Q9ERU9 · RBP2_MOUSE
- ProteinE3 SUMO-protein ligase RanBP2
- GeneRanbp2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3053 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Pathway
Protein modification; protein sumoylation.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 SUMO-protein ligase RanBP2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9ERU9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected in diffuse and discrete intranuclear foci. Cytoplasmic filaments.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000204914 | 1-3053 | E3 SUMO-protein ligase RanBP2 | |||
Sequence: MRRSKADVERYIASVQGSAPSPREKSMKGFYFAKLYYEAKEYDLAKKYISTYINVQERDPKAHRFLGLLYEVEENIDKAVECYKRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGSPAIYKLKEQLLDCKGEDGWNKLFDLIQSELYARPDDIHVNIRLVELYRSNKRLKDAVAHCHEADRNTALRSSLEWNLCVVQTLKEYLESLQCLDSDKSTWRATNKDLLLAYANLMLLTLSTRDVQEGRELLESFDSALQSVKSSVGGNDELSATFLETKGHFYMHVGSLLLKMGQQSDIQWRALSELAALCYLVAFQVPRPKVKLIKGEAGQNLLETMAHDRLSQSGHMLLNLSRGKQDFLKEVVESFANKSGQSALCDALFSSQSSKERSFLGNDDIGNLDGQVPDPDDLARYDTGAVRAHNGSLQHLTWLGLQWNSLSTLPAIRKWLKQLFHHLPQETSRLETNAPESICILDLEVFLLGVIYTSHLQLKEKCNSHHTSYQPLCLPLPVCRQLCTERQKTWWDAVCTLIHRKALPGTSAKLRLLVQREINSLRGQEKHGLQPALLVHWAQSLQKTGSSLNSFYDQREYIGRSVHYWRKVLPLLKMIRKKNSIPEPIDPLFKHFHSVDIQASEIGEYEEDAHITFAILDAVNGNIEDAMTAFESIKNVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIRILDDSDSNTSVVQKLPVPLESVKEMLNSVMQELEDYSEGGTLYKNGCWRSADSELKHSTPSPTKYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSNNSASPHRWPAEPYGQDPAPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKGPVYGMNRLPPQQHIYAYSQQMHTPPVQSSSACMFSQEMYGPPLRFESPATGILSPRGDDYFNYNVQQTSTNPPLPEPGYFTKPPLVAHASRSAESKVIEFGKSNFVQPMQGEVIRPPLTTPAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVAQPPSTAYSNSESLLGLLTSDKPLQGDGYSGLKPISGQASGSRNTFSFGSKNTLTENMGPNQQKNFGFHRSDDMFAFHGPGKSVFTTAASELANKSHETDGGSAHGDEEDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQNILKALGTNTSTAPNHTLRIVKESATQDNKDICKADGGNLNFEFQIVKKEGPYWNCNSCSFKNAATAKKCVSCQNTNPTSNKELLGPPLVENGFAPKTGLENAQDRFATMTANKEGHWDCSVCLVRNEPTVSRCIACQNTKSASSFVQTSFKFGQGDLPKSVDSDFRSVFSKKEGQWECSVCLVRNERSAKKCVACENPGKQFKEWHCSLCSVKNEAHAIKCVACNNPVTPSLSTAPPSFKFGTSEMSKPFRIGFEGMFAKKEGQWDCSLCFVRNEASATHCIACQYPNKQNQPTSCVSAPASSETSRSPKSGFEGLFPKKEGEWECAVCSVQNESSSLKCVACEASKPTHKPHEAPSAFTVGSKSQSNESAGSQVGTEFKSNFPEKNFKVGISEQKFKFGHVDQEKTPSFAFQGGSNTEFKSIKDGFSFCIPVSADGFKFGIQEKGNQEKKSEKHLENDPSFQAHDTSGQKNGSGVVFGQTSSTFTFADLAKSTSREGFQFGKKDPNFKGFSGAGEKLFSSQSGKVAEKANTSSDLEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQVKVTDEENASSGADAPSASDTTAKQNPDNTGPALEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQSGASVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQTMKGTERVWVWTACDFADGERKIEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSHLSTPRESPCGKIAIAVLEETTRERTDLTQGDEVIDTTSEAGETSSTSETTPKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKNSNSEMTSRVQSGSEGKVKPDKCELPQNSDIKQSSDGKVKNLSAFSKENSSTSYTFKTPEKAQEKSKPEDLPSDNDILIVYELTPTPEQKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLNGKLYLDDSEKPLEENLADNDKECVIVWEKKPTVEERAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELRKVCEAQKSQNEKVTDRVGIEHIGETEVTNPVGCKSEEPDSDTKHSSSSPVSGTMDKPVDLSTRKETDMEFPSKGENKPVLFGFGSGTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQTTSKGGEDEDGSDEDVVHNEDIHFEPIVSLPEVEVKSGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRILMRRDQVFKVCANHVITKAMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQQNIIKLQNGHTSLAAELSKDTNPVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKGFGFKNSIFHRVVPDFICQGGDITKYNGTGGQSIYGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKGSVSRRICITECGQL | ||||||
Modified residue | 21 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 779 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 781 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 788 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 837 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 944 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 947 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 954 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1015 | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | ||||||
Modified residue | 1015 | Omega-N-methylarginine; alternate | ||||
Sequence: R | ||||||
Modified residue | 1096 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1101 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1138 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1154 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1243 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1344 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1407 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1438 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1441 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1446 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1528 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1557 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 1557 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Cross-link | 1607 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1616 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 1616 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 1670 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1706 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1814 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 1842 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1845 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1859 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1990 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2083 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2088 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2107 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2117 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2127 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2130 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2134 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2299 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2330 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2348 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 2360 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 2364 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 2430 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | ||||||
Cross-link | 2432 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 2432 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Cross-link | 2449 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 2450 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2503 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 2505 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2576 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2578 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 2627 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 2640 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 2649 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 2729 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 3036 | Phosphoserine | ||||
Sequence: S |
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
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9ERU9 | Prkn Q9WVS6 | 2 | EBI-643756, EBI-973635 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for repeat, compositional bias, region, domain, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 26-59 | TPR 1 | ||||
Sequence: SMKGFYFAKLYYEAKEYDLAKKYISTYINVQERD | ||||||
Repeat | 60-93 | TPR 2 | ||||
Sequence: PKAHRFLGLLYEVEENIDKAVECYKRSVELNPTQ | ||||||
Repeat | 94-128 | TPR 3 | ||||
Sequence: KDLVLKIAELLCKNDVTDGRAKYWVERAAKLFPGS | ||||||
Repeat | 165-201 | TPR 4 | ||||
Sequence: IHVNIRLVELYRSNKRLKDAVAHCHEADRNTALRSSL | ||||||
Repeat | 288-319 | TPR 5 | ||||
Sequence: GHFYMHVGSLLLKMGQQSDIQWRALSELAALC | ||||||
Repeat | 583-616 | TPR 6 | ||||
Sequence: QKTGSSLNSFYDQREYIGRSVHYWRKVLPLLKMI | ||||||
Repeat | 648-681 | TPR 7 | ||||
Sequence: EDAHITFAILDAVNGNIEDAMTAFESIKNVVSYW | ||||||
Compositional bias | 773-795 | Polar residues | ||||
Sequence: SELKHSTPSPTKYSLSPSKSYKY | ||||||
Region | 773-802 | Disordered | ||||
Sequence: SELKHSTPSPTKYSLSPSKSYKYSPKTPPR | ||||||
Repeat | 1000-1001 | 1 | ||||
Sequence: FG | ||||||
Region | 1000-3035 | 20 X 2 AA repeats of F-G | ||||
Sequence: FGKSNFVQPMQGEVIRPPLTTPAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVAQPPSTAYSNSESLLGLLTSDKPLQGDGYSGLKPISGQASGSRNTFSFGSKNTLTENMGPNQQKNFGFHRSDDMFAFHGPGKSVFTTAASELANKSHETDGGSAHGDEEDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQNILKALGTNTSTAPNHTLRIVKESATQDNKDICKADGGNLNFEFQIVKKEGPYWNCNSCSFKNAATAKKCVSCQNTNPTSNKELLGPPLVENGFAPKTGLENAQDRFATMTANKEGHWDCSVCLVRNEPTVSRCIACQNTKSASSFVQTSFKFGQGDLPKSVDSDFRSVFSKKEGQWECSVCLVRNERSAKKCVACENPGKQFKEWHCSLCSVKNEAHAIKCVACNNPVTPSLSTAPPSFKFGTSEMSKPFRIGFEGMFAKKEGQWDCSLCFVRNEASATHCIACQYPNKQNQPTSCVSAPASSETSRSPKSGFEGLFPKKEGEWECAVCSVQNESSSLKCVACEASKPTHKPHEAPSAFTVGSKSQSNESAGSQVGTEFKSNFPEKNFKVGISEQKFKFGHVDQEKTPSFAFQGGSNTEFKSIKDGFSFCIPVSADGFKFGIQEKGNQEKKSEKHLENDPSFQAHDTSGQKNGSGVVFGQTSSTFTFADLAKSTSREGFQFGKKDPNFKGFSGAGEKLFSSQSGKVAEKANTSSDLEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQVKVTDEENASSGADAPSASDTTAKQNPDNTGPALEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQSGASVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQTMKGTERVWVWTACDFADGERKIEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSHLSTPRESPCGKIAIAVLEETTRERTDLTQGDEVIDTTSEAGETSSTSETTPKAVVSPPKFVFGSESVKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKNSNSEMTSRVQSGSEGKVKPDKCELPQNSDIKQSSDGKVKNLSAFSKENSSTSYTFKTPEKAQEKSKPEDLPSDNDILIVYELTPTPEQKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLNGKLYLDDSEKPLEENLADNDKECVIVWEKKPTVEERAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELRKVCEAQKSQNEKVTDRVGIEHIGETEVTNPVGCKSEEPDSDTKHSSSSPVSGTMDKPVDLSTRKETDMEFPSKGENKPVLFGFGSGTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVFGTQTTSKGGEDEDGSDEDVVHNEDIHFEPIVSLPEVEVKSGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRILMRRDQVFKVCANHVITKAMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQQNIIKLQNGHTSLAAELSKDTNPVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKGFGFKNSIFHRVVPDFICQGGDITKYNGTGGQSIYGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFG | ||||||
Repeat | 1099-1100 | 2 | ||||
Sequence: FG | ||||||
Repeat | 1117-1118 | 3 | ||||
Sequence: FG | ||||||
Region | 1147-1171 | Disordered | ||||
Sequence: SHETDGGSAHGDEEDDGPHFEPVVP | ||||||
Compositional bias | 1149-1168 | Basic and acidic residues | ||||
Sequence: ETDGGSAHGDEEDDGPHFEP | ||||||
Domain | 1165-1301 | RanBD1 1 | ||||
Sequence: HFEPVVPLPDKIEVKTGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQNILKA | ||||||
Zinc finger | 1345-1375 | RanBP2-type 1 | ||||
Sequence: KEGPYWNCNSCSFKNAATAKKCVSCQNTNPT | ||||||
Zinc finger | 1410-1439 | RanBP2-type 2 | ||||
Sequence: KEGHWDCSVCLVRNEPTVSRCIACQNTKSA | ||||||
Repeat | 1449-1450 | 4 | ||||
Sequence: FG | ||||||
Zinc finger | 1469-1498 | RanBP2-type 3 | ||||
