Q9ERU9 · RBP2_MOUSE

  • Protein
    E3 SUMO-protein ligase RanBP2
  • Gene
    Ranbp2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

Caution

Despite the presence of a PPIase cyclophilin-type domain, it has probably no peptidyl-prolyl cis-trans isomerase activity.

Pathway

Protein modification; protein sumoylation.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentannulate lamellae
Cellular Componentcytoplasm
Cellular Componentcytoplasmic periphery of the nuclear pore complex
Cellular Componentnuclear envelope
Cellular Componentnuclear inclusion body
Cellular Componentnuclear membrane
Cellular Componentnuclear pore
Cellular Componentnuclear pore cytoplasmic filaments
Cellular Componentnuclear pore nuclear basket
Cellular Componentnucleoplasm
Cellular ComponentSUMO ligase complex
Molecular Functionmetal ion binding
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Molecular Functionprotein-containing complex binding
Molecular FunctionRNA binding
Molecular Functionsmall GTPase binding
Molecular FunctionSUMO ligase activity
Molecular FunctionSUMO transferase activity
Biological Processcentrosome localization
Biological ProcessmRNA transport
Biological ProcessNLS-bearing protein import into nucleus
Biological Processnuclear export
Biological Processnucleocytoplasmic transport
Biological Processprotein folding
Biological Processprotein sumoylation
Biological Processregulation of gluconeogenesis
Biological Processresponse to amphetamine

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 SUMO-protein ligase RanBP2
  • EC number
  • Alternative names
    • Ran-binding protein 2 (RanBP2)

Gene names

    • Name
      Ranbp2

Organism names

  • Taxonomic identifier
  • Strains
    • 129/Ola
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9ERU9
  • Secondary accessions
    • E9QM01
    • Q61992
    • Q8C9K9

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00002049141-3053E3 SUMO-protein ligase RanBP2
Modified residue21Phosphoserine
Modified residue779Phosphothreonine
Modified residue781Phosphoserine
Modified residue788Phosphoserine
Modified residue837Phosphoserine
Modified residue944Asymmetric dimethylarginine
Modified residue947Phosphoserine
Modified residue954Phosphoserine
Modified residue1015Asymmetric dimethylarginine; alternate
Modified residue1015Omega-N-methylarginine; alternate
Modified residue1096Phosphothreonine
Modified residue1101Phosphoserine
Modified residue1138Phosphothreonine
Modified residue1154Phosphoserine
Modified residue1243Phosphoserine
Cross-link1344Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1407Phosphothreonine
Modified residue1438Phosphoserine
Modified residue1441Phosphoserine
Modified residue1446Phosphoserine
Modified residue1528Phosphoserine
Cross-link1557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link1557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link1607Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link1616Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue1670Phosphoserine
Modified residue1706Phosphoserine
Modified residue1814N6-acetyllysine
Modified residue1842Phosphothreonine
Modified residue1845Phosphoserine
Cross-link1859Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1990Phosphothreonine
Modified residue2083Phosphoserine
Modified residue2088Phosphoserine
Modified residue2107Phosphoserine
Modified residue2117Phosphoserine
Modified residue2127Phosphoserine
Modified residue2130Phosphothreonine
Modified residue2134Phosphoserine
Modified residue2299Phosphoserine
Modified residue2330Phosphoserine
Modified residue2348Phosphoserine
Cross-link2360Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue2364Phosphoserine
Cross-link2430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-link2432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link2432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link2449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue2450Phosphothreonine
Modified residue2503Phosphotyrosine
Modified residue2505Phosphoserine
Modified residue2576Phosphoserine
Modified residue2578Phosphothreonine
Cross-link2627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue2640Phosphoserine
Cross-link2649Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue2729Phosphoserine
Modified residue3036Phosphoserine

Post-translational modification

Polyubiquitinated by PRKN, which leads to proteasomal degradation.
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.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Part of the nuclear pore complex (By similarity).
Forms a complex with NXT1, NXF1 and RANGAP1 (By similarity).
Forms a tight complex with RANBP1 and UBE2I (By similarity).
Interacts with SUMO1 but not SUMO2 (By similarity).
Interacts with sumoylated RANGAP1 (By similarity).
Interacts with CDCA8 (By similarity).
Interacts with PML (By similarity).
Interacts with BICD2 (By similarity).
Interacts with PRKN (PubMed:16332688).
Interacts with MCM3AP (By similarity).
Interacts with COX11 (By similarity).
Interacts with synaptic plasticity regulator PANTS (PubMed:35771867).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9ERU9Prkn Q9WVS62EBI-643756, EBI-973635

Protein-protein interaction databases

Miscellaneous

Structure

3D structure databases

Family & Domains

Features

Showing features for repeat, compositional bias, region, domain, zinc finger.

