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 27-MAR-2024, entry version 186. 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 RC 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}. 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; 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; 10090-ENSMUSP00000102095; -. DR ProteomicsDB; 295798; -. DR DNASU; 17776; -. DR GeneID; 17776; -. DR KEGG; mmu:17776; -. DR AGR; MGI:894676; -. DR CTD; 23139; -. DR MGI; MGI:894676; Mast2. DR eggNOG; KOG0606; Eukaryota. DR InParanoid; Q60592; -. DR OrthoDB; 2915765at2759; -. DR BRENDA; 2.7.11.1; 3474. DR BioGRID-ORCS; 17776; 3 hits in 83 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: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; cd00992; PDZ_signaling; 1. DR CDD; cd05609; STKc_MAST; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR037711; MAST. DR InterPro; IPR015022; MAST_pre-PK_dom. 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; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 2; 1. DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 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; MAST3 pre-PK domain-like; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //