ID   BRSK1_RAT               Reviewed;         778 AA.
AC   B2DD29; F1M6Y8;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Serine/threonine-protein kinase BRSK1;
DE            EC=2.7.11.1;
DE            EC=2.7.11.26;
DE   AltName: Full=Brain-specific serine/threonine-protein kinase 1;
DE            Short=BR serine/threonine-protein kinase 1;
DE   AltName: Full=Serine/threonine-protein kinase SAD-B {ECO:0000303|PubMed:16630837};
GN   Name=Brsk1; Synonyms=Sadb {ECO:0000303|PubMed:16630837};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT THR-189.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=18324781; DOI=10.1021/bi702528r;
RA   Fujimoto T., Yurimoto S., Hatano N., Nozaki N., Sueyoshi N., Kameshita I.,
RA   Mizutani A., Mikoshiba K., Kobayashi R., Tokumitsu H.;
RT   "Activation of SAD kinase by Ca2+/calmodulin-dependent protein kinase
RT   kinase.";
RL   Biochemistry 47:4151-4159(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF LYS-63; THR-189 AND SER-193.
RX   PubMed=16630837; DOI=10.1016/j.neuron.2006.03.018;
RA   Inoue E., Mochida S., Takagi H., Higa S., Deguchi-Tawarada M.,
RA   Takao-Rikitsu E., Inoue M., Yao I., Takeuchi K., Kitajima I., Setou M.,
RA   Ohtsuka T., Takai Y.;
RT   "SAD: a presynaptic kinase associated with synaptic vesicles and the active
RT   zone cytomatrix that regulates neurotransmitter release.";
RL   Neuron 50:261-275(2006).
RN   [4]
RP   REGULATION OF TRANSLATION.
RX   PubMed=18794346; DOI=10.1101/gad.1685008;
RA   Choi Y.J., Di Nardo A., Kramvis I., Meikle L., Kwiatkowski D.J., Sahin M.,
RA   He X.;
RT   "Tuberous sclerosis complex proteins control axon formation.";
RL   Genes Dev. 22:2485-2495(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; SER-450; SER-508;
RP   THR-583; SER-586; SER-587 AND SER-601, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Serine/threonine-protein kinase that plays a key role in
CC       polarization of neurons and centrosome duplication. Phosphorylates
CC       CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following
CC       phosphorylation and activation by STK11/LKB1, acts as a key regulator
CC       of polarization of cortical neurons, probably by mediating
CC       phosphorylation of microtubule-associated proteins such as MAPT/TAU at
CC       'Thr-523' and 'Ser-573'. Also regulates neuron polarization by
CC       mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons,
CC       leading to down-regulate WEE1 activity in polarized neurons. Also acts
CC       as a positive regulator of centrosome duplication by mediating
CC       phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131',
CC       leading to translocation of gamma-tubulin and its associated proteins
CC       to the centrosome. Involved in the UV-induced DNA damage checkpoint
CC       response, probably by inhibiting CDK1 activity through phosphorylation
CC       and activation of WEE1, and inhibition of CDC25B and CDC25C (By
CC       similarity). In neurons, localizes to synaptic vesicles and plays a
CC       role in neurotransmitter release, possibly by phosphorylating RIMS1.
CC       {ECO:0000250, ECO:0000269|PubMed:16630837}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-189 by
CC       STK11/LKB1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250}. Synapse {ECO:0000269|PubMed:16630837}. Presynaptic
CC       active zone {ECO:0000269|PubMed:16630837}. Cytoplasmic vesicle,
CC       secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:16630837}.
CC       Note=Nuclear in the absence of DNA damage. Translocated to the nucleus
CC       in response to UV- or MMS-induced DNA damage (By similarity).
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mainly present in brain. Present in presynaptic
CC       nerve terminals (at protein level). {ECO:0000269|PubMed:16630837}.
CC   -!- PTM: Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-
CC       related adapter-alpha (STRADA) pseudo kinase and CAB39. Not
CC       phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated
CC       and activated by CaMKK1. May be inactivated via dephosphorylation of
CC       Thr-189 by PP2C. May be autophosphorylated.
CC       {ECO:0000269|PubMed:18324781}.
CC   -!- MISCELLANEOUS: Protein synthesis is inhibited by the TSC1-TSC2 complex
CC       acting through TORC1 in neurons, leading to regulate neuron
CC       polarization. {ECO:0000305|PubMed:18794346}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR   EMBL; AB365521; BAG28183.1; -; mRNA.
DR   RefSeq; NP_001120809.1; NM_001127337.1.
DR   AlphaFoldDB; B2DD29; -.
DR   SMR; B2DD29; -.
DR   BioGRID; 270382; 2.
DR   IntAct; B2DD29; 1.
DR   STRING; 10116.ENSRNOP00000033679; -.
