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P43487

- RANG_HUMAN

UniProt

P43487 - RANG_HUMAN

Protein

Ran-specific GTPase-activating protein

Gene

RANBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

    GO - Molecular functioni

    1. GDP-dissociation inhibitor activity Source: ProtInc
    2. GTPase activator activity Source: UniProtKB-KW
    3. Ran GTPase binding Source: ProtInc

    GO - Biological processi

    1. intracellular transport Source: InterPro
    2. positive regulation of mitotic centrosome separation Source: Ensembl
    3. regulation of catalytic activity Source: GOC
    4. signal transduction Source: UniProtKB
    5. spindle organization Source: Ensembl
    6. viral process Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_6190. Rev-mediated nuclear export of HIV RNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ran-specific GTPase-activating protein
    Alternative name(s):
    Ran-binding protein 1
    Short name:
    RanBP1
    Gene namesi
    Name:RANBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9847. RANBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. nuclear envelope Source: Reactome
    4. nucleus Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34206.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 201200Ran-specific GTPase-activating proteinPRO_0000213667Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei13 – 131Phosphothreonine1 Publication
    Modified residuei18 – 181Phosphothreonine1 Publication
    Modified residuei21 – 211Phosphoserine1 Publication
    Modified residuei60 – 601Phosphoserine1 Publication
    Modified residuei150 – 1501N6-acetyllysine; alternate1 Publication
    Modified residuei150 – 1501N6-succinyllysine; alternateBy similarity
    Modified residuei183 – 1831N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP43487.
    PaxDbiP43487.
    PeptideAtlasiP43487.
    PRIDEiP43487.

    2D gel databases

    DOSAC-COBS-2DPAGEP43487.
    OGPiP43487.
    REPRODUCTION-2DPAGEIPI00414127.

    PTM databases

    PhosphoSiteiP43487.

    Expressioni

    Gene expression databases

    ArrayExpressiP43487.
    BgeeiP43487.
    CleanExiHS_RANBP1.
    GenevestigatoriP43487.

    Organism-specific databases

    HPAiCAB046463.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MPGP293721EBI-1032909,EBI-1043398

    Protein-protein interaction databases

    BioGridi111838. 25 interactions.
    IntActiP43487. 7 interactions.
    MINTiMINT-1584597.
    STRINGi9606.ENSP00000327583.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 5811
    Beta strandi67 – 7913
    Beta strandi81 – 833
    Beta strandi86 – 927
    Turni93 – 953
    Beta strandi98 – 1036
    Beta strandi117 – 12711
    Beta strandi134 – 1418
    Helixi145 – 16521

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K5DX-ray2.70B/E/H/K1-201[»]
    1K5GX-ray3.10B/E/H/K1-201[»]
    ProteinModelPortaliP43487.
    SMRiP43487. Positions 22-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43487.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 164139RanBD1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RANBP1 family.Curated
    Contains 1 RanBD1 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5171.
    HOGENOMiHOG000176323.
    HOVERGENiHBG006958.
    InParanoidiP43487.
    KOiK15306.
    OMAiPGKNDNA.
    PhylomeDBiP43487.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    [Graphical view]
    PfamiPF00638. Ran_BP1. 1 hit.
    [Graphical view]
    SMARTiSM00160. RanBD. 1 hit.
    [Graphical view]
    PROSITEiPS50196. RANBD1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P43487-1) [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

    MAAAKDTHED HDTSTENTDE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK    50
    MRAKLFRFAS ENDLPEWKER GTGDVKLLKH KEKGAIRLLM RRDKTLKICA 100
    NHYITPMMEL KPNAGSDRAW VWNTHADFAD ECPKPELLAI RFLNAENAQK 150
    FKTKFEECRK EIEEREKKAG SGKNDHAEKV AEKLEALSVK EETKEDAEEK 200
    Q 201
    Length:201
    Mass (Da):23,310
    Last modified:November 1, 1995 - v1
    Checksum:i05FC9B35DADA48C9
    GO
    Isoform 2 (identifier: P43487-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         169-169: Missing.

