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P47736

- RPGP1_HUMAN

UniProt

P47736 - RPGP1_HUMAN

Protein

Rap1 GTPase-activating protein 1

Gene

RAP1GAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state.1 Publication

    GO - Molecular functioni

    1. GTPase activator activity Source: ProtInc
    2. GTPase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. Rap GTPase activator activity Source: UniProtKB
    6. Ras GTPase binding Source: UniProtKB

    GO - Biological processi

    1. GTP catabolic process Source: GOC
    2. positive regulation of Rap GTPase activity Source: UniProtKB
    3. regulation of Ras GTPase activity Source: UniProtKB
    4. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_23898. Rap1 signalling.
    SignaLinkiP47736.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rap1 GTPase-activating protein 1
    Short name:
    Rap1GAP
    Short name:
    Rap1GAP1
    Gene namesi
    Name:RAP1GAP
    Synonyms:KIAA0474, RAP1GA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9858. RAP1GAP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. Golgi membrane Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1001F → E: Impaired dimerization; when associated with E-173. 1 Publication
    Mutagenesisi173 – 1731L → E: Impaired dimerization; when associated with E-100. 1 Publication
    Mutagenesisi207 – 2071E → A: Reduces GTPase activation. 1 Publication
    Mutagenesisi267 – 2671H → A: Abolishes GTPase activation. 1 Publication
    Mutagenesisi286 – 2861R → A: Reduces GTPase activation. 1 Publication
    Mutagenesisi287 – 2871H → A: Abolishes GTPase activation. 1 Publication
    Mutagenesisi290 – 2901N → A or K: Abolishes GTPase activation. 1 Publication
    Mutagenesisi291 – 2911D → A: Abolishes GTPase activation. 1 Publication
    Mutagenesisi388 – 3881R → A or P: Reduces GTPase activation. 1 Publication

    Organism-specific databases

    PharmGKBiPA34220.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 663663Rap1 GTPase-activating protein 1PRO_0000056743Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei484 – 4841Phosphoserine1 Publication
    Modified residuei499 – 4991Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP47736.
    PaxDbiP47736.
    PRIDEiP47736.

    PTM databases

    PhosphoSiteiP47736.

    Expressioni

    Tissue specificityi

    Significant expression seen in the brain, kidney and pancreas. Abundant in the cerebral cortex and expressed at much lower levels in the spinal cord. Not detected in the lymphoid tissues.1 Publication

    Inductioni

    By 12-O-tetradecanoylphorbol-13-acetate (TPA) in promyelocytic HL-60 cells.1 Publication

    Gene expression databases

    ArrayExpressiP47736.
    BgeeiP47736.
    CleanExiHS_RAP1GAP.
    GenevestigatoriP47736.

    Organism-specific databases

    HPAiCAB003851.
    HPA001922.

    Interactioni

    Subunit structurei

    Homodimer and heterodimer with RAP1B.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAP1BP612243EBI-722307,EBI-358143

    Protein-protein interaction databases

    BioGridi111844. 14 interactions.
    IntActiP47736. 9 interactions.
    MINTiMINT-3308298.
    STRINGi9606.ENSP00000363897.

    Structurei

    Secondary structure

    1
    663
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi85 – 884
    Helixi89 – 935
    Turni94 – 963
    Beta strandi100 – 1067
    Turni107 – 1093
    Beta strandi110 – 12112
    Beta strandi124 – 1329
    Beta strandi137 – 1437
    Helixi153 – 1608
    Helixi177 – 18610
    Beta strandi192 – 2009
    Helixi207 – 2115
    Helixi218 – 22710
    Beta strandi228 – 2336
    Beta strandi245 – 2473
    Beta strandi252 – 2587
    Beta strandi263 – 2686
    Helixi269 – 2713
    Helixi282 – 2887
    Beta strandi292 – 3009
    Helixi306 – 3083
    Beta strandi316 – 3238
    Beta strandi327 – 3293
    Beta strandi331 – 3388
    Beta strandi354 – 3585
    Helixi359 – 37618
    Helixi380 – 40930

