A7KAX9 (RHG32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho GTPase-activating protein 32

Alternative name(s):
Brain-specific Rho GTPase-activating protein
GAB-associated Cdc42/Rac GTPase-activating protein
GC-GAP
GTPase regulator interacting with TrkA
Rho-type GTPase-activating protein 32
Rho/Cdc42/Rac GTPase-activating protein RICS
RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling
p200RhoGAP
p250GAP

Gene names

Name:	ARHGAP32
Synonyms:	GRIT, KIAA0712, RICS

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	2087 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity By similarity. Ref.1 Ref.2 Ref.3 Ref.7 Ref.8 Ref.9 Ref.10
Subunit structure	Interacts with NTRK1 (via cytoplasmic domain); the interaction is independent of the phosphorylation state of NTRK1. Interacts with SHC3 (via SH2 domain). Interacts with RASA1 (via SH3 domain); the interaction is necessary for the Ras activation and cell transforming activities of ARHGAP32 By similarity. Interacts with GAB1 and GAB2. Interacts with CRK and CRKL. Found in a complex with CRKL and BCAR1; upon EGF stimulation BCAR1 may be replaced by EGFR. Interacts with NCK1 (via SH3 domain); NCK1 recruits phosphorylated BCAR1 to the complex. Isoform 2 interacts with FYN; the interaction appears to be dependent on tyrosine phosphorylation of ARHGAP32. Interacts with EGFR; the interaction requires EGF stimulation and is increased by SHC3. Interacts with CDC42; the interaction requires constitutively active CDC42. Interacts with CTNNB1, DLG4, CDH2 and GRIN2B By similarity. Ref.1 Ref.2 Ref.7 Ref.9 Ref.10
Subcellular location	Cell junction › synapse › postsynaptic cell membrane › postsynaptic density. Cell projection › dendritic spine By similarity. Cytoplasm › cell cortex. Endosome membrane By similarity. Golgi apparatus membrane By similarity. Endoplasmic reticulum membrane By similarity. Membrane. Note: Association to membrane via PX domain. Associated with cortical actin in undifferentiated neuroblastoma cells, but localized to dendritic spine and postsynaptic density after differentiation By similarity. Colocalizes with EGFR at the cell membrane upon EGF treatment. Colocalizes with GAB2 at the cell membrane. Ref.1 Ref.2 Ref.3
Tissue specificity	Isoform 1 and isoform 2 are highly expressed in brain and testis. Isoform 1 is also expressed in other tissues such as lung, liver and spleen. Ref.1
Domain	The N-terminal PX domain interacts specifically with phosphatidylinositides By similarity.
Post-translational modification	Isoform 2 is phosphorylated on multiple tyrosine residues by FYN. Phosphorylated tyrosine residues undergo dephosphorylation after stimulation of NMDA receptors By similarity. Phosphorylated in vitro by CaMK2 in the presence of calmodulin and calcium; which inhibits GAP activity By similarity. Ref.1 Ref.7
Sequence similarities	Belongs to the PX domain-containing GAP family. Contains 1 PX (phox homology) domain. Contains 1 Rho-GAP domain. Contains 1 SH3 domain.
Sequence caution	The sequence BAA34432.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Endoplasmic reticulum Endosome Golgi apparatus Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	SH3 domain
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of GTPase activity Inferred from electronic annotation. 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_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell actin cytoskeleton Inferred from electronic annotation. Source: Compara cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytosol Traceable author statement. Source: Reactome endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW postsynaptic density Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FYN	P06241	4	EBI-308663,EBI-515315

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: A7KAX9-1)

Also known as: PX-RICS;

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: A7KAX9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-349: Missing.

