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Q9NRY4

- RHG35_HUMAN

UniProt

Q9NRY4 - RHG35_HUMAN

Protein

Rho GTPase-activating protein 35

Gene

ARHGAP35

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May participate in the regulation of retinal development and degeneration. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. GTP binding Source: InterPro
    3. Rho GTPase activator activity Source: Reactome
    4. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. camera-type eye development Source: Ensembl
    3. forebrain development Source: Ensembl
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. negative regulation of vascular permeability Source: Ensembl
    6. neural tube closure Source: Ensembl
    7. positive regulation of Rho GTPase activity Source: GOC
    8. regulation of cell shape Source: Ensembl
    9. regulation of small GTPase mediated signal transduction Source: Reactome
    10. small GTPase mediated signal transduction Source: Reactome
    11. transcription, DNA-templated Source: ProtInc

    Keywords - Molecular functioni

    GTPase activation, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    SignaLinkiQ9NRY4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho GTPase-activating protein 35
    Alternative name(s):
    Glucocorticoid receptor DNA-binding factor 1
    Glucocorticoid receptor repression factor 1
    Short name:
    GRF-1
    Rho GAP p190A
    Short name:
    p190-A
    Gene namesi
    Name:ARHGAP35
    Synonyms:GRF1, GRLF1, KIAA1722
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:4591. ARHGAP35.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA28988.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14991499Rho GTPase-activating protein 35PRO_0000056730Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei308 – 3081Phosphotyrosine1 Publication
    Modified residuei589 – 5891Phosphoserine4 Publications
    Modified residuei773 – 7731Phosphoserine1 Publication
    Modified residuei970 – 9701Phosphoserine2 Publications
    Modified residuei975 – 9751Phosphoserine2 Publications
    Modified residuei1072 – 10721Phosphoserine1 Publication
    Modified residuei1087 – 10871Phosphotyrosine1 Publication
    Modified residuei1105 – 11051Phosphotyrosine; by ABL2 and PTK62 Publications
    Modified residuei1134 – 11341Phosphoserine2 Publications
    Modified residuei1150 – 11501Phosphoserine2 Publications
    Modified residuei1179 – 11791Phosphoserine6 Publications

    Post-translational modificationi

    Phosphorylation of Tyr-1105 by PTK6 promotes the association with RASA1, inactivating RHOA while activating RAS. Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRY4.
    PaxDbiQ9NRY4.
    PRIDEiQ9NRY4.

    PTM databases

    PhosphoSiteiQ9NRY4.

    Expressioni

    Gene expression databases

    BgeeiQ9NRY4.
    CleanExiHS_GRLF1.
    GenevestigatoriQ9NRY4.

    Organism-specific databases

    HPAiCAB037311.

    Interactioni

    Subunit structurei

    Interacts with RASA1. Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm.1 Publication

    Protein-protein interaction databases

    BioGridi109166. 9 interactions.
    IntActiQ9NRY4. 1 interaction.
    STRINGi9606.ENSP00000385720.

    Structurei

    Secondary structure

    1
    1499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 218
    Turni25 – 306
    Helixi35 – 439
    Turni47 – 493
    Helixi60 – 634
    Turni66 – 705
    Beta strandi72 – 798
    Beta strandi91 – 966
    Turni102 – 1043
    Helixi110 – 1123
    Helixi116 – 1205
    Beta strandi123 – 1264
    Helixi136 – 1383
    Helixi142 – 1443
    Helixi151 – 1533
    Beta strandi154 – 1563
    Beta strandi159 – 1657
    Helixi174 – 19017
    Beta strandi195 – 2006
    Helixi202 – 2043
    Helixi207 – 21812
    Beta strandi220 – 2223
    Beta strandi225 – 2273
    Turni230 – 2334
    Helixi236 – 24813
    Turni268 – 2714
    Helixi272 – 28413
    Beta strandi286 – 2883
    Helixi292 – 2998
    Helixi303 – 3119
    Helixi314 – 33017
    Helixi1251 – 12544
    Beta strandi1257 – 12593
    Helixi1263 – 127513
    Turni1280 – 12845
    Helixi1289 – 130113
    Helixi1308 – 13103
    Helixi1314 – 132714
    Beta strandi1328 – 13303
    Helixi1335 – 134410
    Helixi1350 – 136213
    Helixi1366 – 138318
    Helixi1386 – 13894
    Helixi1393 – 140513
    Beta strandi1409 – 14124
    Helixi1414 – 143017
    Helixi1432 – 14365

