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   27-MAR-2024, entry version 189.
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; 103.
DR   IntAct; P30414; 34.
DR   MINT; P30414; -.
DR   STRING; 9606.ENSP00000232978; -.
DR   CarbonylDB; P30414; -.
DR   GlyGen; P30414; 4 sites, 1 O-linked glycan (4 sites).
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; 9606-ENSP00000232978; -.
DR   PeptideAtlas; P30414; -.
DR   ProteomicsDB; 54666; -.
DR   Pumba; P30414; -.
DR   Antibodypedia; 12363; 120 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   AGR; HGNC:7833; -.
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; DSHHKKR; -.
DR   OrthoDB; 5324361at2759; -.
DR   PhylomeDB; P30414; -.
DR   TreeFam; TF318563; -.
DR   PathwayCommons; P30414; -.
DR   SignaLink; P30414; -.
DR   BioGRID-ORCS; 4820; 41 hits in 1156 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 211 other cell types or tissues.
DR   ExpressionAtlas; P30414; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; 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; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   Genevisible; P30414; HS.
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
//