DCLK2_MOUSE
ID DCLK2_MOUSE Reviewed; 756 AA.
AC Q6PGN3; Q1EDG7; Q1EDG8; Q4H483; Q4W8V1; Q8BUU0; Q8BX25;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Serine/threonine-protein kinase DCLK2;
DE EC=2.7.11.1;
DE AltName: Full=CaMK-like CREB regulatory kinase 2;
DE Short=CL2;
DE Short=CLICK-II;
DE Short=CLICK2;
DE AltName: Full=Doublecortin-like and CAM kinase-like 2;
DE AltName: Full=Doublecortin-like kinase 2;
GN Name=Dclk2; Synonyms=Dcamkl2;
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] (ISOFORMS 3; 4 AND 5), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP LYS-422.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=16684769; DOI=10.1074/jbc.m513212200;
RA Ohmae S., Takemoto-Kimura S., Okamura M., Adachi-Morishima A., Nonaka M.,
RA Fuse T., Kida S., Tanji M., Furuyashiki T., Arakawa Y., Narumiya S.,
RA Okuno H., Bito H.;
RT "Molecular identification and characterization of a family of kinases with
RT homology to Ca2+/calmodulin-dependent protein kinases I/IV.";
RL J. Biol. Chem. 281:20427-20439(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Shimomura S., Nagamine T., Sueyoshi N., Kameshita I.;
RT "Molecular cloning and expression of mouse doublecortin like protein
RT kinase.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryonic stem cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=16869982; DOI=10.1186/1471-2164-7-188;
RA Reiner O., Coquelle F.M., Peter B., Levy T., Kaplan A., Sapir T., Orr I.,
RA Barkai N., Eichele G., Bergmann S.;
RT "The evolving doublecortin (DCX) superfamily.";
RL BMC Genomics 7:188-188(2006).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MAPK8IP1; MAPK8IP2; MAPK9;
RP PPP1R9B AND ACTIN.
RX PubMed=16628014; DOI=10.4161/cc.5.9.2715;
RA Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T.,
RA Brody Y., Orr I., Barkai N., Eichele G., Reiner O.;
RT "Common and divergent roles for members of the mouse DCX superfamily.";
RL Cell Cycle 5:976-983(2006).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18075264; DOI=10.1159/000109861;
RA Tuy F.P.D., Saillour Y., Kappeler C., Chelly J., Francis F.;
RT "Alternative transcripts of Dclk1 and Dclk2 and their expression in
RT doublecortin knockout mice.";
RL Dev. Neurosci. 30:171-186(2008).
RN [8]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19342486; DOI=10.1073/pnas.0812687106;
RA Kerjan G., Koizumi H., Han E.B., Dube C.M., Djakovic S.N., Patrick G.N.,
RA Baram T.Z., Heinemann S.F., Gleeson J.G.;
RT "Mice lacking doublecortin and doublecortin-like kinase 2 display altered
RT hippocampal neuronal maturation and spontaneous seizures.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6766-6771(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [10]
RP REVIEW, AND GENE FAMILY.
RX PubMed=20236041; DOI=10.2174/187152410790780118;
RA Dijkmans T.F., van Hooijdonk L.W.A., Fitzsimons C.P., Vreugdenhil E.;
RT "The doublecortin gene family and disorders of neuronal structure.";
RL Cent. Nerv. Syst. Agents Med. Chem. 10:32-46(2010).
CC -!- FUNCTION: Protein kinase with a significantly reduced Ca(2+)+/CAM
CC affinity and dependence compared to other members of the CaMK family.
CC May play a role in the down-regulation of CRE-dependent gene activation
CC probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the
CC resulting retention of TORC2 in the cytoplasm.
CC {ECO:0000269|PubMed:16684769}.
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 -!- SUBUNIT: Binds to and stabilizes microtubules (By similarity).
CC Interacts with MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK9/JNK2,
CC PPP1R9B/NEURABIN-2 and actin. {ECO:0000250,
CC ECO:0000269|PubMed:16628014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16628014, ECO:0000269|PubMed:16684769}.