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K85NMR-A267-331[»]
    3C5HX-ray1.80A13-249[»]
    3FK2X-ray2.80A/B/C/D1212-1439[»]
    ProteinModelPortaliQ9NRY4.
    SMRiQ9NRY4. Positions 13-249, 267-331, 1242-1437.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NRY4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini270 – 32758FF 1Add
    BLAST
    Domaini368 – 42255FF 2Add
    BLAST
    Domaini429 – 48355FF 3Add
    BLAST
    Domaini485 – 55066FF 4Add
    BLAST
    Domaini1249 – 1436188Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1440 – 149051Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 4 FF domains.Curated
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG241832.
    HOVERGENiHBG051844.
    InParanoidiQ9NRY4.
    KOiK05732.
    OMAiVLYRTRC.
    OrthoDBiEOG779NWX.
    TreeFamiTF324451.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR002713. FF_domain.
    IPR027417. P-loop_NTPase.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR001806. Small_GTPase.
    [Graphical view]
    PfamiPF01846. FF. 1 hit.
    PF00071. Ras. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00441. FF. 4 hits.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF81698. SSF81698. 1 hit.
    PROSITEiPS51676. FF. 4 hits.
    PS50238. RHOGAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NRY4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF     50
    HLDHTSVLST SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI 100
    DDQTFQPHRS TALQPYIKRA AATKLASAEK LMYFCTDQLG LEQDFEQKQM 150
    PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF VSNLYNQLAK TKKPIVVVLT 200
    KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF STLVQLIDKS 250
    RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ 300
    ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA 350
    LIPNLDEIDH LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE 400
    RIPFDLMDTV PAEQLYEAHL EKLRNERKRV EMRRAFKENL ETSPFITPGK 450
    PWEEARSFIM NEDFYQWLEE SVYMDIYGKH QKQIIDKAKE EFQELLLEYS 500
    ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER DALILKHIHF 550
    VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL 600
    VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS 650
    FQTPTFQPHG CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL 700
    ILVNKRGDTS GETLHSLIQQ GQQIASKLQC VFLDPASAGI GYGRNINEKQ 750
    ISQVLKGLLD SKRNLNLVSS TASIKDLADV DLRIVMCLMC GDPFSADDIL 800
    FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSVLSY HSSFSIRKSR 850
    LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAVDVLDNDL 900
    SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVEKKNIIEA 950
    THMYDNAAEA CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PSYSLFREDT 1000
    SLPSLSKDHS KLSMELEGND GLSFIMSNFE SKLNNKVPPP VKPKPPVHFE 1050
    ITKGDLSYLD QGHRDGQRKS VSSSPWLPQD GFDPSDYAEP MDAVVKPRNE 1100
    EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT SSLERGRKVS 1150
    IVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG 1200
    DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP 1250
    LTTVVTPEKP IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD 1300
    QDHNLDLAEK DFTVNTVAGA MKSFFSELPD PLVPYNMQID LVEAHKINDR 1350
    EQKLHALKEV LKKFPKENHE VFKYVISHLN KVSHNNKVNL MTSENLSICF 1400
    WPTLMRPDFS TMDALTATRT YQTIIELFIQ QCPFFFYNRP ITEPPGARPS 1450
    SPSAVASTVP FLTSTPVTSQ PSPPQSPPPT PQSPMQPLLP SQLQAEHTL 1499
    Length:1,499
    Mass (Da):170,514
    Last modified:October 3, 2012 - v3
    Checksum:i8CCB493414A7E3E6
    GO

    Sequence cautioni

    The sequence AAF80386.1 differs from that shown. Reason: Unlikely isoform. Aberrant splice sites.
    The sequence AAA58618.1 differs from that shown. Reason: Frameshift at positions 389, 533, 540, 607, 614, 1167, 1241, 1292, 1334 and 1446.
    The sequence AAF80386.1 differs from that shown. Reason: Frameshift at positions 533, 540, 607 and 614.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511R → P in AAF80386. (PubMed:11054565)Curated
    Sequence conflicti309 – 3091V → D in AAF80386. (PubMed:11054565)Curated
    Sequence conflicti362 – 3621S → G in AAF80386. (PubMed:11054565)Curated
    Sequence conflicti414 – 4141Q → A in AAF80386. (PubMed:11054565)Curated
    Sequence conflicti414 – 4141Q → A in AAA58618. (PubMed:1894621)Curated
    Sequence conflicti474 – 4741M → T in AAF80386. (PubMed:11054565)Curated
    Sequence conflicti474 – 4741M → T in AAA58618. (PubMed:1894621)Curated
    Sequence conflicti978 – 9781C → S in AAF80386. (PubMed:11054565)Curated
    Sequence conflicti1292 – 12921M → I in AAF80386. (PubMed:11054565)Curated
    Sequence conflicti1452 – 14532PS → RN in AAA58618. (PubMed:1894621)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051509 mRNA. Translation: BAB21813.2.
    CH471126 Genomic DNA. Translation: EAW57450.1.
    BC150257 mRNA. Translation: AAI50258.1.
    AF159851 mRNA. Translation: AAF80386.1. Sequence problems.
    M73077 mRNA. Translation: AAA58618.1. Frameshift.
    CCDSiCCDS46127.1.
    RefSeqiNP_004482.4. NM_004491.4.
    UniGeneiHs.509447.

