MAST4_MOUSE
ID MAST4_MOUSE Reviewed; 2618 AA.
AC Q811L6; E9QAH7; Q3UVE7; Q62489; Q6ZQE0; Q8BME3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Microtubule-associated serine/threonine-protein kinase 4;
DE EC=2.7.11.1;
GN Name=Mast4 {ECO:0000312|EMBL:AAH42511.1, ECO:0000312|MGI:MGI:1918885};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE23322.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23322.1};
RC TISSUE=Bone marrow {ECO:0000269|PubMed:16141072},
RC Cerebellum {ECO:0000312|EMBL:BAE23322.1}, and Wolffian duct;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH42511.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-2618 (ISOFORM 2).
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH42511.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH42511.1};
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, ECO:0000312|EMBL:BAC97924.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1671-2618 (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC97924.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:CAB01547.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2398-2498 (ISOFORM 1).
RC TISSUE=Cochlea {ECO:0000312|EMBL:CAB01547.1};
RX PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D.,
RA Pujol R., Petit C.;
RT "Cloning of the genes encoding two murine and human cochlear unconventional
RT type I myosins.";
RL Genomics 40:332-341(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-211; SER-1290;
RP SER-1368; SER-1395 AND SER-2549, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, Pancreas, 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).
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:Q60592};
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:Q60592};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q60592};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60592}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14621295, ECO:0000269|PubMed:16141072,
CC ECO:0000269|PubMed:9119401};
CC IsoId=Q811L6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q811L6-2; Sequence=VSP_041616, VSP_052478, VSP_052479,
CC VSP_052480;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK090136; Type=Frameshift; Evidence={ECO:0000269|PubMed:16141072};
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DR EMBL; AK032755; BAC28008.1; -; mRNA.
DR EMBL; AK090136; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK137360; BAE23322.1; -; mRNA.
DR EMBL; AC112791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042511; AAH42511.1; -; mRNA.
DR EMBL; AK129114; BAC97924.1; -; mRNA.
DR EMBL; Z78145; CAB01547.1; -; mRNA.
DR CCDS; CCDS49349.1; -. [Q811L6-1]
DR RefSeq; NP_780380.2; NM_175171.3. [Q811L6-1]
DR AlphaFoldDB; Q811L6; -.
DR SMR; Q811L6; -.
DR BioGRID; 236582; 2.
DR STRING; 10090.ENSMUSP00000128464; -.
DR iPTMnet; Q811L6; -.
DR PhosphoSitePlus; Q811L6; -.
DR jPOST; Q811L6; -.
DR MaxQB; Q811L6; -.
DR PaxDb; Q811L6; -.
DR PeptideAtlas; Q811L6; -.
DR PRIDE; Q811L6; -.
DR ProteomicsDB; 292174; -. [Q811L6-1]
DR ProteomicsDB; 292175; -. [Q811L6-2]
DR Antibodypedia; 627; 106 antibodies from 23 providers.
DR DNASU; 328329; -.
DR Ensembl; ENSMUST00000167058; ENSMUSP00000128464; ENSMUSG00000034751. [Q811L6-1]
DR GeneID; 328329; -.
DR KEGG; mmu:328329; -.
DR UCSC; uc007rsb.2; mouse. [Q811L6-1]
DR CTD; 375449; -.
DR MGI; MGI:1918885; Mast4.
DR VEuPathDB; HostDB:ENSMUSG00000034751; -.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000156399; -.
DR HOGENOM; CLU_000288_9_4_1; -.
DR InParanoid; Q811L6; -.
DR OMA; PLSAHAX; -.
DR OrthoDB; 323328at2759; -.
DR PhylomeDB; Q811L6; -.
DR TreeFam; TF313149; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 328329; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Mast4; mouse.
DR PRO; PR:Q811L6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q811L6; protein.
DR Bgee; ENSMUSG00000034751; Expressed in humerus cartilage element and 223 other tissues.
DR ExpressionAtlas; Q811L6; baseline and differential.
DR Genevisible; Q811L6; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 1.20.1480.20; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015022; MA_Ser/Thr_Kinase_dom.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; SSF140482; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2618
FT /note="Microtubule-associated serine/threonine-protein
FT kinase 4"
FT /id="PRO_0000293629"
FT DOMAIN 568..841
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 842..904
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1139..1227
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1607..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1767..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..2254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2288..2369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2381..2618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1257
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1906..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1964..1995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2005..2031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2116..2150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2165..2194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2434..2462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2473..2492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2508..2532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2597..2618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 691
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 574..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 1395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 1521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 1776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 1819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 1906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 2439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 2517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15021"
FT MOD_RES 2549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 350..521
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041616"
FT VAR_SEQ 1030..1096
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052478"
FT VAR_SEQ 1263..1282
FT /note="SLFKKLAKQPSPLLHTSRSF -> DRKKKKKRELSSRCLPSSNR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052479"
FT VAR_SEQ 1283..2618
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052480"
FT CONFLICT 546
FT /note="M -> T (in Ref. 3; AAH42511)"
FT /evidence="ECO:0000305"
FT CONFLICT 1963
FT /note="A -> T (in Ref. 4; BAC97924)"
FT /evidence="ECO:0000305"
FT CONFLICT 1977
FT /note="K -> I (in Ref. 1; BAC28008)"
FT /evidence="ECO:0000305"
FT CONFLICT 2143
FT /note="S -> G (in Ref. 1; BAC28008)"
FT /evidence="ECO:0000305"
FT CONFLICT 2181
FT /note="A -> ATA (in Ref. 4; BAC97924)"
FT /evidence="ECO:0000305"
FT CONFLICT 2444
FT /note="S -> G (in Ref. 1; BAC28008)"
FT /evidence="ECO:0000305"
FT CONFLICT 2507
