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Q9BRR9 (RHG09_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho GTPase-activating protein 9
Alternative name(s):
Rho-type GTPase-activating protein 9
Gene names
Name:ARHGAP9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length750 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has a substantial GAP activity toward CDC42 and RAC1 and less toward RHOA. Has a role in regulating adhesion of hematopoietic cells to the extracellular matrix. Binds phosphoinositides, and has the highest affinity for phosphatidylinositol 3,4,5-trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate. Ref.1

Subunit structure

Interacts with FASLG. Ref.7

Tissue specificity

Predominantly expressed in peripheral blood leukocytes, spleen, and thymus. Ref.1

Domain

A region including the PH domain and partially overlapping with the Rho-GAP domain mediates interaction with phosphoinositides. Ref.9

Sequence similarities

Contains 1 PH domain.

Contains 1 Rho-GAP domain.

Contains 1 SH3 domain.

Contains 1 WW domain.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BRR9-1)

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: Q9BRR9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     438-456: Missing.
Isoform 3 (identifier: Q9BRR9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-184: Missing.
Isoform 4 (identifier: Q9BRR9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-184: Missing.
     438-456: Missing.
Isoform 5 (identifier: Q9BRR9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     438-456: Missing.
     659-750: ALSESEQCLS...MLTNFTSLFP → G
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 750750Rho GTPase-activating protein 9
PRO_0000056712

Regions

Domain22 – 8867SH3
Domain213 – 24735WW
Domain322 – 435114PH
Domain542 – 749208Rho-GAP
Region342 – 3454Lipid binding
Region397 – 3993Lipid binding
Region432 – 669238Lipid binding

Amino acid modifications

Modified residue4751Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 184184Missing in isoform 3 and isoform 4.
VSP_010340
Alternative sequence438 – 45619Missing in isoform 2, isoform 4 and isoform 5.
VSP_010325
Alternative sequence659 – 75092ALSES…TSLFP → G in isoform 5.
VSP_046391
Natural variant501R → G.
Corresponds to variant rs33927108 [ dbSNP | Ensembl ].
VAR_055830
Natural variant1371R → C.
Corresponds to variant rs3802989 [ dbSNP | Ensembl ].
VAR_055831
Natural variant3701S → A. Ref.3 Ref.5
Corresponds to variant rs11544238 [ dbSNP | Ensembl ].
VAR_055832

Experimental info

Mutagenesis3431K → A: Strongly reduced affinity for phosphoinositides. Ref.9
Mutagenesis3991R → A: Reduced affinity for phosphoinositides. Ref.9
Sequence conflict1521L → F in AAH06107. Ref.2
Sequence conflict1951V → A in BAC03969. Ref.3

Secondary structure

................... 750
Helix Strand Turn

Details...

Sequences

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

Last modified May 10, 2004. Version 2.
Checksum: 7E769DBC3678DB49

FASTA75083,260
        10         20         30         40         50         60 
MLSSRWWPSS WGILGLGPRS PPRGSQLCAL YAFTYTGADG QQVSLAEGDR FLLLRKTNSD 

        70         80         90        100        110        120 
WWLARRLEAP STSRPIFVPA AYMIEESIPS QSPTTVIPGQ LLWTPGPKLF HGSLEELSQA 

       130        140        150        160        170        180 
LPSRAQASSE QPPPLPRKMC RSVSTDNLSP SLLKPFQEGP SGRSLSQEDL PSEASASTAG 

       190        200        210        220        230        240 
PQPLMSEPPV YCNLVDLRRC PRSPPPGPAC PLLQRLDAWE QHLDPNSGRC FYINSLTGCK 

       250        260        270        280        290        300 
SWKPPRRSRS ETNPGSMEGT QTLKRNNDVL QPQAKGFRSD TGTPEPLDPQ GSLSLSQRTS 

       310        320        330        340        350        360 
QLDPPALQAP RPLPQLLDDP HEVEKSGLLN MTKIAQGGRK LRKNWGPSWV VLTGNSLVFY 

       370        380        390        400        410        420 
REPPPTAPSS GWGPAGSRPE SSVDLRGAAL AHGRHLSSRR NVLHIRTIPG HEFLLQSDHE 

       430        440        450        460        470        480 
TELRAWHRAL RTVIERLVRW VEARREAPTG RDQGSGDREN PLELRLSGSG PAELSAGEDE 

       490        500        510        520        530        540 
EEESELVSKP LLRLSSRRSS IRGPEGTEQN RVRNKLKRLI AKRPPLQSLQ ERGLLRDQVF 

       550        560        570        580        590        600 
GCQLESLCQR EGDTVPSFLR LCIAAVDKRG LDVDGIYRVS GNLAVVQKLR FLVDRERAVT 

       610        620        630        640        650        660 
SDGRYVFPEQ PGQEGRLDLD STEWDDIHVV TGALKLFLRE LPQPLVPPLL LPHFRAALAL 

       670        680        690        700        710        720 
SESEQCLSQI QELIGSMPKP NHDTLRYLLE HLCRVIAHSD KNRMTPHNLG IVFGPTLFRP 

       730        740        750 
EQETSDPAAH ALYPGQLVQL MLTNFTSLFP 

« Hide

Isoform 2 [UniParc].

Checksum: B63901EACA109D02
Show »

FASTA73181,150
Isoform 3 [UniParc].

