RANBP2
entrez
5903
canonical
uniprot
P49792
canonical
ensembl
ENSG00000153201
resolver
ensp
ENSP00000283195
resolver
ensp
ENSP00000588042
resolver
enst
ENST00000283195
resolver
genesymbol
RANBP2
resolver
genesymbol_syn
NUP358
resolver
hgnc
HGNC:9848
resolver
uniprot
Q13074
resolver
uniprot
Q15280
resolver
uniprot
Q53TE2
resolver
uniprot
Q59FH7
resolver
uniprot_entry
RBP2_HUMAN
resolver
uniprot_sec
Q13074
resolver
uniprot_sec
Q15280
resolver
uniprot_sec
Q53TE2
resolver
uniprot_sec
Q59FH7
resolver
amino_acid_sequence
MRRSKADVERYIASVQGSTPSPRQKSMKGFYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEDGWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLQSFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKMGQHSSNVQWRALSELAALCYLIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLNLSRGKQDFLKEIVETFANKSGQSALYDALFSSQSPKDTSFLGSDDIGNIDVREPELEDLTRYDVGAIRAHNGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPHETSRLETNAPESICILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIHRKAVPGNVAKLRLLVQHEINTLRAQEKHGLQPALLVHWAECLQKTGSGLNSFYDQREYIGRSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQASEIVEYEEDAHITFAILDAVNGNIEDAVTAFESIKSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIKIIDDSDSNLSVVKKLPVPLESVKEMLNSVMQELEDYSEGGPLYKNGSLRNADSEIKHSTPSPTRYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHRWPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDDYFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLPTQAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDGYSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQKNSGFRRSDDMFTFHGPGKSVFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSILKAPGTNVAMASNQAVRIVKEPTSHDNKDICKSDAGNLNFEFQVAKKEGSWWHCNSCSLKNASTAKKCVSCQNLNPSNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQNTKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCAACQNPRKQSLPATSIPTPASFKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANATRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQNPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQNPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEASATKCIACQCPSKQNQTTAISTPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLKCVACDASKPTHKPIAEAPSAFTLGSEMKLHDSSGSQVGTGFKSNFSEKASKFGNTEQGFKFGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENGTGFQAQDISGQKNGRGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFSSQYGKMANKANTSGDFEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGPTLEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPRESPCGKIAVAVLEETTRERTDVIQGDDVADATSEVEVSSTSETTPKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKSNNSETSSVAQSGSESKVEPKKCELSKNSDIEQSSDSKVKNLFASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTPTAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLDGSEKCRPLEENTADNEKECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKVQEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSITKSISSPSVSSETMDKPVDLSTRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQKGHVSLAAELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITITECGQI
uniprot
proteins
disease_involvement
DISEASE: Encephalopathy, acute, infection-induced, 3 (IIAE3) [MIM:608033]: A rapidly progressive encephalopathy manifesting in susceptible individuals with seizures and coma. It can occur within days in otherwise healthy children after common viral infections such as influenza and parainfluenza, without evidence of viral infection of the brain or inflammatory cell infiltration. Brain T2-weighted magnetic resonance imaging reveals characteristic symmetric lesions present in the thalami, pons and brainstem. {ECO:0000269|PubMed:19118815, ECO:0000269|PubMed:34400285}. Note=The disease is caused by variants 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). {ECO:0000269|PubMed:19118815}.; DISEASE: Note=A chromosomal aberration involving RANBP2 is a cause of chromosome 8p11 myeloproliferative syndrome. Translocation t(2;8)(q12;p11) with FGFR1. Chromosome 8p11 myeloproliferative syndrome is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. {ECO:0000269|PubMed:23041776}.
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
function
FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I (PubMed:11792325, PubMed:12032081, PubMed:15378033, PubMed:15931224, PubMed:22194619). 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 (PubMed:7775481). Binds single-stranded RNA (in vitro) (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the nuclear export pathway (PubMed:10078529). Specific docking site for the nuclear export factor exportin-1 (PubMed:10078529). Inhibits EIF4E-dependent mRNA export (PubMed:22902403). Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB (PubMed:22155184). 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). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357, PubMed:23353830). {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:22194619, ECO:0000269|PubMed:22902403, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7775481, ECO:0000303|PubMed:10078529}.
uniprot
proteins
mass_dalton
358199
uniprot
proteins
mutagenesis
MUTAGEN 2632; /note="V->K: Abolishes interaction with sumoylated RANGAP1."; /evidence="ECO:0000269|PubMed:15388847"; MUTAGEN 2634; /note="I->K: Abolishes interaction with sumoylated RANGAP1."; /evidence="ECO:0000269|PubMed:15388847"; MUTAGEN 2635; /note="V->K: Abolishes interaction with sumoylated RANGAP1."; /evidence="ECO:0000269|PubMed:15388847"; MUTAGEN 2640; /note="P->A: No effect on SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2645; /note="K->A: No effect on SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2651; /note="L->A: Abolishes binding to UBE2I and SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2652; /note="K->A: No effect on SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2653; /note="L->A: Abolishes binding to UBE2I and SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2654; /note="P->A: Impairs SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2655; /note="P->A: No effect on SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2656; /note="T->A: Impairs SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2657; /note="F->A: Abolishes binding to UBE2I and SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2658; /note="F->A: Abolishes binding to UBE2I and SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2659; /note="C->S,A: Impairs SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2676; /note="D->A: Impairs SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2677; /note="F->A: Impairs SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033"; MUTAGEN 2689; /note="Y->A: Impairs SUMOE3 ligase activity."; /evidence="ECO:0000269|PubMed:15378033
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein sumoylation.
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated by PRKN, which leads to proteasomal degradation. {ECO:0000269|PubMed:16332688}.; PTM: 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. {ECO:0000250|UniProtKB:Q9ERU9}.
uniprot
proteins
protein_family
RanBP2 E3 ligase family
uniprot
proteins
pubmed
10078529
uniprot
proteins
pubmed
11792325
uniprot
proteins
pubmed
11839768
uniprot
proteins
pubmed
12032081
uniprot
proteins
pubmed
14729961
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15378033
uniprot
proteins
pubmed
15388847
uniprot
proteins
pubmed
15608651
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15826666
uniprot
proteins
pubmed
15931224
uniprot
proteins
pubmed
16332688
uniprot
proteins
pubmed
16620772
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18946085
uniprot
proteins
pubmed
19118815
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20005110
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20386726
uniprot
proteins
pubmed
20676357
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22155184
uniprot
proteins
pubmed
22194619
uniprot
proteins
pubmed
22902403
uniprot
proteins
pubmed
22959972
uniprot
proteins
pubmed
23041776
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23353830
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
32690953
uniprot
proteins
pubmed
34400285
uniprot
proteins
pubmed
7603572
uniprot
proteins
pubmed
7724562
uniprot
proteins
pubmed
7775481
uniprot
proteins
sequence_length
3224
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7775481}. Nucleus membrane {ECO:0000269|PubMed:11839768}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7603572}. Nucleus envelope {ECO:0000269|PubMed:20386726}. Note=Detected in diffuse and discrete intranuclear foci (PubMed:11839768). Cytoplasmic filaments (PubMed:7775481). {ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:7775481}.
uniprot
proteins