RBP2_PANTR
ID RBP2_PANTR Reviewed; 3224 AA.
AC H2QII6;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=E3 SUMO-protein ligase RanBP2;
DE EC=2.3.2.- {ECO:0000250|UniProtKB:P49792};
DE AltName: Full=358 kDa nucleoporin;
DE AltName: Full=Nuclear pore complex protein Nup358;
DE AltName: Full=Nucleoporin Nup358;
DE AltName: Full=Ran-binding protein 2;
DE Short=RanBP2;
GN Name=RANBP2; Synonyms=NUP358;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) OF 1-145, FUNCTION, SUBCELLULAR
RP LOCATION, RNA-BINDING, AND TPR REPEATS.
RX PubMed=22959972; DOI=10.1016/j.jmb.2012.08.026;
RA Kassube S.A., Stuwe T., Lin D.H., Antonuk C.D., Napetschnig J., Blobel G.,
RA Hoelz A.;
RT "Crystal structure of the N-terminal domain of Nup358/RanBP2.";
RL J. Mol. Biol. 423:752-765(2012).
CC -!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2
CC conjugation by UBE2I. Involved in transport factor (Ran-GTP,
CC karyopherin)-mediated protein import via the F-G repeat-containing
CC domain which acts as a docking site for substrates. Component of the
CC nuclear export pathway. Specific docking site for the nuclear export
CC factor exportin-1. Sumoylates PML at 'Lys-490' which is essential for
CC the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope
CC and cytoplasmic stacks of nuclear pore complex known as annulate
CC lamellae during G2 phase of cell cycle (By similarity). Binds single-
CC stranded RNA (in vitro) (PubMed:22959972). Probable inactive PPIase
CC with no peptidyl-prolyl cis-trans isomerase activity.
CC {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:22959972}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Part of the nuclear pore complex. Forms a complex with NXT1,
CC NXF1 and RANGAP1. Forms a tight complex with RANBP1 and UBE2I.
CC Interacts with SUMO1 but not SUMO2. Interacts with PRKN. Interacts with
CC sumoylated RANGAP1. Interacts with CDCA8. Interacts with PML (isoform
CC PML-4). Interacts with BICD2. Interacts with MCM3AP isoform GANP.
CC Interacts with COX11 (By similarity). {ECO:0000250|UniProtKB:P49792}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22959972}. Nucleus
CC membrane {ECO:0000269|PubMed:22959972}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:22959972}. Nucleus envelope
CC {ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and discrete
CC intranuclear foci. Cytoplasmic filaments.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- DOMAIN: The PPIase cyclophilin-type domain has high structural
CC similarity with PPIA, but has extremely low and barely detectable
CC proline isomerase activity (in vitro). Only about half of the residues
CC that surround the PPIA active site cleft are conserved (By similarity).
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC {ECO:0000305}.
CC -!- PTM: Polyubiquitinated by PRKN, which leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:P49792}.
CC -!- PTM: The inner channel of the NPC has a different redox environment
CC from the cytoplasm and allows the formation of interchain disulfide
CC bonds between some nucleoporins, the significant increase of these
CC linkages upon oxidative stress reduces the permeability of the NPC.
CC {ECO:0000250|UniProtKB:Q9ERU9}.
CC -!- SIMILARITY: Belongs to the RanBP2 E3 ligase family. {ECO:0000305}.
CC -!- CAUTION: Despite the presence of a PPIase cyclophilin-type domain, it
CC has probably no peptidyl-prolyl cis-trans isomerase activity.
CC {ECO:0000250|UniProtKB:P49792}.
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DR EMBL; AACZ03015911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 4GA1; X-ray; 1.15 A; A=1-145.
DR PDB; 4GA2; X-ray; 0.95 A; A=1-145.
DR PDBsum; 4GA1; -.
DR PDBsum; 4GA2; -.
DR SMR; H2QII6; -.
DR STRING; 9598.ENSPTRP00000021122; -.
