Ranbp2
entrez
19386
canonical
uniprot
Q9ERU9
canonical
ensembl
ENSMUSG00000003226
resolver
ensp
ENSMUSP00000003310
resolver
enst
ENSMUST00000003310
resolver
genesymbol
Ranbp2
resolver
uniprot
E9QM01
resolver
uniprot
Q61992
resolver
uniprot
Q8C9K9
resolver
uniprot_entry
RBP2_MOUSE
resolver
uniprot_sec
E9QM01
resolver
uniprot_sec
Q61992
resolver
uniprot_sec
Q8C9K9
resolver
amino_acid_sequence
MRRSKADVERYIASVQGSAPSPREKSMKGFYFAKLYYEAKEYDLAKKYISTYINVQERDPKAHRFLGLLYEVEENIDKAVECYKRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAIYKLKEQLLDCKGEDGWNKLFDLIQSELYARPDDIHVNIRLVELYRSNKRLKDAVAHCHEADRNTALRSSLEWNLCVVQTLKEYLESLQCLDSDKSTWRATNKDLLLAYANLMLLTLSTRDVQEGRELLESFDSALQSVKSSVGGNDELSATFLETKGHFYMHVGSLLLKMGQQSDIQWRALSELAALCYLVAFQVPRPKVKLIKGEAGQNLLETMAHDRLSQSGHMLLNLSRGKQDFLKEVVESFANKSGQSALCDALFSSQSSKERSFLGNDDIGNLDGQVPDPDDLARYDTGAVRAHNGSLQHLTWLGLQWNSLSTLPAIRKWLKQLFHHLPQETSRLETNAPESICILDLEVFLLGVIYTSHLQLKEKCNSHHTSYQPLCLPLPVCRQLCTERQKTWWDAVCTLIHRKALPGTSAKLRLLVQREINSLRGQEKHGLQPALLVHWAQSLQKTGSSLNSFYDQREYIGRSVHYWRKVLPLLKMIRKKNSIPEPIDPLFKHFHSVDIQASEIGEYEEDAHITFAILDAVNGNIEDAMTAFESIKNVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIRILDDSDSNTSVVQKLPVPLESVKEMLNSVMQELEDYSEGGTLYKNGCWRSADSELKHSTPSPTKYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSNNSASPHRWPAEPYGQDPAPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYSQQMHTPPVQSSSACMFSQEMYGPPLRFESPATGILSPRGDDYFNYNVQQTSTNPPLPEPGYFTKPPLVAHASRSAESKVIEFGKSNFVQPMQGEVIRPPLTTPAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVAQPPSTAYSNSESLLGLLTSDKPLQGDGYSGLKPISGQASGSRNTFSFGSKNTLTENMGPNQQKNFGFHRSDDMFAFHGPGKSVFTTAASELANKSHETDGGSAHGDEEDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQNILKALGTNTSTAPNHTLRIVKESATQDNKDICKADGGNLNFEFQIVKKEGPYWNCNSCSFKNAATAKKCVSCQNTNPTSNKELLGPPLVENGFAPKTGLENAQDRFATMTANKEGHWDCSVCLVRNEPTVSRCIACQNTKSASSFVQTSFKFGQGDLPKSVDSDFRSVFSKKEGQWECSVCLVRNERSAKKCVACENPGKQFKEWHCSLCSVKNEAHAIKCVACNNPVTPSLSTAPPSFKFGTSEMSKPFRIGFEGMFAKKEGQWDCSLCFVRNEASATHCIACQYPNKQNQPTSCVSAPASSETSRSPKSGFEGLFPKKEGEWECAVCSVQNESSSLKCVACEASKPTHKPHEAPSAFTVGSKSQSNESAGSQVGTEFKSNFPEKNFKVGISEQKFKFGHVDQEKTPSFAFQGGSNTEFKSIKDGFSFCIPVSADGFKFGIQEKGNQEKKSEKHLENDPSFQAHDTSGQKNGSGVVFGQTSSTFTFADLAKSTSREGFQFGKKDPNFKGFSGAGEKLFSSQSGKVAEKANTSSDLEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQVKVTDEENASSGADAPSASDTTAKQNPDNTGPALEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQSGASVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQTMKGTERVWVWTACDFADGERKIEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSHLSTPRESPCGKIAIAVLEETTRERTDLTQGDEVIDTTSEAGETSSTSETTPKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKNSNSEMTSRVQSGSEGKVKPDKCELPQNSDIKQSSDGKVKNLSAFSKENSSTSYTFKTPEKAQEKSKPEDLPSDNDILIVYELTPTPEQKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLNGKLYLDDSEKPLEENLADNDKECVIVWEKKPTVEERAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELRKVCEAQKSQNEKVTDRVGIEHIGETEVTNPVGCKSEEPDSDTKHSSSSPVSGTMDKPVDLSTRKETDMEFPSKGENKPVLFGFGSGTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQTTSKGGEDEDGSDEDVVHNEDIHFEPIVSLPEVEVKSGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRILMRRDQVFKVCANHVITKAMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQQNIIKLQNGHTSLAAELSKDTNPVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKGFGFKNSIFHRVVPDFICQGGDITKYNGTGGQSIYGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKGSVSRRICITECGQL
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
function
FUNCTION: 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. Inhibits EIF4E-dependent mRNA export. 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. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. {ECO:0000250|UniProtKB:P49792}.
uniprot
proteins
mass_dalton
341121
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein sumoylation.
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated by PRKN, which leads to proteasomal degradation. {ECO:0000250|UniProtKB:P49792}.; 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:0000269|PubMed:23641069}.
uniprot
proteins
protein_family
RanBP2 E3 ligase family
uniprot
proteins
pubmed
11353387
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16332688
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23641069
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
35771867
uniprot
proteins
pubmed
8603673
uniprot
proteins
sequence_length
3053
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49792}. Nucleus membrane {ECO:0000250|UniProtKB:P49792}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49792}. Nucleus envelope {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments. {ECO:0000250|UniProtKB:P49792}.
uniprot
proteins