ID   TNIK_MOUSE              Reviewed;        1323 AA.
AC   P83510;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=Traf2 and NCK-interacting protein kinase;
DE            EC=2.7.11.1;
GN   Name=Tnik; Synonyms=Kiaa0551;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|EMBL:BAC40365.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-327 AND 735-1323 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Hypothalamus, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1323 (ISOFORM 1).
RC   TISSUE=Embryo;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-842 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH TCF7L2 AND CTNNB1, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=19816403; DOI=10.1038/emboj.2009.285;
RA   Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S.,
RA   Heck A.J., Clevers H.;
RT   "The kinase TNIK is an essential activator of Wnt target genes.";
RL   EMBO J. 28:3329-3340(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-187; SER-324; SER-326;
RP   SER-541; THR-552; SER-611; SER-659; SER-735 AND SER-740, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   INTERACTION WITH NEDD4 AND RAP2A.
RX   PubMed=20159449; DOI=10.1016/j.neuron.2010.01.007;
RA   Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M.,
RA   Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E., Umikawa M.,
RA   Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O., Rhee J.,
RA   Brose N.;
RT   "Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite
RT   development.";
RL   Neuron 65:358-372(2010).
CC   -!- FUNCTION: Serine/threonine kinase that acts as an essential activator
CC       of the Wnt signaling pathway. Recruited to promoters of Wnt target
CC       genes and required to activate their expression. May act by
CC       phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-
CC       terminal pathway. May play a role in the response to environmental
CC       stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK
CC       which regulates neuronal dendrite extension and arborization during
CC       development. More generally, it may play a role in cytoskeletal
CC       rearrangements and regulate cell spreading (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:Q9UKE5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9UKE5};
CC   -!- SUBUNIT: Interacts (via the CNH domain) with RAP2A (GTP-bound form
CC       preferentially); the interaction is direct and required for the
CC       activation of TNIK by RAP2A. Interacts with NEDD4; recruits RAP2A to
CC       NEDD4. Interacts with TRAF2 and NCK. Interacts with TCF7L2/TCF4 and
CC       CTNNB1; the interaction is direct. Interacts with TANC1.
CC       {ECO:0000269|PubMed:19816403, ECO:0000269|PubMed:20159449}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19816403}. Cytoplasm
CC       {ECO:0000269|PubMed:19816403}. Recycling endosome {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with recycling
CC       endosomes and the cytoskeletal fraction upon RAP2A overexpression.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P83510-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P83510-2; Sequence=VSP_007351;
CC   -!- PTM: Autophosphorylated. Autophosphorylation is activated by RAP2A and
CC       induces association to the cytoskeletal fraction. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65588.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AK039113; BAC30241.1; -; mRNA.
DR   EMBL; AK041777; BAC31061.2; -; mRNA.
DR   EMBL; AK088459; BAC40365.1; -; mRNA.
DR   EMBL; BC050866; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK122306; BAC65588.2; ALT_SEQ; Transcribed_RNA.
DR   CCDS; CCDS50879.1; -. [P83510-1]
DR   RefSeq; NP_001156480.1; NM_001163008.1. [P83510-1]
DR   AlphaFoldDB; P83510; -.
DR   SMR; P83510; -.
DR   BioGRID; 576981; 261.
DR   DIP; DIP-57467N; -.
DR   IntAct; P83510; 255.
DR   MINT; P83510; -.
DR   STRING; 10090.ENSMUSP00000125081; -.
DR   GlyGen; P83510; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P83510; -.
DR   PhosphoSitePlus; P83510; -.
DR   jPOST; P83510; -.
DR   MaxQB; P83510; -.
DR   PaxDb; 10090-ENSMUSP00000125081; -.
DR   PeptideAtlas; P83510; -.
DR   ProteomicsDB; 259277; -. [P83510-1]
DR   ProteomicsDB; 259278; -. [P83510-2]
DR   Pumba; P83510; -.
DR   Antibodypedia; 2086; 631 antibodies from 33 providers.
DR   DNASU; 665113; -.
DR   Ensembl; ENSMUST00000159236.9; ENSMUSP00000124681.3; ENSMUSG00000027692.17. [P83510-1]
DR   GeneID; 665113; -.
DR   KEGG; mmu:665113; -.
DR   UCSC; uc008oty.1; mouse. [P83510-1]
DR   AGR; MGI:1916264; -.
DR   CTD; 23043; -.
