CTRO_MOUSE
ID CTRO_MOUSE Reviewed; 2055 AA.
AC P49025; O88528; O88937; O88938; Q3UM99; Q8CIJ1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Citron Rho-interacting kinase;
DE Short=CRIK;
DE EC=2.7.11.1 {ECO:0000269|PubMed:9792683};
DE AltName: Full=Rho-interacting, serine/threonine-protein kinase 21;
GN Name=Cit; Synonyms=Crik;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=8543060; DOI=10.1016/0014-5793(95)01351-2;
RA Madaule P., Furuyashiki T., Reid T., Ishizaki T., Watanabe G., Morii N.,
RA Narumiya S.;
RT "A novel partner for the GTP-bound forms of rho and rac.";
RL FEBS Lett. 377:243-248(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-126.
RC TISSUE=Keratinocyte;
RX PubMed=9792683; DOI=10.1074/jbc.273.45.29706;
RA Di Cunto F., Calautti E., Hsiao J., Ong L., Topley G., Turco E.,
RA Dotto G.P.;
RT "Citron Rho-interacting kinase, a novel tissue-specific Ser/Thr kinase
RT encompassing the Rho-Rac-binding protein Citron.";
RL J. Biol. Chem. 273:29706-29711(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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]
RP PROTEIN SEQUENCE OF 246-254, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 373-2055 (ISOFORM 4), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9697773; DOI=10.1038/28873;
RA Madaule P., Eda M., Watanabe N., Fujisawa K., Matsuoka T., Bito H.,
RA Ishizaki T., Narumiya S.;
RT "Role of citron kinase as a target of the small GTPase Rho in
RT cytokinesis.";
RL Nature 394:491-494(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 992-2055 (ISOFORM 5).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11086988; DOI=10.1016/s0896-6273(00)00090-8;
RA Di Cunto F., Imarisio S., Hirsch E., Broccoli V., Bulfone A., Migheli A.,
RA Atzori C., Turco E., Triolo R., Dotto G.P., Silengo L., Altruda F.;
RT "Defective neurogenesis in citron kinase knockout mice by altered
RT cytokinesis and massive apoptosis.";
RL Neuron 28:115-127(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-479, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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: Plays a role in cytokinesis. Required for KIF14 localization
CC to the central spindle and midbody. Probable RHO/RAC effector that
CC binds to the GTP-bound forms of RHO and RAC1. It probably binds p21
CC with a tighter specificity in vivo. Displays serine/threonine protein
CC kinase activity. Plays an important role in the regulation of
CC cytokinesis and the development of the central nervous system.
CC Phosphorylates MYL9/MLC2. {ECO:0000269|PubMed:11086988,
CC ECO:0000269|PubMed:8543060, ECO:0000269|PubMed:9697773,
CC ECO:0000269|PubMed:9792683}.
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:9792683};
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:9792683};
CC -!- SUBUNIT: Interacts with TTC3 (By similarity). Homodimer (Probable).
CC Directly interacts with KIF14 depending on the activation state
CC (stronger interaction with the kinase-dead form). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9792683}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=CRIK;
CC IsoId=P49025-1; Sequence=Displayed;
CC Name=2; Synonyms=CRIK-SK;
CC IsoId=P49025-2; Sequence=VSP_012438, VSP_012439;
CC Name=3; Synonyms=Citron;
CC IsoId=P49025-3; Sequence=VSP_012436, VSP_012437;
CC Name=4;
CC IsoId=P49025-4; Sequence=VSP_016093;
CC Name=5;
CC IsoId=P49025-5; Sequence=VSP_016094, VSP_016095;
CC -!- TISSUE SPECIFICITY: A major signal was observed in testis and brain,
CC but it was also detected in thymus, spleen, kidney, heart and lung.
CC {ECO:0000269|PubMed:11086988, ECO:0000269|PubMed:9792683}.
CC -!- DEVELOPMENTAL STAGE: Detected at 10.5 dpc with highest expression in
CC the developing central nervous system. After 16.5 dpc expression
CC decreases and at two weeks after birth is restricted to the
CC proliferating neuronal precursor cells in the external germinal layer
CC of the cerebellum and subventricular migratory stream.
CC {ECO:0000269|PubMed:11086988}.
CC -!- DISRUPTION PHENOTYPE: Death before reaching adulthood, probably due to
CC lethal epilepsy. Mice display severe defects in the olfactory bulbs,
CC the hippocampus, and the cerebellum. These defects appear to result
CC from impaired cytokinesis followed by the induction of apoptosis in
CC specific neuroblast populations. {ECO:0000269|PubMed:11086988}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72822.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC72823.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH23775.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH51165.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U39904; AAC52341.1; -; mRNA.
DR EMBL; AF086823; AAC72822.1; ALT_FRAME; mRNA.
DR EMBL; AF086824; AAC72823.1; ALT_FRAME; mRNA.
DR EMBL; AK145037; BAE26199.1; -; mRNA.