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SRQX-ray2.90A/B/C/D75-415[»]
    3BRWX-ray3.40A/B/C75-415[»]
    ProteinModelPortaliP47736.
    SMRiP47736. Positions 78-414.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP47736.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 1717GoLocoPROSITE-ProRule annotationAdd
    BLAST
    Domaini181 – 397217Rap-GAPPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 GoLoco domain.PROSITE-ProRule annotation
    Contains 1 Rap-GAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG292109.
    HOGENOMiHOG000231640.
    HOVERGENiHBG016371.
    KOiK17700.
    OrthoDBiEOG7WHH8V.
    PhylomeDBiP47736.
    TreeFamiTF318626.

    Family and domain databases

    InterProiIPR003109. GoLoco_motif.
    IPR000331. Rap_GAP_dom.
    [Graphical view]
    PfamiPF02188. GoLoco. 1 hit.
    PF02145. Rap_GAP. 1 hit.
    [Graphical view]
    SMARTiSM00390. GoLoco. 1 hit.
    [Graphical view]
    PROSITEiPS50877. GOLOCO. 1 hit.
    PS50085. RAPGAP. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P47736-1) [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

    MIEKMQGSRM DEQRCSFPPP LKTEEDYIPY PSVHEVLGRE GPFPLILLPQ    50
    FGGYWIEGTN HEITSIPETE PLQSPTTKVK LECNPTARIY RKHFLGKEHF 100
    NYYSLDAALG HLVFSLKYDV IGDQEHLRLL LRTKCRTYHD VIPISCLTEF 150
    PNVVQMAKLV CEDVNVDRFY PVLYPKASRL IVTFDEHVIS NNFKFGVIYQ 200
    KLGQTSEEEL FSTNEESPAF VEFLEFLGQK VKLQDFKGFR GGLDVTHGQT 250
    GTESVYCNFR NKEIMFHVST KLPYTEGDAQ QLQRKRHIGN DIVAVVFQDE 300
    NTPFVPDMIA SNFLHAYVVV QAEGGGPDGP LYKVSVTARD DVPFFGPPLP 350
    DPAVFRKGPE FQEFLLTKLI NAEYACYKAE KFAKLEERTR AALLETLYEE 400
    LHIHSQSMMG LGGDEDKMEN GSGGGGFFES FKRVIRSRSQ SMDAMGLSNK 450
    KPNTVSTSHS GSFAPNNPDL AKAAGISLIV PGKSPTRKKS GPFGSRRSSA 500
    IGIENIQEVQ EKRESPPAGQ KTPDSGHVSQ EPKSENSSTQ SSPEMPTTKN 550
    RAETAAQRAE ALKDFSRSSS SASSFASVVE ETEGVDGEDT GLESVSSSGT 600
    PHKRDSFIYS TWLEDSVSTT SGGSSPGPSR SPHPDAGKLG DPACPEIKIQ 650
    LEASEQHMPQ LGC 663
    Length:663
    Mass (Da):73,361
    Last modified:November 25, 2008 - v2
    Checksum:i89B307CC67F975DD
    GO
    Isoform 2 (identifier: P47736-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         476-476: I → ISLLIPGKSASRFGRRGSAIGIGTVEE
         626-633: Missing.

    Show »
    Length:681
    Mass (Da):75,187
    Checksum:i7B2B680087CFCCB4
    GO
    Isoform 3 (identifier: P47736-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAQLRPAVPPGRPRRGSLPAGASWQNTDLFEM
         280-280: Missing.

    Note: Contains a phosphoserine at position 17.

    Show »
    Length:693
    Mass (Da):76,592
    Checksum:iBEB784BF1F8E67F3
    GO
    Isoform 4 (identifier: P47736-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSGRKRSFTFGAYGGVDKSFTSRRSVWRSDGQNQHFPQALDLSRVNLVPSYTPSLYPKNTDLFEM

    Note: No experimental confirmation available.