FT /note="D -> E (in Ref. 1; BAE23322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2618 AA; 284004 MW; 493D6B86DA86BA5C CRC64;
MGEKVSEAPE PVPRGCSGHG ARTLVSSAAA VSSEGASSAE SSSGSETLSE EGEPSRFSCR
SQPPRPPGGA LGTRLPAAWA PARVALERGV PTLPLPHPGG AVLPVPQVSS ASQEEQDEEL
DHILSPPPMP FRKCSNPDVA CGLGKSLKYK RQLSEDGKQL RRGSLGGALT GRYLLPNPVA
GQAWPASAET SNLVRMRSQA LGQSAPSLTA SLKELSLPRR GSLCRTSNRK SLIGNGQSPA
LPRPHSPLSA HAGNSPQDSP RNFSPSASAH FSFARRTDGR RWSLASLPSS GYGTNTPSST
VSSSCSSQEK LHQLPYQPTP DELHFLSKHF CTTESIATEN RCRNTPMRPR SRSLSPGRSP
ACCDHEIIMM NHVYKERFPK ATAQMEERLK EIITSYSPDH VLPLADGVLS FTHHQIIELA
RDCLDKSHQG LITSRYFFEL QHKLDKLLQE AHDRSESGEL AFIKQLVRKI LIVIARPARL
LECLEFDPEE FYYLLEAAEG HAKEGQGIKT DIPRYIISQL GLNKDPLEEM AQLGNYDSRT
AETPEMDESV SSSNTSLRLR RKPRESDFET IKLISNGAYG AVYFVRHKES RQRFAMKKIN
KQNLILRNQI QQAFVERDIL TFAENPFVVS MYCSFETRRH LCMVMEYVEG GDCATLMKNM
GPLPVDMARM YFAETVLALE YLHNYGIVHR DLKPDNLLVT SMGHIKLTDF GLSKVGLMSM
TTNLYEGHIE KDAREFLDKQ VCGTPEYIAP EVILRQGYGK PVDWWAMGII LYEFLVGCVP
FFGDTPEELF GQVISDEINW PEKDEAPPPD AQELITLLLR QNPLERLGTG GAYEVKQHRF
FRSLDWNSLL RQKAEFIPQL ESEDDTSYFD TRSEKYHHME TEEEDDTNDE DFTVEIRQFS
SCSHRFSKVF SSIDRITQNS GEDKDDSEDK TKSTTLPSTE TLSWSSEYSE MQQLSTSNSS
DTESNRCKLS SGLLPKLAIS TDGEQDEAVP CSGDPREEPE KPVPPSEECT QEEPEVTTPA
STISSSTLSV GSFSEHLDQI NGRSECVDST DNSSKPSSEP TSHVARQRLE STEKKKISGK
VTKSLSASAL SLMIPGDMFA VSPLGSPMSP HSLSSDPSSS RDSSPSRDSS AASASPHQPI
VIHSSGKNYG FTIRAIRVYV GDSDIYTVHH IVWNVEEGSP AYQAGLKAGD LITHINGEPV
HGLVHTEVIE LLLKSGNKVS ITTTPFENTS IKTGPARRNS YKGRMVRRSK KSKKKESLER
RRSLFKKLAK QPSPLLHTSR SFSCLNRSLS SGESLPGSPT HSLSPRSPTP SYRSTPDFPS
GTNSSQSSSP SSSAPNSPAG SGHIRPSTLH GLAPKLSGQR YRSGRRKSAG SIPLSPLART
PSPTPQPTSP QRSPSPLLGH SLGNAKITQA FPSKMHSPPT IVRHIVRPKS AEPPRSPLLK
RVQSEEKLSP SYGSDKKLLC SRKHSLEVTQ EEVQREQCQR EVTLQSLEEN VCDAPSLSRA
RPVEQGCLKR PVSRKVGRQE SVDDLDRDKL KAKVVVKKPE EKHESHQKPH SLGGDSESYA
LFRLEEREKK VYSKGLERSG HFENTSAELP SVGSLLKDTL HKQASVRASE GVTSDGAACS
LTPGEHSQSL GDFKRASASG ILHDSVCPIS DRPAPGKVEY SEKASQAKEL LRSEKLDSKL
ANIDYLRKKM SLDDKDDSHC AILKPKITSS AHECLPGNPI RPMAGQQETP PASENRAFIN
STHTPQMSAV SFVPLKALAG RVENGGEKAG LAAPESPVRK SPSEYKLEGR SVSCLKPIEG
TLDIALLSGP HASKTELLSP EPAQSPSPGI NVGPCVPLAL PGSSGKKGDS TSLREPSSAN
LKVNKSYLLE PRFLPPSRAL QDSLAASGPE PKSKPERKLI HPSARSPATV TESNLQQKEG
GPATHQDRST DTRNLPGPGQ TLHNVDLPRL CTRAPLPPEG TPAKEKPCLK EPSAKVKSEW
SAVRDDGHRD PCAKLCPAET GKASDSSKPL PSGGRTQPDF YKQTQTSEKA WAHAKTNHKD
SQDEVKSLAR EDSASLLYEK EIGRARKGPE PKPEVPATRC PPQPPGIEGE KREKLSAAPS
LQKQAPKEPD RKEQTSQRPG GSGPQQPPPT KELSNSASWQ HGSSPSHTLK KEPGTKAAAA
EPSTSLHDTP RSATATTTAI ATTTTTTSAG HSDCSSHKAR PGPDPSPSKS KHQDRSLSSQ
KLSAGSAKGK EPVTQPLGGS IREGKGGSKG PVDTFSAVLT TQGKASDVLV QGEGRVSIIV
HTEECPLDAK LKNTNGGCPP EMQAKHPPRQ GHLSEAADQK PLIAGEKQSP SPKHPKPSTV
KDYPSLCRQT DRSPSHQATT GDRKAEGKKC TDALYVAAPE GYKPEASPSL HHGETGLRGS
ERPPMGMGKG FSEPKGKGPG PQKSLAETGK PSGMKRSPSA TVQSSLRSAA PPEKSLSYSA
SFPEAQPGVR EVPAANSSPS SAKATGGTSE FPAPSSRDHR KLQSGGDGRS QMIKSDSLPS
FRLSTSALES HFQDPQVPIA SGHRGRALSV TAATGEPKGR ELAQPPPVRK QNACREATRA
PPAPSTDRSL PLSSEKDFVV RQRRGKETLR SSPHKKAS