DR EMBL; AF070066; AAC27933.1; -; mRNA.
DR EMBL; BC023775; AAH23775.1; ALT_FRAME; mRNA.
DR EMBL; BC051165; AAH51165.1; ALT_FRAME; mRNA.
DR CCDS; CCDS19597.1; -. [P49025-1]
DR PIR; S68420; S68420.
DR RefSeq; XP_006530214.1; XM_006530151.3. [P49025-3]
DR AlphaFoldDB; P49025; -.
DR SMR; P49025; -.
DR BioGRID; 198720; 27.
DR IntAct; P49025; 11.
DR MINT; P49025; -.
DR STRING; 10090.ENSMUSP00000062049; -.
DR iPTMnet; P49025; -.
DR PhosphoSitePlus; P49025; -.
DR EPD; P49025; -.
DR jPOST; P49025; -.
DR MaxQB; P49025; -.
DR PaxDb; P49025; -.
DR PeptideAtlas; P49025; -.
DR PRIDE; P49025; -.
DR ProteomicsDB; 279202; -. [P49025-1]
DR ProteomicsDB; 279203; -. [P49025-2]
DR ProteomicsDB; 279204; -. [P49025-3]
DR ProteomicsDB; 279205; -. [P49025-4]
DR ProteomicsDB; 279206; -. [P49025-5]
DR DNASU; 12704; -.
DR GeneID; 12704; -.
DR UCSC; uc008zep.1; mouse. [P49025-2]
DR UCSC; uc008zet.1; mouse. [P49025-3]
DR CTD; 11113; -.
DR MGI; MGI:105313; Cit.
DR eggNOG; KOG0612; Eukaryota.
DR eggNOG; KOG0976; Eukaryota.
DR InParanoid; P49025; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; P49025; -.
DR Reactome; R-MMU-5625900; RHO GTPases activate CIT. [P49025-3]
DR Reactome; R-MMU-8980692; RHOA GTPase cycle. [P49025-3]
DR Reactome; R-MMU-9013026; RHOB GTPase cycle. [P49025-3]
DR Reactome; R-MMU-9013106; RHOC GTPase cycle. [P49025-3]
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle. [P49025-3]
DR BioGRID-ORCS; 12704; 7 hits in 29 CRISPR screens.
DR ChiTaRS; Cit; mouse.
DR PRO; PR:P49025; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P49025; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0005773; C:vacuole; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase 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:UniProtKB.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0048699; P:generation of neurons; IDA:UniProtKB.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:MGI.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IDA:MGI.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR CDD; cd00029; C1; 1.
DR CDD; cd05601; STKc_CRIK; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR017405; Citron_Rho-interacting_kinase.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR037708; CRIK_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988:SF26; PTHR22988:SF26; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038145; Citron_Rho-interacting_kinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Kinase; Metal-binding; Mitosis; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; SH3-binding; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..2055
FT /note="Citron Rho-interacting kinase"
FT /id="PRO_0000085909"
FT DOMAIN 97..359
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 360..430
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1469..1589
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1617..1907
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT ZN_FING 1388..1437
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1132..1328
FT /note="Interaction with Rho/Rac"
FT REGION 1316..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..2040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 441..1086
FT /evidence="ECO:0000255"
FT COILED 1091..1247
FT /evidence="ECO:0000255"
FT COILED 1275..1325
FT /evidence="ECO:0000255"
FT MOTIF 1979..1984
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1934..1953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 103..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O14578"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14578"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14578"
FT MOD_RES 1237
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1747
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14578"
FT MOD_RES 1966
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14578"
FT MOD_RES 2021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14578"
FT MOD_RES 2041
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14578"
FT VAR_SEQ 1..458
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8543060"
FT /id="VSP_012436"
FT VAR_SEQ 459..466
FT /note="DSQDKCHK -> MLLGEEAM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8543060"
FT /id="VSP_012437"
FT VAR_SEQ 467..494
FT /note="MEQEMTRLHRRVSEVEAVLSQKEVELKA -> VSISTAGLRPCSRILQSIYA
FT EGSAGGHC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9792683"
FT /id="VSP_012438"
FT VAR_SEQ 495..2055
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9792683"
FT /id="VSP_012439"
FT VAR_SEQ 693..735
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9697773"
FT /id="VSP_016093"
FT VAR_SEQ 1279
FT /note="K -> KGLFSRRKEDPALPTQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016094"
FT VAR_SEQ 1602
FT /note="A -> AARDHTSSEHQPVWVE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016095"
FT MUTAGEN 126
FT /note="K->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:9792683"
FT CONFLICT 78
FT /note="Q -> R (in Ref. 3; BAE26199)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="F -> L (in Ref. 3; BAE26199)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="E -> H (in Ref. 3; BAE26199)"
FT /evidence="ECO:0000305"
FT CONFLICT 1945
FT /note="Missing (in Ref. 6; AAH51165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2055 AA; 235389 MW; BDA9A12C14E12DF8 CRC64;
MLKFKYGVRN PPEASASEPI ASRASRLNLF FQGKPPLMTQ QQMSALSREG MLDALFALFE
ECSQPALMKM KHVSSFVQKY SDTIAELREL QPSARDFEVR SLVGCGHFAE VQVVREKATG
DVYAMKIMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNNL YLVMEYQPGG
DFLSLLNRYE DQLDESMIQF YLAELILAVH SVHQMGYVHR DIKPENILID RTGEIKLVDF
GSAAKMNSNK VDAKLPIGTP DYMAPEVLTV MNEDRRGTYG LDCDWWSVGV VAYEMVYGKT
PFTEGTSART FNNIMNFQRF LKFPDDPKVS SELLDLLQSL LCVQKERLKF EGLCCHPFFA
RTDWNNIRNS PPPFVPTLKS DDDTSNFDEP EKNSWVSSSV CQLSPSGFSG EELPFVGFSY
SKALGYLGRS ESVVSSLDSP AKVSSMEKKL LIKSKELQDS QDKCHKMEQE MTRLHRRVSE
VEAVLSQKEV ELKASETQRS LLEQDLATYI TECSSLKRSL EQARMEVSQE DDKALQLLHD
IREQSRKLQE IKEQEYQAQV EEMRLMMNQL EEDLVSARRR SDLYESELRE SRLAAEEFKR
KANECQHKLM KAKDQGKPEV GEYSKLEKIN AEQQLKIQEL QEKLEKAVKA STEATELLQN
IRQAKERAER ELEKLHNRED SSEGIKKKLV EAEERRHSLE NKVKRLETME RRENRLKDDI
QTKSEQIQQM ADKILELEEK HREAQVSAQH LEVHLKQKEQ HYEEKIKVLD NQIKKDLADK
ESLENMMQRH EEEAHEKGKI LSEQKAMINA MDSKIRSLEQ RIVELSEANK LAANSSLFTQ
RNMKAQEEMI SELRQQKFYL ETQAGKLEAQ NRKLEEQLEK ISHQDHSDKS RLLELETRLR
EVSLEHEEQK LELKRQLTEL QLSLQERESQ LTALQAARAA LESQLRQAKT ELEETTAEAE
EEIQALTAHR DEIQRKFDAL RNSCTVITDL EEQLNQLTED NAELNNQNFY LSKQLDEASG
ANDEIVQLRS EVDHLRREIT EREMQLTSQK QTMEALKTTC TMLEEQVLDL EALNDELLEK
ERQWEAWRSV LGDEKSQFEC RVRELQRMLD TEKQSRARAD QRITESRQVV ELAVKEHKAE
ILALQQALKE QKLKAESLSD KLNDLEKKHA MLEMNARSLQ QKLETERELK QRLLEEQAKL
QQQMDLQKNH IFRLTQGLQE ALDRADLLKT ERSDLEYQLE NIQVLYSHEK VKMEGTISQQ
TKLIDFLQAK MDQPAKKKKV PLQYNELKLA LEKEKARCAE LEEALQKTRI ELRSAREEAA
HRKATDHPHP STPATARQQI AMSAIVRSPE HQPSAMSLLA PPSSRRKESS TPEEFSRRLK
ERMHHNIPHR FNVGLNMRAT KCAVCLDTVH FGRQASKCLE CQVMCHPKCS TCLPATCGLP
AEYATHFTEA FCRDKMNSPG LQSKEPGSSL HLEGWMKVPR NNKRGQQGWD RKYIVLEGSK
VLIYDNEARE AGQRPVEEFE LCLPDGDVSI HGAVGASELA NTAKADVPYI LKMESHPHTT
CWPGRTLYLL APSFPDKQRW VTALESVVAG GRVSREKAEA DAKLLGNSLL KLEGDDRLDM
NCTLPFSDQV VLVGTEEGLY ALNVLKNSLT HIPGIGAVFQ IYIIKDLEKL LMIAGEERAL
CLVDVKKVKQ SLAQSHLPAQ PDVSPNIFEA VKGCHLFAAG KIENSLCICA AMPSKVVILR
YNDNLSKYCI RKEIETSEPC SCIHFTNYSI LIGTNKFYEI DMKQYTLDEF LDKNDHSLAP
AVFASSSNSF PVSIVQANSA GQREEYLLCF HEFGVFVDSY GRRSRTDDLK WSRLPLAFAY
REPYLFVTHF NSLEVIEIQA RSSLGSPARA YLEIPNPRYL GPAISSGAIY LASSYQDKLR
VICCKGNLVK ESGTEQHRVP STSRSSPNKR GPPTYNEHIT KRVASSPAPP EGPSHPREPS
TPHRYRDREG RTELRRDKSP GRPLEREKSP GRMLSTRRER SPGRLFEDSS RGRLPAGAVR
TPLSQVNKVW DQSSV
