Q14155 (ARHG7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.9 Ref.10 Ref.12 Ref.13 Ref.18
Subcellular location	Cell junction › focal adhesion By similarity. Cell projection › ruffle By similarity. Cytoplasm › cell cortex By similarity. Cell projection › lamellipodium 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 process	Neurogenesis
Cellular component	Cell junction Cell projection Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	SH3 domain
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process 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 nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome nervous system development Inferred from electronic annotation. Source: UniProtKB-KW 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 protein signal transduction Inferred from electronic annotation. Source: InterPro regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	cell 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_function	Rho 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 phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GIT1	Q9Y2X7	2	EBI-717515,EBI-466061
LRRK2	Q5S007	6	EBI-717515,EBI-5323863
NAA10	P41227	3	EBI-717515,EBI-747693

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 803

803

Rho guanine nucleotide exchange factor 7

PRO_0000080921

Regions

Domain

1 – 132

132

CH

Domain

184 – 243

60

SH3

Domain

271 – 451

181

DH

Domain

473 – 578

106

PH

Amino acid modifications

Modified residue

153

1

Phosphoserine By similarity

Modified residue

176

1

Phosphoserine By similarity

Modified residue

249

1

Phosphoserine Ref.17

Modified residue

518

1

Phosphoserine Ref.15

Modified residue

694

1

Phosphoserine; by CaMK1 Ref.13 Ref.14 Ref.17

Natural variations

Alternative sequence

1 – 178

178

Missing in isoform 1 and isoform 6.

VSP_011032

Alternative sequence

56 – 105

50

Missing in isoform 2.

VSP_011033

Alternative sequence

85 – 177

93

Missing in isoform 5.

VSP_034639

Alternative sequence

85 – 105

21

Missing in isoform 3.

VSP_011034

Alternative sequence

733 – 803

71

TWQGT…ISHQN → SSRKESAPQVLLPEEEKIIV EETKSNGQTVIEEKSLVDTV YALKDEVQELRQDNKKMKKS LEEEQRARKDLEKLVRKVLK NMNDPAWDETNL in isoform 1 and isoform 5.

VSP_011035

Natural variant

790

1

T → A Found in a clear cell renal carcinoma case; somatic mutation. Ref.22

VAR_064694

Experimental info

Sequence conflict

52 – 55

4

TIEK → EEKR in BAD66827. Ref.7

Sequence conflict

343

1

Q → K in AAH33905. Ref.6

Sequence conflict

552

1

M → V in AAH33905. Ref.6

Sequence conflict

595

1

H → D in BAD66827. Ref.7

Sequence conflict

636

1

I → T in AAH50521. Ref.6

Sequence conflict

740

1

M → L in AAH33905. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

803

Helix Strand Turn

Details...

