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P46061

- RAGP1_MOUSE

UniProt

P46061 - RAGP1_MOUSE

Protein

Ran GTPase-activating protein 1

Gene

Rangap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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. Required for postimplantation development.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei564 – 5641Hydrophobic interaction with UBC9By similarity
    Sitei567 – 5671Hydrophobic interaction with UBC9By similarity

    GO - Molecular functioni

    1. Ran GTPase activator activity Source: InterPro

    GO - Biological processi

    1. negative regulation of protein export from nucleus Source: Ensembl
    2. signal transduction Source: InterPro

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ran GTPase-activating protein 1
    Short name:
    RanGAP1
    Gene namesi
    Name:Rangap1
    Synonyms:Fug1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:103071. Rangap1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle 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 By similarity.By similarity

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytoplasm Source: MGI
    3. nuclear membrane Source: UniProtKB-SubCell
    4. perinuclear region of cytoplasm Source: MGI
    5. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi411 – 4111T → D: Greatly reduced phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-444. 1 Publication
    Mutagenesisi444 – 4441S → D: Little change in phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-411. 1 Publication
    Mutagenesisi512 – 5121N → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi516 – 5161T → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi517 – 5171R → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi520 – 5201I → A: No effect on UBC9 binding nor on sumoylation.
    Mutagenesisi521 – 5211H → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi522 – 5221M → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi524 – 5241L → A: No sumoylation. 1 Publication
    Mutagenesisi525 – 5251L → A: Disrupted binding of UCB9, and no sumoylation. 1 Publication
    Mutagenesisi526 – 5261K → A: No UBC9 binding nor sumoylation. 4 Publications
    Mutagenesisi526 – 5261K → R: Absence of sumoylation. Not targeted to the nuclear envelope rim nor to nuclear pore complexes. Disrupted sumoylation. No interaction with SUMO1; when associated with A-564 and with or without SUMO1 A-97. 4 Publications
    Mutagenesisi528 – 5281E → A: No UBC9 binding nor sumoylation. 1 Publication
    Mutagenesisi529 – 5291D → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi531 – 5311I → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi537 – 5371L → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi560 – 5601L → A: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi563 – 5631A → L: No effect on UBC9 binding nor on sumoylation. 1 Publication
    Mutagenesisi564 – 5641F → A: No UBC9 binding nor sumoylation. Not targeted to nuclear core complexes; when associated with R-526. 2 Publications
    Mutagenesisi567 – 5671K → A: No UBC9 binding nor sumoylation. 1 Publication
    Mutagenesisi569 – 5691N → A: No effect on UBC9 binding nor on sumoylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 589588Ran GTPase-activating protein 1PRO_0000056738Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei358 – 3581PhosphoserineBy similarity
    Modified residuei411 – 4111Phosphothreonine; by CDK2By similarity
    Modified residuei430 – 4301PhosphoserineBy similarity
    Modified residuei437 – 4371PhosphoserineBy similarity
    Modified residuei438 – 4381PhosphothreonineBy similarity
    Modified residuei444 – 4441Phosphoserine2 Publications
    Modified residuei526 – 5261N6-acetyllysine; alternateBy similarity
    Cross-linki526 – 526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); 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.2 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 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP46061.
    PaxDbiP46061.
    PRIDEiP46061.

    PTM databases

    PhosphoSiteiP46061.

    Expressioni

    Gene expression databases

    ArrayExpressiP46061.
    BgeeiP46061.
    CleanExiMM_RANGAP1.
    GenevestigatoriP46061.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with TRAF6 By similarity. 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.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi202583. 11 interactions.
    DIPiDIP-17024N.
    IntActiP46061. 3 interactions.
    MINTiMINT-4132270.
    STRINGi10090.ENSMUSP00000057771.