TypeIDPosition(s)Description
Repeat26-59TPR 1
Repeat60-93TPR 2
Repeat94-128TPR 3
Repeat165-201TPR 4
Repeat288-319TPR 5
Repeat583-616TPR 6
Repeat648-681TPR 7
Compositional bias773-795Polar residues
Region773-802Disordered
Repeat1000-10011
Region1000-303520 X 2 AA repeats of F-G
Repeat1099-11002
Repeat1117-11183
Region1147-1171Disordered
Compositional bias1149-1168Basic and acidic residues
Domain1165-1301RanBD1 1
Zinc finger1345-1375RanBP2-type 1
Zinc finger1410-1439RanBP2-type 2
Repeat1449-14504
Zinc finger1469-1498RanBP2-type 3
Zinc finger1494-1527RanBP2-type 4
Repeat1538-15395
Zinc finger1558-1587RanBP2-type 5
Compositional bias1587-1607Polar residues
Region1587-1609Disordered
Zinc finger1617-1646RanBP2-type 6
Region1648-1675Disordered
Compositional bias1656-1675Polar residues
Repeat1696-16976
Repeat1737-17387
Compositional bias1744-1758Basic and acidic residues
Region1744-1772Disordered
Repeat1775-17768
Repeat1798-17999
Region1819-1846Disordered
Compositional bias1828-1846Basic and acidic residues
Domain1849-1985RanBD1 2
Region1984-2124Interaction with BICD2
Compositional bias2030-2057Polar residues
Region2030-2060Disordered
Repeat2097-209810
Compositional bias2111-2132Polar residues
Region2111-2144Disordered
Domain2146-2282RanBD1 3
Region2316-2348Disordered
Compositional bias2323-2345Polar residues
Repeat2354-235511
Repeat2373-237412
Repeat2383-238413
Region2394-2430Disordered
Region2443-2463Disordered
Region2468-2472Interaction with sumoylated RANGAP1
Repeat2470-25221
Region2470-2522Interaction with UBE2I
Region2470-2545Required for E3 SUMO-ligase activity
Region2470-25962 X 50 AA approximate repeats
Region2523-2596Interaction with SUMO1
Repeat2546-25962
Compositional bias2598-2615Basic and acidic residues
Region2598-2666Disordered
Compositional bias2651-2665Basic and acidic residues
Repeat2674-267514
Repeat2676-267715
Repeat2697-269816
Repeat2714-271517
Domain2740-2875RanBD1 4
Domain2896-3052PPIase cyclophilin-type
Repeat2935-293618
Repeat3018-301919
Repeat3034-303520

Domain

Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited.
The PPIase cyclophilin-type domain has high structural similarity with PPIA, but has extremely low and barely detectable proline isomerase activity (in vitro) (By similarity).
Only about half of the residues that surround the PPIA active site cleft are conserved