DR   iPTMnet; B2DD29; -.
DR   PhosphoSitePlus; B2DD29; -.
DR   PaxDb; 10116-ENSRNOP00000033679; -.
DR   Ensembl; ENSRNOT00000097053.1; ENSRNOP00000087514.1; ENSRNOG00000017673.8.
DR   Ensembl; ENSRNOT00055024792; ENSRNOP00055020269; ENSRNOG00055014409.
DR   Ensembl; ENSRNOT00060046487; ENSRNOP00060038644; ENSRNOG00060026686.
DR   Ensembl; ENSRNOT00065055718; ENSRNOP00065045884; ENSRNOG00065032331.
DR   GeneID; 499073; -.
DR   KEGG; rno:499073; -.
DR   UCSC; RGD:1563268; rat.
DR   AGR; RGD:1563268; -.
DR   CTD; 84446; -.
DR   RGD; 1563268; Brsk1.
DR   eggNOG; KOG0588; Eukaryota.
DR   GeneTree; ENSGT00940000161254; -.
DR   HOGENOM; CLU_000288_156_2_1; -.
DR   InParanoid; B2DD29; -.
DR   OMA; MNSLQCF; -.
DR   OrthoDB; 5475340at2759; -.
DR   PhylomeDB; B2DD29; -.
DR   PRO; PR:B2DD29; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000017673; Expressed in frontal cortex and 19 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0150034; C:distal axon; IMP:ARUK-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:UniProtKB-SubCell.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR   GO; GO:0140678; F:molecular function inhibitor activity; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
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:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0008306; P:associative learning; ISO:RGD.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; ISO:RGD.
DR   GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; ISO:RGD.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:RGD.
DR   GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
DR   GO; GO:0050770; P:regulation of axonogenesis; ISO:RGD.
DR   GO; GO:0010975; P:regulation of neuron projection development; ISO:RGD.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR   GO; GO:0009411; P:response to UV; ISO:RGD.
DR   GO; GO:0099504; P:synaptic vesicle cycle; ISO:RGD.
DR   CDD; cd14081; STKc_BRSK1_2; 1.
DR   CDD; cd14340; UBA_BRSK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR048622; BRSK1_2-like_UBA.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015940; UBA.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF95; SERINE_THREONINE-PROTEIN KINASE BRSK1 ISOFORM X1-RELATED; 1.
DR   Pfam; PF21122; KA1_BRSK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF21115; UBA_BRSK; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW   Cytoskeleton; DNA damage; Kinase; Magnesium; Metal-binding; Methylation;
KW   Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase.
FT   CHAIN           1..778
FT                   /note="Serine/threonine-protein kinase BRSK1"
FT                   /id="PRO_0000412649"
FT   DOMAIN          34..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          314..356
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..510
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..754
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         40..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         189
FT                   /note="Phosphothreonine; by LKB1"
FT                   /evidence="ECO:0000269|PubMed:18324781"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         399
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         466
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         481
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         484
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         498
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         508
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         525
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         529
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         535
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         550
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT   MOD_RES         583
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         586
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         587
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         601
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MUTAGEN         63
FT                   /note="K->R: Abolishes kinase activity."
FT                   /evidence="ECO:0000269|PubMed:16630837"
FT   MUTAGEN         189
FT                   /note="T->A: Decreased autophosphorylation; when associated
FT                   with A-193."
FT                   /evidence="ECO:0000269|PubMed:16630837"
FT   MUTAGEN         193
FT                   /note="S->A: Decreased autophosphorylation; when associated
FT                   with A-189."
FT                   /evidence="ECO:0000269|PubMed:16630837"
SQ   SEQUENCE   778 AA;  85183 MW;  A4F1E7E107359BDD CRC64;
     MSSGSKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL GVHCITGQKV
     AVKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY ENKKYLYLVL EHVSGGELFD
     YLVKKGRLTP KEARKFFRQI VSALDFCHSY SICHRDLKPE NLLLDEKNNI RIADFGMASL
     QVGDSLLETS CGSPHYACPE VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL
     EKVKRGVFHM PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP
     GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI YYLLLDRKER
     YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM EVLSITDAGS GGSPVPTRRA
     LEMAQHSQRS RSVSGASTGL SSSPLSSPRS PVFSFSPEPG VGDEARGGGS PTSKTQTLPS
     RGPRGGGAGE QPPPPSARST PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP
     GGGVGGAAWR SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI
     SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA SGGPSVFQKP
     VRFQVDISSS EGPEPSPRRD GSSGGGIYSV TFTLISGPSR RFKRVVETIQ AQLLSTHDQP
     SVQALADEKN GAQTRPAGTP PRSLQPPPGR PDPDLSSSPR RGPSKDKKLL ATNGTPLP
//