NU153_RAT
ID NU153_RAT Reviewed; 1468 AA.
AC P49791;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Nuclear pore complex protein Nup153;
DE AltName: Full=153 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup153;
GN Name=Nup153;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 602-613; 622-645 AND
RP 971-993.
RC STRAIN=Buffalo; TISSUE=Liver;
RX PubMed=8422679; DOI=10.1016/0092-8674(93)90047-t;
RA Sukegawa J., Blobel G.;
RT "A nuclear pore complex protein that contains zinc finger motifs, binds
RT DNA, and faces the nucleoplasm.";
RL Cell 72:29-38(1993).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11839768; DOI=10.1083/jcb.200106046;
RA Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
RT "Tpr is localized within the nuclear basket of the pore complex and has a
RT role in nuclear protein export.";
RL J. Cell Biol. 156:617-630(2002).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15703211; DOI=10.1091/mbc.e04-10-0857;
RA Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.;
RT "Vertebrate Nup53 interacts with the nuclear lamina and is required for the
RT assembly of a Nup93-containing complex.";
RL Mol. Biol. Cell 16:2382-2394(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-97; SER-331 AND SER-339, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP STRUCTURE BY NMR OF 703-755 IN COMPLEX WITH RAN AND ZINC, INTERACTION WITH
RP RAN, AND MUTAGENESIS OF PHE-714 AND PHE-718.
RX PubMed=18611384; DOI=10.1016/j.str.2008.03.014;
RA Schrader N., Koerner C., Koessmeier K., Bangert J.A., Wittinghofer A.,
RA Stoll R., Vetter I.R.;
RT "The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking
RT site at the nuclear pore complex.";
RL Structure 16:1116-1125(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 658-817 IN COMPLEX WITH RAN AND
RP ZINC.
RX PubMed=19505478; DOI=10.1016/j.jmb.2009.06.011;
RA Partridge J.R., Schwartz T.U.;
RT "Crystallographic and biochemical analysis of the Ran-binding zinc finger
RT domain.";
RL J. Mol. Biol. 391:375-389(2009).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), a complex
CC required for the trafficking across the nuclear envelope. Functions as
CC a scaffolding element in the nuclear phase of the NPC essential for
CC normal nucleocytoplasmic transport of proteins and mRNAs. Involved in
CC the quality control and retention of unspliced mRNAs in the nucleus; in
CC association with TPR, regulates the nuclear export of unspliced mRNA
CC species bearing constitutive transport element (CTE) in a NXF1- and
CC KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear
CC membrane at NPC (By similarity). The repeat-containing domain may be
CC involved in anchoring other components of the NPC to the pore membrane.
CC Possible DNA-binding subunit of the nuclear pore complex (NPC) (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds at least 4 zinc ions per subunit.;
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). Interacts with TPR
CC (via coiled coil region); the interaction is direct and provides a link
CC between the core structure and the TPR-containing nuclear basket of the
CC nuclear pore complex (NPC). Interacts with HIKESHI, SENP2 and XPO5 (By
CC similarity). Interacts with RAN; the interaction occurs in a GTP- and
CC GDP-independent manner. Interacts with MCM3AP; this interaction is
CC required for MCM3AP localization at the nuclear pore complex (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P49790,
CC ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:19505478}.
CC -!- INTERACTION:
CC P49791; P62826: RAN; Xeno; NbExp=5; IntAct=EBI-6140533, EBI-286642;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus membrane. Nucleus, nuclear pore
CC complex. Note=Dissociates from the NPC structure early during prophase
CC of mitosis. Integrated in the newly assembled nuclear envelope of
CC postmitotic cells early in G1 (By similarity). Localized to the
CC nucleoplasmic side of the nuclear pore complex (NPC) core structure,
CC forming a fibrous structure called the nuclear basket. Tightly
CC associated with the nuclear membrane and lamina. Colocalized with NUP98
CC and TPR to the nuclear basket at the nucleoplasmic side of the NPC.
CC Detected in diffuse and discrete intranuclear foci. {ECO:0000250}.
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: Phosphorylated in interphase, hyperphosphorylated during mitosis.
CC May play a role in the reversible disassembly of the nuclear pore
CC complex during mitosis.
CC -!- PTM: O-glycosylated during cytokinesis at sites identical or close to
CC phosphorylation sites, this interferes with the phosphorylation status.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NUP153 family. {ECO:0000305}.
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DR EMBL; L06821; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A44345; A44345.
DR PDB; 2K0C; NMR; -; A=703-755.
