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P49792

- RBP2_HUMAN

UniProt

P49792 - RBP2_HUMAN

Protein

E3 SUMO-protein ligase RanBP2

Gene

RANBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB.5 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1351 – 138131RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1415 – 144430RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1479 – 150830RanBP2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1543 – 157230RanBP2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1606 – 163530RanBP2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1665 – 169430RanBP2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1724 – 175330RanBP2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1781 – 181030RanBP2-type 8PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. peptidyl-prolyl cis-trans isomerase activity Source: InterPro
    3. protein binding Source: UniProtKB
    4. Ran GTPase binding Source: ProtInc
    5. RNA binding Source: UniProtKB-KW
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cytokine-mediated signaling pathway Source: Reactome
    3. glucose transport Source: Reactome
    4. hexose transport Source: Reactome
    5. mitotic cell cycle Source: Reactome
    6. mitotic nuclear envelope disassembly Source: Reactome
    7. mRNA transport Source: UniProtKB-KW
    8. negative regulation of glucokinase activity Source: Ensembl
    9. protein folding Source: InterPro
    10. protein import into nucleus Source: ProtInc
    11. protein sumoylation Source: UniProtKB
    12. regulation of gluconeogenesis involved in cellular glucose homeostasis Source: Ensembl
    13. regulation of glucose transport Source: Reactome
    14. small molecule metabolic process Source: Reactome
    15. transmembrane transport Source: Reactome
    16. viral process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    mRNA transport, Protein transport, Translocation, Transport, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    REACT_682. Mitotic Prometaphase.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 SUMO-protein ligase RanBP2 (EC:6.3.2.-)
    Alternative name(s):
    358 kDa nucleoporin
    Nuclear pore complex protein Nup358
    Nucleoporin Nup358
    Ran-binding protein 2
    Short name:
    RanBP2
    p270
    Gene namesi
    Name:RANBP2
    Synonyms:NUP358
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9848. RANBP2.

    Subcellular locationi

    Nucleus. Nucleus membrane. Nucleusnuclear pore complex
    Note: Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. membrane Source: UniProtKB
    3. mitochondrion Source: Ensembl
    4. nuclear inclusion body Source: UniProtKB
    5. nuclear membrane Source: UniProtKB
    6. nuclear pore Source: UniProtKB
    7. nuclear pore nuclear basket Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Encephalopathy, acute, infection-induced, 3 (IIAE3) [MIM:608033]: A rapidly progressive encephalopathy manifesting in susceptible individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry. Mutations in the RANBP2 gene predispose to IIAE3, but by themselves are insufficient to make the phenotype fully penetrant; additional genetic and environmental factors are required (PubMed:19118815).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti585 – 5851T → M in IIAE3. 1 Publication
    VAR_054997
    Natural varianti653 – 6531T → I in IIAE3. 1 Publication
    VAR_054998
    Natural varianti656 – 6561I → V in IIAE3. 1 Publication
    VAR_054999

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2632 – 26321V → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication
    Mutagenesisi2634 – 26341I → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication
    Mutagenesisi2635 – 26351V → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication
    Mutagenesisi2640 – 26401P → A: No effect on SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2645 – 26451K → A: No effect on SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2651 – 26511L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2652 – 26521K → A: No effect on SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2653 – 26531L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2654 – 26541P → A: Impairs SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2655 – 26551P → A: No effect on SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2656 – 26561T → A: Impairs SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2657 – 26571F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2658 – 26581F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2659 – 26591C → S or A: Impairs SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2676 – 26761D → A: Impairs SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2677 – 26771F → A: Impairs SUMO E3 ligase activity. 1 Publication
    Mutagenesisi2689 – 26891Y → A: Impairs SUMO E3 ligase activity. 1 Publication

    Organism-specific databases

    MIMi608033. phenotype.
    Orphaneti263524. Acute necrotizing encephalopathy of childhood.
    88619. Familial acute necrotizing encephalopathy.
    178342. Inflammatory myofibroblastic tumor.
    PharmGKBiPA34209.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 32243224E3 SUMO-protein ligase RanBP2PRO_0000204913Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphothreonine3 Publications
    Modified residuei21 – 211Phosphoserine4 Publications
    Modified residuei781 – 7811Phosphoserine2 Publications
    Modified residuei788 – 7881PhosphoserineBy similarity
    Modified residuei837 – 8371Phosphoserine1 Publication
    Modified residuei948 – 9481Phosphoserine2 Publications
    Modified residuei955 – 9551Phosphoserine3 Publications
    Modified residuei1107 – 11071Phosphoserine1 Publication
    Modified residuei1110 – 11101Phosphoserine2 Publications
    Modified residuei1144 – 11441Phosphothreonine2 Publications
    Modified residuei1160 – 11601Phosphoserine3 Publications
    Modified residuei1396 – 13961Phosphothreonine2 Publications
    Modified residuei1412 – 14121Phosphothreonine1 Publication
    Modified residuei1443 – 14431Phosphoserine1 Publication
    Modified residuei1456 – 14561Phosphoserine2 Publications
    Modified residuei1509 – 15091Phosphoserine2 Publications
    Modified residuei1573 – 15731Phosphoserine1 Publication
    Modified residuei1835 – 18351Phosphoserine1 Publication
    Modified residuei1869 – 18691Phosphoserine1 Publication
    Modified residuei1871 – 18711Phosphoserine1 Publication
    Modified residuei1977 – 19771N6-acetyllysineBy similarity
    Modified residuei2246 – 22461PhosphoserineBy similarity
    Modified residuei2270 – 22701Phosphoserine2 Publications
    Modified residuei2293 – 22931PhosphothreonineBy similarity
    Modified residuei2297 – 22971PhosphoserineBy similarity
    Modified residuei2510 – 25101PhosphoserineBy similarity
    Cross-linki2592 – 2592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei2613 – 26131Phosphothreonine1 Publication
    Modified residuei2668 – 26681Phosphoserine3 Publications
    Modified residuei2741 – 27411Phosphoserine1 Publication
    Modified residuei2743 – 27431Phosphothreonine1 Publication
    Modified residuei2900 – 29001Phosphoserine4 Publications
    Modified residuei3207 – 32071Phosphoserine2 Publications

    Post-translational modificationi

    Polyubiquitinated by PARK2, which leads to proteasomal degradation.1 Publication
    The the inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP49792.
    PaxDbiP49792.
    PeptideAtlasiP49792.
    PRIDEiP49792.

    2D gel databases

    OGPiP49792.

    PTM databases

    PhosphoSiteiP49792.

    Expressioni

    Gene expression databases

    ArrayExpressiP49792.
    BgeeiP49792.
    CleanExiHS_RANBP2.
    GenevestigatoriP49792.

    Organism-specific databases

    HPAiHPA018437.
    HPA023960.

    Interactioni

    Subunit structurei

    Forms a tight complex with RANBP1 and UBE2I. Interacts with SUMO1 but not SUMO2. Interacts with PARK2. Interacts with sumoylated RANGAP1. Interacts with CDCA8. Interacts with PML (isoform PML-4).7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P046263EBI-973138,EBI-641062
    PARK2O6026011EBI-973138,EBI-716346
    PDLIM3Q53GG53EBI-973138,EBI-5658852

    Protein-protein interaction databases

    BioGridi111839. 95 interactions.
    DIPiDIP-37654N.
    IntActiP49792. 40 interactions.
    MINTiMINT-191403.
    STRINGi9606.ENSP00000283195.

    Structurei

    Secondary structure

    1
    3224
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1814
    Helixi22 – 265
    Helixi29 – 3810
    Helixi42 – 5514
    Helixi60 – 7213
    Helixi76 – 8914
    Helixi94 – 10714
    Helixi112 – 12413
    Helixi129 – 14113
    Beta strandi1190 – 120415
    Beta strandi1206 – 12094
    Beta strandi1211 – 122717
    Beta strandi1231 – 12355
    Turni1237 – 12393
    Beta strandi1242 – 12443
    Beta strandi1263 – 12708
    Beta strandi1277 – 12848
    Helixi1288 – 130013
    Beta strandi2028 – 20303
    Beta strandi2032 – 204615
    Turni2047 – 20504
    Beta strandi2051 – 206515
    Beta strandi2071 – 20777
    Turni2078 – 20814
    Beta strandi2082 – 20887
    Beta strandi2095 – 20973
    Beta strandi2105 – 21117
    Beta strandi2113 – 21153
    Beta strandi2117 – 21259
    Helixi2129 – 214517
    Turni2146 – 21483
    Beta strandi2632 – 26376
    Helixi2642 – 26509
    Helixi2657 – 26615
    Beta strandi2663 – 26653
    Helixi2677 – 26826
    Turni2683 – 26864
    Turni2926 – 29294
    Beta strandi2930 – 294415
    Turni2945 – 29484
    Beta strandi2949 – 296315
    Turni2964 – 29674
    Beta strandi2968 – 29747
    Turni2976 – 29783
    Beta strandi2981 – 29866
    Beta strandi2994 – 29963
    Beta strandi3000 – 300910
    Beta strandi3016 – 302611
    Helixi3027 – 304721
    Beta strandi3065 – 30728
    Beta strandi3075 – 308410
    Turni3086 – 30883
    Helixi3090 – 310112
    Turni3102 – 31043
    Beta strandi3112 – 31176
    Turni3118 – 31203
    Beta strandi3121 – 31244
    Turni3127 – 31293
    Beta strandi3130 – 31334
    Beta strandi3157 – 31604
    Beta strandi3168 – 31703
    Beta strandi3172 – 31776
    Helixi3180 – 31823
    Turni3183 – 31853
    Beta strandi3188 – 31947
    Helixi3196 – 32038
    Beta strandi3216 – 32238

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RRPX-ray2.96B/D1171-1304[»]
    1XKENMR-A2028-2154[»]
    1Z5SX-ray3.01D2631-2711[»]
    3UINX-ray2.60D2629-2695[»]
    3UIOX-ray2.60D2631-2695[»]
    3UIPX-ray2.29D2631-2695[»]
    4GA0X-ray1.15A1-145[»]
    4I9YX-ray1.75A/B/C/D/E/F3062-3224[»]
    4L6EX-ray2.50A2907-3050[»]
    4LQWX-ray1.95A/B3057-3224[»]
    ProteinModelPortaliP49792.
    SMRiP49792. Positions 3-145, 176-204, 664-689, 1171-1304, 2027-2154, 2324-2440, 2629-2693, 2925-3048, 3062-3224.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49792.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati26 – 5934TPR 11 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati60 – 9334TPR 21 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati94 – 12835TPR 31 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati165 – 20137TPR 41 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati287 – 31933TPR 51 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati583 – 61634TPR 61 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Repeati648 – 68134TPR 71 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Domaini1171 – 1307137RanBD1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2012 – 2148137RanBD1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2309 – 2445137RanBD1 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati2633 – 26855311 PublicationAdd
    BLAST
    Repeati2711 – 27615121 PublicationAdd
    BLAST
    Domaini2911 – 3046136RanBD1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini3067 – 3223157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2631 – 26355Interaction with sumoylated RANGAP1
    Regioni2633 – 27611292 X 50 AA approximate repeatsAdd
    BLAST
    Regioni2633 – 271078Required for E3 SUMO-ligase activityAdd
    BLAST
    Regioni2633 – 268553Interaction with UBE2IAdd
    BLAST
    Regioni2686 – 276176Interaction with SUMO1Add
    BLAST

    Domaini

    Contains a dozen F-X-F-G repeats in the C-terminal half.1 Publication
    The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro) (PubMed:23353830). Only about half of the residues that surround the PPIA active site cleft are conserved.1 Publication

