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Q9BRR9

- RHG09_HUMAN

UniProt

Q9BRR9 - RHG09_HUMAN

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
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BRR9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 8867SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini213 – 24735WWPROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 435114PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini542 – 749208Rho-GAPPROSITE-ProRule annotationAdd
    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.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation
    Contains 1 WW domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti152 – 1521L → F in AAH06107. 1 PublicationCurated
    Sequence conflicti195 – 1951V → A in BAC03969. (PubMed:14702039)Curated

    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. 2 PublicationsVSP_010340Add
    BLAST
    Alternative sequencei438 – 45619Missing in isoform 2, isoform 4 and isoform 5. 4 PublicationsVSP_010325Add
    BLAST
    Alternative sequencei659 – 75092ALSES…TSLFP → G in isoform 5. 1 PublicationVSP_046391Add
    BLAST

    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

    EnsembliENST00000393791; 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 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

    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: October 1, 2014
    This is version 120 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