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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 sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1351 – 1381RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1415 – 1444RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1479 – 1508RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1543 – 1572RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1606 – 1635RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1665 – 1694RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1724 – 1753RanBP2-type 7PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1781 – 1810RanBP2-type 8PROSITE-ProRule annotationAdd BLAST30

GO - Molecular functioni

GO - Biological processi

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

BioCyciZFISH:ENSG00000153201-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-68877. Mitotic Prometaphase.
UniPathwayiUPA00886.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9848. RANBP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic periphery of the nuclear pore complex Source: Ensembl
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • microtubule associated complex Source: GO_Central
  • mitochondrion Source: GO_Central
  • nuclear envelope Source: Reactome
  • nuclear inclusion body Source: UniProtKB
  • nuclear membrane Source: UniProtKB
  • nuclear pore Source: UniProtKB
  • nuclear pore cytoplasmic filaments Source: GO_Central
  • 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, 3 (IIAE3)1 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).1 Publication
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_054997585T → M in IIAE3. 1 PublicationCorresponds to variant rs121434502dbSNPEnsembl.1
Natural variantiVAR_054998653T → I in IIAE3. 1 PublicationCorresponds to variant rs121434503dbSNPEnsembl.1
Natural variantiVAR_054999656I → V in IIAE3. 1 PublicationCorresponds to variant rs121434504dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2632V → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication1
Mutagenesisi2634I → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication1
Mutagenesisi2635V → K: Abolishes interaction with sumoylated RANGAP1. 1 Publication1
Mutagenesisi2640P → A: No effect on SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2645K → A: No effect on SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2651L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2652K → A: No effect on SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2653L → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2654P → A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2655P → A: No effect on SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2656T → A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2657F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2658F → A: Abolishes binding to UBE2I and SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2659C → S or A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2676D → A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2677F → A: Impairs SUMO E3 ligase activity. 1 Publication1
Mutagenesisi2689Y → A: Impairs SUMO E3 ligase activity. 1 Publication1

Organism-specific databases

DisGeNETi5903.
MalaCardsiRANBP2.
MIMi608033. phenotype.
OpenTargetsiENSG00000153201.
Orphaneti263524. Acute necrotizing encephalopathy of childhood.
88619. Familial acute necrotizing encephalopathy.
178342. Inflammatory myofibroblastic tumor.
PharmGKBiPA34209.

Polymorphism and mutation databases

BioMutaiRANBP2.
DMDMi83305554.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002049131 – 3224E3 SUMO-protein ligase RanBP2Add BLAST3224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19PhosphothreonineCombined sources1
Modified residuei21PhosphoserineCombined sources1
Modified residuei779PhosphothreonineCombined sources1
Modified residuei781PhosphoserineCombined sources1
Modified residuei788PhosphoserineBy similarity1
Modified residuei837PhosphoserineCombined sources1
Modified residuei945Asymmetric dimethylarginineCombined sources1
Modified residuei948PhosphoserineCombined sources1
Modified residuei955PhosphoserineCombined sources1
Modified residuei1016Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei1016Omega-N-methylarginine; alternateCombined sources1
Modified residuei1098PhosphothreonineCombined sources1
Modified residuei1103PhosphoserineCombined sources1
Modified residuei1107PhosphoserineCombined sources1
Modified residuei1110PhosphoserineCombined sources1
Modified residuei1144PhosphothreonineCombined sources1
Modified residuei1160PhosphoserineCombined sources1
Modified residuei1249PhosphoserineCombined sources1
Modified residuei1396PhosphothreonineCombined sources1
Modified residuei1412PhosphothreonineCombined sources1
Cross-linki1414Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1443PhosphoserineCombined sources1
Modified residuei1450PhosphoserineCombined sources1
Modified residuei1456PhosphoserineCombined sources1
Modified residuei1509PhosphoserineCombined sources1
Modified residuei1520PhosphoserineCombined sources1
Modified residuei1573PhosphoserineCombined sources1
Cross-linki1605Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1605Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1664Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1723Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1833PhosphoserineCombined sources1
Modified residuei1835PhosphoserineCombined sources1
Modified residuei1869PhosphoserineCombined sources1
Modified residuei1871PhosphoserineCombined sources1
Modified residuei1977N6-acetyllysineBy similarity1
Modified residuei2005PhosphothreonineBy similarity1
Modified residuei2008PhosphoserineBy similarity1
Modified residuei2153PhosphothreonineBy similarity1
Modified residuei2246PhosphoserineBy similarity1
Modified residuei2251PhosphoserineBy similarity1
Modified residuei2270PhosphoserineCombined sources1
Modified residuei2280PhosphoserineBy similarity1
Modified residuei2290PhosphoserineBy similarity1
Modified residuei2293PhosphothreonineBy similarity1
Modified residuei2297PhosphoserineBy similarity1
Modified residuei2462PhosphoserineBy similarity1
Modified residuei2493PhosphoserineBy similarity1
Modified residuei2510PhosphoserineBy similarity1
Modified residuei2526PhosphoserineCombined sources1
Cross-linki2592Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki2594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2613PhosphothreonineCombined sources1
Modified residuei2666PhosphotyrosineCombined sources1
Modified residuei2668PhosphoserineCombined sources1
Modified residuei2741PhosphoserineCombined sources1
Modified residuei2743PhosphothreonineCombined sources1
Cross-linki2792Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2805PhosphoserineCombined sources1
Modified residuei2900PhosphoserineCombined sources1
Modified residuei3207PhosphoserineCombined sources1

