TNK1_HUMAN
ID TNK1_HUMAN Reviewed; 666 AA.
AC Q13470; O95364; Q8IYI4;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Non-receptor tyrosine-protein kinase TNK1;
DE EC=2.7.10.2;
DE AltName: Full=CD38 negative kinase 1;
GN Name=TNK1 {ECO:0000312|EMBL:AAC99412.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC50427.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-598, TISSUE
RP SPECIFICITY, AND CHROMOSOMAL LOCATION.
RC TISSUE=Umbilical cord blood {ECO:0000312|EMBL:AAC50427.1};
RX PubMed=8632913;
RA Hoehn G.T., Stokland T., Amin S., Ramirez M., Hawkins A.L., Griffin C.A.,
RA Small D., Civin C.I.;
RT "Tnk1: a novel intracellular tyrosine kinase gene isolated from human
RT umbilical cord blood CD34+/Lin-/CD38- stem/progenitor cells.";
RL Oncogene 12:903-913(1996).
RN [2] {ECO:0000312|EMBL:AAC99412.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-598.
RA Hoehn G.T., Felschow D.M., Civin C.I.;
RT "Genomic structure and chromosomal mapping of the human non-receptor
RT tyrosine kinase gene, Tnk1.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH35782.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH35782.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION,
RP AND INTERACTION WITH PLCG1.
RX PubMed=10873601; DOI=10.1006/bbrc.2000.2887;
RA Felschow D.M., Civin C.I., Hoehn G.T.;
RT "Characterization of the tyrosine kinase Tnk1 and its binding with
RT phospholipase C-gamma1.";
RL Biochem. Biophys. Res. Commun. 273:294-301(2000).
RN [5]
RP IDENTIFICATION BY 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 [6]
RP FUNCTION.
RX PubMed=18974114; DOI=10.1158/0008-5472.can-08-1467;
RA Hoare S., Hoare K., Reinhard M.K., Lee Y.J., Oh S.P., May W.S. Jr.;
RT "Tnk1/Kos1 knockout mice develop spontaneous tumors.";
RL Cancer Res. 68:8723-8732(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-255; SER-502; THR-514
RP AND SER-582, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 (ISOFORM 2),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-519, AND
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-502,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND THR-514, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-502, AND
RP 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 [13]
RP IDENTIFICATION BY 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 [14]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-278; LYS-339; LYS-514; CYS-539; CYS-546
RP AND MET-598.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Involved in negative regulation of cell growth. Has tumor
CC suppressor properties. Plays a negative regulatory role in the Ras-MAPK
CC pathway. May function in signaling pathways utilized broadly during
CC fetal development and more selectively in adult tissues and in cells of
CC the lymphohematopoietic system. Could specifically be involved in
CC phospholipid signal transduction. {ECO:0000269|PubMed:10873601,
CC ECO:0000269|PubMed:18974114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Interacts with the SH3 domain of PLCG1 via its Pro-rich
CC domain. {ECO:0000269|PubMed:10873601}.
CC -!- INTERACTION:
CC Q13470; P31947: SFN; NbExp=2; IntAct=EBI-1383444, EBI-476295;
CC Q13470-2; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-11018037, EBI-11978259;
CC Q13470-2; Q13322-4: GRB10; NbExp=3; IntAct=EBI-11018037, EBI-12353035;
CC Q13470-2; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-11018037, EBI-3957636;
CC Q13470-2; O75177-5: SS18L1; NbExp=3; IntAct=EBI-11018037, EBI-12035119;
CC Q13470-2; P15622-3: ZNF250; NbExp=3; IntAct=EBI-11018037, EBI-10177272;
CC Q13470-2; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-11018037, EBI-7233259;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10873601}. Membrane
CC {ECO:0000269|PubMed:10873601}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10873601}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:8632913};
CC IsoId=Q13470-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q13470-2; Sequence=VSP_051663;
CC -!- TISSUE SPECIFICITY: Expressed in all umbilical cord blood, bone marrow
CC and adult blood cell sub-populations and in several leukemia cell
CC lines. Highly expressed in fetal blood, brain, lung, liver and kidney.
CC Detected at lower levels in adult prostate, testis, ovary, small
CC intestine and colon. Not expressed in adult lung, liver, kidney or
CC brain. {ECO:0000269|PubMed:10873601, ECO:0000269|PubMed:8632913}.
CC -!- PTM: Autophosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:10873601}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U43408; AAC50427.1; -; mRNA.
DR EMBL; AF097738; AAC99412.1; -; Genomic_DNA.
DR EMBL; BC035782; AAH35782.1; -; mRNA.
DR CCDS; CCDS45602.1; -. [Q13470-2]
DR CCDS; CCDS58510.1; -. [Q13470-1]
DR RefSeq; NP_001238831.1; NM_001251902.1. [Q13470-1]
DR RefSeq; NP_003976.2; NM_003985.4. [Q13470-2]
DR RefSeq; XP_011522347.1; XM_011524045.2. [Q13470-2]
DR AlphaFoldDB; Q13470; -.
DR SMR; Q13470; -.
DR BioGRID; 114253; 33.
DR IntAct; Q13470; 40.
DR MINT; Q13470; -.
DR STRING; 9606.ENSP00000459799; -.
DR BindingDB; Q13470; -.
DR ChEMBL; CHEMBL5334; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q13470; -.
DR GuidetoPHARMACOLOGY; 2245; -.
DR iPTMnet; Q13470; -.
DR PhosphoSitePlus; Q13470; -.
DR BioMuta; TNK1; -.
DR DMDM; 116242821; -.
DR EPD; Q13470; -.
DR jPOST; Q13470; -.
DR MassIVE; Q13470; -.
DR MaxQB; Q13470; -.
DR PaxDb; Q13470; -.
DR PeptideAtlas; Q13470; -.
DR PRIDE; Q13470; -.
DR ProteomicsDB; 59467; -. [Q13470-1]
DR ProteomicsDB; 59468; -. [Q13470-2]
DR Antibodypedia; 6049; 358 antibodies from 34 providers.
DR DNASU; 8711; -.
DR Ensembl; ENST00000570896.5; ENSP00000458834.1; ENSG00000174292.13. [Q13470-2]
DR Ensembl; ENST00000576812.5; ENSP00000459799.1; ENSG00000174292.13. [Q13470-1]
DR Ensembl; ENST00000639010.1; ENSP00000491712.1; ENSG00000283781.1. [Q13470-2]
DR Ensembl; ENST00000639430.1; ENSP00000491136.1; ENSG00000283781.1. [Q13470-1]
DR Ensembl; ENST00000688331.1; ENSP00000509611.1; ENSG00000174292.13. [Q13470-2]
DR GeneID; 8711; -.
DR KEGG; hsa:8711; -.
DR MANE-Select; ENST00000688331.1; ENSP00000509611.1; NM_003985.6; NP_003976.2. [Q13470-2]
DR UCSC; uc002ggi.5; human. [Q13470-1]
DR CTD; 8711; -.
DR DisGeNET; 8711; -.
DR GeneCards; TNK1; -.
DR HGNC; HGNC:11940; TNK1.
DR HPA; ENSG00000174292; Low tissue specificity.
DR MIM; 608076; gene.
DR neXtProt; NX_Q13470; -.
DR OpenTargets; ENSG00000174292; -.
DR PharmGKB; PA36630; -.
DR VEuPathDB; HostDB:ENSG00000174292; -.
DR eggNOG; KOG0199; Eukaryota.
DR GeneTree; ENSGT00940000162159; -.
DR HOGENOM; CLU_000288_7_39_1; -.
DR InParanoid; Q13470; -.
DR OMA; IMMNLEH; -.
DR OrthoDB; 1008736at2759; -.
DR PhylomeDB; Q13470; -.
DR TreeFam; TF316643; -.
DR PathwayCommons; Q13470; -.
DR SignaLink; Q13470; -.
DR BioGRID-ORCS; 8711; 12 hits in 1112 CRISPR screens.
DR ChiTaRS; TNK1; human.
DR GenomeRNAi; 8711; -.
DR Pharos; Q13470; Tchem.
DR PRO; PR:Q13470; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q13470; protein.
DR Bgee; ENSG00000174292; Expressed in mucosa of transverse colon and 96 other tissues.
DR ExpressionAtlas; Q13470; baseline and differential.
DR Genevisible; Q13470; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..666
FT /note="Non-receptor tyrosine-protein kinase TNK1"
FT /id="PRO_0000088173"
FT DOMAIN 116..377
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 380..445
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 446..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12931,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10028"
FT BINDING 122..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P12931,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P12931,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 411..415
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051663"
FT VARIANT 278
FT /note="V -> I (in dbSNP:rs55939858)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041863"
FT VARIANT 339
FT /note="R -> K (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041864"
FT VARIANT 514
FT /note="T -> K (in dbSNP:rs55641092)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041865"
FT VARIANT 539
FT /note="R -> C (in dbSNP:rs36046975)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041866"
FT VARIANT 546
FT /note="S -> C (in dbSNP:rs56093628)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041867"
FT VARIANT 598
FT /note="V -> M (in dbSNP:rs6503018)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:8632913, ECO:0000269|Ref.2"
FT /id="VAR_041868"
FT CONFLICT 36
FT /note="E -> G (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="R -> S (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="S -> T (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="R -> K (in Ref. 2; AAC99412)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="L -> Q (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> T (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="A -> P (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..348
FT /note="LC -> PS (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="V -> A (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="G -> D (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="A -> T (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="K -> E (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="G -> W (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="V -> A (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="H -> L (in Ref. 1; AAC50427)"
FT /evidence="ECO:0000305"
FT MOD_RES Q13470-2:411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
SQ SEQUENCE 666 AA; 72468 MW; AA7FBEF6CC778181 CRC64;
MLPEAGSLWL LKLLRDIQLA QFYWPILEEL NVTRPEHFDF VKPEDLDGIG MGRPAQRRLS
EALKRLRSGP KSKNWVYKIL GGFAPEHKEP TLPSDSPRHL PEPEGGLKCL IPEGAVCRGE
LLGSGCFGVV HRGLWTLPSG KSVPVAVKSL RVGPEGPMGT ELGDFLREVS VMMNLEHPHV
LRLHGLVLGQ PLQMVMELAP LGSLHARLTA PAPTPPLLVA LLCLFLRQLA GAMAYLGARG
LVHRDLATRN LLLASPRTIK VADFGLVRPL GGARGRYVMG GPRPIPYAWC APESLRHGAF
SSASDVWMFG VTLWEMFSGG EEPWAGVPPY LILQRLEDRA RLPRPPLCSR ALYSLALRCW
APHPADRPSF SHLEGLLQEA GPSEACCVRD VTEPGALRME TGDPITVIEG SSSFHSPDST
IWKGQNGRTF KVGSFPASAV TLADAGGLPA TRPVHRGTPA RGDQHPGSID GDRKKANLWD
APPARGQRRN MPLERMKGIS RSLESVLSLG PRPTGGGSSP PEIRQARAVP QGPPGLPPRP
PLSSSSPQPS QPSRERLPWP KRKPPHNHPM GMPGARKAAA LSGGLLSDPE LQRKIMEVEL
SVHGVTHQEC QTALGATGGD VVSAIRNLKV DQLFHLSSRS RADCWRILEH YQWDLSAASR
YVLARP
