MAST4_HUMAN
ID MAST4_HUMAN Reviewed; 2623 AA.
AC O15021; A6NL49; B5ME48; E7EWQ5; J3QT34; Q05EE6; Q6ZN07; Q8N4X4; Q96LY3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Microtubule-associated serine/threonine-protein kinase 4 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=MAST4 {ECO:0000312|HGNC:HGNC:19037};
GN Synonyms=KIAA0303 {ECO:0000303|PubMed:9205841};
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] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=17086981;
RA Sun L., Gu S., Li X., Sun Y., Zheng D., Yu K., Ji C., Tang R., Xie Y.,
RA Mao Y.;
RT "Identification of a novel human MAST4 gene, a new member of the
RT microtubule associated serine-threonine kinase family.";
RL Mol. Biol. (Mosk.) 40:808-815(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lung;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1074 (ISOFORM 5), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-678 (ISOFORM 2).
RC TISSUE=Brain, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-2623 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-914; SER-1370;
RP SER-1384; SER-1419; SER-1467; SER-1523; SER-1779; SER-1822; SER-1909;
RP SER-2442; SER-2520 AND SER-2552, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1370; SER-1779 AND SER-2520,
RP AND 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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1140-1231.
RG Structural genomics consortium (SGC);
RT "Structure of the Pdz domain of human Microtubule Associated Serine-
RT Threonine Kinase 4.";
RL Submitted (MAY-2009) to the PDB data bank.
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] ARG-920; TRP-1954; LEU-2198; CYS-2290 AND
RP ASP-2467.
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 -!- 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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O15021-5; Sequence=Displayed;
CC Name=2;
CC IsoId=O15021-2; Sequence=VSP_020888;
CC Name=4;
CC IsoId=O15021-4; Sequence=VSP_035852, VSP_035853;
CC Name=3;
CC IsoId=O15021-3; Sequence=VSP_023109;
CC Name=5;
CC IsoId=O15021-6; Sequence=VSP_059373, VSP_059374;
CC -!- TISSUE SPECIFICITY: Highly expressed in most normal human tissues, with
CC an exception of in testis, small intestine, colon and peripheral blood
CC leukocyte. {ECO:0000269|PubMed:17086981}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK131421; Type=Frameshift; Evidence={ECO:0000305};
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; AY830839; AAW52510.1; -; mRNA.
DR EMBL; AC008872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC044799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033215; AAH33215.1; -; mRNA.
DR EMBL; AK057601; BAB71532.1; -; mRNA.
DR EMBL; AK131421; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB002301; BAA20762.1; -; mRNA.
DR CCDS; CCDS47224.1; -. [O15021-4]
DR CCDS; CCDS47225.1; -. [O15021-3]
DR CCDS; CCDS54861.1; -. [O15021-5]
DR CCDS; CCDS75254.1; -. [O15021-2]
DR RefSeq; NP_001158136.1; NM_001164664.1. [O15021-5]
DR RefSeq; NP_001277155.1; NM_001290226.1.
DR RefSeq; NP_001277157.1; NM_001290228.1.
DR RefSeq; NP_001284580.1; NM_001297651.1. [O15021-2]
DR RefSeq; NP_055998.1; NM_015183.2. [O15021-3]
DR RefSeq; NP_942123.1; NM_198828.2. [O15021-4]
DR RefSeq; XP_006714669.1; XM_006714606.3. [O15021-2]
DR PDB; 2W7R; X-ray; 1.60 A; A/B=1140-1231.
DR PDBsum; 2W7R; -.
DR AlphaFoldDB; O15021; -.
DR SMR; O15021; -.
DR BioGRID; 131980; 13.
DR IntAct; O15021; 9.
DR MINT; O15021; -.
DR STRING; 9606.ENSP00000385727; -.
DR ChEMBL; CHEMBL2417351; -.
DR iPTMnet; O15021; -.
DR MetOSite; O15021; -.
DR PhosphoSitePlus; O15021; -.
DR BioMuta; MAST4; -.
DR EPD; O15021; -.
DR jPOST; O15021; -.
DR MassIVE; O15021; -.
DR MaxQB; O15021; -.
DR PaxDb; O15021; -.