Checksum: 68FC77CAF2B9321E
Show »

FASTA56663,292
Isoform 4 [UniParc].

Checksum: BA337CC08F1B433B
Show »

FASTA54761,183
Isoform 5 [UniParc].

Checksum: 163BA91817EE36F2
Show »

FASTA64070,869

References

« Hide 'large scale' references
[1]"Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase activating protein."
Furukawa Y., Kawasoe T., Daigo Y., Nishiwaki T., Ishiguro H., Takahashi M., Kitayama J., Nakamura Y.
Biochem. Biophys. Res. Commun. 284:643-649(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
[2]"Isolation, mapping, and characterization of a novel member of human rho-GAP family."
Kawasoe T., Furukawa Y., Daigo Y., Nishiwaki T., Ishiguro H., Fujita M., Ogawa M., Nakamura Y.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), VARIANT ALA-370.
Tissue: Small intestine and Spleen.
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-370.
Tissue: Lymph and Muscle.
[6]"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] OF 384-750 (ISOFORM 2).
Tissue: Lymph node.
[7]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[8]"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-475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9."
Ceccarelli D.F., Blasutig I.M., Goudreault M., Li Z., Ruston J., Pawson T., Sicheri F.
J. Biol. Chem. 282:13864-13874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 321-440 IN COMPLEXES WITH PHOSPHATIDYLINOSITOL 1,4,5-TRISPHOSPHATE AND PHOSPHATIDYLINOSITOL 1,3,4-TRISPHOSPHATE, DOMAIN, MUTAGENESIS OF LYS-343 AND ARG-399, LIPID-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB051853 mRNA. Translation: BAB56159.1.
AB030239 mRNA. Translation: BAB83128.1.
AK092763 mRNA. Translation: BAC03969.1.
AK301095 mRNA. Translation: BAG62695.1.
AC022506 Genomic DNA. No translation available.
BC006107 mRNA. Translation: AAH06107.1.
BC011820 mRNA. Translation: AAH11820.1.
AL713803 mRNA. Translation: CAD28552.1.
CCDSCCDS44928.1. [Q9BRR9-4]
CCDS44929.1. [Q9BRR9-5]
CCDS8941.2. [Q9BRR9-2]
PIRJC7701.
RefSeqNP_001073625.1. NM_001080156.1. [Q9BRR9-4]
NP_001073626.1. NM_001080157.1. [Q9BRR9-5]
NP_115885.2. NM_032496.2. [Q9BRR9-2]
XP_005269139.1. XM_005269082.1. [Q9BRR9-3]
XP_005269140.1. XM_005269083.1. [Q9BRR9-3]
XP_006719623.1. XM_006719560.1. [Q9BRR9-1]
UniGeneHs.437126.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P0DX-ray1.81A321-440[»]
2P0FX-ray1.91A321-440[»]
2P0HX-ray1.90A321-440[»]
ProteinModelPortalQ9BRR9.
SMRQ9BRR9. Positions 26-86, 321-438, 523-749.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122140. 8 interactions.
IntActQ9BRR9. 8 interactions.
MINTMINT-1190172.
STRING9606.ENSP00000377380.

PTM databases

PhosphoSiteQ9BRR9.

Polymorphism databases

DMDM47117294.

Proteomic databases

MaxQBQ9BRR9.
PaxDbQ9BRR9.
PRIDEQ9BRR9.

Protocols and materials databases

DNASU64333.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356411; ENSP00000348782; ENSG00000123329. [Q9BRR9-1]
ENST00000393791; ENSP00000377380; ENSG00000123329. [Q9BRR9-2]
ENST00000424809; ENSP00000394307; ENSG00000123329. [Q9BRR9-5]
ENST00000430041; ENSP00000397950; ENSG00000123329. [Q9BRR9-4]
GeneID64333.
KEGGhsa:64333.
UCSCuc001snz.3. human. [Q9BRR9-4]
uc001soa.3. human. [Q9BRR9-1]
uc001soc.3. human. [Q9BRR9-2]

Organism-specific databases

CTD64333.
GeneCardsGC12M057866.
H-InvDBHIX0010768.
HGNCHGNC:14130. ARHGAP9.
HPAHPA051447.
MIM610576. gene.
neXtProtNX_Q9BRR9.
PharmGKBPA24962.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279563.
HOGENOMHOG000294167.
HOVERGENHBG005328.
InParanoidQ9BRR9.
OrthoDBEOG7CZK7R.
PhylomeDBQ9BRR9.
TreeFamTF329345.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ9BRR9.

Gene expression databases

ArrayExpressQ9BRR9.
BgeeQ9BRR9.
CleanExHS_ARHGAP9.
GenevestigatorQ9BRR9.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR015767. Rho_GTPase_act.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
IPR001202. WW_dom.
[Graphical view]
PANTHERPTHR23181. PTHR23181. 1 hit.
PfamPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51045. SSF51045. 1 hit.
PROSITEPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGAP9. human.
EvolutionaryTraceQ9BRR9.
GeneWikiARHGAP9.
GenomeRNAi64333.
NextBio66267.
PROQ9BRR9.
SOURCESearch...

Entry information

Entry nameRHG09_HUMAN
AccessionPrimary (citable) accession number: Q9BRR9
Secondary accession number(s): B4DVI3 expand/collapse secondary AC list , E9PDX9, Q8NAF3, Q8TCJ3, Q8WYR0, Q96EZ2, Q96S74
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM