MAST2_MOUSE
ID MAST2_MOUSE Reviewed; 1734 AA.
AC Q60592; Q6P9M1; Q8CHD1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Microtubule-associated serine/threonine-protein kinase 2;
DE EC=2.7.11.1;
GN Name=Mast2 {ECO:0000312|MGI:MGI:894676};
GN Synonyms=Mast205 {ECO:0000303|PubMed:8246979};
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:AAC04312.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster {ECO:0000312|EMBL:AAC04312.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAC04312.1};
RX PubMed=8246979; DOI=10.1128/mcb.13.12.7625-7635.1993;
RA Walden P.D., Cowan N.J.;
RT "A novel 205-kDa testis-specific serine/threonine protein kinase associated
RT with microtubules of the spermatid manchette.";
RL Mol. Cell. Biol. 13:7625-7635(1993).
RN [2] {ECO:0000312|EMBL:AAH60703.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH60703.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH60703.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-1734.
RC TISSUE=Brain;
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 [4] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8902215; DOI=10.1095/biolreprod55.5.1039;
RA Walden P.D., Millette C.F.;
RT "Increased activity associated with the MAST205 protein kinase complex
RT during mammalian spermiogenesis.";
RL Biol. Reprod. 55:1039-1044(1996).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP SNTB2.
RX PubMed=10404183; DOI=10.1038/10165;
RA Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K.,
RA Chamberlain J.S.;
RT "Interactions between beta 2-syntrophin and a family of microtubule-
RT associated serine/threonine kinases.";
RL Nat. Neurosci. 2:611-617(1999).
RN [6] {ECO:0000305}
RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF 482-LYS-LYS-483.
RX PubMed=14764729; DOI=10.4049/jimmunol.172.4.2559;
RA Zhou H., Xiong H., Li H., Plevy S.E., Walden P.D., Sassaroli M.,
RA Prestwich G.D., Unkeless J.C.;
RT "Microtubule-associated serine/threonine kinase-205 kDa and Fc gamma
RT receptor control IL-12 p40 synthesis and NF-kappa B activation.";
RL J. Immunol. 172:2559-2568(2004).
RN [7] {ECO:0000305}
RP FUNCTION, UBIQUITINATION, PHOSPHORYLATION, AND INTERACTION WITH TRAF6.
RX PubMed=15308666; DOI=10.1074/jbc.m404328200;
RA Xiong H., Li H., Chen Y., Zhao J., Unkeless J.C.;
RT "Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and
RT MAST205 stability.";
RL J. Biol. Chem. 279:43675-43683(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1275, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-88; SER-91; SER-149;
RP SER-836; SER-841; SER-1275 AND SER-1711, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, 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 -!- FUNCTION: Appears to link the dystrophin/utrophin network with
CC microtubule filaments via the syntrophins. Phosphorylation of DMD or
CC UTRN may modulate their affinities for associated proteins. Functions
CC in a multi-protein complex in spermatid maturation. Regulates
CC lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a
CC complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B
CC activation. {ECO:0000269|PubMed:10404183, ECO:0000269|PubMed:14764729,
CC ECO:0000269|PubMed:15308666, ECO:0000269|PubMed:8246979,
CC ECO:0000269|PubMed:8902215}.
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:0000269|PubMed:8246979};
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:0000269|PubMed:8246979};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8246979};
CC -!- SUBUNIT: Interacts with CDHR2. {ECO:0000250}.
CC -!- INTERACTION:
CC Q60592; P60484: PTEN; Xeno; NbExp=4; IntAct=EBI-493888, EBI-696162;
CC Q60592; P0CG47: UBB; Xeno; NbExp=2; IntAct=EBI-493888, EBI-413034;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10404183};
CC Peripheral membrane protein {ECO:0000269|PubMed:10404183}; Cytoplasmic
CC side {ECO:0000269|PubMed:10404183}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10404183}. Cell junction
CC {ECO:0000269|PubMed:10404183}. Note=Colocalizes with beta 2-syntrophin
CC and utrophin at neuromuscular junctions.
CC -!- TISSUE SPECIFICITY: Detected in round spermatids and residual bodies
CC but not epididymal spermatozoa (at protein level). Expressed in adult
CC but not fetal testis with levels increasing in parallel with testicular
CC development. Also expressed at high levels in heart, lower levels in
CC all other tissues tested. {ECO:0000269|PubMed:10404183,
CC ECO:0000269|PubMed:8246979, ECO:0000269|PubMed:8902215}.
CC -!- PTM: Phosphorylated and ubiquitinated. N-terminal ubiquitination leads
CC to degradation of MAST2 by proteasome-mediated proteolysis. N-terminal
CC phosphorylation appears to be a prerequisite for ubiquitination.
CC {ECO:0000269|PubMed:14764729, ECO:0000269|PubMed:15308666}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; U02313; AAC04312.1; -; mRNA.
DR EMBL; BC060703; AAH60703.1; -; mRNA.
DR EMBL; AB093264; BAC41448.1; -; mRNA.
DR PIR; A54602; A54602.
DR RefSeq; NP_001036208.1; NM_001042743.2.
DR RefSeq; NP_032667.2; NM_008641.3.
DR RefSeq; XP_017175507.1; XM_017320018.1.
DR AlphaFoldDB; Q60592; -.
DR SMR; Q60592; -.
DR BioGRID; 201600; 5.
DR IntAct; Q60592; 7.
DR MINT; Q60592; -.
DR STRING; 10090.ENSMUSP00000102095; -.
DR iPTMnet; Q60592; -.
DR PhosphoSitePlus; Q60592; -.
DR jPOST; Q60592; -.
DR MaxQB; Q60592; -.
DR PaxDb; Q60592; -.
DR PRIDE; Q60592; -.
DR ProteomicsDB; 295798; -.
DR DNASU; 17776; -.
DR GeneID; 17776; -.
DR KEGG; mmu:17776; -.
DR CTD; 23139; -.
DR MGI; MGI:894676; Mast2.
DR eggNOG; KOG0606; Eukaryota.
DR InParanoid; Q60592; -.
DR OrthoDB; 323328at2759; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 17776; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Mast2; mouse.
DR PRO; PR:Q60592; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60592; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
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 GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032655; P:regulation of interleukin-12 production; IDA:UniProtKB.
DR GO; GO:0048515; P:spermatid differentiation; IDA:UniProtKB.
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; IPR028779; MAST2.
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 PANTHER; PTHR24356:SF136; PTHR24356:SF136; 1.
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 ATP-binding; Cell junction; Cytoplasm; Cytoskeleton; Kinase; Magnesium;
KW Membrane; Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..1734
FT /note="Microtubule-associated serine/threonine-protein
FT kinase 2"
FT /id="PRO_0000086313"
FT DOMAIN 453..726
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 727..795
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1042..1130
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 112..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1705..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 576
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 459..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 942
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 1446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P0Q8"
FT MOD_RES 1711
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 482..483
FT /note="KK->RA: Abolishes LPS-stimulated IL12B synthesis."