    Show »
    Length:727
    Mass (Da):80,645
    Checksum:iB106FC67B06E1615
    GO

    Sequence cautioni

    The sequence AAH54490.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA32319.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti304 – 3041F → L in AAH54490. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071A → T.1 Publication
    Corresponds to variant rs2275363 [ dbSNP | Ensembl ].
    VAR_047792
    Natural varianti257 – 2571C → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035547
    Natural varianti609 – 6091Y → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035548

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAQLRPAVPPGRPRRGSLPA GASWQNTDLFEM in isoform 3. 1 PublicationVSP_040260
    Alternative sequencei1 – 11M → MSGRKRSFTFGAYGGVDKSF TSRRSVWRSDGQNQHFPQAL DLSRVNLVPSYTPSLYPKNT DLFEM in isoform 4. CuratedVSP_047025
    Alternative sequencei280 – 2801Missing in isoform 3. 1 PublicationVSP_040261
    Alternative sequencei476 – 4761I → ISLLIPGKSASRFGRRGSAI GIGTVEE in isoform 2. 1 PublicationVSP_035256
    Alternative sequencei626 – 6338Missing in isoform 2. 1 PublicationVSP_035257

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64788 mRNA. Translation: AAA60252.1.
    AB007943 mRNA. Translation: BAA32319.3. Different initiation.
    AL359815 Genomic DNA. Translation: CAI16250.1.
    AL359815 Genomic DNA. Translation: CAI16255.1.
    CH471134 Genomic DNA. Translation: EAW94980.1.
    CH471134 Genomic DNA. Translation: EAW94981.1.
    AB003930 mRNA. Translation: BAA83674.1.
    BC054490 mRNA. Translation: AAH54490.1. Different initiation.
    CCDSiCCDS218.1. [P47736-1]
    CCDS53276.1. [P47736-2]
    CCDS53277.1. [P47736-4]
    PIRiA39897.
    B39897.
    RefSeqiNP_001139129.1. NM_001145657.1. [P47736-2]
    NP_001139130.1. NM_001145658.1. [P47736-4]
    NP_002876.2. NM_002885.2. [P47736-1]
    UniGeneiHs.148178.

    Genome annotation databases

    EnsembliENST00000290101; ENSP00000290101; ENSG00000076864. [P47736-4]
    ENST00000374765; ENSP00000363897; ENSG00000076864. [P47736-1]
    ENST00000542643; ENSP00000441661; ENSG00000076864. [P47736-2]
    GeneIDi5909.
    KEGGihsa:5909.
    UCSCiuc001bev.3. human. [P47736-1]
    uc001bew.3. human.
    uc001bey.3. human. [P47736-2]

    Polymorphism databases

    DMDMi215273877.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64788 mRNA. Translation: AAA60252.1 .
    AB007943 mRNA. Translation: BAA32319.3 . Different initiation.
    AL359815 Genomic DNA. Translation: CAI16250.1 .
    AL359815 Genomic DNA. Translation: CAI16255.1 .
    CH471134 Genomic DNA. Translation: EAW94980.1 .
    CH471134 Genomic DNA. Translation: EAW94981.1 .
    AB003930 mRNA. Translation: BAA83674.1 .
    BC054490 mRNA. Translation: AAH54490.1 . Different initiation.
    CCDSi CCDS218.1. [P47736-1 ]
    CCDS53276.1. [P47736-2 ]
    CCDS53277.1. [P47736-4 ]
    PIRi A39897.
    B39897.
    RefSeqi NP_001139129.1. NM_001145657.1. [P47736-2 ]
    NP_001139130.1. NM_001145658.1. [P47736-4 ]
    NP_002876.2. NM_002885.2. [P47736-1 ]
    UniGenei Hs.148178.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SRQ X-ray 2.90 A/B/C/D 75-415 [» ]
    3BRW X-ray 3.40 A/B/C 75-415 [» ]
    ProteinModelPortali P47736.
    SMRi P47736. Positions 78-414.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111844. 14 interactions.
    IntActi P47736. 9 interactions.
    MINTi MINT-3308298.
    STRINGi 9606.ENSP00000363897.

    PTM databases

    PhosphoSitei P47736.