DR PeptideAtlas; O15021; -.
DR PRIDE; O15021; -.
DR ProteomicsDB; 18893; -.
DR ProteomicsDB; 48378; -. [O15021-5]
DR ProteomicsDB; 48380; -. [O15021-2]
DR ProteomicsDB; 48381; -. [O15021-3]
DR ProteomicsDB; 48382; -. [O15021-4]
DR Antibodypedia; 627; 106 antibodies from 23 providers.
DR DNASU; 375449; -.
DR Ensembl; ENST00000261569.11; ENSP00000261569.7; ENSG00000069020.19. [O15021-2]
DR Ensembl; ENST00000403625.7; ENSP00000385727.1; ENSG00000069020.19. [O15021-5]
DR Ensembl; ENST00000403666.5; ENSP00000384313.1; ENSG00000069020.19. [O15021-3]
DR Ensembl; ENST00000405643.5; ENSP00000384099.1; ENSG00000069020.19. [O15021-6]
DR Ensembl; ENST00000406374.5; ENSP00000385088.1; ENSG00000069020.19. [O15021-4]
DR GeneID; 375449; -.
DR KEGG; hsa:375449; -.
DR MANE-Select; ENST00000403625.7; ENSP00000385727.1; NM_001164664.2; NP_001158136.1.
DR UCSC; uc003jur.5; human. [O15021-5]
DR CTD; 375449; -.
DR DisGeNET; 375449; -.
DR GeneCards; MAST4; -.
DR HGNC; HGNC:19037; MAST4.
DR HPA; ENSG00000069020; Low tissue specificity.
DR MIM; 618002; gene.
DR neXtProt; NX_O15021; -.
DR OpenTargets; ENSG00000069020; -.
DR PharmGKB; PA134920494; -.
DR VEuPathDB; HostDB:ENSG00000069020; -.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000156399; -.
DR InParanoid; O15021; -.
DR OMA; PLSAHAX; -.
DR OrthoDB; 323328at2759; -.
DR PhylomeDB; O15021; -.
DR TreeFam; TF313149; -.
DR PathwayCommons; O15021; -.
DR SignaLink; O15021; -.
DR BioGRID-ORCS; 375449; 18 hits in 1108 CRISPR screens.
DR ChiTaRS; MAST4; human.
DR EvolutionaryTrace; O15021; -.
DR GenomeRNAi; 375449; -.
DR Pharos; O15021; Tbio.
DR PRO; PR:O15021; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O15021; protein.
DR Bgee; ENSG00000069020; Expressed in cervix squamous epithelium and 211 other tissues.
DR ExpressionAtlas; O15021; baseline and differential.
DR Genevisible; O15021; HS.
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 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2623
FT /note="Microtubule-associated serine/threonine-protein
FT kinase 4"
FT /id="PRO_0000252256"
FT DOMAIN 570..843
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 844..916
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1141..1229
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1714..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1809..1864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..2386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2398..2623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1259
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1815..1834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1844..1864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1965..1979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2069..2084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2212..2238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2342..2364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2439..2486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2602..2623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 693
