENGS HQLIVKARFN FKQTNEDELS 

       190        200        210        220        230        240 
VCKGDIIYVT RVEEGGWWEG TLNGRTGWFP SNYVREIKSS ERPLSPKAVK GFETAPLTKN 

       250        260        270        280        290        300 
YYTVVLQNIL DTEKEYAKEL QSLLVTYLRP LQSNNNLSTV EVTSLLGNFE EVCTFQQTLC 

       310        320        330        340        350        360 
QALEECSKFP ENQHKVGGCL LSLMPHFKSM YLAYCANHPS AVNVLTQHSD ELEQFMENQG 

       370        380        390        400        410        420 
ASSPGILILT TNLSKPFMRL EKYVTLLQEL ERHMEDTHPD HQDILKAIVA FKTLMGQCQD 

       430        440        450        460        470        480 
LRKRKQLELQ ILSEPIQAWE GEDIKNLGNV IFMSQVMVQY GACEEKEERY LMLFSNVLIM 

       490        500        510        520        530        540 
LSASPRMSGF IYQGKIPIAG TVVTRLDEIE GNDCTFEITG NTVERIVVHC NNNQDFQEWL 

       550        560        570        580        590        600 
EQLNRLIRGP ASCSSLSKTS SSSCSAHSSF SSTGQPRGPL EPPQIIKPWS LSCLRPAPPL 

       610        620        630        640        650        660 
RPSAALGYKE RMSYILKESS KSPKTMKKFL HKRKTERKPS EEEYVIRKST AALEEDAQIL 

       670        680        690        700        710        720 
KVIEAYCTSA NFQQGHGSST RKDSIPQVLL PEEEKLIIEE TRSNGQTIME EKSLVDTVYA 

       730        740        750        760        770 
LKDEVRELKQ ENKRMKQCLE EELKSRRDLE KLVRRLLKQT DECIRGESSS KTSILP 

« Hide

Isoform 2 [UniParc].

Checksum: B336793DC9A235ED
Show »

FASTA62270,791

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Brain and Placenta.
[2]"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].
Tissue: Adipose tissue.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 AND 2).
Tissue: Testis.
[6]"Mutations in ARHGEF6, encoding a guanine nucleotide exchange factor for Rho GTPases, in patients with X-linked mental retardation."
Kutsche K., Yntema H., Brandt A., Jantke I., Nothwang H.G., Orth U., Boavida M.G., David D., Chelly J., Fryns J.-P., Moraine C., Ropers H.-H., Hamel B.C.J., van Bokhoven H., Gal A.
Nat. Genet. 26:247-250(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-3 (ISOFORM 1), DISEASE.
[7]"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-776 (ISOFORM 1).
Tissue: Bone marrow.
[8]"Characterization of ARHGEF6, a guanine nucleotide exchange factor for Rho GTPases and a candidate gene for X-linked mental retardation: mutation screening in Borjeson-Forssman-Lehmann syndrome and MRX27."
Lower K.M., Gecz J.
Am. J. Med. Genet. 100:43-48(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor."
Mishima W., Suzuki A., Yamaji S., Yoshimi R., Ueda A., Kaneko T., Tanaka J., Miwa Y., Ohno S., Ishigatsubo Y.
Genes Cells 9:193-204(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARVB.
[11]"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-126; SER-144; SER-150; SER-640 AND SER-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"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, IDENTIFICATION IN A COMPLEX WITH BIN2 AND GIT2.
[13]"Solution structure of the CH domain and the SH3 domain in RAC/CDC42 guanine nucleotide exchange factor (GEF) 6."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 4-222.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK291742 mRNA. Translation: BAF84431.1.
AK294929 mRNA. Translation: BAH11929.1.
BX537390 mRNA. Translation: CAD97632.1.
AL683813, AL135783 Genomic DNA. Translation: CAI39443.1.
AL135783, AL683813 Genomic DNA. Translation: CAI42899.1.
AL135783 Genomic DNA. Translation: CAI42903.1.
CH471150 Genomic DNA. Translation: EAW88460.1.
CH471150 Genomic DNA. Translation: EAW88461.1.
BC039856 mRNA. Translation: AAH39856.1.
BC043505 mRNA. Translation: AAH43505.1. Different termination.
AF207831 mRNA. Translation: AAG27169.1.
D13631 mRNA. Translation: BAA02796.1. Different initiation.
D25304 mRNA. Translation: BAA04985.1.
CCDSCCDS14660.1. [Q15052-1]
RefSeqNP_004831.1. NM_004840.2. [Q15052-1]
XP_005262558.1. XM_005262501.1. [Q15052-2]
UniGeneHs.522795.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJYNMR-A160-222[»]
1WYRNMR-A4-111[»]
ProteinModelPortalQ15052.
SMRQ15052. Positions 4-111, 154-552, 711-762.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114847. 18 interactions.
IntActQ15052. 15 interactions.
MINTMINT-2791937.
STRING9606.ENSP00000250617.

PTM databases

PhosphoSiteQ15052.

Polymorphism databases

DMDM17371603.

Proteomic databases

MaxQBQ15052.
PaxDbQ15052.
PRIDEQ15052.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250617; ENSP00000250617; ENSG00000129675. [Q15052-1]
ENST00000370620; ENSP00000359654; ENSG00000129675. [Q15052-2]
ENST00000370622; ENSP00000359656; ENSG00000129675. [Q15052-2]
GeneID9459.
KEGGhsa:9459.
UCSCuc004fab.3. human. [Q15052-1]

Organism-specific databases

CTD9459.
GeneCardsGC0XM135747.
HGNCHGNC:685. ARHGEF6.
HPAHPA003578.
MIM300267. gene.
300436. phenotype.
neXtProtNX_Q15052.
Orphanet777. X-linked non-syndromic intellectual disability.
PharmGKBPA24976.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314429.
HOGENOMHOG000231381.
HOVERGENHBG050569.
InParanoidQ15052.
KOK05729.
OMANKATEDQ.
OrthoDBEOG708W04.
PhylomeDBQ15052.
TreeFamTF316105.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressQ15052.
BgeeQ15052.
CleanExHS_ARHGEF6.
GenevestigatorQ15052.

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.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
[Graphical view]
PfamPF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.
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.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGEF6. human.
EvolutionaryTraceQ15052.
GeneWikiARHGEF6.
GenomeRNAi9459.
NextBio35442.
PROQ15052.
SOURCESearch...

Entry information

Entry nameARHG6_HUMAN
AccessionPrimary (citable) accession number: Q15052
Secondary accession number(s): A6NMW9 expand/collapse secondary AC list , A8K6S7, B1AL37, Q15396, Q5JQ66, Q7Z3W1, Q86XH0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: July 9, 2014
This is version 160 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 X

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