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P49792 - RBP2_HUMAN

UniProt

P49792 - RBP2_HUMAN

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Protein

E3 SUMO-protein ligase RanBP2

Gene

RANBP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein modification; protein sumoylation.

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. Ran GTPase binding Source: ProtInc
  4. RNA binding Source: UniProtKB-KW
  5. 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. protein folding Source: InterPro
  9. protein import into nucleus Source: ProtInc
  10. protein sumoylation Source: UniProtKB
  11. regulation of glucose transport Source: Reactome
  12. small molecule metabolic process Source: Reactome
  13. transmembrane transport Source: Reactome
  14. viral process Source: Reactome
Complete GO annotation...

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_267668. Transcriptional regulation by small RNAs.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6354. Viral Messenger RNA Synthesis.
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9848. RANBP2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
  3. nuclear inclusion body Source: UniProtKB
  4. nuclear membrane Source: UniProtKB
  5. nuclear pore Source: UniProtKB
  6. nuclear pore nuclear basket Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Involvement in diseasei

Encephalopathy, acute, infection-induced, 31 Publication

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).

Disease descriptionA 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.

See also OMIM:608033
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

BgeeiP49792.
CleanExiHS_RANBP2.
ExpressionAtlasiP49792. baseline and differential.
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. 103 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 – 1814Combined sources
Helixi22 – 265Combined sources
Helixi29 – 3810Combined sources
Helixi42 – 5514Combined sources
Helixi60 – 7213Combined sources
Helixi76 – 8914Combined sources
Helixi94 – 10714Combined sources
Helixi112 – 12413Combined sources
Helixi129 – 14113Combined sources
Beta strandi1190 – 120415Combined sources
Beta strandi1206 – 12094Combined sources
Beta strandi1211 – 122717Combined sources
Beta strandi1231 – 12355Combined sources
Turni1237 – 12393Combined sources
Beta strandi1242 – 12443Combined sources
Beta strandi1263 – 12708Combined sources
Beta strandi1277 – 12848Combined sources
Helixi1288 – 130013Combined sources
Beta strandi2028 – 20303Combined sources
Beta strandi2032 – 204615Combined sources
Turni2047 – 20504Combined sources
Beta strandi2051 – 206515Combined sources
Beta strandi2071 – 20777Combined sources
Turni2078 – 20814Combined sources
Beta strandi2082 – 20887Combined sources
Beta strandi2095 – 20973Combined sources
Beta strandi2105 – 21117Combined sources
Beta strandi2113 – 21153Combined sources
Beta strandi2117 – 21259Combined sources
Helixi2129 – 214517Combined sources
Turni2146 – 21483Combined sources
Beta strandi2632 – 26376Combined sources
Helixi2642 – 26509Combined sources
Helixi2657 – 26615Combined sources
Beta strandi2663 – 26653Combined sources
Helixi2677 – 26826Combined sources
Turni2683 – 26864Combined sources
Turni2926 – 29294Combined sources
Beta strandi2930 – 294415Combined sources
Turni2945 – 29484Combined sources
Beta strandi2949 – 296315Combined sources
Turni2964 – 29674Combined sources
Beta strandi2968 – 29747Combined sources
Turni2976 – 29783Combined sources
Beta strandi2981 – 29866Combined sources
Beta strandi2994 – 29963Combined sources
Beta strandi3000 – 300910Combined sources
Beta strandi3016 – 302611Combined sources
Helixi3027 – 304721Combined sources
Beta strandi3065 – 30728Combined sources
Beta strandi3075 – 308410Combined sources
Turni3086 – 30883Combined sources
Helixi3090 – 310112Combined sources
Turni3102 – 31043Combined sources
Beta strandi3112 – 31176Combined sources
Turni3118 – 31203Combined sources
Beta strandi3121 – 31244Combined sources
Turni3127 – 31293Combined sources
Beta strandi3130 – 31334Combined sources
Beta strandi3157 – 31604Combined sources
Beta strandi3168 – 31703Combined sources
Beta strandi3172 – 31776Combined sources
Helixi3180 – 31823Combined sources
Turni3183 – 31853Combined sources
Beta strandi3188 – 31947Combined sources
Helixi3196 – 32038Combined sources
Beta strandi3216 – 32238Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 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.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiP49792.
KOiK12172.
OMAiPGKQNQT.
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_dom.
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