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 576..584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811L6"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811L6"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811L6"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811L6"
FT MOD_RES 1419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..225
FT /note="MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEG
FT EPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGS
FT SASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGA
FT LTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSF ->
FT MDMSDPNFWTVLSNFTLPHLRSGNRLRRTQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020888"
FT VAR_SEQ 1..225
FT /note="MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEG
FT EPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGS
FT SASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGA
FT LTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSF ->
FT MDESSILRRRGLQKELSLPRRGSLIDSQKWNCLVKR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17086981"
FT /id="VSP_023109"
FT VAR_SEQ 1..225
FT /note="MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEG
FT EPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGS
FT SASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGA
FT LTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSF ->
FT MKAQRERLQIPGLTLDLTPRSLSPTPSSPGSPCSPLLAFHFWS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_059373"
FT VAR_SEQ 225..250
FT /note="FCRTSNRKSLIGNGQSPALPRPHSPL -> LIDSQKWNCLVKRPVCPNAGRT
FT SPLG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035852"
FT VAR_SEQ 251..2623
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035853"
FT VAR_SEQ 277
FT /note="R -> RRND (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_059374"
FT VARIANT 77
FT /note="A -> P (in dbSNP:rs6867856)"
FT /id="VAR_059768"
FT VARIANT 920
FT /note="Q -> R"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040787"
FT VARIANT 1954
FT /note="R -> W"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040788"
FT VARIANT 2198
FT /note="P -> L (in dbSNP:rs752429440)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040789"
FT VARIANT 2290
FT /note="S -> C"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040790"
FT VARIANT 2467
FT /note="E -> D (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040791"
FT CONFLICT 350
FT /note="R -> H (in Ref. 4; AK131421)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="M -> T (in Ref. 4; AK131421)"
FT /evidence="ECO:0000305"
FT CONFLICT 674..678
FT /note="FAETV -> YIVKL (in Ref. 4; BAB71532)"
FT /evidence="ECO:0000305"
FT CONFLICT 1624
FT /note="R -> P (in Ref. 1; AAW52510 and 5; BAA20762)"
FT /evidence="ECO:0000305"
FT CONFLICT 1799
FT /note="K -> E (in Ref. 1; AAW52510 and 5; BAA20762)"
FT /evidence="ECO:0000305"
FT STRAND 1142..1145
FT /evidence="ECO:0007829|PDB:2W7R"
FT STRAND 1153..1161
FT /evidence="ECO:0007829|PDB:2W7R"
FT STRAND 1168..1177
FT /evidence="ECO:0007829|PDB:2W7R"
FT HELIX 1182..1186
FT /evidence="ECO:0007829|PDB:2W7R"
FT STRAND 1193..1197
FT /evidence="ECO:0007829|PDB:2W7R"