Sequence: KEGQWECSVCLVRNERSAKKCVACENPGKQ | ||||||
Zinc finger | 1494-1527 | RanBP2-type 4 | ||||
Sequence: NPGKQFKEWHCSLCSVKNEAHAIKCVACNNPVTP | ||||||
Repeat | 1538-1539 | 5 | ||||
Sequence: FG | ||||||
Zinc finger | 1558-1587 | RanBP2-type 5 | ||||
Sequence: KEGQWDCSLCFVRNEASATHCIACQYPNKQ | ||||||
Compositional bias | 1587-1607 | Polar residues | ||||
Sequence: QNQPTSCVSAPASSETSRSPK | ||||||
Region | 1587-1609 | Disordered | ||||
Sequence: QNQPTSCVSAPASSETSRSPKSG | ||||||
Zinc finger | 1617-1646 | RanBP2-type 6 | ||||
Sequence: KEGEWECAVCSVQNESSSLKCVACEASKPT | ||||||
Region | 1648-1675 | Disordered | ||||
Sequence: KPHEAPSAFTVGSKSQSNESAGSQVGTE | ||||||
Compositional bias | 1656-1675 | Polar residues | ||||
Sequence: FTVGSKSQSNESAGSQVGTE | ||||||
Repeat | 1696-1697 | 6 | ||||
Sequence: FG | ||||||
Repeat | 1737-1738 | 7 | ||||
Sequence: FG | ||||||
Compositional bias | 1744-1758 | Basic and acidic residues | ||||
Sequence: NQEKKSEKHLENDPS | ||||||
Region | 1744-1772 | Disordered | ||||
Sequence: NQEKKSEKHLENDPSFQAHDTSGQKNGSG | ||||||
Repeat | 1775-1776 | 8 | ||||
Sequence: FG | ||||||
Repeat | 1798-1799 | 9 | ||||
Sequence: FG | ||||||
Region | 1819-1846 | Disordered | ||||
Sequence: QSGKVAEKANTSSDLEKDDDAYKTEDSD | ||||||
Compositional bias | 1828-1846 | Basic and acidic residues | ||||
Sequence: NTSSDLEKDDDAYKTEDSD | ||||||
Domain | 1849-1985 | RanBD1 2 | ||||
Sequence: HFEPVVQMPEKVELVTGEEDEKVLYSQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLD | ||||||
Region | 1984-2124 | Interaction with BICD2 | ||||
Sequence: LDIPLQTPHKLVDTGRAAKLIQRAEEMKSGLKDFKTFLTNDQVKVTDEENASSGADAPSASDTTAKQNPDNTGPALEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKSPAKLNQS | ||||||
Compositional bias | 2030-2057 | Polar residues | ||||
Sequence: DEENASSGADAPSASDTTAKQNPDNTGP | ||||||
Region | 2030-2060 | Disordered | ||||
Sequence: DEENASSGADAPSASDTTAKQNPDNTGPALE | ||||||
Repeat | 2097-2098 | 10 | ||||
Sequence: FG | ||||||
Compositional bias | 2111-2132 | Polar residues | ||||
Sequence: ALSPSKSPAKLNQSGASVGTDE | ||||||
Region | 2111-2144 | Disordered | ||||
Sequence: ALSPSKSPAKLNQSGASVGTDEESDVTQEEERDG | ||||||
Domain | 2146-2282 | RanBD1 3 | ||||
Sequence: YFEPVVPLPDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQTMKGTERVWVWTACDFADGERKIEHLAVRFKLQDVADSFKKIFDEAKTAQEK | ||||||
Region | 2316-2348 | Disordered | ||||
Sequence: RTDLTQGDEVIDTTSEAGETSSTSETTPKAVVS | ||||||
Compositional bias | 2323-2345 | Polar residues | ||||
Sequence: DEVIDTTSEAGETSSTSETTPKA | ||||||
Repeat | 2354-2355 | 11 | ||||
Sequence: FG | ||||||
Repeat | 2373-2374 | 12 | ||||
Sequence: FG | ||||||
Repeat | 2383-2384 | 13 | ||||
Sequence: FG | ||||||
Region | 2394-2430 | Disordered | ||||
Sequence: SNSEMTSRVQSGSEGKVKPDKCELPQNSDIKQSSDGK | ||||||
Region | 2443-2463 | Disordered | ||||
Sequence: STSYTFKTPEKAQEKSKPEDL | ||||||
Region | 2468-2472 | Interaction with sumoylated RANGAP1 | ||||
Sequence: DILIV | ||||||
Repeat | 2470-2522 | 1 | ||||
Sequence: LIVYELTPTPEQKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLN | ||||||
Region | 2470-2522 | Interaction with UBE2I | ||||
Sequence: LIVYELTPTPEQKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLN | ||||||
Region | 2470-2545 | Required for E3 SUMO-ligase activity | ||||
Sequence: LIVYELTPTPEQKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLNGKLYLDDSEKPLEENLADNDKEC | ||||||
Region | 2470-2596 | 2 X 50 AA approximate repeats | ||||
Sequence: LIVYELTPTPEQKALAEKLLLPSTFFCYKNRPGYVSEEEEDDEDYEMAVKKLNGKLYLDDSEKPLEENLADNDKECVIVWEKKPTVEERAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELRKVC | ||||||
Region | 2523-2596 | Interaction with SUMO1 | ||||