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
    Contains 4 RanBD1 domains.PROSITE-ProRule annotation
    Contains 8 RanBP2-type zinc fingers.PROSITE-ProRule annotation
    Contains 7 TPR repeats.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1351 – 138131RanBP2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1415 – 144430RanBP2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1479 – 150830RanBP2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1543 – 157230RanBP2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1606 – 163530RanBP2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1665 – 169430RanBP2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1724 – 175330RanBP2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1781 – 181030RanBP2-type 8PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, TPR repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5171.
    HOGENOMiHOG000089994.
    HOVERGENiHBG092361.
    InParanoidiP49792.
    KOiK12172.
    OMAiSATKCIA.
    OrthoDBiEOG7X0VG5.
    PhylomeDBiP49792.
    TreeFamiTF314797.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    2.30.29.30. 4 hits.
    2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR022011. IR1-M.
    IPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    IPR001876. Znf_RanBP2.
    [Graphical view]
    PfamiPF12185. IR1-M. 2 hits.
    PF00160. Pro_isomerase. 1 hit.
    PF00638. Ran_BP1. 4 hits.
    PF00515. TPR_1. 1 hit.
    PF00641. zf-RanBP. 8 hits.
    [Graphical view]
    PRINTSiPR00153. CSAPPISMRASE.
    SMARTiSM00160. RanBD. 4 hits.
    SM00547. ZnF_RBZ. 8 hits.
    [Graphical view]
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    PS50196. RANBD1. 4 hits.
    PS50005. TPR. 1 hit.
    PS50293. TPR_REGION. 1 hit.
    PS01358. ZF_RANBP2_1. 8 hits.
    PS50199. ZF_RANBP2_2. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P49792-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC     50
    TYINVQERDP KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI 100
    AELLCKNDVT DGRAKYWLER AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL 150
    FDLIQSELYV RPDDVHVNIR LVEVYRSTKR LKDAVAHCHE AERNIALRSS 200
    LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA NLMLLTLSTR 250
    DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM 300
    GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR 350
    LSQSGHMLLN LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF 400
    LGSDDIGNID VREPELEDLT RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL 450
    PGIRKWLKQL FHHLPHETSR LETNAPESIC ILDLEVFLLG VVYTSHLQLK 500
    EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH RKAVPGNVAK 550
    LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG 600
    RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA 650
    HITFAILDAV NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS 700
    PEEQEECKNY LRKTRDYLIK IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM 750
    QELEDYSEGG PLYKNGSLRN ADSEIKHSTP SPTRYSLSPS KSYKYSPKTP 800
    PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR WPTENYGPDS 850
    VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG 900
    PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA 950
    TGILSPRGDD YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE 1000
    FGKTNFVQPM PGEGLRPSLP TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ 1050
    VVTQPPPAAY SNSESLLGLL TSDKPLQGDG YSGAKPIPGG QTIGPRNTFN 1100
    FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS VFGTPTLETA 1150
    NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK 1200
    LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP 1250
    DMKLTPNAGS DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE 1300
    AQSILKAPGT NVAMASNQAV RIVKEPTSHD NKDICKSDAG NLNFEFQVAK 1350
    KEGSWWHCNS CSLKNASTAK KCVSCQNLNP SNKELVGPPL AETVFTPKTS 1400
    PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN TKSANKSGSS 1450
    FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA 1500
    ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS 1550
    SCLVRNEANA TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE 1600