    Structurei

    Secondary structure

    1
    589
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi436 – 4416
    Helixi445 – 4506
    Helixi455 – 4617
    Helixi468 – 48013
    Helixi486 – 50520
    Helixi511 – 52111
    Helixi538 – 54912
    Helixi555 – 5573
    Helixi558 – 5658
    Helixi577 – 58812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KPSX-ray2.50B/D420-589[»]
    ProteinModelPortaliP46061.
    SMRiP46061. Positions 21-370, 434-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46061.

    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 – 31524LRR 5Add
    BLAST
    Repeati320 – 34324LRR 6Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi525 – 5284SUMO conjugationBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi359 – 39941Asp/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.
    GeneTreeiENSGT00440000039203.
    HOVERGENiHBG017720.
    InParanoidiQ6NZB5.
    KOiK14319.
    OMAiSFNSNAF.
    OrthoDBiEOG70W3DV.
    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.

    P46061-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASEDIAKLA ETLAKTQVAG GQLSFKGKGL KLNTAEDAKD VIKEIEEFDG    50
    LEALRLEGNT VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRSEIPPAL 100
    ISLGEGLITA GAQLVELDLS DNAFGPDGVR GFEALLKSPA CFTLQELKLN 150
    NCGMGIGGGK ILAAALTECH RKSSAQGKPL ALKVFVAGRN RLENDGATAL 200
    AEAFGIIGTL EEVHMPQNGI NHPGVTALAQ AFAINPLLRV INLNDNTFTE 250
    KGGVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAVRG GLPKLKELNL 300
    SFCEIKRDAA LVVAEAVADK AELEKLDLNG NALGEEGCEQ LQEVMDSFNM 350
    AKVLASLSDD EGEDEDEEEE GEEDDEEEED EEDEEDDDEE EEEQEEEEEP 400
    PQRGSGEEPA TPSRKILDPN SGEPAPVLSS PTPTDLSTFL SFPSPEKLLR 450
    LGPKVSVLIV QQTDTSDPEK VVSAFLKVAS VFRDDASVKT AVLDAIDALM 500
    KKAFSCSSFN SNTFLTRLLI HMGLLKSEDK IKAIPSLHGP LMVLNHVVRQ 550
    DYFPKALAPL LLAFVTKPNG ALETCSFARH NLLQTLYNI 589
    Length:589
    Mass (Da):63,531
    Last modified:July 27, 2011 - v2
    Checksum:i775ADE3A53EFD558
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811A → R in AAA17681. (PubMed:8314081)Curated
    Sequence conflicti413 – 4131S → L in AAB60517. (PubMed:7891706)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08110 mRNA. Translation: AAA17681.1.
    U20857 Genomic RNA. Translation: AAB60517.1.
    AK146670 mRNA. Translation: BAE27347.1.
    AK159009 mRNA. Translation: BAE34767.1.
    AK159525 mRNA. Translation: BAE35154.1.
    BC066213 mRNA. Translation: AAH66213.1.
    BC071200 mRNA. Translation: AAH71200.1.
    CCDSiCCDS27670.1.
    PIRiA36983.
    T52070.
    RefSeqiNP_001139646.1. NM_001146174.1.
    NP_035371.4. NM_011241.4.
    UniGeneiMm.270975.
    Mm.475271.

    Genome annotation databases

    EnsembliENSMUST00000052374; ENSMUSP00000057771; ENSMUSG00000022391.
    ENSMUST00000170134; ENSMUSP00000126849; ENSMUSG00000022391.
    ENSMUST00000171115; ENSMUSP00000130046; ENSMUSG00000022391.
    GeneIDi19387.
    KEGGimmu:19387.
    UCSCiuc007wxb.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08110 mRNA. Translation: AAA17681.1 .
    U20857 Genomic RNA. Translation: AAB60517.1 .
    AK146670 mRNA. Translation: BAE27347.1 .
    AK159009 mRNA. Translation: BAE34767.1 .
    AK159525 mRNA. Translation: BAE35154.1 .
    BC066213 mRNA. Translation: AAH66213.1 .
    BC071200 mRNA. Translation: AAH71200.1 .
    CCDSi CCDS27670.1.
    PIRi A36983.
    T52070.
    RefSeqi NP_001139646.1. NM_001146174.1.
    NP_035371.4. NM_011241.4.
    UniGenei Mm.270975.
    Mm.475271.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KPS X-ray 2.50 B/D 420-589 [» ]
    ProteinModelPortali P46061.
    SMRi P46061. Positions 21-370, 434-589.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202583. 11 interactions.
    DIPi DIP-17024N.
    IntActi P46061. 3 interactions.
    MINTi MINT-4132270.
    STRINGi 10090.ENSMUSP00000057771.