CC Note=Colocalizes with microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q6PGN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGN3-2; Sequence=VSP_012797;
CC Name=3; Synonyms=alpha;
CC IsoId=Q6PGN3-3; Sequence=VSP_038892, VSP_012797;
CC Name=4; Synonyms=beta1;
CC IsoId=Q6PGN3-4; Sequence=VSP_038892, VSP_038895, VSP_038896;
CC Name=5; Synonyms=beta2;
CC IsoId=Q6PGN3-5; Sequence=VSP_038892, VSP_012797, VSP_038895,
CC VSP_038896;
CC Name=6;
CC IsoId=Q6PGN3-6; Sequence=VSP_038893, VSP_038894;
CC -!- TISSUE SPECIFICITY: Expressed in the central and peripheral nervous
CC system including the brain, spinal cord, cranial and dorsal root
CC ganglia and in the parasympathetic ganglia. Present in neurons, but not
CC in glial cells, in most forebrain areas. Strong expression in the
CC hippocampal CA1 pyramidal cell layer. Expressed in the photoreceptor
CC sensory cilium complex and in eyes. Also detected in individual cells
CC of the olfactory epithelium. {ECO:0000269|PubMed:16684769,
CC ECO:0000269|PubMed:16869982, ECO:0000269|PubMed:18075264,
CC ECO:0000269|PubMed:19342486}.
CC -!- DEVELOPMENTAL STAGE: At 17.5 dpc, predominantly expressed in the
CC central nervous system, throughout the forebrain, midbrain, hindbrain,
CC and the spinal cord. Expressed in the developing neocortex and at low
CC levels in the ventricular zone, especially in the outer neuroblastic
CC layer. In the developing retina, strongly expressed in the postmitotic
CC inner neuroblastic layer. Also found in the developing ovary and, to a
CC lower extent, throughout the kidney. {ECO:0000269|PubMed:16684769,
CC ECO:0000269|PubMed:16869982, ECO:0000269|PubMed:18075264}.
CC -!- DOMAIN: The doublecortin domains are involved in the colocalization
CC with microtubules.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Frequent spontaneous seizures that originate in
CC the hippocampus, with most animals dying in the first few months of
CC life. {ECO:0000269|PubMed:19342486}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AY968049; AAY40243.1; -; mRNA.
DR EMBL; AY968050; AAY40244.1; -; mRNA.
DR EMBL; AY968051; AAY40245.1; -; mRNA.
DR EMBL; AB198721; BAE06836.1; -; mRNA.
DR EMBL; AK049179; BAC33590.1; -; mRNA.
DR EMBL; AK082633; BAC38555.1; -; mRNA.
DR EMBL; BC056921; AAH56921.1; -; mRNA.
DR CCDS; CCDS17448.1; -. [Q6PGN3-1]
DR CCDS; CCDS79936.1; -. [Q6PGN3-2]
DR RefSeq; NP_001182425.1; NM_001195496.1. [Q6PGN3-3]
DR RefSeq; NP_001182426.1; NM_001195497.1. [Q6PGN3-2]
DR RefSeq; NP_001182427.1; NM_001195498.1. [Q6PGN3-4]
DR RefSeq; NP_001182428.1; NM_001195499.1. [Q6PGN3-5]
DR RefSeq; NP_081815.3; NM_027539.5. [Q6PGN3-1]
DR AlphaFoldDB; Q6PGN3; -.
DR SMR; Q6PGN3; -.
DR BioGRID; 214240; 5.
DR STRING; 10090.ENSMUSP00000029719; -.
DR iPTMnet; Q6PGN3; -.
DR PhosphoSitePlus; Q6PGN3; -.
DR SwissPalm; Q6PGN3; -.
DR EPD; Q6PGN3; -.
DR MaxQB; Q6PGN3; -.
DR PaxDb; Q6PGN3; -.
DR PeptideAtlas; Q6PGN3; -.
DR PRIDE; Q6PGN3; -.
DR ProteomicsDB; 279494; -. [Q6PGN3-1]
DR ProteomicsDB; 279495; -. [Q6PGN3-2]
DR ProteomicsDB; 279496; -. [Q6PGN3-3]
DR ProteomicsDB; 279497; -. [Q6PGN3-4]
DR ProteomicsDB; 279498; -. [Q6PGN3-5]
DR ProteomicsDB; 279499; -. [Q6PGN3-6]
DR Antibodypedia; 16499; 180 antibodies from 34 providers.
DR DNASU; 70762; -.
DR Ensembl; ENSMUST00000029719; ENSMUSP00000029719; ENSMUSG00000028078. [Q6PGN3-1]
DR Ensembl; ENSMUST00000191752; ENSMUSP00000141707; ENSMUSG00000028078. [Q6PGN3-6]
DR Ensembl; ENSMUST00000195561; ENSMUSP00000142267; ENSMUSG00000028078. [Q6PGN3-2]
DR GeneID; 70762; -.
DR KEGG; mmu:70762; -.
