Reviewed, UniProtKB/Swiss-Prot Q13017 (RHG05_HUMAN)

Names and origin

Protein names

Recommended name:
    Rho GTPase-activating protein 5
Alternative name(s):
    Rho-type GTPase-activating protein 5
    p190-B

Gene names

Name:	ARHGAP5
Synonyms:	RHOGAP5

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1502 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	GTPase-activating protein for Rho family members. May play a role in the reduction of the p21rasGTPase-activating potential of p120GAP.
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Note: Also membrane-associated when found in fibrillar patterns that colocalize with the alpha5-beta1 integrin receptor (ITGA5/ITGB1) for fibronectin.
Tissue specificity	Expressed in kidney, brain, liver and lung.
Sequence similarities	Contains 4 FF domains. Contains 1 Rho-GAP domain.
Sequence caution	The sequence AAA95963.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAH32723.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	GTPase activation
PTM	Nitration Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	Rho protein signal transduction Ref.1 Traceable author statement. Source: ProtInc cell adhesion Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Ref.1 Traceable author statement. Source: ProtInc extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: InterPro GTPase activity Ref.1 Traceable author statement. Source: ProtInc Rho GTPase activator activity Ref.1 Traceable author statement. Source: ProtInc SH2 domain binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13017-1)

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: Q13017-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1240-1240: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q13017-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1265: Missing.
     1266-1288: DLVTAEKPIPLFVEKCVEFIEDT → MSLPPPPPGPLPLRRRRRRPTLL

Note: No experimental confirmation available.

Isoform 4 (identifier: Q13017-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1261: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1502

1502

Rho GTPase-activating protein 5

PRO_0000056702

Regions

Domain

269 – 325

57

FF 1

Domain

365 – 420

56

FF 2

Domain

427 – 482

56

FF 3

Domain

483 – 537

55

FF 4

Domain

1262 – 1449

188

Rho-GAP

Compositional bias

1225 – 1245

21

Lys-rich

Amino acid modifications

Modified residue

550

1

Nitrated tyrosine

Modified residue

765

1

Phosphoserine Ref.6

Modified residue

968

1

Phosphoserine Ref.7

Modified residue

1109

1

Phosphotyrosine Ref.10

Modified residue

1115

1

Phosphoserine Ref.7

Modified residue

1124

1

Phosphoserine Ref.7

Modified residue

1129

1

Phosphothreonine Ref.7

Modified residue

1138

1

Phosphoserine Ref.7

Modified residue

1173

1

Phosphoserine Ref.7

Modified residue

1176

1

Phosphoserine Ref.7

Modified residue

1195

1

Phosphoserine Ref.7

Modified residue

1202

1

Phosphoserine Ref.6 Ref.7

Modified residue

1218

1

Phosphoserine Ref.7

Natural variations

Alternative sequence

1 – 1265

1265

Missing in isoform 3.

VSP_034164

Alternative sequence

1 – 1261

1261

Missing in isoform 4.

VSP_034165

Alternative sequence

1240

1

Missing in isoform 2.

VSP_034166

Alternative sequence

1266 – 1288

23

DLVTA…FIEDT → MSLPPPPPGPLPLRRRRRRP TLL in isoform 3.

VSP_034167

Natural variant

17

1

I → V: dbSNP rs17386818.

VAR_043980

Experimental info

Sequence conflict

80

1

Q → R in AAH50059. Ref.2

Sequence conflict

80

1

Q → R in BAD92988. Ref.4

Sequence conflict

409

1

E → G in BAF85655. Ref.3

Sequence conflict

541

1

L → F in BAD92988. Ref.4

Sequence conflict

620

1

D → G in BAF85655. Ref.3

Sequence conflict

1383

1

D → G in AAH50059. Ref.2

Secondary structure

1

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1502

Helix Strand Turn

Details...