Sequence similarities

Belongs to the RanBP2 E3 ligase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    3,053
  • Mass (Da)
    341,121
  • Last updated
    2011-07-27 v2
  • Checksum
    62FD4249DEE466AE
MRRSKADVERYIASVQGSAPSPREKSMKGFYFAKLYYEAKEYDLAKKYISTYINVQERDPKAHRFLGLLYEVEENIDKAVECYKRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAIYKLKEQLLDCKGEDGWNKLFDLIQSELYARPDDIHVNIRLVELYRSNKRLKDAVAHCHEADRNTALRSSLEWNLCVVQTLKEYLESLQCLDSDKSTWRATNKDLLLAYANLMLLTLSTRDVQEGRELLESFDSALQSVKSSVGGNDELSATFLETKGHFYMHVGSLLLKMGQQSDIQWRALSELAALCYLVAFQVPRPKVKLIKGEAGQNLLETMAHDRLSQSGHMLLNLSRGKQDFLKEVVESFANKSGQSALCDALFSSQSSKERSFLGNDDIGNLDGQVPDPDDLARYDTGAVRAHNGSLQHLTWLGLQWNSLSTLPAIRKWLKQLFHHLPQETSRLETNAPESICILDLEVFLLGVIYTSHLQLKEKCNSHHTSYQPLCLPLPVCRQLCTERQKTWWDAVCTLIHRKALPGTSAKLRLLVQREINSLRGQEKHGLQPALLVHWAQSLQKTGSSLNSFYDQREYIGRSVHYWRKVLPLLKMIRKKNSIPEPIDPLFKHFHSVDIQASEIGEYEEDAHITFAILDAVNGNIEDAMTAFESIKNVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIRILDDSDSNTSVVQKLPVPLESVKEMLNSVMQELEDYSEGGTLYKNGCWRSADSELKHSTPSPTKYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSNNSASPHRWPAEPYGQDPAPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYSQQMHTPPVQSSSACMFSQEMYGPPLRFESPATGILSPRGDDYFNYNVQQTSTNPPLPEPGYFTKPPLVAHASRSAESKVIEFGKSNFVQPMQGEVIRPPLTTPAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVAQPPSTAYSNSESLLGLLTSDKPLQGDGYSGLKPISGQASGSRNTFSFGSKNTLTENMGPNQQKNFGFHRSDDMFAFHGPGKSVFTTAASELANKSHETDGGSAHGDEEDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQNILKALGTNTSTAPNHTLRIVKESATQDNKDICKADGGNLNFEFQIVKKEGPYWNCNSCSFKNAATAKKCVSCQNTNPTSNKELLGPPLVENGFAPKTGLENAQDRFATMTANKEGHWDCSVCLVRNEPTVSRCIACQNTKSASSFVQTSFKFGQGDLPKSVDSDFRSVFSKKEGQWECSVCLVRNERSAKKCVACENPGKQFKEWHCSLCSVKNEAHAIKCVACNNPVTPSLSTAPPSFKFGTSEMSKPFRIGFEGMFAKKEGQWDCSLCFVRNEASATHCIACQYPNKQNQPTSCVSAPASSETSRSPKSGFEGLFPKKEGEWECAVCSVQNESSSLKCVACEASKPTHKPHEAPSAFTVGSKSQSNESAGSQVGTEFKSNFPEKNFKVGISEQKFKFGHVDQEKTPSFAFQGGSNTEFKSIKDGFSFCIPVSADGFKFGIQEKGNQEKKSEKHLENDPSFQAHDTSGQKNGSGVVFGQTSSTFTFADLAKSTSREGFQFGKKDPNFKGFSGAGEKLFSSQSGKVAEKANTSSDLEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQVKVTDEENASSGADAPSASDTTAKQNPDNTGPALEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQSGASVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQTMKGTERVWVWTACDFADGERKIEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSHLSTPRESPCGKIAIAVLEETTRERTDLTQGDEVIDTTSEAGETSSTSETTPKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKNSNSEMTSRVQSGSEGKVKPDKCELPQNSDIKQSSDGKVKNLSAFSKENSSTSYTFKTPEKAQEKSKPEDLPSDNDILIVYELTPTPEQKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLNGKLYLDDSEKPLEENLADNDKECVIVWEKKPTVEERAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELRKVCEAQKSQNEKVTDRVGIEHIGETEVTNPVGCKSEEPDSDTKHSSSSPVSGTMDKPVDLSTRKETDMEFPSKGENKPVLFGFGSGTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQTTSKGGEDEDGSDEDVVHNEDIHFEPIVSLPEVEVKSGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRILMRRDQVFKVCANHVITKAMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQQNIIKLQNGHTSLAAELSKDTNPVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKGFGFKNSIFHRVVPDFICQGGDITKYNGTGGQSIYGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKGSVSRRICITECGQL

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict213-222in Ref. 3; BAC31101
Compositional bias773-795Polar residues
Sequence conflict985-1001in Ref. 4; CAA60778
Sequence conflict1086-1089in Ref. 4; CAA60778
Compositional bias1149-1168Basic and acidic residues
Sequence conflict1269in Ref. 4; CAA60778
Sequence conflict1273in Ref. 4; CAA60778
Sequence conflict1276in Ref. 4; CAA60778
Sequence conflict1280in Ref. 4; CAA60778
Sequence conflict1293in Ref. 4; CAA60778
Sequence conflict1297in Ref. 4; CAA60778
Compositional bias1587-1607Polar residues
Compositional bias1656-1675Polar residues
Compositional bias1744-1758Basic and acidic residues
Compositional bias1828-1846Basic and acidic residues
Sequence conflict1861in Ref. 4; CAA60778
Compositional bias2030-2057Polar residues
Compositional bias2111-2132Polar residues
Compositional bias2323-2345Polar residues
Compositional bias2598-2615Basic and acidic residues
Compositional bias2651-2665Basic and acidic residues
Sequence conflict2868-2869in Ref. 1; AAG17403

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF279458
EMBL· GenBank· DDBJ
AAG17403.1
EMBL· GenBank· DDBJ
Genomic DNA
AC158593
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AK041932
EMBL· GenBank· DDBJ
BAC31101.1
EMBL· GenBank· DDBJ
mRNA
X87337
EMBL· GenBank· DDBJ
CAA60778.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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