M3K20_MOUSE
ID M3K20_MOUSE Reviewed; 802 AA.
AC Q9ESL4; Q3V1X8; Q8BR73; Q9ESL3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 20;
DE EC=2.7.11.25;
DE AltName: Full=Human cervical cancer suppressor gene 4 protein;
DE Short=HCCS-4;
DE AltName: Full=Leucine zipper- and sterile alpha motif kinase ZAK;
DE AltName: Full=Leucine zipper- and sterile alpha motif-containing kinase;
DE AltName: Full=MLK-like mitogen-activated protein triple kinase;
DE AltName: Full=Mitogen-activated protein kinase kinase kinase MLT;
DE AltName: Full=Mixed lineage kinase-related kinase;
DE Short=MLK-related kinase;
DE Short=MRK;
DE AltName: Full=Sterile alpha motif- and leucine zipper-containing kinase AZK;
GN Name=Map3k20 {ECO:0000312|MGI:MGI:2443258}; Synonyms=Mltk, Zak;
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:BAB16442.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AUTOPHOSPHORYLATION, HOMODIMERIZATION, AND MUTAGENESIS OF LYS-45.
RC TISSUE=Heart {ECO:0000269|PubMed:11042189};
RX PubMed=11042189; DOI=10.1074/jbc.m008595200;
RA Gotoh I., Adachi M., Nishida E.;
RT "Identification and characterization of a novel MAP kinase kinase kinase,
RT MLTK.";
RL J. Biol. Chem. 276:4276-4286(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAH23718.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH23718.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH23718.1};
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]
RP PROTEIN SEQUENCE OF 225-233, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634; SER-638; SER-649 AND
RP SER-650, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND SER-453
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
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 FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=26755636; DOI=10.1101/gr.199430.115;
RA Spielmann M., Kakar N., Tayebi N., Leettola C., Nuernberg G., Sowada N.,
RA Lupianez D.G., Harabula I., Floettmann R., Horn D., Chan W.L., Wittler L.,
RA Yilmaz R., Altmueller J., Thiele H., van Bokhoven H., Schwartz C.E.,
RA Nuernberg P., Bowie J.U., Ahmad J., Kubisch C., Mundlos S., Borck G.;
RT "Exome sequencing and CRISPR/Cas genome editing identify mutations of ZAK
RT as a cause of limb defects in humans and mice.";
RL Genome Res. 26:183-191(2016).
CC -!- FUNCTION: Stress-activated component of a protein kinase signal
CC transduction cascade. Regulates the JNK and p38 pathways
CC (PubMed:11042189). Part of a signaling cascade that begins with the
CC activation of the adrenergic receptor ADRA1B and leads to the
CC activation of MAPK14 (By similarity). Pro-apoptotic. Role in regulation
CC of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2
CC (By similarity). Involved in limb development (PubMed:26755636).
CC {ECO:0000250|UniProtKB:Q9NYL2, ECO:0000269|PubMed:11042189,
CC ECO:0000269|PubMed:26755636}.
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=2.7.11.25;
CC Evidence={ECO:0000269|PubMed:11042189};
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=2.7.11.25; Evidence={ECO:0000269|PubMed:11042189};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11042189};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation by PKN1 and
CC autophosphorylation on Thr-161 and Ser-165.
CC {ECO:0000250|UniProtKB:Q9NYL2}.
CC -!- SUBUNIT: Homodimer (PubMed:11042189). Interacts with PKN1 and ZNF33A.
CC Component of a signaling complex containing at least AKAP13, PKN1,
CC MAPK14, MAP3K20 and MAP2K3. Within this complex, AKAP13 interacts
CC directly with PKN1, which in turn recruits MAPK14, MAP2K3 and MAP3K20.
CC {ECO:0000250|UniProtKB:Q9NYL2, ECO:0000269|PubMed:11042189}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11042189}. Nucleus
CC {ECO:0000269|PubMed:11042189}. Note=Appears to shuttle between nucleus
CC and cytoplasm. {ECO:0000269|PubMed:11042189}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:11042189}; Synonyms=Alpha;
CC IsoId=Q9ESL4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11042189}; Synonyms=Beta;
CC IsoId=Q9ESL4-2; Sequence=VSP_051745, VSP_051746;
CC Name=3 {ECO:0000305};
CC IsoId=Q9ESL4-3; Sequence=VSP_051747, VSP_051748;
CC -!- DEVELOPMENTAL STAGE: Mainly expressed in heart and developing limbs.
CC {ECO:0000269|PubMed:26755636}.
CC -!- DISRUPTION PHENOTYPE: Knockout results in fully penetrant lethality at
CC 9.5 dpc due to severe cardiac edema and growth retardation. Embryos
CC show polydactyly of the feet. {ECO:0000269|PubMed:26755636}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; AB049731; BAB16442.1; -; mRNA.
DR EMBL; AB049732; BAB16443.1; -; mRNA.
DR EMBL; AK045444; BAC32371.1; -; mRNA.
DR EMBL; AK132186; BAE21021.1; -; mRNA.
DR EMBL; BC023718; AAH23718.1; -; mRNA.
DR CCDS; CCDS38143.1; -. [Q9ESL4-1]
DR CCDS; CCDS50605.1; -. [Q9ESL4-2]
DR RefSeq; NP_001158263.1; NM_001164791.1. [Q9ESL4-2]
DR RefSeq; NP_075544.1; NM_023057.5. [Q9ESL4-1]
DR RefSeq; NP_835185.2; NM_178084.4. [Q9ESL4-3]
DR RefSeq; XP_006500060.1; XM_006499997.2. [Q9ESL4-1]
DR AlphaFoldDB; Q9ESL4; -.
DR SMR; Q9ESL4; -.
DR BioGRID; 211161; 3.
DR STRING; 10090.ENSMUSP00000088334; -.
DR ChEMBL; CHEMBL4523452; -.
DR iPTMnet; Q9ESL4; -.
DR PhosphoSitePlus; Q9ESL4; -.
DR EPD; Q9ESL4; -.
DR jPOST; Q9ESL4; -.
DR MaxQB; Q9ESL4; -.
DR PaxDb; Q9ESL4; -.
DR PeptideAtlas; Q9ESL4; -.
DR PRIDE; Q9ESL4; -.
DR ProteomicsDB; 295749; -. [Q9ESL4-1]
DR ProteomicsDB; 295750; -. [Q9ESL4-2]
DR ProteomicsDB; 295751; -. [Q9ESL4-3]
DR Antibodypedia; 2065; 320 antibodies from 34 providers.
DR DNASU; 65964; -.
DR Ensembl; ENSMUST00000090824; ENSMUSP00000088334; ENSMUSG00000004085. [Q9ESL4-1]
DR Ensembl; ENSMUST00000135469; ENSMUSP00000118983; ENSMUSG00000004085. [Q9ESL4-2]
DR GeneID; 65964; -.
DR KEGG; mmu:65964; -.
DR UCSC; uc008kbs.2; mouse. [Q9ESL4-3]
DR UCSC; uc008kbv.2; mouse. [Q9ESL4-1]
DR CTD; 51776; -.
DR MGI; MGI:2443258; Map3k20.
DR VEuPathDB; HostDB:ENSMUSG00000004085; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000161352; -.
DR HOGENOM; CLU_019131_1_0_1; -.
DR InParanoid; Q9ESL4; -.
DR OMA; QSNTPFF; -.
DR OrthoDB; 938929at2759; -.
DR PhylomeDB; Q9ESL4; -.
DR TreeFam; TF106505; -.
DR BioGRID-ORCS; 65964; 6 hits in 70 CRISPR screens.
DR ChiTaRS; Zak; mouse.
DR PRO; PR:Q9ESL4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ESL4; protein.
DR Bgee; ENSMUSG00000004085; Expressed in interventricular septum and 210 other tissues.
DR ExpressionAtlas; Q9ESL4; baseline and differential.
DR Genevisible; Q9ESL4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; ISO:MGI.
DR GO; GO:0060173; P:limb development; IMP:UniProtKB.
DR GO; GO:0038066; P:p38MAPK cascade; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1904291; P:positive regulation of mitotic DNA damage checkpoint; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cytoplasm;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT CHAIN 2..802
FT /note="Mitogen-activated protein kinase kinase kinase 20"
FT /id="PRO_0000086339"
FT DOMAIN 16..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 339..410
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 287..308
FT /note="Leucine-zipper"
FT REGION 624..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80192,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P80192,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 161
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 165
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 628
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYL2"
FT VAR_SEQ 285..289
FT /note="CEIEA -> WVAPA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051747"
FT VAR_SEQ 290..802
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051748"
FT VAR_SEQ 332..454
FT /note="PSFEIGAWTEDDVYFWVQQLVRKGESSVEMSGYASLFKENNITGKRLLLLEE
FT EDLKDMGIVSKGHIIHFKSAIEKLTHDYLNLFHFPPLIKDSGGEPEENEEKIVNLELVF
FT GFHLKPGTGPQD -> LPLSARMSEESYFESKTEESNSAEMSCQITAASNGEGHGMNPG
FT LQAMMLMGFGDVFSMNKAGAVLHSGMQINMQAKQNSSKTTCKRRGKKVNMALGFSDFDL
FT SEGDDDDHDGDDAENDVDNSE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11042189"
FT /id="VSP_051745"
FT VAR_SEQ 455..802
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11042189"
FT /id="VSP_051746"
FT MUTAGEN 45
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:11042189"
FT CONFLICT 171
FT /note="P -> Q (in Ref. 2; BAC32371)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9ESL4-2:434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9ESL4-2:453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 802 AA; 91720 MW; D431DF8F312A43CC CRC64;
MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI EKEAEILSVL
SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE EMDMEHIMTW ATDVAKGMHY
LHMEAPVKVI HRDLKSRNVV IAADGVLKIC DFGASRFHNH TTHMSLVGTF PWMAPEVIQS
LPVSETCDTY SYGVVLWEML TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH
QCWEADAKKR PSFKQIISIL ESMSNDTNLP DQCNSFLHNK AEWRCEIEAT LERLKKLERD
LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYFWVQQ LVRKGESSVE
MSGYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF KSAIEKLTHD YLNLFHFPPL
IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT GPQDCKWKMY MEMDGDEVAI TYIKDVTFNT
SLPDAEILKM TKPPFVMEKW IVGIAEDQTV ECTVTYENDV RTPKLTKHVH SIQWDRTKPQ
DEVKAVQLAI QTLFSSSEGN PGSRSDSSAD CQWLDTLRMR QIASHTSLQR SQSNPILGSP
FFPYFANQDS YAAAVRRTQT PVKYQQITPS INPSRSSSPT QYGLSRNFSS LNLSSRDSGF
SSLNDSSSER GRYSDRSRNK YYRGSVSLNS SPKGRYGGKS QHSTPSRERY SGKFYRLPQS
ALNTHQSPDF KRSPNDHDRR VPRTIPGMPL HPETASKAGE EESRVSEGGW TKVEYRKKTH
RQLSAKTSKE RTRGNYRGRR NF