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, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49792.
MaxQBiP49792.
PaxDbiP49792.
PeptideAtlasiP49792.
PRIDEiP49792.

2D gel databases

OGPiP49792.

PTM databases

iPTMnetiP49792.
PhosphoSitePlusiP49792.
SwissPalmiP49792.

Expressioni

Gene expression databases

BgeeiENSG00000153201.
CleanExiHS_RANBP2.
ExpressionAtlasiP49792. baseline and differential.
GenevisibleiP49792. HS.

Organism-specific databases

HPAiCAB034063.
HPA018437.
HPA023960.
HPA049497.
HPA051675.

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

GO - Molecular functioni

  • Ran GTPase binding Source: GO_Central

Protein-protein interaction databases

BioGridi111839. 146 interactors.
DIPiDIP-37654N.
IntActiP49792. 62 interactors.
MINTiMINT-191403.
STRINGi9606.ENSP00000283195.

Structurei

Secondary structure

13224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 18Combined sources14
Helixi22 – 26Combined sources5
Helixi29 – 38Combined sources10
Helixi42 – 55Combined sources14
Helixi60 – 72Combined sources13
Helixi76 – 89Combined sources14
Helixi94 – 107Combined sources14
Helixi112 – 124Combined sources13
Helixi129 – 141Combined sources13
Beta strandi1191 – 1205Combined sources15
Turni1206 – 1209Combined sources4
Beta strandi1210 – 1224Combined sources15
Turni1225 – 1227Combined sources3
Beta strandi1230 – 1236Combined sources7
Turni1237 – 1239Combined sources3
Beta strandi1242 – 1247Combined sources6
Beta strandi1255 – 1257Combined sources3
Beta strandi1260 – 1270Combined sources11
Beta strandi1277 – 1284Combined sources8
Helixi1288 – 1302Combined sources15
Beta strandi2028 – 2030Combined sources3
Beta strandi2032 – 2046Combined sources15
Turni2047 – 2050Combined sources4
Beta strandi2051 – 2065Combined sources15
Beta strandi2071 – 2077Combined sources7
Turni2078 – 2081Combined sources4
Beta strandi2082 – 2088Combined sources7
Beta strandi2095 – 2097Combined sources3
Beta strandi2105 – 2111Combined sources7
Beta strandi2113 – 2115Combined sources3
Beta strandi2117 – 2125Combined sources9
Helixi2129 – 2145Combined sources17
Turni2146 – 2148Combined sources3
Beta strandi2632 – 2637Combined sources6
Helixi2642 – 2650Combined sources9
Helixi2657 – 2661Combined sources5
Beta strandi2663 – 2665Combined sources3
Helixi2677 – 2682Combined sources6
Turni2683 – 2686Combined sources4
Beta strandi2710 – 2712Combined sources3
Turni2926 – 2929Combined sources4
Beta strandi2930 – 2944Combined sources15
Turni2945 – 2948Combined sources4
Beta strandi2949 – 2963Combined sources15
Turni2964 – 2967Combined sources4