DR UCSC; uc008prl.3; mouse. [Q6PGN3-1]
DR UCSC; uc008prm.3; mouse. [Q6PGN3-5]
DR UCSC; uc008prn.3; mouse. [Q6PGN3-4]
DR UCSC; uc008pro.3; mouse. [Q6PGN3-3]
DR UCSC; uc008prp.3; mouse. [Q6PGN3-2]
DR UCSC; uc008prq.3; mouse. [Q6PGN3-6]
DR CTD; 166614; -.
DR MGI; MGI:1918012; Dclk2.
DR VEuPathDB; HostDB:ENSMUSG00000028078; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000154895; -.
DR InParanoid; Q6PGN3; -.
DR OMA; XNGTPSS; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q6PGN3; -.
DR TreeFam; TF318770; -.
DR BioGRID-ORCS; 70762; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Dclk2; mouse.
DR PRO; PR:Q6PGN3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6PGN3; protein.
DR Bgee; ENSMUSG00000028078; Expressed in animal zygote and 191 other tissues.
DR ExpressionAtlas; Q6PGN3; baseline and differential.
DR Genevisible; Q6PGN3; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0004672; F:protein 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; IEA:UniProtKB-KW.
DR GO; GO:0021766; P:hippocampus development; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR GO; GO:0021860; P:pyramidal neuron development; IGI:MGI.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
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 Pfam; PF03607; DCX; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00537; DCX; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..756
FT /note="Serine/threonine-protein kinase DCLK2"
FT /id="PRO_0000085923"
FT DOMAIN 72..158
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 196..279
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 393..650
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..741
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 514
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 399..407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N568"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N568"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5MPA9"
FT MOD_RES 665
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5MPA9"
FT VAR_SEQ 320
FT /note="V -> VKRAGHSSAYSTAKSPV (in isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:16684769, ECO:0000303|Ref.2"
FT /id="VSP_038892"
FT VAR_SEQ 352
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:16684769, ECO:0000303|Ref.2"
FT /id="VSP_012797"
FT VAR_SEQ 625..651
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038893"
FT VAR_SEQ 691..756
FT /note="NTALDKEGQIFCSKLCQDSSRPSREQTSPVPPSAQEAPPPLESPRPPGPPAT
FT SGCDLAGTWRRHRD -> VSGTQSSASESRGWPSWSCCLDSQGSAHGSWCLPCSCLHGG
FT LPGM (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038894"
FT VAR_SEQ 691..699
FT /note="NTALDKEGQ -> VQGHEHGSR (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16684769"
FT /id="VSP_038895"
FT VAR_SEQ 700..756
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16684769"
FT /id="VSP_038896"
FT MUTAGEN 422
FT /note="K->A: Loss of kinase activity. No effect on
FT colocalization with microtubules."
FT /evidence="ECO:0000269|PubMed:16684769"
FT CONFLICT 33
FT /note="G -> D (in Ref. 1; AAY40245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 82979 MW; C658F0999547B779 CRC64;
MASTRSIELE HFEERDKRPR PGSRRGAPSS SGGSSISGPK GNGLIPSPAH SAHCSFYRTR
TLQALSSEKK AKKARFYRNG DRYFKGLVFA ISNDRFRSFD ALLIELTRSL SDNVNLPQGV
RTIYTIDGSR KVTSLDELLE GESYVCASNE PFRKVDYTKN VNPNWSVNIK GGTTRTLAVA
SAKSEVKESK DFIKPKLVTV IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TEAIKLDSGV
VKRLCTLDGK QVTCLQDFFG DDDVFIACGP EKYRYAQDDF VLDHSECRVL KSSYSRASAA
KYSGSRSPGF SRRSKSPASV NGTPSSQLST PKSTKSSSSS PTSPGSFRGL KQISAQGRSS
SNVNGGPELD RCLSPEGVNG NRCSESFPLL EKYRIGKVIG DGNFAVVKEC VDRYTGKEFA
LKIIDKAKCC GKEHLIENEV SILRRVKHPN IIMLVEEMET ATDLFLVMEL VKGGDLFDAI
TSSTKYTERD GSAMVYNLAN ALRYLHSLSI VHRDIKPENL LVCEYPDGTK SLKLGDFGLA
TVVEGPLYTV CGTPTYVAPE IIAETGYGLK VDVWAAGVIT YILLCGFPPF RSENNLQEDL
FDQILAGKLE FPAPYWDNIT DSAKELISQM LQVNVEARCT AGEILSHPWV SDDASQENNM
QAEVTGKLKQ HFNNALPKQN STTTGVSVIM NTALDKEGQI FCSKLCQDSS RPSREQTSPV
PPSAQEAPPP LESPRPPGPP ATSGCDLAGT WRRHRD
