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Q9BRR9

- RHG09_HUMAN

UniProt

Q9BRR9 - RHG09_HUMAN

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Protein

Rho GTPase-activating protein 9

Gene
ARHGAP9
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. GTPase activator activity Source: MGI
  2. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB

GO - Biological processi

  1. positive regulation of GTPase activity Source: GOC
  2. regulation of small GTPase mediated signal transduction Source: Reactome
  3. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
SignaLinkiQ9BRR9.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 9
Alternative name(s):
Rho-type GTPase-activating protein 9
Gene namesi
Name:ARHGAP9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:14130. ARHGAP9.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi343 – 3431K → A: Strongly reduced affinity for phosphoinositides. 1 Publication
Mutagenesisi399 – 3991R → A: Reduced affinity for phosphoinositides. 1 Publication

Organism-specific databases

PharmGKBiPA24962.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 750750Rho GTPase-activating protein 9PRO_0000056712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei475 – 4751Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BRR9.
PaxDbiQ9BRR9.
PRIDEiQ9BRR9.

PTM databases

PhosphoSiteiQ9BRR9.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9BRR9.
BgeeiQ9BRR9.
CleanExiHS_ARHGAP9.
GenevestigatoriQ9BRR9.

Organism-specific databases

HPAiHPA051447.

Interactioni

Subunit structurei

Interacts with FASLG.1 Publication

Protein-protein interaction databases

BioGridi122140. 8 interactions.
IntActiQ9BRR9. 8 interactions.
MINTiMINT-1190172.
STRINGi9606.ENSP00000377380.

Structurei

Secondary structure

1
750
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi322 – 33615
Beta strandi346 – 36116
Helixi368 – 3703
Beta strandi380 – 3845
Beta strandi389 – 3924
Turni394 – 3963
Beta strandi398 – 4069
Beta strandi412 – 4165
Helixi420 – 43920

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P0DX-ray1.81A321-440[»]
2P0FX-ray1.91A321-440[»]
2P0HX-ray1.90A321-440[»]
ProteinModelPortaliQ9BRR9.
SMRiQ9BRR9. Positions 26-86, 321-438, 523-749.

Miscellaneous databases

EvolutionaryTraceiQ9BRR9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 8867SH3Add
BLAST
Domaini213 – 24735WWAdd
BLAST
Domaini322 – 435114PHAdd
BLAST
Domaini542 – 749208Rho-GAPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni342 – 3454Lipid binding
Regioni397 – 3993Lipid binding
Regioni432 – 669238Lipid bindingAdd
BLAST

Domaini

A region including the PH domain and partially overlapping with the Rho-GAP domain mediates interaction with phosphoinositides.1 Publication

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 Rho-GAP domain.
Contains 1 SH3 domain.
Contains 1 WW domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG279563.
HOGENOMiHOG000294167.
HOVERGENiHBG005328.
InParanoidiQ9BRR9.
OrthoDBiEOG7CZK7R.
PhylomeDBiQ9BRR9.
TreeFamiTF329345.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR015767. Rho_GTPase_act.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
IPR001202. WW_dom.
[Graphical view]
PANTHERiPTHR23181. PTHR23181. 1 hit.
PfamiPF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51045. SSF51045. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BRR9-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MLSSRWWPSS WGILGLGPRS PPRGSQLCAL YAFTYTGADG QQVSLAEGDR    50
FLLLRKTNSD WWLARRLEAP STSRPIFVPA AYMIEESIPS QSPTTVIPGQ 100
LLWTPGPKLF HGSLEELSQA LPSRAQASSE QPPPLPRKMC RSVSTDNLSP 150
SLLKPFQEGP SGRSLSQEDL PSEASASTAG PQPLMSEPPV YCNLVDLRRC 200
PRSPPPGPAC PLLQRLDAWE QHLDPNSGRC FYINSLTGCK SWKPPRRSRS 250
ETNPGSMEGT QTLKRNNDVL QPQAKGFRSD TGTPEPLDPQ GSLSLSQRTS 300
QLDPPALQAP RPLPQLLDDP HEVEKSGLLN MTKIAQGGRK LRKNWGPSWV 350
VLTGNSLVFY REPPPTAPSS GWGPAGSRPE SSVDLRGAAL AHGRHLSSRR 400
NVLHIRTIPG HEFLLQSDHE TELRAWHRAL RTVIERLVRW VEARREAPTG 450
RDQGSGDREN PLELRLSGSG PAELSAGEDE EEESELVSKP LLRLSSRRSS 500
IRGPEGTEQN RVRNKLKRLI AKRPPLQSLQ ERGLLRDQVF GCQLESLCQR 550
EGDTVPSFLR LCIAAVDKRG LDVDGIYRVS GNLAVVQKLR FLVDRERAVT 600
SDGRYVFPEQ PGQEGRLDLD STEWDDIHVV TGALKLFLRE LPQPLVPPLL 650
LPHFRAALAL SESEQCLSQI QELIGSMPKP NHDTLRYLLE HLCRVIAHSD 700
KNRMTPHNLG IVFGPTLFRP EQETSDPAAH ALYPGQLVQL MLTNFTSLFP 750
Length:750
Mass (Da):83,260
Last modified:May 10, 2004 - v2
Checksum:i7E769DBC3678DB49
GO
Isoform 2 (identifier: Q9BRR9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     438-456: Missing.

Show »
Length:731
Mass (Da):81,150
Checksum:iB63901EACA109D02
GO
Isoform 3 (identifier: Q9BRR9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-184: Missing.