Isoform 3 (identifier: A7KAX9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-290: Missing.
     567-612: FSGRISMAMQ...AQARTQAQVN → LPHFSARTEL...LVQITVCISI
     613-2087: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2087

2087

Rho GTPase-activating protein 32

PRO_0000345203

Regions

Domain

131 – 245

115

PX; atypical

Domain

259 – 321

63

SH3

Domain

372 – 567

196

Rho-GAP

Region

1391 – 1711

321

Interaction with GAB2

Region

1685 – 2087

403

Interaction with FYN

Compositional bias

1031 – 1036

6

Poly-Pro

Compositional bias

1305 – 1310

6

Poly-Pro

Amino acid modifications

Modified residue

706

1

Phosphoserine Ref.12

Modified residue

856

1

Phosphoserine By similarity

Modified residue

892

1

Phosphoserine By similarity

Modified residue

952

1

Phosphoserine By similarity

Modified residue

1203

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 349

349

Missing in isoform 2.

VSP_034933

Alternative sequence

1 – 290

290

Missing in isoform 3.

VSP_034934

Alternative sequence

567 – 612

46

FSGRI…QAQVN → LPHFSARTELIVPFPLRLLR KQFTPPLLGPMSPLNPLVQI TVCISI in isoform 3.

VSP_034935

Alternative sequence

613 – 2087

1475

Missing in isoform 3.

VSP_034936

Experimental info

Mutagenesis

173

1

Y → A: Loss of binding to phospholipids. Cytoplasmic localization. Ref.3

Mutagenesis

407

1

R → A: Mild effect on GAP activity and neurite-promotion upon nerve growth factor stimulation. Ref.1 Ref.3 Ref.8 Ref.9 Ref.10

Mutagenesis

407

1

R → I: Loss of GAP activity. Ref.1 Ref.3 Ref.8 Ref.9 Ref.10

Mutagenesis

407

1

R → M: Loss of GAP activity. In isoform 1, no inhibitory effect on neurite extension. Ref.1 Ref.3 Ref.8 Ref.9 Ref.10

Mutagenesis

447

1

K → A: Loss of GAP activity. Ref.9

Secondary structure

1

.

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2087

Helix Strand Turn

Details...

Helix

374 – 381

8

Helix

387 – 399

13

Turn

403 – 407

5

Helix

412 – 423

12

Turn

433 – 437

5

Helix

439 – 452

14

Turn

460 – 462

3

Helix

463 – 470

8

Beta strand

472 – 474

3

Helix

475 – 486

12

Helix

491 – 508

18

Helix

511 – 514

4

Helix

518 – 529

12

Helix

553 – 561

9

Helix

563 – 566

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PX-RICS) [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 075E5B4902857D06	FASTA	2,087	230,529
	10 20 30 40 50 60 METESESSTL GDDSVFWLES EVIIQVTDCE EEEREEKFRK MKSSVHSEED DFVPELHRNV 70 80 90 100 110 120 HPRERPDWEE TLSAMARGAD VPEIPGDLTL KTCGSTASMK VKHVKKLPFT KGHFPKMAEC 130 140 150 160 170 180 AHFHYENVEF GSIQLSLSEE QNEVMKNGCE SKELVYLVQI ACQGKSWIVK RSYEDFRVLD 190 200 210 220 230 240 KHLHLCIYDR RFSQLSELPR SDTLKDSPES VTQMLMAYLS RLSAIAGNKI NCGPALTWME 250 260 270 280 290 300 IDNKGNHLLV HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW 310 320 330 340 350 360 RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM KSRPTKQKLK 370 380 390 400 410 420 QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG VASNIQRLRH 430 440 450 460 470 480 EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV SAATDEERLI 490 500 510 520 530 540 KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF 550 560 570 580 590 600 SGTAAFMEVR IQSVVVEFIL NHVDVLFSGR ISMAMQEGAA SLSRPKSLLV SSPSTKLLTL 610 620 630 640 650 660 EEAQARTQAQ VNSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERKRPQN KMKKSPVGSW 670 680 690 700 710 720 RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT LRSAKSEESL TSLHAVDGDS 730 740 750 760 770 780 KLFRPRRPRS SSDALSASFN GEMLGNRCNS YDNLPHDNES EEEGGLLHIP ALMSPHSAED 790 800 810 820 830 840 VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SPGYSKDKPS ANKKDAETGS 850 860 870 880 890 900 SQCQTPGSTA SSEPVSPLQE KLSPFFTLDL SPTEDKSSKP SSFTEKVVYA FSPKIGRKLS 910 920 930 940 950 960 KSPSMSISEP ISVTLPPRVS EVIGTVSNTT AQNASSSTWD KCVEERDATN RSPTQIVKMK 970 980 990 1000 1010 1020 TNETVAQEAY ESEVQPLDQV AAEEVELPGK EDQSVSSSQS KAVASGQTQT GAVTHDPPQD 1030 1040 1050 1060 1070 1080 SVPVSSVSLI PPPPPPKNVA RMLALALAES AQQASTQSLK RPGTSQAGYT NYGDIAVATT 1090 1100 1110 1120 1130 1140 EDNLSSSYSA VALDKAYFQT DRPAEQFHLQ NNAPGNCDHP LPETTATGDP THSNTTESGE 1150 1160 1170 1180 1190 1200 QHHQVDLTGN QPHQAYLSGD PEKARITSVP LDSEKSDDHV SFPEDQSGKN SMPTVSFLDQ 1210 1220 1230 1240 1250 1260 DQSPPRFYSG DQPPSYLGAS VDKLHHPLEF ADKSPTPPNL PSDKIYPPSG SPEENTSTAT 1270 1280 1290 1300 1310 1320 MTYMTTTPAT AQMSTKEASW DVAEQPTTAD FAAATLQRTH RTNRPLPPPP SQRSAEQPPV 1330 1340 1350 1360 1370 1380 VGQVQAATNI GLNNSHKVQG VVPVPERPPE PRAMDDPASA FISDSGAAAA QCPMATAVQP 1390 1400 1410 1420 1430 1440 GLPEKVRDGA RVPLLHLRAE SVPAHPCGFP APLPPTRMME SKMIAAIHSS SADATSSSNY 1450 1460 1470 1480 1490 1500 HSFVTASSTS VDDALPLPLP VPQPKHASQK TVYSSFARPD VTTEPFGPDN CLHFNMTPNC 1510 1520 1530 1540 1550 1560 QYRPQSVPPH HNKLEQHQVY GARSEPPASM GLRYNTYVAP GRNASGHHSK PCSRVEYVSS 1570 1580 1590 1600 1610 1620 LSSSVRNTCY PEDIPPYPTI RRVQSLHAPP SSMIRSVPIS RTEVPPDDEP AYCPRPLYQY 1630 1640 1650 1660 1670 1680 KPYQSSQARS DYHVTQLQPY FENGRVHYRY SPYSSSSSSY YSPDGALCDV DAYGTVQLRP 1690 1700 1710 1720 1730 1740 LHRLPNRDFA FYNPRLQGKS LYSYAGLAPR PRANVTGYFS PNDHNVVSMP PAADVKHTYT 1750 1760 1770 1780 1790 1800 SWDLEDMEKY RMQSIRRESR ARQKVKGPVM SQYDNMTPAV QDDLGGIYVI HLRSKSDPGK 1810 1820 1830 1840 1850 1860 TGLLSVAEGK ESRHAAKAIS PEGEDRFYRR HPEAEMDRAH HHGGHGSTQP EKPSLPQKQS 1870 1880 1890 1900 1910 1920 SLRSRKLPDM GCSLPEHRAH QEASHRQFCE SKNGPPYPQG AGQLDYGSKG IPDTSEPVSY 1930 1940 1950 1960 1970 1980 HNSGVKYAAS GQESLRLNHK EVRLSKEMER PWVRQPSAPE KHSRDCYKEE EHLTQSIVPP 1990 2000 2010 2020 2030 2040 PKPERSHSLK LHHTQNVERD PSVLYQYQPH GKRQSSVTVV SQYDNLEDYH SLPQHQRGVF 2050 2060 2070 2080 GGGGMGTYVP PGFPHPQSRT YATALGQGAF LPAELSLQHP ETQIHAE