Beta strand

1258 – 1262

5

Helix

1264 – 1267

4

Helix

1276 – 1287

12

Turn

1293 – 1297

5

Helix

1302 – 1314

13

Helix

1320 – 1323

4

Helix

1327 – 1340

14

Beta strand

1341 – 1343

3

Turn

1348 – 1350

3

Helix

1351 – 1358

8

Helix

1363 – 1373

11

Turn

1374 – 1376

3

Helix

1381 – 1397

17

Helix

1399 – 1402

4

Helix

1406 – 1417

12

Helix

1434 – 1443

10

Helix

1445 – 1448

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 10, 2008. Version 2. Checksum: 2E01B5B1D007984D	FASTA	1,502	172,460
	10 20 30 40 50 60 MMAKNKEPRP PSYTISIVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY PEHTSVLSTI 70 80 90 100 110 120 DFGGRVVNND HFLYWGDIIQ NSEDGVECKI HVIEQTEFID DQTFLPHRST NLQPYIKRAA 130 140 150 160 170 180 ASKLQSAEKL MYICTDQLGL EQDFEQKQMP EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV 190 200 210 220 230 240 NNLFVQLSKS KKPVIIAATK CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFT 250 260 270 280 290 300 ALVQMLDKTR SKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH 310 320 330 340 350 360 PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIN TLPRAFNTLL PNLEEIEHLN 370 380 390 400 410 420 WSEALKLMEK RADFQLCFVV LEKTPWDETD HIDKINDRRI PFDLLSTLEA EKVYQNHVQH 430 440 450 460 470 480 LISEKRRVEM KEKFKKTLEK IQFISPGQPW EEVMCFVMED EAYKYITEAD SKEVYGRHQR 490 500 510 520 530 540 EIVEKAKEEF QEMLFEHSEL FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES 550 560 570 580 590 600 LLLKHIGFVY HPTKETCLSG QNCTDIKVEQ LLASSLLQLD HGRLRLYHDS TNIDKVNLFI 610 620 630 640 650 660 LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYFLSQLWT AAFKPHGCFC 670 680 690 700 710 720 VFNSIESLSF IGEFIGKIRT EASQIRKDKY MANLPFTLIL ANQRDSISKN LPILRHQGQQ 730 740 750 760 770 780 LANKLQCPFV DVPAGTYPRK FNETQIKQAL RGVLESVKHN LDVVSPIPAN KDLSEADLRI 790 800 810 820 830 840 VMCAMCGDPF SVDLILSPFL DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI 850 860 870 880 890 900 GVRKDELVHG YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL 910 920 930 940 950 960 MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL SDNTRESTHQ 970 980 990 1000 1010 1020 SEDVFLPSPR DCFPYNNYPD SDDDTEAPPP YSPIGDDVQL LPTPSDRSRY RLDLEGNEYP 1030 1040 1050 1060 1070 1080 IHSTPNCHDH ERNHKVPPPI KPKPVVPKTN VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA 1090 1100 1110 1120 1130 1140 HPEDMDPSDN YAEPIDTIFK QKGYSDEIYV VPDDSQNRIK IRNSFVNNTQ GDEENGFSDR 1150 1160 1170 1180 1190 1200 TSKSHGERRP SKYKYKSKTL FSKAKSYYRR THSDASDDEA FTTSKTKRKG RHRGSEEDPL 1210 1220 1230 1240 1250 1260 LSPVETWKGG IDNPAITSDQ ELDDKKMKKK THKVKEDKKQ KKKTKNFNPP TRRNWESNYF 1270 1280 1290 1300 1310 1320 GMPLQDLVTA EKPIPLFVEK CVEFIEDTGL CTEGLYRVSG NKTDQDNIQK QFDQDHNINL 1330 1340 1350 1360 1370 1380 VSMEVTVNAV AGALKAFFAD LPDPLIPYSL HPELLEAAKI PDKTERLHAL KEIVKKFHPV 1390 1400 1410 1420 1430 1440 NYDVFRYVIT HLNRVSQQHK INLMTADNLS ICFWPTLMRP DFENREFLST TKIHQSVVET 1450 1460 1470 1480 1490 1500 FIQQCQFFFY NGEIVETTNI VAPPPPSNPG QLVEPMVPLQ LPPPLQPQLI QPQLQTDPLG II
	Isoform 2. Checksum: 801C2D39400ACA51	FASTA	1,501	172,332
	10 20 30 40 50 60 MMAKNKEPRP PSYTISIVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY PEHTSVLSTI 70 80 90 100 110 120 DFGGRVVNND HFLYWGDIIQ NSEDGVECKI HVIEQTEFID DQTFLPHRST NLQPYIKRAA 130 140 150 160 170 180 ASKLQSAEKL MYICTDQLGL EQDFEQKQMP EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV 190 200 210 220 230 240 NNLFVQLSKS KKPVIIAATK CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFT 250 260 270 280 290 300 ALVQMLDKTR SKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH 310 320 330 340 350 360 PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIN TLPRAFNTLL PNLEEIEHLN 370 380 390 400 410 420 WSEALKLMEK RADFQLCFVV LEKTPWDETD HIDKINDRRI PFDLLSTLEA EKVYQNHVQH 430 440 450 460 470 480 LISEKRRVEM KEKFKKTLEK IQFISPGQPW EEVMCFVMED EAYKYITEAD SKEVYGRHQR 490 500 510 520 530 540 EIVEKAKEEF QEMLFEHSEL FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES 550 560 570 580 590 600 LLLKHIGFVY HPTKETCLSG QNCTDIKVEQ LLASSLLQLD HGRLRLYHDS TNIDKVNLFI 610 620 630 640 650 660 LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYFLSQLWT AAFKPHGCFC 670 680 690 700 710 