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P46060

- RAGP1_HUMAN

UniProt

P46060 - RAGP1_HUMAN

Protein

Ran GTPase-activating protein 1

Gene

RANGAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei562 – 5621Hydrophobic interaction with UBC9By similarity
    Sitei565 – 5651Hydrophobic interaction with UBC9By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. Ran GTPase activator activity Source: ProtInc

    GO - Biological processi

    1. mitotic cell cycle Source: Reactome
    2. negative regulation of protein export from nucleus Source: BHF-UCL
    3. positive regulation of Ran GTPase activity Source: GOC
    4. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ran GTPase-activating protein 1
    Short name:
    RanGAP1
    Gene namesi
    Name:RANGAP1
    Synonyms:KIAA1835, SD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9854. RANGAP1.

    Subcellular locationi

    Cytoplasm. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle pole By similarity
    Note: Cytoplasmic during interphase. Targeted to the nuclear rim after sumoylation. During mitosis, associates with mitotic spindles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation.

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytoplasm Source: ProtInc
    3. cytosol Source: Reactome
    4. nuclear membrane Source: UniProtKB-SubCell
    5. nuclear pore Source: ProtInc
    6. perinuclear region of cytoplasm Source: Ensembl
    7. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi524 – 5241K → R: No association with mitotic spindles during mitosis. 1 Publication

    Organism-specific databases

    PharmGKBiPA34216.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 587586Ran GTPase-activating protein 1PRO_0000056737Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
    Modified residuei358 – 3581Phosphoserine1 Publication
    Modified residuei409 – 4091Phosphothreonine; by CDK21 Publication
    Modified residuei428 – 4281Phosphoserine4 Publications
    Modified residuei435 – 4351Phosphoserine1 Publication
    Modified residuei436 – 4361Phosphothreonine1 Publication
    Modified residuei442 – 4421Phosphoserine6 Publications
    Modified residuei524 – 5241N6-acetyllysine; alternate1 Publication
    Cross-linki524 – 524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate

    Post-translational modificationi

    Phosphorylated occurs before nuclear envelope breakdown and continues throughout mitosis. Phosphorylated by the M-phase kinase cyclin B/Cdk1, in vitro. Differential timimg of dephosphorylation occurs during phases of mitosis. The phosphorylated form remains associated with RANBP2/NUP358 and the SUMO E2-conjugating enzyme, UBC9, on nuclear pore complex (NPC) diassembly and during mitosis.6 Publications
    Sumoylated with SUMO1. Sumoylation is necessary for targeting to the nuclear envelope (NE), and for association with mitotic spindles and kinetochores during mitosis. Also required for interaction with RANBP2 and is mediated by UBC9.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP46060.
    PaxDbiP46060.
    PRIDEiP46060.

    PTM databases

    PhosphoSiteiP46060.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, thymus and testis.1 Publication

    Gene expression databases

    ArrayExpressiP46060.
    BgeeiP46060.
    CleanExiHS_RANGAP1.
    GenevestigatoriP46060.

    Organism-specific databases

    HPAiCAB004293.
    HPA050110.

    Interactioni

    Subunit structurei

    Homodimer. Forms a tight complex in association with RANBP2/NUP358 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2. Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2/NUP358. The SUMO1/RANGAP1/UBC9/NUP358 complex associates with nuclear pore complexes. Interacts with TRAF6.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SUMO1P631654EBI-396091,EBI-80140
    UBE2IP632794EBI-396091,EBI-80168

    Protein-protein interaction databases

    BioGridi111840. 76 interactions.
    DIPiDIP-29079N.
    IntActiP46060. 17 interactions.
    MINTiMINT-3016328.
    STRINGi9606.ENSP00000348577.

