RANBP2
E3 SUMO-protein ligase RanBP2
Also known as: ADANE, ANE1, NUP358, RBP2_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P49792
- Gene
- RANBP2
- Ensembl
- ENSG00000153201
- Chromosome
- 2
- Canonical length
- 3224 aa
- Protein class
- Cancer-related genes, Disease related genes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Transporters
- Subcellular location
- Nucleoplasm,Nuclear membrane,Vesicles,Cytosol
OverviewNCBI Gene
RAN is a small GTP-binding protein of the RAS superfamily that is associated with the nuclear membrane and is thought to control a variety of cellular functions through its interactions with other proteins. This gene encodes a very large RAN-binding protein that immunolocalizes to the nuclear pore complex. The protein is a giant scaffold and mosaic cyclophilin-related nucleoporin implicated in the Ran-GTPase cycle. The encoded protein directly interacts with the E2 enzyme UBC9 and strongly enhances SUMO1 transfer from UBC9 to the SUMO1 target SP100. These findings place sumoylation at the cytoplasmic filaments of the nuclear pore complex and suggest that, for some substrates, modification and nuclear import are linked events. This gene is partially duplicated in a gene cluster that lies in a hot spot for recombination on chromosome 2q. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
3224 residues, UniProt reviewed canonical sequence.
>P49792|RANBP2
1 MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP
61 KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWLER
121 AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVEVYRSTKR
181 LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA
241 NLMLLTLSTR DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM
301 GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR LSQSGHMLLN
361 LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF LGSDDIGNID VREPELEDLT
421 RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL PGIRKWLKQL FHHLPHETSR LETNAPESIC
481 ILDLEVFLLG VVYTSHLQLK EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH
541 RKAVPGNVAK LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG
601 RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA HITFAILDAV
661 NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIK
721 IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM QELEDYSEGG PLYKNGSLRN ADSEIKHSTP
781 SPTRYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR
841 WPTENYGPDS VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
901 PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA TGILSPRGDD
961 YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE FGKTNFVQPM PGEGLRPSLP
1021 TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ VVTQPPPAAY SNSESLLGLL TSDKPLQGDG
1081 YSGAKPIPGG QTIGPRNTFN FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS
1141 VFGTPTLETA NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK
1201 LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP DMKLTPNAGS
1261 DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE AQSILKAPGT NVAMASNQAV
1321 RIVKEPTSHD NKDICKSDAG NLNFEFQVAK KEGSWWHCNS CSLKNASTAK KCVSCQNLNP
1381 SNKELVGPPL AETVFTPKTS PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN
1441 TKSANKSGSS FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA
1501 ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS SCLVRNEANA
1561 TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE GMFTKKEGQW DCSVCLVRNE
1621 ASATKCIACQ NPGKQNQTTS AVSTPASSET SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA
1681 SATKCIACQN PGKQNQTTSA VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS
1741 ATKCIACQCP SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK
1801 CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS KFGNTEQGFK
1861 FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF GISEPGNQEK KSEKPLENGT
1921 GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS
1981 SQYGKMANKA NTSGDFEKDD DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV
2041 KLFRFDAEVS QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG
2101 SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP LQTPHKLVDT
2161 GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG TGAAGASDTT IKPNPENTGP
2221 TLEWDNYDLR EDALDDSVSS SSVHASPLAS SPVRKNLFRF GESTTGFNFS FKSALSPSKS
2281 PAKLNQSGTS VGTDEESDVT QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY
2341 RYDKDVGQWK ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER
2401 VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT PHVSRSSTPR
2461 ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST SETTPKAVVS PPKFVFGSES
2521 VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN APLKSNNSET SSVAQSGSES KVEPKKCELS
2581 KNSDIEQSSD SKVKNLFASF PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP
2641 TAEQKALATK LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE
2701 ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG EDFQSELQKV
2761 QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT KSISSPSVSS ETMDKPVDLS
2821 TRKEIDTDST SQGESKIVSF GFGSSTGLSF ADLASSNSGD FAFGSKDKNF QWANTGAAVF
2881 GTQSVGTQSA GKVGEDEDGS DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL
2941 YRWDRDVSQW KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN
3001 NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG HVSLAAELSK
3061 ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC TGEKGFGFKN SIFHRVIPDF
3121 VCQGGDITKH DGTGGQSIYG DKFEDENFDV KHTGPGLLSM ANQGQNTNNS QFVITLKKAE
3181 HLDFKHVVFG FVKDGMDTVK KIESFGSPKG SVCRRITITE CGQILocalizationUniProt · AlphaFold · HPA
Whether an antibody against RANBP2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0
- Highest tissue expression
- 42 nTPM
Expression across tissuesHPA
Tissue
- bone marrow: 42 nTPM
- parathyroid gland: 32 nTPM
- epididymis: 30 nTPM
- skeletal muscle: 28 nTPM
- tongue: 28 nTPM
- thyroid gland: 27 nTPM
Single-cell type
- mast cells: 554 nCPM
- innate lymphoid cells: 547 nCPM
- pdcs: 537 nCPM
- neutrophils: 507 nCPM
- lactotrophs: 443 nCPM
- monocytes: 379 nCPM
Immune cell
- MAIT T-cell: 3.3 nTPM
- naive CD8 T-cell: 2.6 nTPM
- non-classical monocyte: 2.4 nTPM
- memory CD8 T-cell: 2.3 nTPM
- gdT-cell: 2.1 nTPM
- basophil: 2 nTPM
Brain region
- choroid plexus: 59 nTPM
- cerebral cortex: 51 nTPM
- cerebellum: 46 nTPM
- white matter: 42 nTPM
- basal ganglia: 40 nTPM
- hippocampal formation: 39 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about RANBP2.
Disease | AllUniProt
Conditions RANBP2 is implicated in, by any mechanism.
- Encephalopathy, acute, infection-induced, 3 (IIAE3) MIM:608033
Disease | GeneticClinVar
5 pathogenic / likely-pathogenic of 1,334 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Familial acute necrotizing encephalopathy
- See cases
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.14
- gnomAD pLI
- 1
- gnomAD missense Z
- -0.78
- DepMap mean gene effect
- -0.54
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- centrosome localization
- intracellular glucose homeostasis
- mRNA transport
- negative regulation of transcription by RNA polymerase II
- NLS-bearing protein import into nucleus
- nuclear export
- nucleocytoplasmic transport
- protein folding
- protein sumoylation
- regulation of gluconeogenesis
- response to amphetamine
Molecular functions
- kinase activator activity
- protein-containing complex binding
- protein-macromolecule adaptor activity
- RNA binding
- small GTPase binding
- SUMO ligase activity
- SUMO transferase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Ran binding domain
- Zinc finger, RanBP2-type
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain
- Tetratricopeptide-like helical domain superfamily
- PH-like domain superfamily
- Tetratricopeptide repeat
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site
- Cyclophilin-like domain superfamily
- Zinc finger, RanBP2-type superfamily
- Ran binding protein RanBP1-like
- Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
- RanBP1 domain
- Zn-finger in Ran binding protein and others
- Nup358/RanBP2 E3 ligase domain
- Nup358/RanBP2 E3 ligase domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of RANBP2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads RANBP2 as an antibody target. Whether an autoantibody or antibody against RANBP2 could matter depends on whether native RANBP2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
RANBP2 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label RANBP2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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