ID   MARK2_MOUSE             Reviewed;         776 AA.
AC   Q05512; Q3T9L3; Q6PDR4; Q8BR95;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Serine/threonine-protein kinase MARK2;
DE            EC=2.7.11.1;
DE            EC=2.7.11.26;
DE   AltName: Full=ELKL motif kinase 1;
DE            Short=EMK-1;
DE   AltName: Full=MAP/microtubule affinity-regulating kinase 2;
DE   AltName: Full=PAR1 homolog;
DE   AltName: Full=PAR1 homolog b;
DE            Short=Par-1b;
DE            Short=mPar-1b;
GN   Name=Mark2; Synonyms=Emk;
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 2).
RC   TISSUE=Embryo;
RX   PubMed=8358177; DOI=10.1007/bf00360595;
RA   Inglis J.D., Lee M., Hill R.E.;
RT   "Emk, a protein kinase with homologs in yeast maps to mouse chromosome
RT   19.";
RL   Mamm. Genome 4:401-403(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=NOD; TISSUE=Spleen;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=129; TISSUE=Mammary gland;
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   [4]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=10491259; DOI=10.1006/dbio.1999.9379;
RA   Bessone S., Vidal F., Le Bouc Y., Epelbaum J., Bluet-Pajot M.T., Darmon M.;
RT   "EMK protein kinase-null mice: dwarfism and hypofertility associated with
RT   alterations in the somatotrope and prolactin pathways.";
RL   Dev. Biol. 214:87-101(1999).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11287624; DOI=10.1128/mcb.21.9.3206-3219.2001;
RA   Hurov J.B., Stappenbeck T.S., Zmasek C.M., White L.S., Ranganath S.H.,
RA   Russell J.H., Chan A.C., Murphy K.M., Piwnica-Worms H.;
RT   "Immune system dysfunction and autoimmune disease in mice lacking Emk (Par-
RT   1) protein kinase.";
RL   Mol. Cell. Biol. 21:3206-3219(2001).
RN   [6]
RP   IDENTIFICATION BY 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   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17372192; DOI=10.1073/pnas.0701179104;
RA   Hurov J.B., Huang M., White L.S., Lennerz J., Choi C.S., Cho Y.R.,
RA   Kim H.J., Prior J.L., Piwnica-Worms D., Cantley L.C., Kim J.K.,
RA   Shulman G.I., Piwnica-Worms H.;
RT   "Loss of the Par-1b/MARK2 polarity kinase leads to increased metabolic
RT   rate, decreased adiposity, and insulin hypersensitivity in vivo.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5680-5685(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; SER-483 AND SER-568, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
RC   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: Serine/threonine-protein kinase. Involved in cell polarity
CC       and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX,
CC       HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the
CC       microtubule-associated protein MAPT/TAU. Plays a key role in cell
CC       polarity by phosphorylating the microtubule-associated proteins MAP2,
CC       MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules,
CC       and their disassembly. Regulates epithelial cell polarity by
CC       phosphorylating RAB11FIP2. Involved in the regulation of neuronal
CC       migration through its dual activities in regulating cellular polarity
CC       and microtubule dynamics, possibly by phosphorylating and regulating
CC       DCX. Regulates axogenesis by phosphorylating KIF13B, promoting
CC       interaction between KIF13B and 14-3-3 and inhibiting microtubule-
CC       dependent accumulation of KIF13B. Also required for neurite outgrowth
CC       and establishment of neuronal polarity. Regulates localization and
CC       activity of some histone deacetylases by mediating phosphorylation of
CC       HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and
CC       export from the nucleus. Also acts as a positive regulator of the Wnt
CC       signaling pathway, probably by mediating phosphorylation of dishevelled
CC       proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision
CC       to build a columnar versus a hepatic epithelial cell apparently by
CC       promoting a switch from a direct to a transcytotic mode of apical
CC       protein delivery. Essential for the asymmetric development of membrane
CC       domains of polarized epithelial cells. {ECO:0000250|UniProtKB:Q7KZI7}.
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: Inhibited by PAK5; inhibition is independent of
CC       the kinase activity of PAK5. Activated by phosphorylation on Thr-208.
CC       Inhibited by phosphorylation at Ser-212 and Thr-593. Inhibited by
CC       hymenialdisine (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with PAK5; leading to inhibit the protein
CC       kinase activity (By similarity). Interacts with MAPT/TAU. Interacts
CC       with MTCL1; the interaction is direct and increases MARK2 microtubule-
CC       binding ability. Interacts (when phosphorylated at Thr-593) with YWHAZ
CC       (By similarity). Interacts with YWHAB, YWHAG and YWHAQ (By similarity).