    Structurei

    Secondary structure

    1
    587
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi434 – 4396
    Helixi443 – 4486
    Helixi453 – 4597
    Helixi466 – 47712
    Helixi484 – 50219
    Beta strandi503 – 5075
    Helixi509 – 51911
    Helixi536 – 54510
    Beta strandi548 – 5514
    Helixi553 – 5553
    Helixi556 – 5649
    Helixi568 – 5714
    Helixi574 – 58613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z5SX-ray3.01C418-587[»]
    2GRNX-ray1.80B419-587[»]
    2GROX-ray1.70B419-587[»]
    2GRPX-ray2.05B419-587[»]
    2GRQX-ray1.70B419-587[»]
    2GRRX-ray1.30B419-587[»]
    2IO2X-ray2.90C418-587[»]
    2IO3X-ray3.20C418-587[»]
    2IY0X-ray2.77C432-587[»]
    3UINX-ray2.60C419-587[»]
    3UIOX-ray2.60C419-587[»]
    3UIPX-ray2.29C419-587[»]
    ProteinModelPortaliP46060.
    SMRiP46060. Positions 21-349, 431-587.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46060.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati48 – 7124LRR 1Add
    BLAST
    Repeati111 – 13424LRR 2Add
    BLAST
    Repeati207 – 23024LRR 3Add
    BLAST
    Repeati235 – 25824LRR 4Add
    BLAST
    Repeati292 – 31928LRR 5Add
    BLAST
    Repeati320 – 34324LRR 6Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi523 – 5264SUMO conjugation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi359 – 39941Asp/Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi359 – 39739Asp/Glu-rich (highly acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the RNA1 family.Curated
    Contains 6 LRR (leucine-rich) repeats.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG5238.
    HOGENOMiHOG000195026.
    HOVERGENiHBG017720.
    InParanoidiP46060.
    KOiK14319.
    OMAiSFNSNAF.
    OrthoDBiEOG70W3DV.
    PhylomeDBiP46060.
    TreeFamiTF318283.

    Family and domain databases

    Gene3Di1.25.40.200. 1 hit.
    InterProiIPR009109. Ran_GTPase_activating_1_C.
    IPR027038. RanGap.
    [Graphical view]
    PANTHERiPTHR24113. PTHR24113. 1 hit.
    PfamiPF07834. RanGAP1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF69099. SSF69099. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P46060-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASEDIAKLA ETLAKTQVAG GQLSFKGKSL KLNTAEDAKD VIKEIEDFDS    50
    LEALRLEGNT VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRTEIPPAL 100
    ISLGEGLITA GAQLVELDLS DNAFGPDGVQ GFEALLKSSA CFTLQELKLN 150
    NCGMGIGGGK ILAAALTECH RKSSAQGKPL ALKVFVAGRN RLENDGATAL 200
    AEAFRVIGTL EEVHMPQNGI NHPGITALAQ AFAVNPLLRV INLNDNTFTE 250
    KGAVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAIRG GLPKLKELNL 300
    SFCEIKRDAA LAVAEAMADK AELEKLDLNG NTLGEEGCEQ LQEVLEGFNM 350
    AKVLASLSDD EDEEEEEEGE EEEEEAEEEE EEDEEEEEEE EEEEEEEPQQ 400
    RGQGEKSATP SRKILDPNTG EPAPVLSSPP PADVSTFLAF PSPEKLLRLG 450
    PKSSVLIAQQ TDTSDPEKVV SAFLKVSSVF KDEATVRMAV QDAVDALMQK 500
    AFNSSSFNSN TFLTRLLVHM GLLKSEDKVK AIANLYGPLM ALNHMVQQDY 550
    FPKALAPLLL AFVTKPNSAL ESCSFARHSL LQTLYKV 587
    Length:587
    Mass (Da):63,542
    Last modified:November 1, 1995 - v1
    Checksum:i3C18068AAC06B98F
    GO

    Sequence cautioni

    The sequence BAB47464.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti133 – 1331E → Q.
    Corresponds to variant rs2229752 [ dbSNP | Ensembl ].
    VAR_029240

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82260 mRNA. Translation: CAA57714.1.
    AB058738 mRNA. Translation: BAB47464.1. Different initiation.
    CR456557 mRNA. Translation: CAG30443.1.
    AL035681 Genomic DNA. Translation: CAB63073.1.
    BC014044 mRNA. Translation: AAH14044.1.
    BC041396 mRNA. Translation: AAH41396.1.
    CCDSiCCDS14012.1.
    PIRiJC5300.
    RefSeqiNP_001265580.1. NM_001278651.1.
    NP_002874.1. NM_002883.3.
    XP_006724352.1. XM_006724289.1.
    UniGeneiHs.183800.

    Genome annotation databases

    EnsembliENST00000356244; ENSP00000348577; ENSG00000100401.
    ENST00000405486; ENSP00000385866; ENSG00000100401.
    ENST00000455915; ENSP00000401470; ENSG00000100401.
    GeneIDi5905.
    KEGGihsa:5905.
    UCSCiuc003azs.3. human.