    GMFTKKEGQW DCSVCLVRNE ASATKCIACQ NPGKQNQTTS AVSTPASSET 1650
    SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA SATKCIACQN PGKQNQTTSA 1700
    VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS ATKCIACQCP 1750
    SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK 1800
    CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS 1850
    KFGNTEQGFK FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF 1900
    GISEPGNQEK KSEKPLENGT GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL 1950
    AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS SQYGKMANKA NTSGDFEKDD 2000
    DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV KLFRFDAEVS 2050
    QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG 2100
    SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP 2150
    LQTPHKLVDT GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG 2200
    TGAAGASDTT IKPNPENTGP TLEWDNYDLR EDALDDSVSS SSVHASPLAS 2250
    SPVRKNLFRF GESTTGFNFS FKSALSPSKS PAKLNQSGTS VGTDEESDVT 2300
    QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY RYDKDVGQWK 2350
    ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER 2400
    VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT 2450
    PHVSRSSTPR ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST 2500
    SETTPKAVVS PPKFVFGSES VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN 2550
    APLKSNNSET SSVAQSGSES KVEPKKCELS KNSDIEQSSD SKVKNLFASF 2600
    PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP TAEQKALATK 2650
    LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE 2700
    ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG 2750
    EDFQSELQKV QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT 2800
    KSISSPSVSS ETMDKPVDLS TRKEIDTDST SQGESKIVSF GFGSSTGLSF 2850
    ADLASSNSGD FAFGSKDKNF QWANTGAAVF GTQSVGTQSA GKVGEDEDGS 2900
    DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL YRWDRDVSQW 2950
    KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN 3000
    NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG 3050
    HVSLAAELSK ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC 3100
    TGEKGFGFKN SIFHRVIPDF VCQGGDITKH DGTGGQSIYG DKFEDENFDV 3150
    KHTGPGLLSM ANQGQNTNNS QFVITLKKAE HLDFKHVVFG FVKDGMDTVK 3200
    KIESFGSPKG SVCRRITITE CGQI 3224
    Length:3,224
    Mass (Da):358,199
    Last modified:December 6, 2005 - v2
    Checksum:i4CD9A3D5E77183FB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti777 – 7771H → R in AAC41758. (PubMed:7775481)Curated
    Sequence conflicti2207 – 22071S → A in AAA85838. (PubMed:7724562)Curated
    Sequence conflicti2210 – 22101T → P in AAA85838. (PubMed:7724562)Curated
    Sequence conflicti2216 – 22161E → V in AAA85838. (PubMed:7724562)Curated
    Sequence conflicti2436 – 24361F → C in AAA85838. (PubMed:7724562)Curated
    Sequence conflicti2475 – 24751T → P in AAA85838. (PubMed:7724562)Curated
    Sequence conflicti2531 – 25311K → N in AAA85838. (PubMed:7724562)Curated
    Sequence conflicti2545 – 25451F → C(PubMed:7724562)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti548 – 5481V → L.
    Corresponds to variant rs1057954 [ dbSNP | Ensembl ].
    VAR_029765
    Natural varianti580 – 5801E → K.
    Corresponds to variant rs4012065 [ dbSNP | Ensembl ].
    VAR_029766
    Natural varianti581 – 5811C → Y.
    Corresponds to variant rs1057957 [ dbSNP | Ensembl ].
    VAR_029767
    Natural varianti585 – 5851T → M in IIAE3. 1 Publication
    VAR_054997
    Natural varianti653 – 6531T → I in IIAE3. 1 Publication
    VAR_054998
    Natural varianti656 – 6561I → V in IIAE3. 1 Publication
    VAR_054999
    Natural varianti725 – 7251S → G.
    Corresponds to variant rs17414315 [ dbSNP | Ensembl ].
    VAR_050575
    Natural varianti784 – 7841R → K.1 Publication
    Corresponds to variant rs2912838 [ dbSNP | Ensembl ].
    VAR_023939
    Natural varianti1870 – 18701P → L.
    Corresponds to variant rs2889846 [ dbSNP | Ensembl ].
    VAR_029768
    Natural varianti1892 – 18921P → A.
    Corresponds to variant rs12770 [ dbSNP | Ensembl ].
    VAR_014886
    Natural varianti1892 – 18921P → R.
    Corresponds to variant rs12770 [ dbSNP | Ensembl ].
    VAR_050576