Show »
Length:566
Mass (Da):63,292
Checksum:i68FC77CAF2B9321E
GO
Isoform 4 (identifier: Q9BRR9-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-184: Missing.
     438-456: Missing.

Show »
Length:547
Mass (Da):61,183
Checksum:iBA337CC08F1B433B
GO
Isoform 5 (identifier: Q9BRR9-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:640
Mass (Da):70,869
Checksum:i163BA91817EE36F2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501R → G.
Corresponds to variant rs33927108 [ dbSNP | Ensembl ].
VAR_055830
Natural varianti137 – 1371R → C.
Corresponds to variant rs3802989 [ dbSNP | Ensembl ].
VAR_055831
Natural varianti370 – 3701S → A.2 Publications
Corresponds to variant rs11544238 [ dbSNP | Ensembl ].
VAR_055832

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 184184Missing in isoform 3 and isoform 4. VSP_010340Add
BLAST
Alternative sequencei438 – 45619Missing in isoform 2, isoform 4 and isoform 5. VSP_010325Add
BLAST
Alternative sequencei659 – 75092ALSES…TSLFP → G in isoform 5. VSP_046391Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521L → F in AAH06107. 1 Publication
Sequence conflicti195 – 1951V → A in BAC03969. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS44928.1. [Q9BRR9-4]
CCDS44929.1. [Q9BRR9-5]
CCDS8941.2. [Q9BRR9-2]
PIRiJC7701.
RefSeqiNP_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]
UniGeneiHs.437126.

Genome annotation databases

EnsembliENST00000356411; ENSP00000348782; ENSG00000123329. [Q9BRR9-1]
ENST00000393791; ENSP00000377380; ENSG00000123329. [Q9BRR9-2]
ENST00000424809; ENSP00000394307; ENSG00000123329. [Q9BRR9-5]
ENST00000430041; ENSP00000397950; ENSG00000123329. [Q9BRR9-4]
GeneIDi64333.
KEGGihsa:64333.
UCSCiuc001snz.3. human. [Q9BRR9-4]
uc001soa.3. human. [Q9BRR9-1]
uc001soc.3. human. [Q9BRR9-2]

Polymorphism databases

DMDMi47117294.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS44928.1. [Q9BRR9-4 ]
CCDS44929.1. [Q9BRR9-5 ]
CCDS8941.2. [Q9BRR9-2 ]
PIRi JC7701.
RefSeqi NP_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 ]
UniGenei Hs.437126.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P0D X-ray 1.81 A 321-440 [» ]
2P0F X-ray 1.91 A 321-440 [» ]
2P0H X-ray 1.90 A 321-440 [» ]
ProteinModelPortali Q9BRR9.
SMRi Q9BRR9. Positions 26-86, 321-438, 523-749.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122140. 8 interactions.
IntActi Q9BRR9. 8 interactions.
MINTi MINT-1190172.
STRINGi 9606.ENSP00000377380.

PTM databases

PhosphoSitei Q9BRR9.

Polymorphism databases

DMDMi 47117294.

Proteomic databases

MaxQBi Q9BRR9.
PaxDbi Q9BRR9.
PRIDEi Q9BRR9.

Protocols and materials databases

DNASUi 64333.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356411 ; ENSP00000348782 ; ENSG00000123329 . [Q9BRR9-1 ]
ENST00000393791 ; ENSP00000377380 ; ENSG00000123329 . [Q9BRR9-2 ]
ENST00000424809 ; ENSP00000394307 ; ENSG00000123329 . [Q9BRR9-5 ]
ENST00000430041 ; ENSP00000397950 ; ENSG00000123329 . [Q9BRR9-4 ]
GeneIDi 64333.
KEGGi hsa:64333.
UCSCi uc001snz.3. human. [Q9BRR9-4 ]
uc001soa.3. human. [Q9BRR9-1 ]
uc001soc.3. human. [Q9BRR9-2 ]

Organism-specific databases

CTDi 64333.
GeneCardsi GC12M057866.
H-InvDB HIX0010768.
HGNCi HGNC:14130. ARHGAP9.
HPAi HPA051447.
MIMi 610576. gene.
neXtProti NX_Q9BRR9.
PharmGKBi PA24962.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279563.
HOGENOMi HOG000294167.
HOVERGENi HBG005328.
InParanoidi Q9BRR9.
OrthoDBi EOG7CZK7R.
PhylomeDBi Q9BRR9.
TreeFami TF329345.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.
SignaLinki Q9BRR9.

Miscellaneous databases

ChiTaRSi ARHGAP9. human.
EvolutionaryTracei Q9BRR9.
GeneWikii ARHGAP9.
GenomeRNAii 64333.
NextBioi 66267.
PROi Q9BRR9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BRR9.
Bgeei Q9BRR9.
CleanExi HS_ARHGAP9.
Genevestigatori Q9BRR9.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR015767. Rho_GTPase_act.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001452. SH3_domain.
IPR001202. WW_dom.
[Graphical view ]
PANTHERi PTHR23181. PTHR23181. 1 hit.
Pfami PF00169. PH. 1 hit.
PF00620. RhoGAP. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00324. RhoGAP. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51045. SSF51045. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50238. RHOGAP. 1 hit.
PS50002. SH3. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiRHG09_HUMAN
AccessioniPrimary (citable) accession number: Q9BRR9
Secondary accession number(s): B4DVI3
, E9PDX9, Q8NAF3, Q8TCJ3, Q8WYR0, Q96EZ2, Q96S74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: September 3, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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