Helix

3 – 13

11

Helix

27 – 35

9

Helix

39 – 48

10

Helix

63 – 79

17

Helix

109 – 113

5

Helix

118 – 135

18

Beta strand

188 – 191

4

Beta strand

210 – 215

6

Beta strand

218 – 226

9

Beta strand

229 – 240

12

Helix

271 – 301

31

Turn

302 – 304

3

Beta strand

305 – 310

6

Helix

311 – 313

3

Helix

316 – 338

23

Helix

346 – 378

33

Turn

379 – 381

3

Helix

382 – 385

4

Turn

386 – 389

4

Turn

395 – 397

3

Helix

398 – 402

5

Turn

406 – 408

3

Helix

409 – 411

3

Helix

413 – 422

10

Beta strand

428 – 430

3

Helix

432 – 453

22

Turn

454 – 456

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 4 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: 613EBA839E6FDBFD	FASTA	803	90,012
	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
	Isoform 1 [UniParc]. Checksum: B5B5A83F0EBC28D2	FASTA	646	73,140
	10 20 30 40 50 60 MTDNSNNQLV VRAKFNFQQT NEDELSFSKG DVIHVTRVEE GGWWEGTLNG RTGWFPSNYV 70 80 90 100 110 120 REVKASEKPV SPKSGTLKSP PKGFDTTAIN KSYYNVVLQN ILETENEYSK ELQTVLSTYL 130 140 150 160 170 180 RPLQTSEKLS SANISYLMGN LEEICSFQQM LVQSLEECTK LPEAQQRVGG CFLNLMPQMK 190 200 210 220 230 240 TLYLTYCANH PSAVNVLTEH SEELGEFMET KGASSPGILV LTTGLSKPFM RLDKYPTLLK 250 260 270 280 290 300 ELERHMEDYH TDRQDIQKSM AAFKNLSAQC QEVRKRKELE LQILTEAIRN WEGDDIKTLG 310 320 330 340 350 360 NVTYMSQVLI QCAGSEEKNE RYLLLFPNVL LMLSASPRMS GFIYQGKLPT TGMTITKLED 370 380 390 400 410 420 SENHRNAFEI SGSMIERILV SCNNQQDLQE WVEHLQKQTK VTSVGNPTIK PHSVPSHTLP 430 440 450 460 470 480 SHPVTPSSKH ADSKPAPLTP AYHTLPHPSH HGTPHTTINW GPLEPPKTPK PWSLSCLRPA 490 500 510 520 530 540 PPLRPSAALC YKEDLSKSPK TMKKLLPKRK PERKPSDEEF ASRKSTAALE EDAQILKVIE 550 560 570 580 590 600 AYCTSAKTRQ TLNSSSRKES APQVLLPEEE KIIVEETKSN GQTVIEEKSL VDTVYALKDE 610 620 630 640 VQELRQDNKK MKKSLEEEQR ARKDLEKLVR KVLKNMNDPA WDETNL
	Isoform 2 [UniParc]. Checksum: 04178E64ACF43846	FASTA	753	84,477
	10 20 30 40 50 60 MNSAEQTVTW LITLGVLESP KKTISDPEGF LQASLKDGVV LCRLLERLLP GTIEKTFDAN 70 80 90 100 110 120 DLYQGQNFNK VLSSLVTLNK VTADIGLGSD SVCARPSSHR IKSFDSLGSQ SLHTRTSKLF 130 140 150 160 170 180 QGQYRSLDMT DNSNNQLVVR AKFNFQQTNE DELSFSKGDV IHVTRVEEGG WWEGTLNGRT 190 200 210 220 230 240 GWFPSNYVRE VKASEKPVSP KSGTLKSPPK GFDTTAINKS YYNVVLQNIL ETENEYSKEL 250 260 270 280 290 300 QTVLSTYLRP LQTSEKLSSA NISYLMGNLE EICSFQQMLV QSLEECTKLP EAQQRVGGCF 310 320 330 340 350 360 LNLMPQMKTL YLTYCANHPS AVNVLTEHSE ELGEFMETKG ASSPGILVLT TGLSKPFMRL 370 380 390 400 410 420 DKYPTLLKEL ERHMEDYHTD RQDIQKSMAA FKNLSAQCQE VRKRKELELQ ILTEAIRNWE 430 440 450 460 470 480 GDDIKTLGNV TYMSQVLIQC AGSEEKNERY LLLFPNVLLM LSASPRMSGF IYQGKLPTTG 490 500 510 520 530 540 MTITKLEDSE NHRNAFEISG SMIERILVSC NNQQDLQEWV EHLQKQTKVT SVGNPTIKPH 550 560 570 580 590 600 SVPSHTLPSH PVTPSSKHAD SKPAPLTPAY HTLPHPSHHG TPHTTINWGP LEPPKTPKPW 610 620 630 640 650 660 SLSCLRPAPP LRPSAALCYK EDLSKSPKTM KKLLPKRKPE RKPSDEEFAS RKSTAALEED 670 680 690 700 710 720 AQILKVIEAY CTSAKTRQTL NSTWQGTDLM HNHVLADDDQ PSLDSLGRRS SLSRLEPSDL 730 740 750 SEDSDYDSIW TAHSYRMGST SRKSCCSYIS HQN
	Isoform 3 [UniParc]. Checksum: 9C602026D90A6D01	FASTA	782	87,770
	10 20 30 40 50 60 MNSAEQTVTW LITLGVLESP KKTISDPEGF LQASLKDGVV LCRLLERLLP GTIEKVYPEP 70 80 90 100 110 120 RSESECLSNI REFLRGCGAS LRLETFDAND LYQGQNFNKV LSSLVTLNKV TADIGLGSDS 130 140 150 160 170 180 VCARPSSHRI KSFDSLGSQS LHTRTSKLFQ GQYRSLDMTD NSNNQLVVRA KFNFQQTNED 190 200 210 220 230 240 ELSFSKGDVI HVTRVEEGGW WEGTLNGRTG WFPSNYVREV KASEKPVSPK SGTLKSPPKG 250 260 270 280 290 300 FDTTAINKSY YNVVLQNILE TENEYSKELQ TVLSTYLRPL QTSEKLSSAN ISYLMGNLEE 310 320 330 340 350 360 ICSFQQMLVQ SLEECTKLPE AQQRVGGCFL NLMPQMKTLY LTYCANHPSA VNVLTEHSEE 370 380 390 400 410 420 LGEFMETKGA SSPGILVLTT GLSKPFMRLD KYPTLLKELE RHMEDYHTDR QDIQKSMAAF 430 440 450 460 470 480 KNLSAQCQEV RKRKELELQI LTEAIRNWEG DDIKTLGNVT YMSQVLIQCA GSEEKNERYL 490 500 510 520 530 540 LLFPNVLLML SASPRMSGFI YQGKLPTTGM TITKLEDSEN HRNAFEISGS MIERILVSCN 550 560 570 580 590 600 NQQDLQEWVE HLQKQTKVTS VGNPTIKPHS VPSHTLPSHP VTPSSKHADS KPAPLTPAYH 610 620 630 640 650 660 TLPHPSHHGT PHTTINWGPL EPPKTPKPWS LSCLRPAPPL RPSAALCYKE DLSKSPKTMK 670 680 690 700 710 720 KLLPKRKPER KPSDEEFASR KSTAALEEDA QILKVIEAYC TSAKTRQTLN STWQGTDLMH 730 740 750 760 770 780 NHVLADDDQP SLDSLGRRSS LSRLEPSDLS EDSDYDSIWT AHSYRMGSTS RKSCCSYISH QN
	Isoform 5 [UniParc]. Checksum: E82D55E6187DADB2	FASTA	731	82,571
	10 20 30 40 50 60 MNSAEQTVTW LITLGVLESP KKTISDPEGF LQASLKDGVV LCRLLERLLP GTIEKVYPEP 70 80 90 100 110 120 RSESECLSNI REFLRGCGAS LRLEDMTDNS NNQLVVRAKF NFQQTNEDEL SFSKGDVIHV 130 140 150 160 170 180 TRVEEGGWWE GTLNGRTGWF PSNYVREVKA SEKPVSPKSG TLKSPPKGFD TTAINKSYYN 190 200 210 220 230 240 VVLQNILETE NEYSKELQTV LSTYLRPLQT SEKLSSANIS YLMGNLEEIC SFQQMLVQSL 250 260 270 280 290 300 EECTKLPEAQ QRVGGCFLNL MPQMKTLYLT YCANHPSAVN VLTEHSEELG EFMETKGASS 310 320 330 340 350 360 PGILVLTTGL SKPFMRLDKY PTLLKELERH MEDYHTDRQD IQKSMAAFKN LSAQCQEVRK 370 380 390 400 410 420 RKELELQILT EAIRNWEGDD IKTLGNVTYM SQVLIQCAGS EEKNERYLLL FPNVLLMLSA 430 440 450 460 470 480 SPRMSGFIYQ GKLPTTGMTI TKLEDSENHR NAFEISGSMI ERILVSCNNQ QDLQEWVEHL 490 500 510 520 530 540 QKQTKVTSVG NPTIKPHSVP SHTLPSHPVT PSSKHADSKP APLTPAYHTL PHPSHHGTPH 550 560 570 580 590 600 TTINWGPLEP PKTPKPWSLS CLRPAPPLRP SAALCYKEDL SKSPKTMKKL LPKRKPERKP 610 620 630 640 650 660 SDEEFASRKS TAALEEDAQI LKVIEAYCTS AKTRQTLNSS SRKESAPQVL LPEEEKIIVE 670 680 690 700 710 720 ETKSNGQTVI EEKSLVDTVY ALKDEVQELR QDNKKMKKSL EEEQRARKDL EKLVRKVLKN 730 MNDPAWDETN L
	Isoform 6 [UniParc]. Checksum: 25DAD75DD4B0AC2E	FASTA	625	70,450
	10 20 30 40 50 60 MTDNSNNQLV VRAKFNFQQT NEDELSFSKG DVIHVTRVEE GGWWEGTLNG RTGWFPSNYV 70 80 90 100 110 120 REVKASEKPV SPKSGTLKSP PKGFDTTAIN KSYYNVVLQN ILETENEYSK ELQTVLSTYL 130 140 150 160 170 180 RPLQTSEKLS SANISYLMGN LEEICSFQQM LVQSLEECTK LPEAQQRVGG CFLNLMPQMK 190 200 210 220 230 240 TLYLTYCANH PSAVNVLTEH SEELGEFMET KGASSPGILV LTTGLSKPFM RLDKYPTLLK 250 260 270 280 290 300 ELERHMEDYH TDRQDIQKSM AAFKNLSAQC QEVRKRKELE LQILTEAIRN WEGDDIKTLG 310 320 330 340 350 360 NVTYMSQVLI QCAGSEEKNE RYLLLFPNVL LMLSASPRMS GFIYQGKLPT TGMTITKLED 370 380 390 400 410 420 SENHRNAFEI SGSMIERILV SCNNQQDLQE WVEHLQKQTK VTSVGNPTIK PHSVPSHTLP 430 440 450 460 470 480 SHPVTPSSKH ADSKPAPLTP AYHTLPHPSH HGTPHTTINW GPLEPPKTPK PWSLSCLRPA 490 500 510 520 530 540 PPLRPSAALC YKEDLSKSPK TMKKLLPKRK PERKPSDEEF ASRKSTAALE EDAQILKVIE 550 560 570 580 590 600 AYCTSAKTRQ TLNSTWQGTD LMHNHVLADD DQPSLDSLGR RSSLSRLEPS DLSEDSDYDS 610 620 IWTAHSYRMG STSRKSCCSY ISHQN