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41840 Genomic DNA. Translation: AAC41758.1.
    D42063 mRNA. Translation: BAA07662.1.
    AC010095 Genomic DNA. Translation: AAY14984.1.
    AB209483 mRNA. Translation: BAD92720.1.
    U19248 mRNA. Translation: AAA85838.1.
    CCDSiCCDS2079.1.
    PIRiS58884.
    RefSeqiNP_006258.3. NM_006267.4.
    UniGeneiHs.199561.
    Hs.715056.

    Genome annotation databases

    EnsembliENST00000283195; ENSP00000283195; ENSG00000153201.
    GeneIDi5903.
    KEGGihsa:5903.
    UCSCiuc002tem.4. human.

    Polymorphism databases

    DMDMi83305554.

    Keywords - Coding sequence diversityi

    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
    L41840 Genomic DNA. Translation: AAC41758.1 .
    D42063 mRNA. Translation: BAA07662.1 .
    AC010095 Genomic DNA. Translation: AAY14984.1 .
    AB209483 mRNA. Translation: BAD92720.1 .
    U19248 mRNA. Translation: AAA85838.1 .
    CCDSi CCDS2079.1.
    PIRi S58884.
    RefSeqi NP_006258.3. NM_006267.4.
    UniGenei Hs.199561.
    Hs.715056.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RRP X-ray 2.96 B/D 1171-1304 [» ]
    1XKE NMR - A 2028-2154 [» ]
    1Z5S X-ray 3.01 D 2631-2711 [» ]
    3UIN X-ray 2.60 D 2629-2695 [» ]
    3UIO X-ray 2.60 D 2631-2695 [» ]
    3UIP X-ray 2.29 D 2631-2695 [» ]
    4GA0 X-ray 1.15 A 1-145 [» ]
    4I9Y X-ray 1.75 A/B/C/D/E/F 3062-3224 [» ]
    4L6E X-ray 2.50 A 2907-3050 [» ]
    4LQW X-ray 1.95 A/B 3057-3224 [» ]
    ProteinModelPortali P49792.
    SMRi P49792. Positions 3-145, 176-204, 664-689, 1171-1304, 2027-2154, 2324-2440, 2629-2693, 2925-3048, 3062-3224.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111839. 95 interactions.
    DIPi DIP-37654N.
    IntActi P49792. 40 interactions.
    MINTi MINT-191403.
    STRINGi 9606.ENSP00000283195.

    PTM databases

    PhosphoSitei P49792.

    Polymorphism databases

    DMDMi 83305554.

    2D gel databases

    OGPi P49792.

    Proteomic databases

    MaxQBi P49792.
    PaxDbi P49792.
    PeptideAtlasi P49792.
    PRIDEi P49792.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000283195 ; ENSP00000283195 ; ENSG00000153201 .
    GeneIDi 5903.
    KEGGi hsa:5903.
    UCSCi uc002tem.4. human.

    Organism-specific databases

    CTDi 5903.
    GeneCardsi GC02P109335.
    H-InvDB HIX0002358.
    HGNCi HGNC:9848. RANBP2.
    HPAi HPA018437.
    HPA023960.
    MIMi 601181. gene.
    608033. phenotype.
    neXtProti NX_P49792.
    Orphaneti 263524. Acute necrotizing encephalopathy of childhood.
    88619. Familial acute necrotizing encephalopathy.
    178342. Inflammatory myofibroblastic tumor.
    PharmGKBi PA34209.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5171.
    HOGENOMi HOG000089994.
    HOVERGENi HBG092361.
    InParanoidi P49792.
    KOi K12172.
    OMAi SATKCIA.
    OrthoDBi EOG7X0VG5.
    PhylomeDBi P49792.
    TreeFami TF314797.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
    REACT_682. Mitotic Prometaphase.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_9395. Nuclear import of Rev protein.