        10         20         30         40         50
MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC 
        60         70         80         90        100
TYINVQERDP KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI 
       110        120        130        140        150
AELLCKNDVT DGRAKYWLER AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL 
       160        170        180        190        200
FDLIQSELYV RPDDVHVNIR LVEVYRSTKR LKDAVAHCHE AERNIALRSS 
       210        220        230        240        250
LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA NLMLLTLSTR 
       260        270        280        290        300
DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM 
       310        320        330        340        350
GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR 
       360        370        380        390        400
LSQSGHMLLN LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF 
       410        420        430        440        450
LGSDDIGNID VREPELEDLT RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL 
       460        470        480        490        500
PGIRKWLKQL FHHLPHETSR LETNAPESIC ILDLEVFLLG VVYTSHLQLK 
       510        520        530        540        550
EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH RKAVPGNVAK 
       560        570        580        590        600
LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG 
       610        620        630        640        650
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA 
       660        670        680        690        700
HITFAILDAV NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS 
       710        720        730        740        750
PEEQEECKNY LRKTRDYLIK IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM 
       760        770        780        790        800
QELEDYSEGG PLYKNGSLRN ADSEIKHSTP SPTRYSLSPS KSYKYSPKTP 
       810        820        830        840        850
PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR WPTENYGPDS 
       860        870        880        890        900
VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG 
       910        920        930        940        950
PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA 
       960        970        980        990       1000
TGILSPRGDD YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE 
      1010       1020       1030       1040       1050
FGKTNFVQPM PGEGLRPSLP TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ 
      1060       1070       1080       1090       1100
VVTQPPPAAY SNSESLLGLL TSDKPLQGDG YSGAKPIPGG QTIGPRNTFN 
      1110       1120       1130       1140       1150
FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS VFGTPTLETA 
      1160       1170       1180       1190       1200
NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK 
      1210       1220       1230       1240       1250
LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP 
      1260       1270       1280       1290       1300
DMKLTPNAGS DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE 
      1310       1320       1330       1340       1350
AQSILKAPGT NVAMASNQAV RIVKEPTSHD NKDICKSDAG NLNFEFQVAK 
      1360       1370       1380       1390       1400
KEGSWWHCNS CSLKNASTAK KCVSCQNLNP SNKELVGPPL AETVFTPKTS 
      1410       1420       1430       1440       1450
PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN TKSANKSGSS 
      1460       1470       1480       1490       1500
FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA 
      1510       1520       1530       1540       1550
ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS 
      1560       1570       1580       1590       1600
SCLVRNEANA TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE 
      1610       1620       1630       1640       1650
GMFTKKEGQW DCSVCLVRNE ASATKCIACQ NPGKQNQTTS AVSTPASSET 
      1660       1670       1680       1690       1700
SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA SATKCIACQN PGKQNQTTSA 
      1710       1720       1730       1740       1750
VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS ATKCIACQCP 
      1760       1770       1780       1790       1800
SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK 
      1810       1820       1830       1840       1850
CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS 
      1860       1870       1880       1890       1900
KFGNTEQGFK FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF 
      1910       1920       1930       1940       1950
GISEPGNQEK KSEKPLENGT GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL 
      1960       1970       1980       1990       2000
AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS SQYGKMANKA NTSGDFEKDD 
      2010       2020       2030       2040       2050
DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV KLFRFDAEVS 
      2060       2070       2080       2090       2100
QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG 
      2110       2120       2130       2140       2150
SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP 
      2160       2170       2180       2190       2200
LQTPHKLVDT GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG 
      2210       2220       2230       2240       2250
TGAAGASDTT IKPNPENTGP TLEWDNYDLR EDALDDSVSS SSVHASPLAS 
      2260       2270       2280       2290       2300
SPVRKNLFRF GESTTGFNFS FKSALSPSKS PAKLNQSGTS VGTDEESDVT 
      2310       2320       2330       2340       2350
QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY RYDKDVGQWK 
      2360       2370       2380       2390       2400
ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER 
      2410       2420       2430       2440       2450
VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT 
      2460       2470       2480       2490       2500
PHVSRSSTPR ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST 
      2510       2520       2530       2540       2550
SETTPKAVVS PPKFVFGSES VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN 
      2560       2570       2580       2590       2600
APLKSNNSET SSVAQSGSES KVEPKKCELS KNSDIEQSSD SKVKNLFASF 
      2610       2620       2630       2640       2650
PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP TAEQKALATK 
      2660       2670       2680       2690       2700
LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE 
      2710       2720       2730       2740       2750
ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG 
      2760       2770       2780       2790       2800
EDFQSELQKV QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT 
      2810       2820       2830       2840       2850
KSISSPSVSS ETMDKPVDLS TRKEIDTDST SQGESKIVSF GFGSSTGLSF 
      2860       2870       2880       2890       2900
ADLASSNSGD FAFGSKDKNF QWANTGAAVF GTQSVGTQSA GKVGEDEDGS 
      2910       2920       2930       2940       2950
DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL YRWDRDVSQW 
      2960       2970       2980       2990       3000
KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN 
      3010       3020       3030       3040       3050
NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG 
      3060       3070       3080       3090       3100
HVSLAAELSK ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC 
      3110       3120       3130       3140       3150
TGEKGFGFKN SIFHRVIPDF VCQGGDITKH DGTGGQSIYG DKFEDENFDV 
      3160       3170       3180       3190       3200
KHTGPGLLSM ANQGQNTNNS QFVITLKKAE HLDFKHVVFG FVKDGMDTVK 
      3210       3220 
KIESFGSPKG SVCRRITITE CGQI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 1171-1304, 2027-2154, 2324-2440, 2629-2693, 2925-3048, 3062-3224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111839. 103 interactions.
DIPiDIP-37654N.
IntActiP49792. 40 interactions.
MINTiMINT-191403.
STRINGi9606.ENSP00000283195.

PTM databases

PhosphoSiteiP49792.

Polymorphism databases

DMDMi83305554.

2D gel databases

OGPiP49792.

Proteomic databases

MaxQBiP49792.
PaxDbiP49792.
PeptideAtlasiP49792.
PRIDEiP49792.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5903.
GeneCardsiGC02P109335.
H-InvDBHIX0002358.
HGNCiHGNC:9848. RANBP2.
HPAiHPA018437.
HPA023960.
MIMi601181. gene.
608033. phenotype.
neXtProtiNX_P49792.
Orphaneti263524. Acute necrotizing encephalopathy of childhood.
88619. Familial acute necrotizing encephalopathy.
178342. Inflammatory myofibroblastic tumor.
PharmGKBiPA34209.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5171.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiP49792.
KOiK12172.
OMAiPGKQNQT.
OrthoDBiEOG7X0VG5.
PhylomeDBiP49792.
TreeFamiTF314797.

Enzyme and pathway databases

UniPathwayiUPA00886.
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_267668. Transcriptional regulation by small RNAs.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6354. Viral Messenger RNA Synthesis.
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

ChiTaRSiRANBP2. human.
EvolutionaryTraceiP49792.
GeneWikiiRANBP2.
GenomeRNAii5903.
NextBioi22964.
PROiP49792.
SOURCEiSearch...

Gene expression databases

BgeeiP49792.
CleanExiHS_RANBP2.
ExpressionAtlasiP49792. baseline and differential.
GenevestigatoriP49792.

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_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 171 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.