CC       {ECO:0000250|UniProtKB:O08679, ECO:0000250|UniProtKB:Q7KZI7}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Lateral cell membrane {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q7KZI7}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q7KZI7}. Note=Phosphorylation at Thr-593 by
CC       PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ
CC       promotes relocation from the cell membrane to the cytoplasm.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q05512-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q05512-2; Sequence=VSP_013341;
CC       Name=3;
CC         IsoId=Q05512-3; Sequence=VSP_013342;
CC       Name=4;
CC         IsoId=Q05512-4; Sequence=VSP_013342, VSP_022597;
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult kidney and testis, lower
CC       levels in heart, brain, spleen, lung and liver. Expressed in the head
CC       and neural fold in 8 dpc embryos, the limb buds, telencephalic
CC       vesicles, eyes, branchial archs and heart at 11.5 dpc, the ectoderm at
CC       13 dpc and epiderm, hair and whisker follicles at 15 dpc.
CC       {ECO:0000269|PubMed:10491259}.
CC   -!- DOMAIN: The UBA domain does not seem to bind ubiquitin and ubiquitin-
CC       like and might play a role in regulating the enzyme conformation and
CC       localization. Activation of the kinase activity following
CC       phosphorylation at Thr-208 is accompanied by a conformational change
CC       that alters the orientation of the UBA domain with respect to the
CC       catalytic domain (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The KA1 domain mediates binding to phospholipids and targeting
CC       to membranes. {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in
CC       complex with STE20-related adapter-alpha (STRADA) pseudo kinase and
CC       CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase
CC       activity, leading to phosphorylation and detachment of MAPT/TAU from
CC       microtubules. Phosphorylation at Ser-212 by GSK3-beta (GSK3B) inhibits
CC       the kinase activity. Phosphorylation by CaMK1 promotes activity and is
CC       required to promote neurite outgrowth. Phosphorylation at Thr-593 by
CC       PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity
CC       and promotes binding to 14-3-3 protein YWHAZ, leading to relocation
CC       from cell membrane to cytoplasm (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice have no embryonic defect and are viable.
CC       They do not display obvious neuronal phenotype, possibly due to genetic
CC       redundancy with Mark1, Mark3 and Mark4. They however show an overall
CC       proportionate dwarfism and a peculiar hypofertility: homozygotes are
CC       not fertile when intercrossed, but are fertile in other types of
CC       crosses. They also show immune-cell dysfunction. As mice age, they
CC       develop splenomegaly, lymphadenopathy, membranoproliferative
CC       glomerulonephritis, and lymphocytic infiltrates in the lungs, parotid
CC       glands and kidneys. Moreover, mice are lean, insulin hypersensitive,
CC       resistant to high-fat-diet-induced weight gain, and hypermetabolic.
CC       {ECO:0000269|PubMed:10491259, ECO:0000269|PubMed:11287624,
CC       ECO:0000269|PubMed:17372192}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32312.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X70764; CAA50040.1; -; mRNA.
DR   EMBL; AK045329; BAC32312.1; ALT_FRAME; mRNA.
DR   EMBL; AK172444; BAE43007.1; -; mRNA.
DR   EMBL; BC058556; AAH58556.1; -; mRNA.
DR   CCDS; CCDS37903.1; -. [Q05512-4]
DR   CCDS; CCDS37904.1; -. [Q05512-1]
DR   CCDS; CCDS50378.1; -. [Q05512-3]
DR   PIR; I48609; I48609.
DR   RefSeq; NP_001073857.1; NM_001080388.2.
DR   RefSeq; NP_001073858.1; NM_001080389.2.
DR   RefSeq; NP_001073859.1; NM_001080390.2.
DR   RefSeq; NP_031954.2; NM_007928.3.
DR   AlphaFoldDB; Q05512; -.
DR   SMR; Q05512; -.
DR   BioGRID; 199437; 31.
DR   IntAct; Q05512; 15.
DR   MINT; Q05512; -.
DR   STRING; 10090.ENSMUSP00000131684; -.
DR   GlyGen; Q05512; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q05512; -.
DR   PhosphoSitePlus; Q05512; -.
DR   EPD; Q05512; -.
DR   jPOST; Q05512; -.
DR   MaxQB; Q05512; -.
DR   PaxDb; 10090-ENSMUSP00000131684; -.
DR   PeptideAtlas; Q05512; -.