    Polymorphism databases

    DMDMi1172922.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82260 mRNA. Translation: CAA57714.1 .
    AB058738 mRNA. Translation: BAB47464.1 . Different initiation.
    CR456557 mRNA. Translation: CAG30443.1 .
    AL035681 Genomic DNA. Translation: CAB63073.1 .
    BC014044 mRNA. Translation: AAH14044.1 .
    BC041396 mRNA. Translation: AAH41396.1 .
    CCDSi CCDS14012.1.
    PIRi JC5300.
    RefSeqi NP_001265580.1. NM_001278651.1.
    NP_002874.1. NM_002883.3.
    XP_006724352.1. XM_006724289.1.
    UniGenei Hs.183800.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z5S X-ray 3.01 C 418-587 [» ]
    2GRN X-ray 1.80 B 419-587 [» ]
    2GRO X-ray 1.70 B 419-587 [» ]
    2GRP X-ray 2.05 B 419-587 [» ]
    2GRQ X-ray 1.70 B 419-587 [» ]
    2GRR X-ray 1.30 B 419-587 [» ]
    2IO2 X-ray 2.90 C 418-587 [» ]
    2IO3 X-ray 3.20 C 418-587 [» ]
    2IY0 X-ray 2.77 C 432-587 [» ]
    3UIN X-ray 2.60 C 419-587 [» ]
    3UIO X-ray 2.60 C 419-587 [» ]
    3UIP X-ray 2.29 C 419-587 [» ]
    ProteinModelPortali P46060.
    SMRi P46060. Positions 21-349, 431-587.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111840. 76 interactions.
    DIPi DIP-29079N.
    IntActi P46060. 17 interactions.
    MINTi MINT-3016328.
    STRINGi 9606.ENSP00000348577.

    PTM databases

    PhosphoSitei P46060.

    Polymorphism databases

    DMDMi 1172922.

    Proteomic databases

    MaxQBi P46060.
    PaxDbi P46060.
    PRIDEi P46060.

    Protocols and materials databases

    DNASUi 5905.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356244 ; ENSP00000348577 ; ENSG00000100401 .
    ENST00000405486 ; ENSP00000385866 ; ENSG00000100401 .
    ENST00000455915 ; ENSP00000401470 ; ENSG00000100401 .
    GeneIDi 5905.
    KEGGi hsa:5905.
    UCSCi uc003azs.3. human.

    Organism-specific databases

    CTDi 5905.
    GeneCardsi GC22M041641.
    HGNCi HGNC:9854. RANGAP1.
    HPAi CAB004293.
    HPA050110.
    MIMi 602362. gene.
    neXtProti NX_P46060.
    PharmGKBi PA34216.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5238.
    HOGENOMi HOG000195026.
    HOVERGENi HBG017720.
    InParanoidi P46060.
    KOi K14319.
    OMAi SFNSNAF.
    OrthoDBi EOG70W3DV.
    PhylomeDBi P46060.
    TreeFami TF318283.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi RANGAP1. human.
    EvolutionaryTracei P46060.
    GeneWikii RANGAP1.
    GenomeRNAii 5905.
    NextBioi 22968.
    PROi P46060.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46060.
    Bgeei P46060.
    CleanExi HS_RANGAP1.
    Genevestigatori P46060.

    Family and domain databases

    Gene3Di 1.25.40.200. 1 hit.
    InterProi IPR009109. Ran_GTPase_activating_1_C.
    IPR027038. RanGap.
    [Graphical view ]
    PANTHERi PTHR24113. PTHR24113. 1 hit.
    Pfami PF07834. RanGAP1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69099. SSF69099. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport."
      Bischoff F.R., Krebber H., Kempf T., Hermes I., Ponstingl H.
      Proc. Natl. Acad. Sci. U.S.A. 92:1749-1753(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "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.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Kidney.
    7. "Ubiquitous expression and testis-specific alternative polyadenylation of mRNA for the human Ran GTPase activator RanGAP1."
      Krebber H., Ponstingl H.
      Gene 180:7-11(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles."
      Joseph J., Tan S.-H., Karpova T.S., McNally J.G., Dasso M.
      J. Cell Biol. 156:595-602(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524.
    9. "RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly."
      Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.
      J. Cell Biol. 164:965-971(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-409; SER-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH SUMO1; RANBP2 AND UBE2I.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification."
      Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J.
      J. Biol. Chem. 283:5081-5089(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF6.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-428 AND SER-442, 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-428; SER-435; THR-436 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
      Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
      J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-8 AND LYS-524, ACETYLATION AT ALA-2.
      Tissue: Cervix carcinoma.
    17. "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-428 AND SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
      Reverter D., Lima C.D.
      Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 418-587 IN COMPLEX WITH SUMO1; RANBP2 AND UBE2I.
    21. "SUMO protease SENP1 induces isomerization of the scissile peptide bond."
      Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.
      Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 432-587 IN COMPLEX WITH SUMO1 AND SENP1.

    Entry informationi

    Entry nameiRAGP1_HUMAN
    AccessioniPrimary (citable) accession number: P46060
    Secondary accession number(s): Q96JJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 164 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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