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UniProtKB - 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. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle (PubMed:20386726).6 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

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionLigase, RNA-binding
Biological processmRNA transport, Protein transport, Translocation, Transport, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

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-4551638. SUMOylation of chromatin organization proteins.
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9848. RANBP2.

Subcellular locationi

GO - Cellular componenti

  • annulate lamellae Source: UniProtKB
  • centrosome Source: GO_Central
  • cytoplasm Source: GO_Central
  • cytoplasmic periphery of the nuclear pore complex Source: Ensembl
  • cytosol Source: Reactome
  • host cell Source: GOC
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nuclear envelope Source: UniProtKB
  • 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 dbSNP:rs121434502Ensembl.1
Natural variantiVAR_054998653T → I in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434503Ensembl.1
Natural variantiVAR_054999656I → V in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434504Ensembl.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
Cross-linki1350Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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-linki1596Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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-linki1655Glycyl 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-linki1714Glycyl 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
Cross-linki2022Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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
Cross-linki2522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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
Cross-linki2594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki2612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)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
Cross-linki2815Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2900PhosphoserineCombined sources1
Modified residuei3207PhosphoserineCombined sources1

Post-translational modificationi

Polyubiquitinated by PRKN, 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.
HPA067564.

Interactioni

Subunit structurei

Forms a tight complex with RANBP1 and UBE2I. Interacts with SUMO1 but not SUMO2. Interacts with PRKN. Interacts with sumoylated RANGAP1. Interacts with CDCA8. Interacts with PML (isoform PML-4). Interacts with BICD2 (PubMed:20386726).8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein complex binding Source: Ensembl
  • Ran GTPase binding Source: GO_Central
Complete GO annotation...

Protein-protein interaction databases

BioGridi111839. 153 interactors.
DIPiDIP-37654N.
IntActiP49792. 63 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
Regioni2147 – 2287Interaction with BICD21 PublicationAdd BLAST141
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

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.
GeneTreeiENSGT00880000137938.
HOGENOMiHOG000089994.
HOVERGENiHBG092361.
InParanoidiP49792.
KOiK12172.
OMAiTKKEGQW.
OrthoDBiEOG091G0BGL.
PhylomeDBiP49792.
TreeFamiTF314797.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.30.29.30. 4 hits.
2.40.100.10. 1 hit.
InterProiView protein in InterPro
IPR029000. 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.
PfamiView protein in Pfam
PF12185. IR1-M. 2 hits.
PF00160. Pro_isomerase. 1 hit.
PF00638. Ran_BP1. 4 hits.
PF00641. zf-RanBP. 8 hits.
PRINTSiPR00153. CSAPPISMRASE.
SMARTiView protein in SMART
SM00160. RanBD. 4 hits.
SM00028. TPR. 1 hit.
SM00547. ZnF_RBZ. 8 hits.
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50729. SSF50729. 4 hits.
SSF50891. SSF50891. 1 hit.
SSF90209. SSF90209. 7 hits.
PROSITEiView protein in PROSITE
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.

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 dbSNP:rs1057954Ensembl.1
Natural variantiVAR_029766580E → K. Corresponds to variant dbSNP:rs4012065Ensembl.1
Natural variantiVAR_029767581C → Y. Corresponds to variant dbSNP:rs1057957Ensembl.1
Natural variantiVAR_054997585T → M in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434502Ensembl.1
Natural variantiVAR_054998653T → I in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434503Ensembl.1
Natural variantiVAR_054999656I → V in IIAE3. 1 PublicationCorresponds to variant dbSNP:rs121434504Ensembl.1
Natural variantiVAR_050575725S → G. Corresponds to variant dbSNP:rs17414315Ensembl.1
Natural variantiVAR_023939784R → K1 PublicationCorresponds to variant dbSNP:rs2912838Ensembl.1
Natural variantiVAR_0297681870P → L. Corresponds to variant dbSNP:rs2889846Ensembl.1
Natural variantiVAR_0148861892P → A. Corresponds to variant dbSNP:rs12770Ensembl.1
Natural variantiVAR_0505761892P → R. Corresponds to variant dbSNP:rs12770Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiRBP2_HUMAN
AccessioniPrimary (citable) accession number: P49792
Secondary accession number(s): Q13074
, Q15280, Q53TE2, Q59FH7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 6, 2005
Last modified: August 30, 2017
This is version 200 of the entry and version 2 of the sequence. See 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