    Show »
    Length:200
    Mass (Da):23,239
    Checksum:i11E4114E1392C43D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611E → V in BAD97226. (PubMed:10591208)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161E → D in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036567
    Natural varianti145 – 1451A → V.
    Corresponds to variant rs5746863 [ dbSNP | Ensembl ].
    VAR_053629

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei169 – 1691Missing in isoform 2. 2 PublicationsVSP_055104

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83617 mRNA. Translation: CAA58592.1.
    D38076 mRNA. Translation: BAA07269.1.
    CR456556 mRNA. Translation: CAG30442.1.
    AK223506 mRNA. Translation: BAD97226.1.
    AC006547 Genomic DNA. No translation available.
    CCDSiCCDS13775.1. [P43487-1]
    CCDS63408.1. [P43487-2]
    PIRiS54290.
    RefSeqiNP_001265568.1. NM_001278639.1.
    NP_001265569.1. NM_001278640.1.
    NP_002873.1. NM_002882.3.
    UniGeneiHs.24763.

    Genome annotation databases

    EnsembliENST00000331821; ENSP00000327583; ENSG00000099901. [P43487-1]
    ENST00000402752; ENSP00000384925; ENSG00000099901. [P43487-2]
    GeneIDi5902.
    KEGGihsa:5902.
    UCSCiuc002zro.1. human. [P43487-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83617 mRNA. Translation: CAA58592.1 .
    D38076 mRNA. Translation: BAA07269.1 .
    CR456556 mRNA. Translation: CAG30442.1 .
    AK223506 mRNA. Translation: BAD97226.1 .
    AC006547 Genomic DNA. No translation available.
    CCDSi CCDS13775.1. [P43487-1 ]
    CCDS63408.1. [P43487-2 ]
    PIRi S54290.
    RefSeqi NP_001265568.1. NM_001278639.1.
    NP_001265569.1. NM_001278640.1.
    NP_002873.1. NM_002882.3.
    UniGenei Hs.24763.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K5D X-ray 2.70 B/E/H/K 1-201 [» ]
    1K5G X-ray 3.10 B/E/H/K 1-201 [» ]
    ProteinModelPortali P43487.
    SMRi P43487. Positions 22-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111838. 25 interactions.
    IntActi P43487. 7 interactions.
    MINTi MINT-1584597.
    STRINGi 9606.ENSP00000327583.

    PTM databases

    PhosphoSitei P43487.

    2D gel databases

    DOSAC-COBS-2DPAGE P43487.
    OGPi P43487.
    REPRODUCTION-2DPAGE IPI00414127.

    Proteomic databases

    MaxQBi P43487.
    PaxDbi P43487.
    PeptideAtlasi P43487.
    PRIDEi P43487.

    Protocols and materials databases

    DNASUi 5902.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331821 ; ENSP00000327583 ; ENSG00000099901 . [P43487-1 ]
    ENST00000402752 ; ENSP00000384925 ; ENSG00000099901 . [P43487-2 ]
    GeneIDi 5902.
    KEGGi hsa:5902.
    UCSCi uc002zro.1. human. [P43487-1 ]

    Organism-specific databases

    CTDi 5902.
    GeneCardsi GC22P020103.
    HGNCi HGNC:9847. RANBP1.
    HPAi CAB046463.
    MIMi 601180. gene.
    neXtProti NX_P43487.
    PharmGKBi PA34206.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5171.
    HOGENOMi HOG000176323.
    HOVERGENi HBG006958.
    InParanoidi P43487.
    KOi K15306.
    OMAi PGKNDNA.
    PhylomeDBi P43487.

    Enzyme and pathway databases

    Reactomei REACT_6190. Rev-mediated nuclear export of HIV RNA.

    Miscellaneous databases

    ChiTaRSi RANBP1. human.
    EvolutionaryTracei P43487.
    GeneWikii RANBP1.
    GenomeRNAii 5902.
    NextBioi 22960.
    PROi P43487.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43487.
    Bgeei P43487.
    CleanExi HS_RANBP1.
    Genevestigatori P43487.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    [Graphical view ]
    Pfami PF00638. Ran_BP1. 1 hit.
    [Graphical view ]
    SMARTi SM00160. RanBD. 1 hit.
    [Graphical view ]
    PROSITEi PS50196. RANBD1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1."
      Bischoff F.R., Krebber H., Smirnova E., Dong W., Ponstingl H.
      EMBO J. 14:705-715(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4."
      Hayashi N., Yokoyama N., Seki T., Azuma Y., Ohba T., Nishimoto T.
      Mol. Gen. Genet. 247:661-669(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Blood.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Coronary arterial endothelium.
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; THR-18 AND SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "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-150 AND LYS-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-16.

    Entry informationi

    Entry nameiRANG_HUMAN
    AccessioniPrimary (citable) accession number: P43487
    Secondary accession number(s): Q53EY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 134 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