DR   ProteomicsDB; 295830; -. [Q05512-1]
DR   ProteomicsDB; 295831; -. [Q05512-2]
DR   ProteomicsDB; 295832; -. [Q05512-3]
DR   ProteomicsDB; 295833; -. [Q05512-4]
DR   Pumba; Q05512; -.
DR   DNASU; 13728; -.
DR   GeneID; 13728; -.
DR   KEGG; mmu:13728; -.
DR   UCSC; uc008gks.2; mouse. [Q05512-4]
DR   UCSC; uc008gkt.2; mouse. [Q05512-3]
DR   AGR; MGI:99638; -.
DR   CTD; 2011; -.
DR   MGI; MGI:99638; Mark2.
DR   eggNOG; KOG0586; Eukaryota.
DR   InParanoid; Q05512; -.
DR   OrthoDB; 5475340at2759; -.
DR   PhylomeDB; Q05512; -.
DR   BioGRID-ORCS; 13728; 9 hits in 81 CRISPR screens.
DR   ChiTaRS; Mark2; mouse.
DR   PRO; PR:Q05512; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q05512; Protein.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0045180; C:basal cortex; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0097427; C:microtubule bundle; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0140677; F:molecular function activator activity; ISO:MGI.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR   GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0061564; P:axon development; ISO:MGI.
DR   GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR   GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; ISO:MGI.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
DR   GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd12201; MARK2_C; 1.
DR   CDD; cd14072; STKc_MARK; 1.
DR   CDD; cd14406; UBA_MARK2; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR001772; KA1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR049508; MARK1-4_cat.
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:SF56; SERINE_THREONINE-PROTEIN KINASE MARK2; 1.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF103243; KA1-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50032; KA1; 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   Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW   Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Kinase;
KW   Lipid-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Wnt signaling pathway.
FT   CHAIN           1..776
FT                   /note="Serine/threonine-protein kinase MARK2"
FT                   /id="PRO_0000086302"
FT   DOMAIN          53..304
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          323..362
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          727..776
FT                   /note="KA1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         59..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         58
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         91
FT                   /note="Phosphoserine; by CaMK1"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         92
FT                   /note="Phosphoserine; by CaMK1"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         93
FT                   /note="Phosphoserine; by CaMK1"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         208
FT                   /note="Phosphothreonine; by LKB1 and TAOK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         212
FT                   /note="Phosphoserine; by GSK3-beta"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         274
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         275
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         294
FT                   /note="Phosphothreonine; by CaMK1"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         408
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08679"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         464
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         566
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         568
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         589
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         593
FT                   /note="Phosphothreonine; by PKC/PRKCZ"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         616
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7KZI7"
FT   VAR_SEQ         321..339
FT                   /note="PDYKDPRRTELMVSMGYTR -> LTTGPRDRVDGVNGLHT (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:8358177"
FT                   /id="VSP_013341"
FT   VAR_SEQ         502..555
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_013342"
FT   VAR_SEQ         640
FT                   /note="V -> VRRNLSFRFA (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022597"
FT   CONFLICT        161..162
FT                   /note="SA -> LH (in Ref. 1; CAA50040)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="L -> P (in Ref. 1; CAA50040)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        760
FT                   /note="S -> Y (in Ref. 2; BAC32312)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   776 AA;  86306 MW;  533C8DE0B5EC507E CRC64;
     MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI GNYRLLKTIG
     KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE VRIMKVLNHP NIVKLFEVIE
     TEKTLYLVME YASGGEVFDY LVAHGRMKEK EARAKFRQIV SAVQYCHQKF IVHRDLKAEN
     LLLDADMNIK IADFGFSNEF TFGNKLDTFC GSPPYAAPEL FQGKKIDGPE VDVWSLGVIL
     YTLVSGSLPF DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK
     DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR YNEVMATYLL
     LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS ANPKQRRSSD QAVPAIPTSN
     SYSKKTQSNN AENKRPEEET GRKASSTAKV PASPLPGLDR KKTTPAPSTN SVLSTSTNRS
     RNSPLLDRAS LGQASIQNGK DSLTMPGSRA STASASAAVS AARPRQHQKS MSASVHPNKA
     SGLPPTESNC EVPRPSTAPQ RVPVASPSAH NISSSSGAPD RTNFPRGVSS RSTFHAGQLR
     QVRDQQNLPY GVTPASPSGH SQGRRGASGS IFSKFTSKFV RRNLNEPESK DRVETLRPHV
     VGSGGTDKDK EEFREAKPRS LRFTWSMKTT SSMEPNEMMR EIRKVLDANS CQSELHERYM
     LLCVHGTPGH ENFVQWEMEV CKLPRLSLNG VRFKRISGTS MAFKNIASKI ANELKL
//