    Polymorphism databases

    DMDMi 215273877.

    Proteomic databases

    MaxQBi P47736.
    PaxDbi P47736.
    PRIDEi P47736.

    Protocols and materials databases

    DNASUi 5909.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290101 ; ENSP00000290101 ; ENSG00000076864 . [P47736-4 ]
    ENST00000374765 ; ENSP00000363897 ; ENSG00000076864 . [P47736-1 ]
    ENST00000542643 ; ENSP00000441661 ; ENSG00000076864 . [P47736-2 ]
    GeneIDi 5909.
    KEGGi hsa:5909.
    UCSCi uc001bev.3. human. [P47736-1 ]
    uc001bew.3. human.
    uc001bey.3. human. [P47736-2 ]

    Organism-specific databases

    CTDi 5909.
    GeneCardsi GC01M021922.
    HGNCi HGNC:9858. RAP1GAP.
    HPAi CAB003851.
    HPA001922.
    MIMi 600278. gene.
    neXtProti NX_P47736.
    PharmGKBi PA34220.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292109.
    HOGENOMi HOG000231640.
    HOVERGENi HBG016371.
    KOi K17700.
    OrthoDBi EOG7WHH8V.
    PhylomeDBi P47736.
    TreeFami TF318626.

    Enzyme and pathway databases

    Reactomei REACT_23898. Rap1 signalling.
    SignaLinki P47736.

    Miscellaneous databases

    EvolutionaryTracei P47736.
    GeneWikii RAP1GAP.
    GenomeRNAii 5909.
    NextBioi 22986.
    PROi P47736.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47736.
    Bgeei P47736.
    CleanExi HS_RAP1GAP.
    Genevestigatori P47736.

    Family and domain databases

    InterProi IPR003109. GoLoco_motif.
    IPR000331. Rap_GAP_dom.
    [Graphical view ]
    Pfami PF02188. GoLoco. 1 hit.
    PF02145. Rap_GAP. 1 hit.
    [Graphical view ]
    SMARTi SM00390. GoLoco. 1 hit.
    [Graphical view ]
    PROSITEi PS50877. GOLOCO. 1 hit.
    PS50085. RAPGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1."
      Rubinfeld B., Munemitsu S., Clark R., Conroy L., Watt K., Crosier W.J., McCormick F., Polakis P.
      Cell 65:1033-1042(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-107.
      Tissue: Brain.
    2. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
      Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
      DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Activation of the ERK/MAPK pathway by an isoform of rap1GAP associated with G alpha(i)."
      Mochizuki N., Ohba Y., Kiyokawa E., Kurata T., Murakami Y., Ozaki Y., Kitakabe A., Nagashima K., Matsuda M.
      Nature 400:891-894(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-100 (ISOFORM 3).
      Tissue: Brain.
    6. "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: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    7. "Human SPA-1 product selectively expressed in lymphoid tissues is a specific GTPase-activating protein for Rap1 and Rap2."
      Kurachi H., Wada Y., Tsukamoto N., Maeda M., Kubota H., Hattori M., Iwai K., Minato N.
      J. Biol. Chem. 272:28081-28088(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-17 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The GTPase-activating protein Rap1GAP uses a catalytic asparagine."
      Daumke O., Weyand M., Chakrabarti P.P., Vetter I.R., Wittinghofer A.
      Nature 429:197-201(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 75-415, FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-100; LEU-173; GLU-207; HIS-267; ARG-286; HIS-287; ASN-290; ASP-291 AND ARG-388.
    13. "The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues."
      Scrima A., Thomas C., Deaconescu D., Wittinghofer A.
      EMBO J. 27:1145-1153(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH RAP1B, SUBUNIT.
    14. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-257 AND CYS-609.

    Entry informationi

    Entry nameiRPGP1_HUMAN
    AccessioniPrimary (citable) accession number: P47736
    Secondary accession number(s): J3QSS6
    , O75062, Q5T3S9, Q5T3T4, Q7Z5S8, Q9UQ51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 125 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 1
      Human chromosome 1: 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