	Isoform 2 [UniParc]. Checksum: 49B5C6F92BDE9A27	FASTA	1,738	190,970
	10 20 30 40 50 60 MKSRPTKQKL KQRGILKERV FGCDLGEHLL NSGFEVPQVL QSCTAFIERY GIVDGIYRLS 70 80 90 100 110 120 GVASNIQRLR HEFDSEHVPD LTKEPYVQDI HSVGSLCKLY FRELPNPLLT YQLYEKFSDA 130 140 150 160 170 180 VSAATDEERL IKIHDVIQQL PPPHYRTLEF LMRHLSLLAD YCSITNMHAK NLAIVWAPNL 190 200 210 220 230 240 LRSKQIESAC FSGTAAFMEV RIQSVVVEFI LNHVDVLFSG RISMAMQEGA ASLSRPKSLL 250 260 270 280 290 300 VSSPSTKLLT LEEAQARTQA QVNSPIVTEN KYIEVGEGPA ALQGKFHTII EFPLERKRPQ 310 320 330 340 350 360 NKMKKSPVGS WRSFFNLGKS SSVSKRKLQR NESEPSEMKA MALKGGRAEG TLRSAKSEES 370 380 390 400 410 420 LTSLHAVDGD SKLFRPRRPR SSSDALSASF NGEMLGNRCN SYDNLPHDNE SEEEGGLLHI 430 440 450 460 470 480 PALMSPHSAE DVDLSPPDIG VASLDFDPMS FQCSPPKAES ECLESGASFL DSPGYSKDKP 490 500 510 520 530 540 SANKKDAETG SSQCQTPGST ASSEPVSPLQ EKLSPFFTLD LSPTEDKSSK PSSFTEKVVY 550 560 570 580 590 600 AFSPKIGRKL SKSPSMSISE PISVTLPPRV SEVIGTVSNT TAQNASSSTW DKCVEERDAT 610 620 630 640 650 660 NRSPTQIVKM KTNETVAQEA YESEVQPLDQ VAAEEVELPG KEDQSVSSSQ SKAVASGQTQ 670 680 690 700 710 720 TGAVTHDPPQ DSVPVSSVSL IPPPPPPKNV ARMLALALAE SAQQASTQSL KRPGTSQAGY 730 740 750 760 770 780 TNYGDIAVAT TEDNLSSSYS AVALDKAYFQ TDRPAEQFHL QNNAPGNCDH PLPETTATGD 790 800 810 820 830 840 PTHSNTTESG EQHHQVDLTG NQPHQAYLSG DPEKARITSV PLDSEKSDDH VSFPEDQSGK 850 860 870 880 890 900 NSMPTVSFLD QDQSPPRFYS GDQPPSYLGA SVDKLHHPLE FADKSPTPPN LPSDKIYPPS 910 920 930 940 950 960 GSPEENTSTA TMTYMTTTPA TAQMSTKEAS WDVAEQPTTA DFAAATLQRT HRTNRPLPPP 970 980 990 1000 1010 1020 PSQRSAEQPP VVGQVQAATN IGLNNSHKVQ GVVPVPERPP EPRAMDDPAS AFISDSGAAA 1030 1040 1050 1060 1070 1080 AQCPMATAVQ PGLPEKVRDG ARVPLLHLRA ESVPAHPCGF PAPLPPTRMM ESKMIAAIHS 1090 1100 1110 1120 1130 1140 SSADATSSSN YHSFVTASST SVDDALPLPL PVPQPKHASQ KTVYSSFARP DVTTEPFGPD 1150 1160 1170 1180 1190 1200 NCLHFNMTPN CQYRPQSVPP HHNKLEQHQV YGARSEPPAS MGLRYNTYVA PGRNASGHHS 1210 1220 1230 1240 1250 1260 KPCSRVEYVS SLSSSVRNTC YPEDIPPYPT IRRVQSLHAP PSSMIRSVPI SRTEVPPDDE 1270 1280 1290 1300 1310 1320 PAYCPRPLYQ YKPYQSSQAR SDYHVTQLQP YFENGRVHYR YSPYSSSSSS YYSPDGALCD 1330 1340 1350 1360 1370 1380 VDAYGTVQLR PLHRLPNRDF AFYNPRLQGK SLYSYAGLAP RPRANVTGYF SPNDHNVVSM 1390 1400 1410 1420 1430 1440 PPAADVKHTY TSWDLEDMEK YRMQSIRRES RARQKVKGPV MSQYDNMTPA VQDDLGGIYV 1450 1460 1470 1480 1490 1500 IHLRSKSDPG KTGLLSVAEG KESRHAAKAI SPEGEDRFYR RHPEAEMDRA HHHGGHGSTQ 1510 1520 1530 1540 1550 1560 PEKPSLPQKQ SSLRSRKLPD MGCSLPEHRA HQEASHRQFC ESKNGPPYPQ GAGQLDYGSK 1570 1580 1590 1600 1610 1620 GIPDTSEPVS YHNSGVKYAA SGQESLRLNH KEVRLSKEME RPWVRQPSAP EKHSRDCYKE 1630 1640 1650 1660 1670 1680 EEHLTQSIVP PPKPERSHSL KLHHTQNVER DPSVLYQYQP HGKRQSSVTV VSQYDNLEDY 1690 1700 1710 1720 1730 HSLPQHQRGV FGGGGMGTYV PPGFPHPQSR TYATALGQGA FLPAELSLQH PETQIHAE
	Isoform 3 [UniParc]. Checksum: CE60526885AED792	FASTA	322	36,669
	10 20 30 40 50 60 MPPKVLSTWW RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM 70 80 90 100 110 120 KSRPTKQKLK QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG 130 140 150 160 170 180 VASNIQRLRH EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV 190 200 210 220 230 240 SAATDEERLI KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL 250 260 270 280 290 300 RSKQIESACF SGTAAFMEVR IQSVVVEFIL NHVDVLLPHF SARTELIVPF PLRLLRKQFT 310 320 PPLLGPMSPL NPLVQITVCI SI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Grit, a GTPase-activating protein for the Rho family, regulates neurite extension through association with the TrkA receptor and N-Shc and CrkL/Crk adapter molecules." Nakamura T., Komiya M., Sone K., Hirose E., Gotoh N., Morii H., Ohta Y., Mori N. Mol. Cell. Biol. 22:8721-8734(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH NTRK1; SHC3; BCAR1; EGFR; CRK AND CRKL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF ARG-407. Tissue: Brain.
[2]	"GC-GAP, a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2." Zhao C., Ma H., Bossy-Wetzel E., Lipton S.A., Zhang Z., Feng G.S. J. Biol. Chem. 278:34641-34653(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH GAB1 AND GAB2; BCAR1; CRK AND NCK1, SUBCELLULAR LOCATION. Tissue: Brain.
[3]	"PX-RICS, a novel splicing variant of RICS, is a main isoform expressed during neural development." Hayashi T., Okabe T., Nasu-Nishimura Y., Sakaue F., Ohwada S., Matsuura K., Akiyama T., Nakamura T. Genes Cells 12:929-939(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-173 AND ARG-407.
[4]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[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 2 AND 3). Tissue: Colon and Eye.
[7]	"p250GAP, a neural RhoGAP protein, is associated with and phosphorylated by Fyn." Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T., Yamamoto T. Biochem. Biophys. Res. Commun. 306:151-155(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FYN, PHOSPHORYLATION (ISOFORM 2).
[8]	"Characterization of a brain-specific Rho GTPase-activating protein, p200RhoGAP." Moon S.Y., Zang H., Zheng Y. J. Biol. Chem. 278:4151-4159(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-407.
[9]	"RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is involved in the beta-catenin-N-cadherin and N-methyl-D-aspartate receptor signaling." Okabe T., Nakamura T., Nishimura Y.N., Kohu K., Ohwada S., Morishita Y., Akiyama T. J. Biol. Chem. 278:9920-9927(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CTNNB1, MUTAGENESIS OF ARG-407 AND LYS-447.
[10]	"p250GAP, a novel brain-enriched GTPase-activating protein for Rho family GTPases, is involved in the N-methyl-d-aspartate receptor signaling." Nakazawa T., Watabe A.M., Tezuka T., Yoshida Y., Yokoyama K., Umemori H., Inoue A., Okabe S., Manabe T., Yamamoto T. Mol. Biol. Cell 14:2921-2934(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GRIN2B, MUTAGENESIS OF ARG-407.
[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-1203, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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-706, MASS SPECTROMETRY.
[13]	"Crystal structure of the Rho-GAP domain of RICS." Structural genomics consortium (SGC) Submitted (SEP-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 367-577.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB079856 mRNA. Translation: BAC24802.1.
AY194287 mRNA. Translation: AAO43677.1.
EF127492 mRNA. Translation: ABO33171.1.
AB018255 mRNA. Translation: BAA34432.2. Different initiation.
CH471065 Genomic DNA. Translation: EAW67740.1.
BC000277 mRNA. Translation: AAH00277.2.
BC104898 mRNA. Translation: AAI04899.1.
BC113429 mRNA. Translation: AAI13430.1.