DR PaxDb; H2QII6; -.
DR eggNOG; KOG0864; Eukaryota.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_000378_1_0_1; -.
DR InParanoid; H2QII6; -.
DR TreeFam; TF314797; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005642; C:annulate lamellae; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR022011; IR1-M.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23138; PTHR23138; 2.
DR Pfam; PF12185; IR1-M; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00638; Ran_BP1; 4.
DR Pfam; PF00641; zf-RanBP; 8.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00028; TPR; 1.
DR SMART; SM00547; ZnF_RBZ; 8.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR SUPFAM; SSF90209; SSF90209; 7.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50196; RANBD1; 4.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 8.
DR PROSITE; PS50199; ZF_RANBP2_2; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disulfide bond; Isopeptide bond; Membrane;
KW Metal-binding; Methylation; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; RNA-binding;
KW TPR repeat; Transferase; Translocation; Transport; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..3224
FT /note="E3 SUMO-protein ligase RanBP2"
FT /id="PRO_0000424524"
FT REPEAT 26..59
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 60..93
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 94..128
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 165..201
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 287..319
FT /note="TPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 583..616
FT /note="TPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 648..681
FT /note="TPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 1001..1002
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1101..1102
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1142..1143
FT /note="3"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT DOMAIN 1171..1307
FT /note="RanBD1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 1459..1460
FT /note="4"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1523..1524
FT /note="5"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1586..1587
FT /note="6"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1852..1853
FT /note="7"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1861..1862
FT /note="8"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1900..1901
FT /note="9"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1938..1939
FT /note="10"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 1961..1962
FT /note="11"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT DOMAIN 2012..2148
FT /note="RanBD1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 2260..2261
FT /note="12"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT DOMAIN 2309..2445
FT /note="RanBD1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 2516..2517
FT /note="13"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2535..2536
FT /note="14"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2545..2546
FT /note="15"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2633..2685
FT /note="1"
FT /evidence="ECO:0000269|PubMed:22959972"
FT REPEAT 2711..2761
FT /note="2"
FT /evidence="ECO:0000269|PubMed:22959972"
FT REPEAT 2840..2841
FT /note="16"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2842..2843
FT /note="17"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2863..2864
FT /note="18"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 2880..2881
FT /note="19"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT DOMAIN 2911..3046
FT /note="RanBD1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT DOMAIN 3067..3223
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 3106..3107
FT /note="20"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 3189..3190
FT /note="21"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REPEAT 3205..3206
FT /note="22"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT ZN_FING 1351..1381
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1415..1444
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1479..1508
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1543..1572
FT /note="RanBP2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1606..1635
FT /note="RanBP2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1665..1694
FT /note="RanBP2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1724..1753
FT /note="RanBP2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1781..1810
FT /note="RanBP2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 767..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..3206
FT /note="22 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 1138..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2147..2287
FT /note="Interaction with BICD2"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT REGION 2188..2224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2274..2307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2556..2629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2631..2635
FT /note="Interaction with sumoylated RANGAP1"
FT /evidence="ECO:0000250"
FT REGION 2633..2761
FT /note="2 X 50 AA approximate repeats"
FT REGION 2633..2710
FT /note="Required for E3 SUMO-ligase activity"
FT /evidence="ECO:0000250"
FT REGION 2633..2685
FT /note="Interaction with UBE2I"
FT /evidence="ECO:0000250"
FT REGION 2686..2761
FT /note="Interaction with SUMO1"
FT /evidence="ECO:0000250"
FT REGION 2791..2818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2202..2221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2274..2295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2556..2573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2574..2588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2589..2612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2613..2629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2795..2815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 779