    Miscellaneous databases

    ChiTaRSi RANBP2. human.
    EvolutionaryTracei P49792.
    GeneWikii RANBP2.
    GenomeRNAii 5903.
    NextBioi 22964.
    PROi P49792.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49792.
    Bgeei P49792.
    CleanExi HS_RANBP2.
    Genevestigatori P49792.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    2.30.29.30. 4 hits.
    2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR022011. IR1-M.
    IPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    IPR001876. Znf_RanBP2.
    [Graphical view ]
    Pfami PF12185. IR1-M. 2 hits.
    PF00160. Pro_isomerase. 1 hit.
    PF00638. Ran_BP1. 4 hits.
    PF00515. TPR_1. 1 hit.
    PF00641. zf-RanBP. 8 hits.
    [Graphical view ]
    PRINTSi PR00153. CSAPPISMRASE.
    SMARTi SM00160. RanBD. 4 hits.
    SM00547. ZnF_RBZ. 8 hits.
    [Graphical view ]
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    PS50196. RANBD1. 4 hits.
    PS50005. TPR. 1 hit.
    PS50293. TPR_REGION. 1 hit.
    PS01358. ZF_RANBP2_1. 8 hits.
    PS50199. ZF_RANBP2_2. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region."
      Wu J., Matunis M.J., Kraemer D., Blobel G., Coutavas E.
      J. Biol. Chem. 270:14209-14213(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-784.
      Tissue: Blood.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-3224.
      Tissue: Brain.
    5. "The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif."
      Beddow A.L., Richards S.A., Orem N.R., Macara I.G.
      Proc. Natl. Acad. Sci. U.S.A. 92:3328-3332(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2205-2546.
      Tissue: Hippocampus.
    6. "The nucleoporin RanBP2 has SUMO1 E3 ligase activity."
      Pichler A., Gast A., Seeler J.S., Dejean A., Melchior F.
      Cell 108:109-120(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUMOYLATION.
    7. Cited for: FUNCTION.
    8. "Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
      Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
      J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. Cited for: FUNCTION, INTERACTION WITH UBE2I, SUMOYLATION AT LYS-2592, MUTAGENESIS OF PRO-2640; LYS-2645; LEU-2651; LYS-2652; LEU-2653; PRO-2654; PRO-2655; THR-2656; PHE-2657; PHE-2658; CYS-2659; ASP-2676; PHE-2677 AND TYR-2689.
    11. "Identification of a SUMO-binding motif that recognizes SUMO-modified proteins."
      Song J., Durrin L.K., Wilkinson T.A., Krontiris T.G., Chen Y.
      Proc. Natl. Acad. Sci. U.S.A. 101:14373-14378(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUMOYLATED RANGAP1, MUTAGENESIS OF VAL-2632; ILE-2634 AND VAL-2635.
    12. "Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection."
      Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.
      Nat. Struct. Mol. Biol. 12:67-74(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUMO1 AND UBE2I.
    13. "A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers."
      Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H., Chock P.B.
      Arch. Biochem. Biophys. 453:70-74(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Parkin ubiquitinates and promotes the degradation of RanBP2."
      Um J.W., Min D.S., Rhim H., Kim J., Paik S.R., Chung K.C.
      J. Biol. Chem. 281:3595-3603(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARK2, UBIQUITINATION.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND THR-1144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-781; SER-948; SER-955; SER-1110; THR-1144; SER-1160; THR-1396; SER-1443; SER-1456; SER-1509; SER-1573; SER-1869; SER-2270; THR-2613; SER-2668; SER-2741; THR-2743 AND SER-2900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    21. "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].
    22. "RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin."
      Klein U.R., Haindl M., Nigg E.A., Muller S.
      Mol. Biol. Cell 20:410-418(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDCA8.
    23. "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 THR-19; SER-21; SER-955; SER-1107; THR-1396; SER-1871; SER-2270; SER-2668 AND SER-2900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "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 THR-19; SER-21; SER-781; SER-837; SER-948; SER-955; SER-1110; SER-1160; THR-1412; SER-1509; SER-1835; SER-2900 AND SER-3207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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-1160; SER-1456; SER-2668; SER-2900 AND SER-3207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport."
      Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A.
      Nature 398:39-46(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 1171-1304.
    28. "Solution structure of the Ran-binding domain 2 of RanBP2 and its interaction with the C terminus of Ran."
      Geyer J.P., Doker R., Kremer W., Zhao X., Kuhlmann J., Kalbitzer H.R.
      J. Mol. Biol. 348:711-725(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2028-2154.
    29. "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 2631-2711 IN COMPLEX WITH SUMO1; RANGAP1 AND UBE2I, SUBUNIT, FUNCTION.
    30. "Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2."
      Gareau J.R., Reverter D., Lima C.D.
      J. Biol. Chem. 287:4740-4751(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 2631-2695 IN COMPLEX WITH SUMO1; RANGAP1 AND UBE2I, SUBUNIT, FUNCTION.
    31. Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 1-145, TPR REPEATS.
    32. "Structural and functional analysis of the C-terminal domain of Nup358/RanBP2."
      Lin D.H., Zimmermann S., Stuwe T., Stuwe E., Hoelz A.
      J. Mol. Biol. 425:1318-1329(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3062-3224, DOMAIN, ABSENCE OF ROTAMASE ACTIVITY, SUBCELLULAR LOCATION.
    33. Cited for: VARIANTS IIAE3 MET-585; ILE-653 AND VAL-656.

    Entry informationi

    Entry nameiRBP2_HUMAN
    AccessioniPrimary (citable) accession number: P49792
    Secondary accession number(s): Q13074
    , Q15280, Q53TE2, Q59FH7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 167 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 2
      Human chromosome 2: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3