720 VFNSIESLSF IGEFIGKIRT EASQIRKDKY MANLPFTLIL ANQRDSISKN LPILRHQGQQ 730 740 750 760 770 780 LANKLQCPFV DVPAGTYPRK FNETQIKQAL RGVLESVKHN LDVVSPIPAN KDLSEADLRI 790 800 810 820 830 840 VMCAMCGDPF SVDLILSPFL DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI 850 860 870 880 890 900 GVRKDELVHG YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL 910 920 930 940 950 960 MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL SDNTRESTHQ 970 980 990 1000 1010 1020 SEDVFLPSPR DCFPYNNYPD SDDDTEAPPP YSPIGDDVQL LPTPSDRSRY RLDLEGNEYP 1030 1040 1050 1060 1070 1080 IHSTPNCHDH ERNHKVPPPI KPKPVVPKTN VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA 1090 1100 1110 1120 1130 1140 HPEDMDPSDN YAEPIDTIFK QKGYSDEIYV VPDDSQNRIK IRNSFVNNTQ GDEENGFSDR 1150 1160 1170 1180 1190 1200 TSKSHGERRP SKYKYKSKTL FSKAKSYYRR THSDASDDEA FTTSKTKRKG RHRGSEEDPL 1210 1220 1230 1240 1250 1260 LSPVETWKGG IDNPAITSDQ ELDDKKMKKK THKVKEDKKK KKTKNFNPPT RRNWESNYFG 1270 1280 1290 1300 1310 1320 MPLQDLVTAE KPIPLFVEKC VEFIEDTGLC TEGLYRVSGN KTDQDNIQKQ FDQDHNINLV 1330 1340 1350 1360 1370 1380 SMEVTVNAVA GALKAFFADL PDPLIPYSLH PELLEAAKIP DKTERLHALK EIVKKFHPVN 1390 1400 1410 1420 1430 1440 YDVFRYVITH LNRVSQQHKI NLMTADNLSI CFWPTLMRPD FENREFLSTT KIHQSVVETF 1450 1460 1470 1480 1490 1500 IQQCQFFFYN GEIVETTNIV APPPPSNPGQ LVEPMVPLQL PPPLQPQLIQ PQLQTDPLGI I
	Isoform 3. Checksum: C5044B056AC7297A	FASTA	237	26,979
	10 20 30 40 50 60 MSLPPPPPGP LPLRRRRRRP TLLGLCTEGL YRVSGNKTDQ DNIQKQFDQD HNINLVSMEV 70 80 90 100 110 120 TVNAVAGALK AFFADLPDPL IPYSLHPELL EAAKIPDKTE RLHALKEIVK KFHPVNYDVF 130 140 150 160 170 180 RYVITHLNRV SQQHKINLMT ADNLSICFWP TLMRPDFENR EFLSTTKIHQ SVVETFIQQC 190 200 210 220 230 QFFFYNGEIV ETTNIVAPPP PSNPGQLVEP MVPLQLPPPL QPQLIQPQLQ TDPLGII
	Isoform 4. Checksum: 63966DC0890DDB5E	FASTA	241	27,411
	10 20 30 40 50 60 MPLQDLVTAE KPIPLFVEKC VEFIEDTGLC TEGLYRVSGN KTDQDNIQKQ FDQDHNINLV 70 80 90 100 110 120 SMEVTVNAVA GALKAFFADL PDPLIPYSLH PELLEAAKIP DKTERLHALK EIVKKFHPVN 130 140 150 160 170 180 YDVFRYVITH LNRVSQQHKI NLMTADNLSI CFWPTLMRPD FENREFLSTT KIHQSVVETF 190 200 210 220 230 240 IQQCQFFFYN GEIVETTNIV APPPPSNPGQ LVEPMVPLQL PPPLQPQLIQ PQLQTDPLGI I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking." Burbelo P.D., Miyamoto S., Utani A., Brill S., Yamada K.M., Hall A., Yamada Y. J. Biol. Chem. 270:30919-30926(1995) [PubMed: 8537347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Mesangial cell.
[2]	"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; 3 AND 4). Tissue: Brain, Testis and Uterus.
[3]	"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] OF 1-1239 (ISOFORM 1). Tissue: Trachea.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 364-1499 (ISOFORM 2). Tissue: Brain.
[5]	"Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry." Zhan X., Desiderio D.M. Anal. Biochem. 354:279-289(2006) [PubMed: 16777052] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-550, MASS SPECTROMETRY. Tissue: Pituitary adenoma.
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765 AND SER-1202, MASS SPECTROMETRY.
[7]	"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-968; SER-1115; SER-1124; THR-1129; SER-1138; SER-1173; SER-1176; SER-1195; SER-1202 AND SER-1218, MASS SPECTROMETRY.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"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-1218, MASS SPECTROMETRY.
[10]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1109, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195 AND SER-1202, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"Solution structure of the N-terminus extended RhoGAP domain from human Rho GTPase activating protein 5 variant." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1245-1456.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U17032 mRNA. Translation: AAA95963.1. Frameshift.
BC032723 mRNA. Translation: AAH32723.1. Sequence problems.
BC050059 mRNA. Translation: AAH50059.1.
BC075799 mRNA. Translation: AAH75799.1.
BC129928 mRNA. Translation: AAI29929.1.
BC129929 mRNA. Translation: AAI29930.1.
AK292966 mRNA. Translation: BAF85655.1.
AB209751 mRNA. Translation: BAD92988.1.

