NKTR_HUMAN
ID NKTR_HUMAN Reviewed; 1462 AA.
AC P30414;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=NK-tumor recognition protein {ECO:0000305|PubMed:8421688};
DE Short=NK-TR protein {ECO:0000303|PubMed:8421688};
DE AltName: Full=Natural-killer cells cyclophilin-related protein;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase NKTR {ECO:0000305|PubMed:20676357};
DE Short=PPIase {ECO:0000305|PubMed:20676357};
DE EC=5.2.1.8 {ECO:0000269|PubMed:20676357};
DE AltName: Full=Rotamase;
GN Name=NKTR {ECO:0000312|HGNC:HGNC:7833};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND CAUTION.
RC TISSUE=Blood;
RX PubMed=8421688; DOI=10.1073/pnas.90.2.542;
RA Anderson S.K., Gallinger S., Roder J., Frey J., Young H.A., Ortaldo J.R.;
RT "A cyclophilin-related protein involved in the function of natural killer
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:542-546(1993).
RN [2]
RP SEQUENCE REVISION.
RA Anderson S.K.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Anderson S.K.;
RT "Structure of the human NKTR gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463; SER-887; SER-889 AND
RP SER-891, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 AND SER-1146, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-463; SER-1146 AND
RP THR-1155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-416; SER-463;
RP SER-471; SER-648; SER-866; SER-889; SER-1077; SER-1146; THR-1155 AND
RP SER-1203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-323; LYS-581; LYS-1057 AND
RP LYS-1258, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-581 AND LYS-1177, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-323; LYS-1057 AND LYS-1258, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-323; LYS-581 AND LYS-666, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-323; LYS-578; LYS-581; LYS-639;
RP LYS-656; LYS-666; LYS-1057; LYS-1163; LYS-1177; LYS-1216; LYS-1225 AND
RP LYS-1258, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16] {ECO:0007744|PDB:2HE9}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 7-179, FUNCTION, CATALYTIC
RP ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding (PubMed:20676357). Component of a putative tumor-recognition
CC complex involved in the function of NK cells (PubMed:8421688).
CC {ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:8421688}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000269|PubMed:20676357};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000305|PubMed:20676357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8421688}.
CC -!- CAUTION: A report has suggested that the protein is expressed at the
CC cell surface, associated with the cell membrane via its N-terminus.
CC However, there is no direct evidence for that localization and the
CC properties of the protein argue against it.
CC {ECO:0000305|PubMed:8421688}.
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DR EMBL; L04288; AAA35734.2; -; mRNA.
DR EMBL; AF184110; AAD56402.1; -; Genomic_DNA.
DR CCDS; CCDS2702.1; -.
DR PIR; A47328; A47328.
DR RefSeq; NP_005376.2; NM_005385.3.
DR PDB; 2HE9; X-ray; 2.00 A; A/B=7-179.
DR PDBsum; 2HE9; -.
DR AlphaFoldDB; P30414; -.
DR SMR; P30414; -.
DR BioGRID; 110885; 85.
DR IntAct; P30414; 32.
DR MINT; P30414; -.
DR STRING; 9606.ENSP00000232978; -.
DR CarbonylDB; P30414; -.
DR iPTMnet; P30414; -.
DR PhosphoSitePlus; P30414; -.
DR BioMuta; NKTR; -.
DR DMDM; 8039798; -.
DR EPD; P30414; -.
DR jPOST; P30414; -.
DR MassIVE; P30414; -.
DR MaxQB; P30414; -.
DR PaxDb; P30414; -.
DR PeptideAtlas; P30414; -.
DR PRIDE; P30414; -.
DR ProteomicsDB; 54666; -.
DR Antibodypedia; 12363; 105 antibodies from 22 providers.
DR DNASU; 4820; -.
DR Ensembl; ENST00000232978.13; ENSP00000232978.8; ENSG00000114857.19.
DR GeneID; 4820; -.
DR KEGG; hsa:4820; -.
DR MANE-Select; ENST00000232978.13; ENSP00000232978.8; NM_005385.4; NP_005376.2.
DR UCSC; uc003clo.4; human.
DR CTD; 4820; -.
DR DisGeNET; 4820; -.
DR GeneCards; NKTR; -.
DR HGNC; HGNC:7833; NKTR.
DR HPA; ENSG00000114857; Low tissue specificity.
DR MIM; 161565; gene.
DR neXtProt; NX_P30414; -.
DR OpenTargets; ENSG00000114857; -.
DR PharmGKB; PA31641; -.
DR VEuPathDB; HostDB:ENSG00000114857; -.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000158548; -.
DR HOGENOM; CLU_004527_0_0_1; -.
DR InParanoid; P30414; -.
DR OMA; THTDRYI; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P30414; -.
DR TreeFam; TF318563; -.
DR PathwayCommons; P30414; -.
DR SignaLink; P30414; -.
DR BioGRID-ORCS; 4820; 36 hits in 1076 CRISPR screens.
DR ChiTaRS; NKTR; human.
DR EvolutionaryTrace; P30414; -.
DR GeneWiki; NKTR; -.
DR GenomeRNAi; 4820; -.
DR Pharos; P30414; Tbio.
DR PRO; PR:P30414; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P30414; protein.
DR Bgee; ENSG00000114857; Expressed in pylorus and 209 other tissues.
DR ExpressionAtlas; P30414; baseline and differential.
DR Genevisible; P30414; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
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 Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Isomerase; Isopeptide bond; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Rotamase; Ubl conjugation.
FT CHAIN 1..1462
FT /note="NK-tumor recognition protein"
FT /id="PRO_0000064217"
FT DOMAIN 10..175
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 187..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1348
FT /note="Arg/Ser tandem repeat-rich"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..457
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..567
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1012
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1335
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1371..1385
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30415"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30415"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1155
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 581
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 656
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 666
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1057
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VARIANT 271
FT /note="V -> G (in dbSNP:rs35726114)"
FT /id="VAR_061765"
FT VARIANT 861
FT /note="L -> V (in dbSNP:rs33969824)"
FT /id="VAR_051773"
FT VARIANT 935
FT /note="S -> L (in dbSNP:rs35770315)"
FT /id="VAR_051774"
FT VARIANT 1182
FT /note="M -> T (in dbSNP:rs34897686)"
FT /id="VAR_061766"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:2HE9"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2HE9"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:2HE9"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2HE9"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2HE9"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2HE9"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2HE9"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:2HE9"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2HE9"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:2HE9"
SQ SEQUENCE 1462 AA; 165677 MW; D98A1147763EF527 CRC64;
MGAQDRPQCH FDIEINREPV GRIMFQLFSD ICPKTCKNFL CLCSGEKGLG KTTGKKLCYK
GSTFHRVVKN FMIQGGDFSE GNGKGGESIY GGYFKDENFI LKHDRAFLLS MANRGKHTNG
SQFFITTKPA PHLDGVHVVF GLVISGFEVI EQIENLKTDA ASRPYADVRV IDCGVLATKS
IKDVFEKKRK KPTHSEGSDS SSNSSSSSES SSESELEHER SRRRKHKRRP KVKRSKKRRK
EASSSEEPRN KHAMNPKGHS ERSDTNEKRS VDSSAKREKP VVRPEEIPPV PENRFLLRRD
MPVVTAEPEP KIPDVAPIVS DQKPSVSKSG RKIKGRGTIR YHTPPRSRSC SESDDDDSSE
TPPHWKEEMQ RLRAYRPPSG EKWSKGDKLS DPCSSRWDER SLSQRSRSWS YNGYYSDLST
ARHSGHHKKR RKEKKVKHKK KGKKQKHCRR HKQTKKRRIL IPSDIESSKS STRRMKSSCD
RERSSRSSSL SSHHSSKRDW SKSDKDVQSS LTHSSRDSYR SKSHSQSYSR GSSRSRTASK
SSSHSRSRSK SRSSSKSGHR KRASKSPRKT ASQLSENKPV KTEPLRATMA QNENVVVQPV
VAENIPVIPL SDSPPPSRWK PGQKPWKPSY ERIQEMKAKT THLLPIQSTY SLANIKETGS
SSSYHKREKN SESDQSTYSK YSDRSSESSP RSRSRSSRSR SYSRSYTRSR SLASSHSRSR
SPSSRSHSRN KYSDHSQCSR SSSYTSISSD DGRRAKRRLR SSGKKNSVSH KKHSSSSEKT
LHSKYVKGRD RSSCVRKYSE SRSSLDYSSD SEQSSVQATQ SAQEKEKQGQ MERTHNKQEK
NRGEEKSKSE RECPHSKKRT LKENLSDHLR NGSKPKRKNY AGSKWDSESN SERDVTKNSK
NDSHPSSDKE EGEATSDSES EVSEIHIKVK PTTKSSTNTS LPDDNGAWKS SKQRTSTSDS
EGSCSNSENN RGKPQKHKHG SKENLKREHT KKVKEKLKGK KDKKHKAPKR KQAFHWQPPL
EFGEEEEEEI DDKQVTQESK EKKVSENNET IKDNILKTEK SSEEDLSGKH DTVTVSSDLD
QFTKDDSKLS ISPTALNTEE NVACLQNIQH VEESVPNGVE DVLQTDDNME ICTPDRSSPA
KVEETSPLGN ARLDTPDINI VLKQDMATEH PQAEVVKQES SMSESKVLGE VGKQDSSSAS
LASAGESTGK KEVAEKSQIN LIDKKWKPLQ GVGNLAAPNA ATSSAVEVKV LTTVPEMKPQ
GLRIEIKSKN KVRPGSLFDE VRKTARLNRR PRNQESSSDE QTPSRDDDSQ SRSPSRSRSK
SETKSRHRTR SVSYSHSRSR SRSSTSSYRS RSYSRSRSRG WYSRGRTRSR SSSYRSYKSH
RTSSRSRSRS SSYDPHSRSR SYTYDSYYSR SRSRSRSQRS DSYHRGRSYN RRSRSCRSYG
SDSESDRSYS HHRSPSESSR YS