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 945
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1016
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 1016
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1098
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1144
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1412
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1835
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1871
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 1977
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2005
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2008
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2153
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2613
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2666
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2743
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 2900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT MOD_RES 3207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1655
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1714
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 1723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2022
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 2594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2612
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2792
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT CROSSLNK 2815
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49792"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:4GA2"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:4GA2"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:4GA2"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:4GA2"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:4GA2"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:4GA2"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:4GA2"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4GA2"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:4GA2"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:4GA2"
SQ SEQUENCE 3224 AA; 358148 MW; 005EBC43EDEAACBB CRC64;
MRRSKADVER YIASVQGSTP SPRQKSIKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP
KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
AAKLFPGSPA VYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVEVYRSTKR
LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA
NLMLLTLSTR DVQESRELLE SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM
GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR LSQSGHMLLN
LSRGKQDFLR EIVETFANKS GQSALYDALF SSQSPKDTSF LGSDDIGNID VREPELEDLA
RYDVGAIRAH DGSLQHLTWL GLQWNSLPAL PGIRKWLKQL FHHLPQETSR LETNAPESIC
ILDLEVFLLG VVYTSHLQLK EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH
RKAVPGNAAK LRLLVQHEIN TLRAQEKHGL QPALLVHWAK CLQKTGSGLN SFYDQREYIG
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA HITFAILDVV
NGNIEDAMTA FESIQSVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIK
IIDDSDSNLS VVKKLPVPLE SVKEMLKSVM QELEAYSEGG PLYTNGSLRN ADSEIKHSTP
SHTRYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR
WPTENYGPDS VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA TGILSPRGDD
YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE FGKTNFVQPM PGEGLRPSLP
TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ VVTQPPPAAY SNSESLLGLL TSDKPLQGDG
YSGAKPIPGG QTIGPRNTFN FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS
VFGTPTLETA NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK
LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP DMKLTPNAGS
DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE AQSILKAPGT NVATASNQAV
RIVKEPTSHD NKDICKSDAG NLNFEFQFAK KEGSWWHCNS CSLKNASTAK KCVSCQNLNP
SNKELVGPPL AETVFTPKTS PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN
TKSANKSGSS FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA
ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS SCLVRNEANA
TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE GMFTKKEGQW DCSVCLVRNE
ASATKCVACQ NPGKQNQTTS AVSTPASSET SRAPKSGFEG MFTKKEGQWD CSVCLVRNEA
SATKCIACQS PGKQNQTTSA VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS
ATKCIACQCP SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK
CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSPGSQVGTG FKSNFSEKAS KFGNTEQGFK
FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF GISEPGNQEK KSEKPLENDT
GFQAQDISGQ KNGSGVIFGQ TSSTFTFADL AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS
SQYGKMANKA NTSGDFEKDD DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV
KLFRFDAEVS QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG
SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP LQTPHKLVDT
GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG TGAAGASDTT IKPNPENTGP
TLEWDNYDLR EDALDDSVSS SSVHASPLAS SPVRKNLFRF GESTTGFNFS FKSALSPSKS
PGKLNQSGTS VGTDEESDVT QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY
RYDKDVGQWK ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER
VWLWTAYDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT PHVSRSSTPR
ESPCGKIAVA VLEETTRERT DVTQGDDVAD AASEVEVSST SETTTKAVVS PPKFVFGSES
VKSIFSSEKS KPFAFGNTSA TGSLFGFSFN APLKSNNSET SSVAQSGSES KVEPNKCELS
KNSDIEQSSD SKVKNLSASF PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP
TAEQKALATK LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL EGSEKCRPLE
ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG EDFQSELQKV
QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT KSISSPSVSS ETMDKPVDLS
TRKEIDTDST SQGESKIVSF GFGSSTGLSF ADLASSNSGD FAFGSKDKNF QWANTGAAVF
GTQSVGTQSA GKVGEDEDGS DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL
YRWDRDVSQW KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN
NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG HVSLAAELSK
ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC TGEKGFGFKN SIFHRVIPDF
VCQGGDITKH DGTGGQSIYG DKFEDENFDV KHTGPGLLSM ANQGQNTNNS QFFITLKKAE
LLDFKHVVFG FVKDGMDTVK KIESFGSPKG SVCRRITITE CGQI