Beta strandi2968 – 2974Combined sources7
Turni2976 – 2978Combined sources3
Beta strandi2981 – 2986Combined sources6
Beta strandi2994 – 2996Combined sources3
Beta strandi3000 – 3009Combined sources10
Beta strandi3016 – 3026Combined sources11
Helixi3027 – 3047Combined sources21
Beta strandi3065 – 3072Combined sources8
Beta strandi3075 – 3084Combined sources10
Turni3086 – 3088Combined sources3
Helixi3090 – 3101Combined sources12
Turni3102 – 3104Combined sources3
Beta strandi3112 – 3117Combined sources6
Turni3118 – 3120Combined sources3
Beta strandi3121 – 3124Combined sources4
Turni3127 – 3129Combined sources3
Beta strandi3130 – 3133Combined sources4
Beta strandi3157 – 3160Combined sources4
Beta strandi3168 – 3170Combined sources3
Beta strandi3172 – 3177Combined sources6
Helixi3180 – 3182Combined sources3
Turni3183 – 3185Combined sources3
Beta strandi3188 – 3194Combined sources7
Helixi3196 – 3203Combined sources8
Beta strandi3216 – 3223Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RRPX-ray2.96B/D1171-1304[»]
1XKENMR-A2028-2154[»]
1Z5SX-ray3.01D2631-2711[»]
2LASNMR-B2705-2717[»]
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[»]
5CLLX-ray2.45B/D1155-1321[»]
5CLQX-ray3.20B/D1155-1321[»]
ProteinModelPortaliP49792.
SMRiP49792.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49792.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati26 – 59TPR 1PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati60 – 93TPR 2PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati94 – 128TPR 3PROSITE-ProRule annotation1 PublicationAdd BLAST35
Repeati165 – 201TPR 4PROSITE-ProRule annotation1 PublicationAdd BLAST37
Repeati287 – 319TPR 5PROSITE-ProRule annotation1 PublicationAdd BLAST33
Repeati583 – 616TPR 6PROSITE-ProRule annotation1 PublicationAdd BLAST34
Repeati648 – 681TPR 7PROSITE-ProRule annotation1 PublicationAdd BLAST34
Domaini1171 – 1307RanBD1 1PROSITE-ProRule annotationAdd BLAST137
Domaini2012 – 2148RanBD1 2PROSITE-ProRule annotationAdd BLAST137
Domaini2309 – 2445RanBD1 3PROSITE-ProRule annotationAdd BLAST137
Repeati2633 – 268511 PublicationAdd BLAST53
Repeati2711 – 276121 PublicationAdd BLAST51
Domaini2911 – 3046RanBD1 4PROSITE-ProRule annotationAdd BLAST136
Domaini3067 – 3223PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2631 – 2635Interaction with sumoylated RANGAP15
Regioni2633 – 27612 X 50 AA approximate repeatsAdd BLAST129
Regioni2633 – 2710Required for E3 SUMO-ligase activityAdd BLAST78
Regioni2633 – 2685Interaction with UBE2IAdd BLAST53
Regioni2686 – 2761Interaction with SUMO11 PublicationAdd BLAST76