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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), MASS SPECTROMETRY.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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. , 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.

IPI

IPI00449907.
IPI00449908.
IPI00449909.
IPI00900260.
IPI00900378.
IPI00947263.

RefSeq

NP_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.

UniGene

Hs.508738.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BY1	NMR	-	A	260-467	[»]
1ZSG	NMR	-	A	179-243	[»]
2L3G	NMR	-	A	1-137	[»]

ProteinModelPortal

Q14155.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14155. 8 interactions.

MINT

MINT-92779.

PTM databases

PhosphoSite

Q14155.

Polymorphism databases

DMDM

50403776.

Proteomic databases

PaxDb

Q14155.

PRIDE

Q14155.

Protocols and materials databases

DNASU

8874.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000317133; ENSP00000325994; ENSG00000102606.
ENST00000370623; ENSP00000359657; ENSG00000102606.
ENST00000375723; ENSP00000364875; ENSG00000102606.
ENST00000375736; ENSP00000364888; ENSG00000102606.
ENST00000375739; ENSP00000364891; ENSG00000102606.
ENST00000375741; ENSP00000364893; ENSG00000102606.
ENST00000426073; ENSP00000397068; ENSG00000102606.

GeneID

8874.

KEGG

hsa:8874.

UCSC

uc001vrr.2. human.
uc001vrs.2. human.
uc001vrt.2. human.
uc001vrv.4. human.

Organism-specific databases

CTD

8874.

GeneCards

GC13P111766.

H-InvDB

HIX0037536.

HGNC

HGNC:15607. ARHGEF7.

HPA

HPA004744.

MIM

605477. gene.

neXtProt

NX_Q14155.

PharmGKB

PA24977.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG314429.

HOVERGEN

HBG050569.

InParanoid

Q14155.

KO

K13710.

OMA

DHELGMV.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.
pi3kcipathway. Class I PI3K signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q14155.

Bgee

Q14155.

Genevestigator

Q14155.

GermOnline

ENSG00000102606. Homo sapiens.

Family and domain databases

Gene3D

1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.

InterPro

IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

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

PRINTS

PR00452. SH3DOMAIN.

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. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARHGEF7. human.

EvolutionaryTrace

Q14155.

GenomeRNAi

8874.

NextBio

33313.

SOURCE

Search...

Entry information

Entry name

ARHG7_HUMAN

Accession

Primary (citable) accession number: Q14155
Secondary accession number(s): B1ALK6 , 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:	May 1, 2013
This is version 145 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.