IPI

IPI00013988.
IPI00646885.
IPI00744108.
IPI00895772.

PIR

B59431.

RefSeq

NP_001025226.1.
NP_001164.2.

UniGene

Hs.592313

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EE4	NMR	-	A	1255-1456	[»]
2EE5	NMR	-	A	1245-1456	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q13017.

PTM databases

PhosphoSite

Q13017.

Proteomic databases

PRIDE

Q13017.

Genome annotation databases

Ensembl

ENST00000345122; ENSP00000371897; ENSG00000100852; Homo sapiens. [Genome view]

GeneID

394.

KEGG

hsa:394.

UCSC

uc001wrl.1. human.
uc001wrm.1. human.
uc001wro.1. human.
uc001wrp.1. human.

Organism-specific databases

CTD

394.

GeneCards

GC14P031615.

H-InvDB

HIX0011585.

HGNC

HGNC:675. ARHGAP5.

MIM

602680. gene.

PharmGKB

PA24959.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q13017.

InParanoid

Q13017.

OMA

KTRGKPK.

OrthoDB

EOG9H74X3.

Enzyme and pathway databases

Reactome

REACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpress

Q13017.

Bgee

Q13017.

CleanEx

HS_ARHGAP5.

Genevestigator

Q13017.

GermOnline

ENSG00000100852. Homo sapiens.

Family and domain databases

InterPro

IPR002713. FF_domain.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP.
[Graphical view]

Gene3D

G3DSA:1.10.555.10. RhoGAP. 1 hit.

Pfam

PF01846. FF. 2 hits.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]

PROSITE

PS50238. RHOGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

1643.

PMAP-CutDB

Q13017.

SOURCE

Search...

Entry information

Entry name

RHG05_HUMAN

Accession

Primary (citable) accession number: Q13017
Secondary accession number(s): A1L375 , A1L376, A8KAA1, Q05BE8, Q05BU8, Q59ER0, Q6DHZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	June 10, 2008
Last modified:	December 15, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.