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)DescriptionActionsGraphical viewLength
Zinc fingeri1351 – 1381RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri1415 – 1444RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1479 – 1508RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1543 – 1572RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1606 – 1635RanBP2-type 5PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1665 – 1694RanBP2-type 6PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1724 – 1753RanBP2-type 7PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri1781 – 1810RanBP2-type 8PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat, TPR repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0864. Eukaryota.
KOG0865. Eukaryota.
COG0652. LUCA.
COG5171. LUCA.
GeneTreeiENSGT00840000129823.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiP49792.
KOiK12172.
OMAiPGKQNQT.
OrthoDBiEOG091G0BGL.
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_dom-like.
IPR000156. Ran_bind_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF12185. IR1-M. 2 hits.
PF00160. Pro_isomerase. 1 hit.
PF00638. Ran_BP1. 4 hits.
PF00641. zf-RanBP. 8 hits.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00160. RanBD. 4 hits.
SM00028. TPR. 1 hit.
SM00547. ZnF_RBZ. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50729. SSF50729. 4 hits.
SSF50891. SSF50891. 1 hit.
SSF90209. SSF90209. 7 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti777H → R in AAC41758 (PubMed:7775481).Curated1
Sequence conflicti2207S → A in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2210T → P in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2216E → V in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2436F → C in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2475T → P in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2531K → N in AAA85838 (PubMed:7724562).Curated1
Sequence conflicti2545F → C (PubMed:7724562).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029765548V → L.Corresponds to variant rs1057954dbSNPEnsembl.1
Natural variantiVAR_029766580E → K.Corresponds to variant rs4012065dbSNPEnsembl.1
Natural variantiVAR_029767581C → Y.Corresponds to variant rs1057957dbSNPEnsembl.1
Natural variantiVAR_054997585T → M in IIAE3. 1 PublicationCorresponds to variant rs121434502dbSNPEnsembl.1
Natural variantiVAR_054998653T → I in IIAE3. 1 PublicationCorresponds to variant rs121434503dbSNPEnsembl.1
Natural variantiVAR_054999656I → V in IIAE3. 1 PublicationCorresponds to variant rs121434504dbSNPEnsembl.1
Natural variantiVAR_050575725S → G.Corresponds to variant rs17414315dbSNPEnsembl.1
Natural variantiVAR_023939784R → K.1 PublicationCorresponds to variant rs2912838dbSNPEnsembl.1
Natural variantiVAR_0297681870P → L.Corresponds to variant rs2889846dbSNPEnsembl.1
Natural variantiVAR_0148861892P → A.Corresponds to variant rs12770dbSNPEnsembl.1
Natural variantiVAR_0505761892P → R.Corresponds to variant rs12770dbSNPEnsembl.1

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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RRPX-ray2.96B/D1171-1304[»]
1XKENMR-A2028-2154[»]
1Z5SX-ray3.01D2631-2711[»]
2LASNMR-B2705-2717[»]
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[»]
5CLLX-ray2.45B/D1155-1321[»]
5CLQX-ray3.20B/D1155-1321[»]
ProteinModelPortaliP49792.
SMRiP49792.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111839. 146 interactors.
DIPiDIP-37654N.
IntActiP49792. 62 interactors.
MINTiMINT-191403.
STRINGi9606.ENSP00000283195.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP49792.
PhosphoSitePlusiP49792.
SwissPalmiP49792.

Polymorphism and mutation databases

BioMutaiRANBP2.
DMDMi83305554.

2D gel databases

OGPiP49792.

Proteomic databases

EPDiP49792.
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.
DisGeNETi5903.
GeneCardsiRANBP2.
H-InvDBHIX0002358.
HGNCiHGNC:9848. RANBP2.
HPAiCAB034063.
HPA018437.
HPA023960.
HPA049497.
HPA051675.
MalaCardsiRANBP2.
MIMi601181. gene.
608033. phenotype.
neXtProtiNX_P49792.
OpenTargetsiENSG00000153201.
Orphaneti263524. Acute necrotizing encephalopathy of childhood.
88619. Familial acute necrotizing encephalopathy.
178342. Inflammatory myofibroblastic tumor.
PharmGKBiPA34209.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0864. Eukaryota.
KOG0865. Eukaryota.
COG0652. LUCA.
COG5171. LUCA.
GeneTreeiENSGT00840000129823.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiP49792.
KOiK12172.
OMAiPGKQNQT.
OrthoDBiEOG091G0BGL.
PhylomeDBiP49792.
TreeFamiTF314797.

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciZFISH:ENSG00000153201-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-191859. snRNP Assembly.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-68877. Mitotic Prometaphase.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000153201.
CleanExiHS_RANBP2.
ExpressionAtlasiP49792. baseline and differential.
GenevisibleiP49792. HS.

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_dom-like.
IPR000156. Ran_bind_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF12185. IR1-M. 2 hits.
PF00160. Pro_isomerase. 1 hit.
PF00638. Ran_BP1. 4 hits.
PF00641. zf-RanBP. 8 hits.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00160. RanBD. 4 hits.
SM00028. TPR. 1 hit.
SM00547. ZnF_RBZ. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50729. SSF50729. 4 hits.
SSF50891. SSF50891. 1 hit.
SSF90209. SSF90209. 7 hits.
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...

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: November 30, 2016
This is version 192 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

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 one 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.