FT /evidence="ECO:0000269|PubMed:14764729"
FT CONFLICT 162
FT /note="R -> RSHGHRTD (in Ref. 2; AAH60703)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="R -> A (in Ref. 2; AAH60703)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..278
FT /note="PSLT -> LAD (in Ref. 2; AAH60703)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="R -> C (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1228
FT /note="Missing (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1502
FT /note="T -> S (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1521
FT /note="V -> L (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1734 AA; 190534 MW; 97292FACD85F12E3 CRC64;
MVTGLSPLLF RKLSNPDIFA PTGKVKLQRQ LSQDDCKLRR GSLASSLSGK QLLPLSSSVH
SSVGQVTWQS TGEASNLVRM RNQSLGQSAP SLTAGLKELS LPRRGSFCRT SNRKSLIVTS
STSPTLPRPH SPLHGHTGNS PLDSPRNFSP NAPAHFSFVP ARRTDGRRWS LASLPSSGYG
TNTPSSTVSS SCSSQEKLHQ LPFQPTADEL HFLTKHFSTE NVPDEEGRRS PRMRPRSRSL
SPGRSPVSFD SEIIMMNHVY KERFPKATAQ MEERPSLTFI SSNTPDSVLP LADGALSFIH
HQVIEMARDC LDKSRSGLIT SHYFYELQEN LEKLLQDAHE RSESSDVAFV IQLVKKLMII
IARPARLLEC LEFDPEEFYH LLEAAEGHAK EGHGIKCDIP RYIVSQLGLT RDPLEEMAQL
SSYDSPDTPE TDDSVEGRGV SQPSQKTPSE EDFETIKLIS NGAYGAVFLV RHKSTRQRFA
MKKINKQNLI LRNQIQQAFV ERDILTFAEN PFVVSMFCSF ETKRHLCMVM EYVEGGDCAT
LLKNIGALPV DMVRLYFAET VLALEYLHNY GIVHRDLKPD NLLITSMGHI KLTDFGLSKI
GLMSLTTNLY EGHIEKDARE FLDKQVCGTP EYIAPEVILR QGYGKPVDWW AMGIILYEFL
VGCVPFFGDT PEELFGQVIS DEIVWPEGDD ALPPDAQDLT SKLLHQNPLE RLGTSSAYEV
KQHPFFMGLD WTGLLRQKAE FIPQLESEDD TSYFDTRSER YHHVDSEDEE EVSEDGCLEI
RQFSSCSPRF SKVYSSMERL SLLEERRTPP PTKRSLSEEK EDHSDGLAGL KGRDRSWVIG
SPEILRKRLS VSESSHTESD SSPPMTVRHR CSGLPDGPHC PEETSSTPRK QQQEGIWVLI
PPSGEGSSRP VPERPLERQL KLDEEPPGQS SRCCPALETR GRGTPQLAEE ATAKAISDLA
VRRARHRLLS GDSIEKRTTR PVNKVIKSAS ATALSLLIPS EHHACSPLAS PMSPHSQSSN
PSSRDSSPSR DFLPALGSLR PPIIIHRAGK KYGFTLRAIR VYMGDTDVYT VHHMVWHVED
GGPASEAGLR QGDLITHVNG EPVHGLVHTE VVELVLKSGN KVSISTTPLE NTSIKVGPAR
KGSYKAKMAR RSKRSKGKDG QESRKRSSLF RKITKQASLL HTSRSLSSLN RSLSSGESGP
GSPTHSHSLS PRSPPQGYRV APDAVHSVGG NSSQSSSPSS SVPSSPAGSG HTRPSSLHGL
APKLQRQYRS PRRKSAGSIP LSPLAHTPSP PATAASPQRS PSPLSGHGSQ SFPTKLHLSP
PLGRQLSRPK SAEPPRSPLL KRVQSAEKLA AALAAAEKKL APSRKHSLDL PHGELKKELT
PREASPLEVV GTRSVLSGKG PLPGKGVLQP APSRALGTLR QDRAERRESL QKQEAIREVD
SSEDDTDEEP ENSQATQEPR LSPHPEASHN LLPKGSGEGT EEDTFLHRDL KKQGPVLSGL
VTGATLGSPR VDVPGLSPRK VSRPQAFEEA TNPLQVPSLS RSGPTSPTPS EGCWKAQHLH
TQALTALCPS FSELTPTGCS AATSTSGKPG TWSWKFLIEG PDRASTNKTI TRKGEPANSQ
DTNTTVPNLL KNLSPEEEKP QPPSVPGLTH PLLEVPSQNW PWESECEQME KEEPSLSITE
VPDSSGDRRQ DIPCRAHPLS PETRPSLLWK SQELGGQQDH QDLALTSDEL LKQT
