Q15052 (ARHG6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	776 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Tissue specificity	Ubiquitous.
Involvement in disease	Defects in ARHGEF6 are the cause of mental retardation X-linked type 46 (MRX46) [MIM:300436]. Mental retardation is a mental disorder characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs. 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
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Mental retardation
Domain	SH3 domain
Molecular function	Guanine-nucleotide releasing factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	JNK cascade Non-traceable author statement. Source: UniProtKB apoptotic process Non-traceable author statement. Source: UniProtKB cell junction assembly Traceable author statement. Source: Reactome induction of apoptosis by extracellular signals Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	GTPase activator activity Non-traceable author statement. Source: UniProtKB Rho guanyl-nucleotide exchange factor activity Non-traceable author statement Ref.6. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NAA10	P41227	3	EBI-1642523,EBI-747693

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.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 776

776

Rho guanine nucleotide exchange factor 6

PRO_0000080917

Regions

Domain

1 – 110

110

CH

Domain

160 – 219

60

SH3

Domain

241 – 421

181

DH

Domain

443 – 548

106

PH

Amino acid modifications

Modified residue

122

1

Phosphoserine By similarity

Modified residue

126

1

Phosphoserine Ref.17

Modified residue

144

1

Phosphoserine Ref.17

Modified residue

150

1

Phosphoserine Ref.17

Modified residue

188

1

Phosphotyrosine Ref.17

Modified residue

225

1

Phosphoserine Ref.10

Modified residue

488

1

Phosphoserine Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17

Modified residue

640

1

Phosphoserine Ref.17

Modified residue

650

1

Phosphothreonine By similarity

Modified residue

684

1

Phosphoserine Ref.10 Ref.15 Ref.17

Modified residue

751

1

N6-acetyllysine Ref.18

Natural variations

Alternative sequence

1 – 154

154

Missing in isoform 2.

VSP_015782

Natural variant

297

1

Q → H.
Corresponds to variant rs5974620 [ dbSNP | Ensembl ].

VAR_051981

Experimental info

Sequence conflict

199

1

E → G in CAD97632. Ref.2

Secondary structure

1

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776

Helix Strand Turn

Details...

Helix

4 – 14

11

Helix

27 – 37

11

Helix

39 – 48

10

Helix

63 – 80

18

Helix

87 – 91

5

Helix

96 – 110

15

Beta strand

163 – 166

4

Beta strand

187 – 191

5

Beta strand

194 – 196

3

Beta strand

198 – 202

5

Beta strand

205 – 209

5

Turn

211 – 213

3

Beta strand

214 – 216

3

Helix

219 – 222

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 5D2622314E46341B	FASTA	776	87,499
	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
	Isoform 2 [UniParc]. Checksum: B336793DC9A235ED	FASTA	622	70,791
	10 20 30 40 50 60 MTENGSHQLI VKARFNFKQT NEDELSVCKG DIIYVTRVEE GGWWEGTLNG RTGWFPSNYV 70 80 90 100 110 120 REIKSSERPL SPKAVKGFET APLTKNYYTV VLQNILDTEK EYAKELQSLL VTYLRPLQSN 130 140 150 160 170 180 NNLSTVEVTS LLGNFEEVCT FQQTLCQALE ECSKFPENQH KVGGCLLSLM PHFKSMYLAY 190 200 210 220 230 240 CANHPSAVNV LTQHSDELEQ FMENQGASSP GILILTTNLS KPFMRLEKYV TLLQELERHM 250 260 270 280 290 300 EDTHPDHQDI LKAIVAFKTL MGQCQDLRKR KQLELQILSE PIQAWEGEDI KNLGNVIFMS 310 320 330 340 350 360 QVMVQYGACE EKEERYLMLF SNVLIMLSAS PRMSGFIYQG KIPIAGTVVT RLDEIEGNDC 370 380 390 400 410 420 TFEITGNTVE RIVVHCNNNQ DFQEWLEQLN RLIRGPASCS SLSKTSSSSC SAHSSFSSTG 430 440 450 460 470 480 QPRGPLEPPQ IIKPWSLSCL RPAPPLRPSA ALGYKERMSY ILKESSKSPK TMKKFLHKRK 490 500 510 520 530 540 TERKPSEEEY VIRKSTAALE EDAQILKVIE AYCTSANFQQ GHGSSTRKDS IPQVLLPEEE 550 560 570 580 590 600 KLIIEETRSN GQTIMEEKSL VDTVYALKDE VRELKQENKR MKQCLEEELK SRRDLEKLVR 610 620 RLLKQTDECI RGESSSKTSI LP

References

	« Hide 'large scale' referencesShow '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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: 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: 17974005] [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. , 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: 15772651] [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. , 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: 15489334] [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: 11017088] [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: 7584026] [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: 11337747] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-684, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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-488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY.
[17]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-144; SER-150; TYR-188; SER-488; SER-640 AND SER-684, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-751, MASS SPECTROMETRY.
[19]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"Solution structure of 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 159-222.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK291742 mRNA. Translation: BAF84431.1.
BX537390 mRNA. Translation: CAD97632.1.
AL683813, AL135783 Genomic DNA. Translation: CAI39443.1.
AL135783, AL683813 Genomic DNA. Translation: CAI42899.1.
CH471150 Genomic DNA. Translation: EAW88460.1.
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.

IPI

IPI00014256.
IPI00640748.

RefSeq

NP_004831.1. NM_004840.2.

UniGene

Hs.522795.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UJY	NMR	-	A	160-222	[»]
1WYR	NMR	-	A	4-111	[»]

ProteinModelPortal

Q15052.

SMR

Q15052. Positions 4-111, 159-552, 711-762.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15052. 3 interactions.

MINT

MINT-2791937.

STRING

Q15052.

PTM databases

PhosphoSite

Q15052.

Polymorphism databases

DMDM

17371603.

Proteomic databases

PRIDE

Q15052.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000250617; ENSP00000250617; ENSG00000129675.

GeneID

9459.

KEGG

hsa:9459.

UCSC

uc004fab.1. human.

Organism-specific databases

CTD

9459.

GeneCards

GC0XM135747.

H-InvDB

HIX0017082.

HGNC

HGNC:685. ARHGEF6.

HPA

HPA003578.

MIM

300267. gene.
300436. phenotype.

neXtProt

NX_Q15052.

Orphanet

777. X-linked nonsyndromic intellectual deficit.

PharmGKB

PA24976.

HUGE

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GenAtlas

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Phylogenomic databases

eggNOG

prNOG17559.

HOVERGEN

HBG050569.

InParanoid

Q15052.

OMA

GSVEKYC.

OrthoDB

EOG4CVG6B.

PhylomeDB

Q15052.

Enzyme and pathway databases

Pathway_Interaction_DB

pi3kcipathway. Class I PI3K signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

Q15052.

Bgee

Q15052.

CleanEx

HS_ARHGEF6.

Genevestigator

Q15052.

GermOnline

ENSG00000129675. Homo sapiens.

Family and domain databases

InterPro

IPR001715. CH-domain.
IPR000219. DH-domain.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 1 hit.
G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:1.20.900.10. RhoGEF. 1 hit.

KO

K05729.

Pfam

PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.

SMART

SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.
SSF48065. DH-domain. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50021. CH. 1 hit.
PS00741. DH_1. False negative.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

35442.

SOURCE

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Entry information

Entry name

ARHG6_HUMAN

Accession

Primary (citable) accession number: Q15052
Secondary accession number(s): A6NMW9 , A8K6S7, Q15396, Q5JQ66, Q7Z3W1, Q86XH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	January 25, 2012
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.