DR PDB; 3CH5; X-ray; 2.10 A; B=703-754.
DR PDB; 3GJ3; X-ray; 1.79 A; B=723-750.
DR PDB; 3GJ4; X-ray; 2.15 A; B/D=790-817.
DR PDB; 3GJ5; X-ray; 1.79 A; B/D=848-876.
DR PDB; 3GJ6; X-ray; 2.70 A; B=658-686.
DR PDB; 3GJ7; X-ray; 1.93 A; B/D=658-750.
DR PDB; 3GJ8; X-ray; 1.82 A; B/D=790-876.
DR PDBsum; 2K0C; -.
DR PDBsum; 3CH5; -.
DR PDBsum; 3GJ3; -.
DR PDBsum; 3GJ4; -.
DR PDBsum; 3GJ5; -.
DR PDBsum; 3GJ6; -.
DR PDBsum; 3GJ7; -.
DR PDBsum; 3GJ8; -.
DR AlphaFoldDB; P49791; -.
DR SMR; P49791; -.
DR CORUM; P49791; -.
DR DIP; DIP-46027N; -.
DR IntAct; P49791; 4.
DR STRING; 10116.ENSRNOP00000001979; -.
DR GlyGen; P49791; 4 sites.
DR iPTMnet; P49791; -.
DR PhosphoSitePlus; P49791; -.
DR PaxDb; P49791; -.
DR PRIDE; P49791; -.
DR RGD; 3216; Nup153.
DR eggNOG; KOG4719; Eukaryota.
DR InParanoid; P49791; -.
DR PhylomeDB; P49791; -.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR EvolutionaryTrace; P49791; -.
DR PRO; PR:P49791; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005642; C:annulate lamellae; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:1990875; C:nucleoplasmic side of nuclear pore; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:RGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0046832; P:negative regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR013913; Nup153_N.
DR InterPro; IPR018892; Retro-transposon_transp_CS.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23193; PTHR23193; 1.
DR Pfam; PF08604; Nup153; 1.
DR Pfam; PF10599; Nup_retrotrp_bd; 1.
DR Pfam; PF00641; zf-RanBP; 4.
DR SMART; SM00547; ZnF_RBZ; 4.
DR SUPFAM; SSF90209; SSF90209; 4.
DR PROSITE; PS01358; ZF_RANBP2_1; 4.
DR PROSITE; PS50199; ZF_RANBP2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; DNA-binding;
KW Glycoprotein; Isopeptide bond; Membrane; Metal-binding; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; Ubl conjugation;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT CHAIN 2..1468
FT /note="Nuclear pore complex protein Nup153"
FT /id="PRO_0000204843"
FT REPEAT 237..238
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 652..653
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 714..715
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 782..783
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 898..899
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 919..920
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 954..955
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 976..977
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 993..994
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 1017..1018
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 1077..1078
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 1111..1112
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 1128..1129
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 1166..1167
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 1205..1206
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 1221..1222
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 1233..1234
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 1268..1269
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 1282..1283
FT /note="19"
FT /evidence="ECO:0000305"
FT REPEAT 1284..1285
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 1299..1300
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 1312..1313
FT /note="22"
FT /evidence="ECO:0000305"
FT REPEAT 1320..1321
FT /note="23"
FT /evidence="ECO:0000305"
FT REPEAT 1334..1335
FT /note="24"
FT /evidence="ECO:0000305"
FT REPEAT 1356..1357
FT /note="25"
FT /evidence="ECO:0000305"
FT REPEAT 1368..1369
FT /note="26"
FT /evidence="ECO:0000305"
FT REPEAT 1377..1378
FT /note="27"
FT /evidence="ECO:0000305"
FT REPEAT 1390..1391
FT /note="28"
FT /evidence="ECO:0000305"
FT REPEAT 1410..1411
FT /note="29"
FT /evidence="ECO:0000305"
FT ZN_FING 657..687
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 721..750
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 789..818
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 846..875
FT /note="RanBP2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..1411
FT /note="29 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 387..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 667
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 730
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 795
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 798
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 809
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 812
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 852
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 855
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 866
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT BINDING 869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:18611384,
FT ECO:0000269|PubMed:19505478"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 385
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 717
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 947
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 1454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MOD_RES 1456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT CARBOHYD 534
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 544
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 902
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1106
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49790"
FT MUTAGEN 714
FT /note="F->A: Reduces affinity for RAN; when associated with
FT A-718."
FT /evidence="ECO:0000269|PubMed:18611384"
FT MUTAGEN 718
FT /note="F->A: Reduces affinity for RAN; when associated with
FT A-714."
FT /evidence="ECO:0000269|PubMed:18611384"
FT TURN 665..667
FT /evidence="ECO:0007829|PDB:3GJ6"
FT TURN 679..681
FT /evidence="ECO:0007829|PDB:3GJ6"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:2K0C"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:3GJ3"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:2K0C"
FT TURN 742..744
FT /evidence="ECO:0007829|PDB:3GJ3"
FT TURN 796..798
FT /evidence="ECO:0007829|PDB:3GJ4"
FT TURN 810..812
FT /evidence="ECO:0007829|PDB:3GJ4"
FT TURN 853..855
FT /evidence="ECO:0007829|PDB:3GJ5"
FT TURN 867..869
FT /evidence="ECO:0007829|PDB:3GJ5"
SQ SEQUENCE 1468 AA; 152824 MW; C3DFD9697C556A7C CRC64;
MASGAGGIGG GGGGGKIRTR RCHQGPVKPY QQGRPQHQGI LSRVTESVKN IVPGWLQRYF
NKSENACSCS VNADEVPRWP ENREDEREIY VDENTNTDDG RTTPEPTGSN TEEPSTTSTA
SNYPDVLTRP SLHRSHLNFS VLESPALHCQ PSTSSAFPIG SSGFSLVKEI KDSTSQHDDD
NISTTSGFSS RASEKDIAVS KNTSLPPLWS PEAERSHSLS QHTAISSKKP AFNLSAFGTL
STSLGNSSIL KTSQLGDSPF YPGKTTYGGA AAAVRQNKVR STPYQAPVRR QMKAKQLNAQ
SYGVTSSTAR RILQSLEKMS SPLADAKRIP SAVSSPLNSP LDRSGIDSTV FQAKKEKVDS
QYPPVQRLMT PKPVSIATNR TVYFKPSLTP SGDLRKTNQR IDKKNSTVDE KNISRQNREQ
ESGFSYPNFS IPAANGLSSG VGGGGGKMRR ERTTHFVASK PSEEEEVEVP LLPQISLPIS
SSSLPTFNFS SPAISAASSS SVSPSQPLSN KVQMTSLGST GNPVFTFSSP IVKSTQADVL
PPASIGFTFS VPLAKTELSG PNSSSETVLS SSVTAQDNTV VNSSSSKKRS APCEDPFTPA
KILREGSVLD ILKTPGFMSP KVDSPALQPT TTSSIVYTRP AISTFSSSGV EFGESLKAGS
SWQCDTCLLQ NKVTDNKCIA CQAAKLPLKE TAKQTGIGTP SKSDKPASTS GTGFGDKFKP
AIGTWDCDTC LVQNKPEAVK CVACETPKPG TGVKRALPLT VASESPVTAS SSTTVTTGTL
GFGDKFKRPV GSWECPVCCV SNKAEDSRCV SCTSEKPGLV SASSSNSVPV SLPSGGCLGL
DKFKKPEGSW DCEVCLVQNK ADSTKCIACE SAKPGTKSEF KGFGTSSSLN PAPSAFKFGI
PSSSSGLSQT FTSTGNFKFG DQGGFKLGTS SDSGSTNTMN TNFKFPKPTG DFKFGVLPDS
KPEEIKNDSK NDNFQFGPSS GLSNPASSAP FQFGVSTLGQ QEKKEELPQS SSAGFSFGAG
VANPSSAAID TTVTSENKSG FNFGTIDTKS VSVTPFTYKT TEAKKEDASA TKGGFTFGKV
DSAALSSPSM FVLGRTEEKQ QEPVTSTSLV FGKKADNEEP KCQPVFSFGN SEQTKDESSS
KPTFSFSVAK PSVKESDQLA KATFAFGNQT NTTTDQGAAK PAFSFLNSSS SSSSTPATSS
SASIFGSSTS SSSPPVAAFV FGQASNPVSS SAFGNSAESS TSQPLLFPQD GKPATTSSTA
SAAPPFVFGT GASSNSTVSS GFTFGATTTS SSSGSFFVFG TGHSAPSASP AFGANQTPTF
GQSQGASQPN PPSFGSISSS TALFSAGSQP VPPPTFGTVS SSSQPPVFGQ QPSQSAFGSG
TANASSVFQF GSSTTNFNFT NNNPSGVFTF GASPSTPAAA AQPSGSGGFS FSQSPASFTV
GSNGKNMFSS SGTSVSGRKI KTAVRRKK