FT HELIX 1207..1215
FT /evidence="ECO:0007829|PDB:2W7R"
FT TURN 1216..1219
FT /evidence="ECO:0007829|PDB:2W7R"
FT STRAND 1220..1226
FT /evidence="ECO:0007829|PDB:2W7R"
SQ SEQUENCE 2623 AA; 284097 MW; 983747097AC218E7 CRC64;
MGEKVSEAPE PVPRGCSGHG SRTPASALVA ASSPGASSAE SSSGSETLSE EGEPGGFSRE
HQPPPPPPLG GTLGARAPAA WAPASVLLER GVLALPPPLP GGAVPPAPRG SSASQEEQDE
ELDHILSPPP MPFRKCSNPD VASGPGKSLK YKRQLSEDGR QLRRGSLGGA LTGRYLLPNP
VAGQAWPASA ETSNLVRMRS QALGQSAPSL TASLKELSLP RRGSFCRTSN RKSLIGNGQS
PALPRPHSPL SAHAGNSPQD SPRNFSPSAS AHFSFARRTD GRRWSLASLP SSGYGTNTPS
STVSSSCSSQ EKLHQLPYQP TPDELHFLSK HFCTTESIAT ENRCRNTPMR PRSRSLSPGR
SPACCDHEII MMNHVYKERF PKATAQMEER LKEIITSYSP DNVLPLADGV LSFTHHQIIE
LARDCLDKSH QGLITSRYFL ELQHKLDKLL QEAHDRSESG ELAFIKQLVR KILIVIARPA
RLLECLEFDP EEFYYLLEAA EGHAKEGQGI KTDIPRYIIS QLGLNKDPLE EMAHLGNYDS
GTAETPETDE SVSSSNASLK LRRKPRESDF ETIKLISNGA YGAVYFVRHK ESRQRFAMKK
INKQNLILRN QIQQAFVERD ILTFAENPFV VSMYCSFETR RHLCMVMEYV EGGDCATLMK
NMGPLPVDMA RMYFAETVLA LEYLHNYGIV HRDLKPDNLL VTSMGHIKLT DFGLSKVGLM
SMTTNLYEGH IEKDAREFLD KQVCGTPEYI APEVILRQGY GKPVDWWAMG IILYEFLVGC
VPFFGDTPEE LFGQVISDEI NWPEKDEAPP PDAQDLITLL LRQNPLERLG TGGAYEVKQH
RFFRSLDWNS LLRQKAEFIP QLESEDDTSY FDTRSEKYHH METEEEDDTN DEDFNVEIRQ
FSSCSHRFSK VFSSIDRITQ NSAEEKEDSV DKTKSTTLPS TETLSWSSEY SEMQQLSTSN
SSDTESNRHK LSSGLLPKLA ISTEGEQDEA ASCPGDPHEE PGKPALPPEE CAQEEPEVTT
PASTISSSTL SVGSFSEHLD QINGRSECVD STDNSSKPSS EPASHMARQR LESTEKKKIS
GKVTKSLSAS ALSLMIPGDM FAVSPLGSPM SPHSLSSDPS SSRDSSPSRD SSAASASPHQ
PIVIHSSGKN YGFTIRAIRV YVGDSDIYTV HHIVWNVEEG SPACQAGLKA GDLITHINGE
PVHGLVHTEV IELLLKSGNK VSITTTPFEN TSIKTGPARR NSYKSRMVRR SKKSKKKESL
ERRRSLFKKL AKQPSPLLHT SRSFSCLNRS LSSGESLPGS PTHSLSPRSP TPSYRSTPDF
PSGTNSSQSS SPSSSAPNSP AGSGHIRPST LHGLAPKLGG QRYRSGRRKS AGNIPLSPLA
RTPSPTPQPT SPQRSPSPLL GHSLGNSKIA QAFPSKMHSP PTIVRHIVRP KSAEPPRSPL
LKRVQSEEKL SPSYGSDKKH LCSRKHSLEV TQEEVQREQS QREAPLQSLD ENVCDVPPLS
RARPVEQGCL KRPVSRKVGR QESVDDLDRD KLKAKVVVKK ADGFPEKQES HQKSHGPGSD
LENFALFKLE EREKKVYPKA VERSSTFENK ASMQEAPPLG SLLKDALHKQ ASVRASEGAM
SDGRVPAEHR QGGGDFRRAP APGTLQDGLC HSLDRGISGK GEGTEKSSQA KELLRCEKLD
SKLANIDYLR KKMSLEDKED NLCPVLKPKM TAGSHECLPG NPVRPTGGQQ EPPPASESRA
FVSSTHAAQM SAVSFVPLKA LTGRVDSGTE KPGLVAPESP VRKSPSEYKL EGRSVSCLKP
IEGTLDIALL SGPQASKTEL PSPESAQSPS PSGDVRASVP PVLPSSSGKK NDTTSARELS
PSSLKMNKSY LLEPWFLPPS RGLQNSPAVS LPDPEFKRDR KGPHPTARSP GTVMESNPQQ
REGSSPKHQD HTTDPKLLTC LGQNLHSPDL ARPRCPLPPE ASPSREKPGL RESSERGPPT
ARSERSAARA DTCREPSMEL CFPETAKTSD NSKNLLSVGR THPDFYTQTQ AMEKAWAPGG
KTNHKDGPGE ARPPPRDNSS LHSAGIPCEK ELGKVRRGVE PKPEALLARR SLQPPGIESE
KSEKLSSFPS LQKDGAKEPE RKEQPLQRHP SSIPPPPLTA KDLSSPAARQ HCSSPSHASG
REPGAKPSTA EPSSSPQDPP KPVAAHSESS SHKPRPGPDP GPPKTKHPDR SLSSQKPSVG
ATKGKEPATQ SLGGSSREGK GHSKSGPDVF PATPGSQNKA SDGIGQGEGG PSVPLHTDRA
PLDAKPQPTS GGRPLEVLEK PVHLPRPGHP GPSEPADQKL SAVGEKQTLS PKHPKPSTVK
DCPTLCKQTD NRQTDKSPSQ PAANTDRRAE GKKCTEALYA PAEGDKLEAG LSFVHSENRL
KGAERPAAGV GKGFPEARGK GPGPQKPPTE ADKPNGMKRS PSATGQSSFR STALPEKSLS
CSSSFPETRA GVREASAASS DTSSAKAAGG MLELPAPSNR DHRKAQPAGE GRTHMTKSDS
LPSFRVSTLP LESHHPDPNT MGGASHRDRA LSVTATVGET KGKDPAPAQP PPARKQNVGR
DVTKPSPAPN TDRPISLSNE KDFVVRQRRG KESLRSSPHK KAL