    PTM databases

    PhosphoSitei P46061.

    Proteomic databases

    MaxQBi P46061.
    PaxDbi P46061.
    PRIDEi P46061.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000052374 ; ENSMUSP00000057771 ; ENSMUSG00000022391 .
    ENSMUST00000170134 ; ENSMUSP00000126849 ; ENSMUSG00000022391 .
    ENSMUST00000171115 ; ENSMUSP00000130046 ; ENSMUSG00000022391 .
    GeneIDi 19387.
    KEGGi mmu:19387.
    UCSCi uc007wxb.2. mouse.

    Organism-specific databases

    CTDi 5905.
    MGIi MGI:103071. Rangap1.

    Phylogenomic databases

    eggNOGi COG5238.
    GeneTreei ENSGT00440000039203.
    HOVERGENi HBG017720.
    InParanoidi Q6NZB5.
    KOi K14319.
    OMAi SFNSNAF.
    OrthoDBi EOG70W3DV.
    TreeFami TF318283.

    Enzyme and pathway databases

    Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.

    Miscellaneous databases

    ChiTaRSi RANGAP1. mouse.
    EvolutionaryTracei P46061.
    NextBioi 296501.
    PROi P46061.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46061.
    Bgeei P46061.
    CleanExi MM_RANGAP1.
    Genevestigatori P46061.

    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. "A murine homolog of the yeast RNA1 gene is required for postimplantation development."
      Degregori J., Russ A., von Melchner H., Rayburn H., Priyaranjan P., Jenkins N.A., Copeland N.G., Ruley H.E.
      Genes Dev. 8:265-276(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Separate domains of the Ran GTPase interact with different factors to regulate nuclear protein import and RNA processing."
      Ren M., Villamarin A., Shih A., Coutavas E., Moore M.S., Locurcio M., Clarke V., Oppenheim J.D., D'Eustachio P., Rush M.G.
      Mol. Cell. Biol. 15:2117-2124(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Liver and Visual cortex.
    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].
      Strain: 129 and C57BL/6J.
      Tissue: Mammary tumor.
    5. "Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association."
      Mahajan R., Gerace L., Melchior F.
      J. Cell Biol. 140:259-270(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-526.
    6. "SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex."
      Matunis M.J., Wu J., Blobel G.
      J. Cell Biol. 140:499-509(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-526 AND PHE-564.
    7. "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-411 AND SER-444, MUTAGENESIS OF THR-411 AND SER-444.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    9. "SUMO modification through rapamycin-mediated heterodimerization reveals a dual role for Ubc9 in targeting RanGAP1 to nuclear pore complexes."
      Zhu S., Zhang H., Matunis M.J.
      Exp. Cell Res. 312:1042-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-526, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-526.
    10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. "Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1."
      Bernier-Villamor V., Sampson D.A., Matunis M.J., Lima C.D.
      Cell 108:345-356(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 420-589 IN COMPLEX WITH SUMO1 AND HUMAN UBE2I, MUTAGENESIS OF ASN-512; THR-516; ARG-517; HIS-521; MET-522; LEU-524; LEU-525; LYS-526; GLU-528; ASP-529; ILE-531; LEU-537; LEU-560; ALA-563; PHE-564; LYS-567 AND ASN-569.

    Entry informationi

    Entry nameiRAGP1_MOUSE
    AccessioniPrimary (citable) accession number: P46061
    Secondary accession number(s): Q60801, Q6NZB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3