    Genome annotation databases

    EnsembliENST00000404338; ENSP00000385720; ENSG00000160007.
    GeneIDi2909.
    KEGGihsa:2909.
    UCSCiuc010ekv.3. human.

    Polymorphism databases

    DMDMi408360250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051509 mRNA. Translation: BAB21813.2 .
    CH471126 Genomic DNA. Translation: EAW57450.1 .
    BC150257 mRNA. Translation: AAI50258.1 .
    AF159851 mRNA. Translation: AAF80386.1 . Sequence problems.
    M73077 mRNA. Translation: AAA58618.1 . Frameshift.
    CCDSi CCDS46127.1.
    RefSeqi NP_004482.4. NM_004491.4.
    UniGenei Hs.509447.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K85 NMR - A 267-331 [» ]
    3C5H X-ray 1.80 A 13-249 [» ]
    3FK2 X-ray 2.80 A/B/C/D 1212-1439 [» ]
    ProteinModelPortali Q9NRY4.
    SMRi Q9NRY4. Positions 13-249, 267-331, 1242-1437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109166. 9 interactions.
    IntActi Q9NRY4. 1 interaction.
    STRINGi 9606.ENSP00000385720.

    PTM databases

    PhosphoSitei Q9NRY4.

    Polymorphism databases

    DMDMi 408360250.

    Proteomic databases

    MaxQBi Q9NRY4.
    PaxDbi Q9NRY4.
    PRIDEi Q9NRY4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000404338 ; ENSP00000385720 ; ENSG00000160007 .
    GeneIDi 2909.
    KEGGi hsa:2909.
    UCSCi uc010ekv.3. human.

    Organism-specific databases

    CTDi 2909.
    GeneCardsi GC19P047422.
    H-InvDB HIX0015264.
    HGNCi HGNC:4591. ARHGAP35.
    HPAi CAB037311.
    MIMi 605277. gene.
    neXtProti NX_Q9NRY4.
    PharmGKBi PA28988.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG241832.
    HOVERGENi HBG051844.
    InParanoidi Q9NRY4.
    KOi K05732.
    OMAi VLYRTRC.
    OrthoDBi EOG779NWX.
    TreeFami TF324451.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
    SignaLinki Q9NRY4.

    Miscellaneous databases

    ChiTaRSi ARHGAP35. human.
    EvolutionaryTracei Q9NRY4.
    GeneWikii GRLF1.
    GenomeRNAii 2909.
    NextBioi 11533.
    PROi Q9NRY4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NRY4.
    CleanExi HS_GRLF1.
    Genevestigatori Q9NRY4.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR002713. FF_domain.
    IPR027417. P-loop_NTPase.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR001806. Small_GTPase.
    [Graphical view ]
    Pfami PF01846. FF. 1 hit.
    PF00071. Ras. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00441. FF. 4 hits.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF81698. SSF81698. 1 hit.
    PROSITEi PS51676. FF. 4 hits.
    PS50238. RHOGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "p190-A, a human tumor suppressor gene, maps to the chromosomal region 19q13.3 that is reportedly deleted in some gliomas."
      Tikoo A., Czekay S., Viars C., White S., Heath J.K., Arden K., Maruta H.
      Gene 257:23-31(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1491.
      Tissue: Mammary cancer.
    6. "Molecular cloning and characterization of a factor that binds the human glucocorticoid receptor gene and represses its expression."
      LeClerc S., Palaniswami R., Xie B.X., Govindan M.V.
      J. Biol. Chem. 266:17333-17340(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 377-1453, FUNCTION.
      Tissue: Mammary cancer.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Breast tumor kinase phosphorylates p190RhoGAP to regulate rho and ras and promote breast carcinoma growth, migration, and invasion."
      Shen C.H., Chen H.Y., Lin M.S., Li F.Y., Chang C.C., Kuo M.L., Settleman J., Chen R.H.
      Cancer Res. 68:7779-7787(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-1105.
    10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-970 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-970; SER-975; SER-1150 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-589; SER-773; SER-975; SER-1072; TYR-1087; TYR-1105; SER-1134 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-589; SER-1134; SER-1150 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding."
      Bonet R., Ruiz L., Aragon E., Martin-Malpartida P., Macias M.J.
      J. Mol. Biol. 389:230-237(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 267-331, PHOSPHORYLATION AT TYR-308, INTERACTION WITH GTF2I.

    Entry informationi

    Entry nameiRHG35_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRY4
    Secondary accession number(s): A7E2A4, Q14452, Q9C0E1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2003
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3