DR   MGI; MGI:1916264; Tnik.
DR   VEuPathDB; HostDB:ENSMUSG00000027692; -.
DR   eggNOG; KOG0587; Eukaryota.
DR   GeneTree; ENSGT00950000183196; -.
DR   InParanoid; P83510; -.
DR   OrthoDB; 2904475at2759; -.
DR   Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR   BioGRID-ORCS; 665113; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Tnik; mouse.
DR   PRO; PR:P83510; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P83510; Protein.
DR   Bgee; ENSMUSG00000027692; Expressed in superior cervical ganglion and 210 other cell types or tissues.
DR   ExpressionAtlas; P83510; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; ISO:MGI.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR   GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR   GO; GO:0030033; P:microvillus assembly; ISO:MGI.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR   GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd06637; STKc_TNIK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; P83510; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Endosome;
KW   Kinase; Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Wnt signaling pathway.
FT   CHAIN           1..1323
FT                   /note="Traf2 and NCK-interacting protein kinase"
FT                   /id="PRO_0000086762"
FT   DOMAIN          25..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          1010..1297
FT                   /note="CNH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT   REGION          284..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..1010
FT                   /note="Mediates interaction with NEDD4"
FT                   /evidence="ECO:0000250"
FT   REGION          397..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..336
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..761
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..794
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..812
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         31..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         187
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         531
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         552
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         579
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         611
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         649
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         651
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         659
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         672
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         691
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         737
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   MOD_RES         740
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         922
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKE5"
FT   VAR_SEQ         926..962
FT                   /note="YGIGSSTKASFTPFVDPRVYQTSPTDEDEEDDESSAA -> SLK (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_007351"
FT   CONFLICT        735
FT                   /note="S -> C (in Ref. 1; BAC40365)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1323 AA;  150367 MW;  B8289189530251D2 CRC64;
     MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL AAIKVMDVTG
     DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ LWLVMEFCGA GSVTDLIKNT
     KGNTLKEEWI AYICREILRG LSHLHQHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR
     ALFLIPRNPA PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
     QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL RRDFLRLQLA
     NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE QRRRLEEQQR REKELRKQQE
     REQRRHYEEQ MRREEERRRA EHEQEYKRKQ LEEQRQAERL QRQLKQERDY LVSLQHQRQE
     QRPLEKKPLY HYKEGMSPSE KPAWAKEVEE RSRLNRQSSP AMPHKVANRI SDPNLPPRSE
     SFSISGVQPA RTPPMLRPVD PQIPQLVAVK SQGPALTASQ SVHEQPTKGL SGFQEALNVT
     SHRVEMPRQN SDPTSENPPL PTRIEKFDRS SWLRQEEDIP PKVPQRTTSI SPALARKNSP
     GNGSALGPRL GSQPIRASNP DLRRTEPVLE SSLQRTSSGS SSSSSTPSSQ PSSQGGSQPG
     SQAGSSERSR VRANSKSEGS PVLPHEPSKV KPEESRDITR PSRPADLTAL AKELRELRIE
     ETNRPLKKVT DYSSSSEESE SSEEEEEDGE SETHDGTVAV SDIPRLIPTG APGNNEQYNM
     GMVGTHGLET SHADTFGGSI SREGTLMIRE TAEEKKRSGH SDSNGFAGHI NLPDLVQQSH
     SPAGTPTEGL GRVSTHSQEM DSGAEYGIGS STKASFTPFV DPRVYQTSPT DEDEEDDESS
     AAALFTSELL RQEQAKLNEA RKISVVNVNP TNIRPHSDTP EIRKYKKRFN SEILCAALWG
     VNLLVGTENG LMLLDRSGQG KVYNLINRRR FQQMDVLEGL NVLVTISGKK NKLRVYYLSW
     LRNRILHNDP EVEKKQGWIT VGDLEGCIHY KVVKYERIKF LVIALKNAVE IYAWAPKPYH
     KFMAFKSFAD LQHKPLLVDL TVEEGQRLKV IFGSHTGFHV IDVDSGNSYD IYIPSHIQGN
     ITPHAIVILP KTDGMEMLVC YEDEGVYVNT YGRITKDVVL QWGEMPTSVA YIHSNQIMGW
     GEKAIEIRSV ETGHLDGVFM HKRAQRLKFL CERNDKVFFA SVRSGGSSQV FFMTLNRNSM
     MNW
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