IPI

IPI00787743.
IPI00900354.
IPI01018779.

RefSeq

NP_001136157.1. NM_001142685.1.
NP_055530.2. NM_014715.3.

UniGene

Hs.440379.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IUG	X-ray	1.77	A/B	367-577	[»]

ProteinModelPortal

A7KAX9.

ModBase

Search...

Protein-protein interaction databases

IntAct

A7KAX9. 6 interactions.

MINT

MINT-2867388.

Proteomic databases

PaxDb

A7KAX9.

PRIDE

A7KAX9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310343; ENSP00000310561; ENSG00000134909.
ENST00000392657; ENSP00000376425; ENSG00000134909.
ENST00000527272; ENSP00000432862; ENSG00000134909.

GeneID

9743.

KEGG

hsa:9743.

UCSC

uc001qez.3. human.

Organism-specific databases

CTD

9743.

GeneCards

GC11M128834.

H-InvDB

HIX0010264.

HGNC

HGNC:17399. ARHGAP32.

HPA

HPA038389.

MIM

608541. gene.

neXtProt

NX_A7KAX9.

PharmGKB

PA165543138.

HUGE

Search...

GenAtlas

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Phylogenomic databases

eggNOG

NOG311367.

HOGENOM

HOG000090208.

HOVERGEN

HBG108407.

InParanoid

A7KAX9.

OMA

VVSQYDN.

OrthoDB

EOG46MBHP.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

A7KAX9.

Bgee

A7KAX9.

Genevestigator

A7KAX9.

Family and domain databases

Gene3D

1.10.555.10. 1 hit.
3.30.1520.10. 1 hit.

InterPro

IPR001683. Phox.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00787. PX. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

SMART

SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF64268. PX. 1 hit.
SSF48350. Rho_GAP. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50195. PX. False negative.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ARHGAP32. human.

EvolutionaryTrace

A7KAX9.

GenomeRNAi

9743.

NextBio

36663.

SOURCE

Search...

Entry information

Entry name

RHG32_HUMAN

Accession

Primary (citable) accession number: A7KAX9
Secondary accession number(s): O94820 , Q86YL6, Q8IUG4, Q9BWG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	September 11, 2007
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 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.