Sequence: GKLYLDDSEKPLEENLADNDKECVIVWEKKPTVEERAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELRKVC | ||||||
Repeat | 2546-2596 | 2 | ||||
Sequence: VIVWEKKPTVEERAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELRKVC | ||||||
Compositional bias | 2598-2615 | Basic and acidic residues | ||||
Sequence: AQKSQNEKVTDRVGIEHI | ||||||
Region | 2598-2666 | Disordered | ||||
Sequence: AQKSQNEKVTDRVGIEHIGETEVTNPVGCKSEEPDSDTKHSSSSPVSGTMDKPVDLSTRKETDMEFPSK | ||||||
Compositional bias | 2651-2665 | Basic and acidic residues | ||||
Sequence: VDLSTRKETDMEFPS | ||||||
Repeat | 2674-2675 | 14 | ||||
Sequence: FG | ||||||
Repeat | 2676-2677 | 15 | ||||
Sequence: FG | ||||||
Repeat | 2697-2698 | 16 | ||||
Sequence: FG | ||||||
Repeat | 2714-2715 | 17 | ||||
Sequence: FG | ||||||
Domain | 2740-2875 | RanBD1 4 | ||||
Sequence: HFEPIVSLPEVEVKSGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRILMRRDQVFKVCANHVITKAMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQQNIIK | ||||||
Domain | 2896-3052 | PPIase cyclophilin-type | ||||
Sequence: FFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKGFGFKNSIFHRVVPDFICQGGDITKYNGTGGQSIYGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKGSVSRRICITECGQ | ||||||
Repeat | 2935-2936 | 18 | ||||
Sequence: FG | ||||||
Repeat | 3018-3019 | 19 | ||||
Sequence: FG | ||||||
Repeat | 3034-3035 | 20 | ||||
Sequence: FG |
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
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,053
- Mass (Da)341,121
- Last updated2011-07-27 v2
- Checksum62FD4249DEE466AE
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 213-222 | in Ref. 3; BAC31101 | ||||
Sequence: EYLESLQCLD → VGETYFSTVF | ||||||
Compositional bias | 773-795 | Polar residues | ||||
Sequence: SELKHSTPSPTKYSLSPSKSYKY | ||||||
Sequence conflict | 985-1001 | in Ref. 4; CAA60778 | ||||
Sequence: LVAHASRSAESKVIEFG → IPGSRFKVSRIKGYRIWL | ||||||
Sequence conflict | 1086-1089 | in Ref. 4; CAA60778 | ||||
Sequence: ISGQ → YLA | ||||||
Compositional bias | 1149-1168 | Basic and acidic residues | ||||
Sequence: ETDGGSAHGDEEDDGPHFEP | ||||||
Sequence conflict | 1269 | in Ref. 4; CAA60778 | ||||
Sequence: L → F | ||||||
Sequence conflict | 1273 | in Ref. 4; CAA60778 | ||||
Sequence: E → G | ||||||
Sequence conflict | 1276 | in Ref. 4; CAA60778 | ||||
Sequence: A → S | ||||||
Sequence conflict | 1280 | in Ref. 4; CAA60778 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 1293 | in Ref. 4; CAA60778 | ||||
Sequence: E → G | ||||||
Sequence conflict | 1297 | in Ref. 4; CAA60778 | ||||
Sequence: N → D | ||||||
Compositional bias | 1587-1607 | Polar residues | ||||
Sequence: QNQPTSCVSAPASSETSRSPK | ||||||
Compositional bias | 1656-1675 | Polar residues | ||||
Sequence: FTVGSKSQSNESAGSQVGTE | ||||||
Compositional bias | 1744-1758 | Basic and acidic residues | ||||
Sequence: NQEKKSEKHLENDPS | ||||||
Compositional bias | 1828-1846 | Basic and acidic residues | ||||
Sequence: NTSSDLEKDDDAYKTEDSD | ||||||
Sequence conflict | 1861 | in Ref. 4; CAA60778 | ||||
Sequence: E → D | ||||||
Compositional bias | 2030-2057 | Polar residues | ||||
Sequence: DEENASSGADAPSASDTTAKQNPDNTGP | ||||||
Compositional bias | 2111-2132 | Polar residues | ||||
Sequence: ALSPSKSPAKLNQSGASVGTDE | ||||||
Compositional bias | 2323-2345 | Polar residues | ||||
Sequence: DEVIDTTSEAGETSSTSETTPKA | ||||||
Compositional bias | 2598-2615 | Basic and acidic residues | ||||
Sequence: AQKSQNEKVTDRVGIEHI | ||||||
Compositional bias | 2651-2665 | Basic and acidic residues | ||||
Sequence: VDLSTRKETDMEFPS | ||||||
Sequence conflict | 2868-2869 | in Ref. 1; AAG17403 | ||||
Sequence: EC → DS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |