ID   KKCC2_MOUSE             Reviewed;         588 AA.
AC   Q8C078; Q80TS0; Q8BXM8; Q8C0G3; Q8CH42; Q8QZT7;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase kinase 2;
DE            Short=CaM-KK 2;
DE            Short=CaM-kinase kinase 2;
DE            Short=CaMKK 2;
DE            EC=2.7.11.17;
DE   AltName: Full=Calcium/calmodulin-dependent protein kinase kinase beta;
DE            Short=CaM-KK beta;
DE            Short=CaM-kinase kinase beta;
DE            Short=CaMKK beta;
GN   Name=Camkk2; Synonyms=Kiaa0787;
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 1), AND TISSUE SPECIFICITY.
RX   PubMed=12654522; DOI=10.1016/s0169-328x(02)00698-8;
RA   Vinet J., Carra S., Blom J.M.C., Harvey M., Brunello N., Barden N.,
RA   Tascedda F.;
RT   "Cloning of mouse Ca2+/calmodulin-dependent protein kinase kinase beta
RT   (CaMKKbeta) and characterization of CaMKKbeta and CaMKKalpha distribution
RT   in the adult mouse brain.";
RL   Brain Res. Mol. Brain Res. 111:216-221(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, Retina, and Testis;
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 2).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 207-588 (ISOFORM 5).
RC   TISSUE=Brain;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14586002; DOI=10.1523/jneurosci.23-30-09752.2003;
RA   Peters M., Mizuno K., Ris L., Angelo M., Godaux E., Giese K.P.;
RT   "Loss of Ca2+/calmodulin kinase kinase beta affects the formation of some,
RT   but not all, types of hippocampus-dependent long-term memory.";
RL   J. Neurosci. 23:9752-9760(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-133, AND
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-129; SER-133;
RP   SER-137; SER-495 AND SER-572, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Lung, 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: Calcium/calmodulin-dependent protein kinase belonging to a
CC       proposed calcium-triggered signaling cascade involved in a number of
CC       cellular processes. Phosphorylates CAMK1, CAMK4 and CAMK1D (By
CC       similarity). Efficiently phosphorylates 5'-AMP-activated protein kinase
CC       (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1.
CC       This phosphorylation is stimulated in response to Ca(2+) signals (By
CC       similarity). May play a role in neurite growth. Isoform 2 may promote
CC       neurite elongation, while isoform 1 may promoter neurite branching (By
CC       similarity). May be involved in hippocampal activation of CREB1.
CC       {ECO:0000250, ECO:0000269|PubMed:14586002}.
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=2.7.11.17;
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=2.7.11.17;
CC   -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin may relieve intrasteric autoinhibition. Autophosphorylation
CC       does not alter activity or regulation by Ca(2+)/calmodulin. In part,
CC       activity is independent on Ca(2+)/calmodulin (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with calmodulin. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8C078; P49593: PPM1F; Xeno; NbExp=2; IntAct=EBI-937199, EBI-719945;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96RR4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q96RR4}. Cell projection, neuron projection
CC       {ECO:0000250|UniProtKB:Q96RR4}. Note=Predominantly nuclear in
CC       unstimulated cells, relocalizes into cytoplasm and neurites after
CC       forskolin induction. {ECO:0000250|UniProtKB:Q96RR4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8C078-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C078-2; Sequence=VSP_012155;
CC       Name=3;
CC         IsoId=Q8C078-3; Sequence=VSP_012151, VSP_012152, VSP_012154;
CC       Name=4;
CC         IsoId=Q8C078-4; Sequence=VSP_012150, VSP_012153;
CC       Name=5;
CC         IsoId=Q8C078-5; Sequence=VSP_012156;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested. A differential
CC       expression pattern compared to CAMKK1 is observed in the brain.
CC       {ECO:0000269|PubMed:12654522}.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC       region and may be involved in intrasteric autoinhibition.
CC   -!- DOMAIN: The RP domain (arginine/proline-rich) is involved in the
CC       recognition of CAMKI and CAMK4 as substrates. {ECO:0000250}.
CC   -!- PTM: Autophosphorylated and phosphorylated by PKA. Each isoform may
CC       show a different pattern of phosphorylation. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice are unable to form spatial long-term memory.
CC       {ECO:0000269|PubMed:14586002}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF453383; AAN75696.1; -; mRNA.
DR   EMBL; AK031399; BAC27387.1; -; mRNA.
DR   EMBL; AK032070; BAC27681.1; -; mRNA.
DR   EMBL; AK044660; BAC32023.1; -; mRNA.
DR   EMBL; BC023103; AAH23103.1; -; mRNA.
DR   EMBL; AK122370; BAC65652.1; -; mRNA.
DR   CCDS; CCDS19655.1; -. [Q8C078-2]
DR   CCDS; CCDS80395.1; -. [Q8C078-1]
DR   RefSeq; NP_001186605.1; NM_001199676.1. [Q8C078-1]
DR   RefSeq; NP_663333.1; NM_145358.2. [Q8C078-2]
DR   RefSeq; XP_006530293.1; XM_006530230.3. [Q8C078-5]
DR   RefSeq; XP_006530294.1; XM_006530231.3. [Q8C078-5]
DR   RefSeq; XP_017176252.1; XM_017320763.1. [Q8C078-1]
DR   AlphaFoldDB; Q8C078; -.
DR   SMR; Q8C078; -.
DR   BioGRID; 228904; 10.
DR   IntAct; Q8C078; 4.
DR   MINT; Q8C078; -.
DR   STRING; 10090.ENSMUSP00000107297; -.
DR   BindingDB; Q8C078; -.
DR   ChEMBL; CHEMBL4295888; -.
DR   iPTMnet; Q8C078; -.
DR   PhosphoSitePlus; Q8C078; -.
DR   SwissPalm; Q8C078; -.
DR   EPD; Q8C078; -.
DR   jPOST; Q8C078; -.
DR   MaxQB; Q8C078; -.
DR   PaxDb; 10090-ENSMUSP00000107297; -.
DR   PeptideAtlas; Q8C078; -.
DR   ProteomicsDB; 264761; -. [Q8C078-1]
DR   ProteomicsDB; 264762; -. [Q8C078-2]
DR   ProteomicsDB; 264763; -. [Q8C078-3]
DR   ProteomicsDB; 264764; -. [Q8C078-4]
DR   ProteomicsDB; 264765; -. [Q8C078-5]
DR   Pumba; Q8C078; -.
DR   Antibodypedia; 19059; 457 antibodies from 35 providers.
DR   DNASU; 207565; -.
DR   Ensembl; ENSMUST00000111668.8; ENSMUSP00000107297.5; ENSMUSG00000029471.14. [Q8C078-1]
DR   Ensembl; ENSMUST00000200109.5; ENSMUSP00000143732.2; ENSMUSG00000029471.14. [Q8C078-2]
DR   GeneID; 207565; -.
DR   KEGG; mmu:207565; -.
DR   UCSC; uc008zlz.3; mouse. [Q8C078-1]
DR   UCSC; uc008zma.3; mouse. [Q8C078-2]
DR   UCSC; uc008zmb.1; mouse. [Q8C078-5]
DR   UCSC; uc008zmc.2; mouse. [Q8C078-4]
DR   AGR; MGI:2444812; -.
DR   CTD; 10645; -.
DR   MGI; MGI:2444812; Camkk2.
DR   VEuPathDB; HostDB:ENSMUSG00000029471; -.
DR   eggNOG; KOG0585; Eukaryota.
DR   GeneTree; ENSGT00940000161828; -.
DR   InParanoid; Q8C078; -.
DR   OMA; EPRSECR; -.
DR   OrthoDB; 5489318at2759; -.
DR   PhylomeDB; Q8C078; -.
DR   TreeFam; TF313013; -.
DR   Reactome; R-MMU-111932; CaMK IV-mediated phosphorylation of CREB.
DR   Reactome; R-MMU-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR   Reactome; R-MMU-9619229; Activation of RAC1 downstream of NMDARs.
DR   BioGRID-ORCS; 207565; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Camkk2; mouse.
DR   PRO; PR:Q8C078; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8C078; Protein.
DR   Bgee; ENSMUSG00000029471; Expressed in motor neuron and 254 other cell types or tissues.
DR   ExpressionAtlas; Q8C078; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; ISO:MGI.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0061762; P:CAMKK-AMPK signaling cascade; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR43895; CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE KINASE-RELATED; 1.
DR   PANTHER; PTHR43895:SF39; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE KINASE 2; 1.
DR   Pfam; PF00069; Pkinase; 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   Genevisible; Q8C078; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Cell projection; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RR4"
FT   CHAIN           2..588
FT                   /note="Calcium/calmodulin-dependent protein kinase kinase
FT                   2"
FT                   /id="PRO_0000086145"
FT   DOMAIN          165..446
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..226
FT                   /note="RP domain"
FT   REGION          205..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..477
FT                   /note="Autoinhibitory domain"
FT                   /evidence="ECO:0000250"
FT   REGION          475..500
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          497..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..588
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        312
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         171..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RR4"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RR4"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RR4"
FT   MOD_RES         572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         485..503
FT                   /note="ILVKTMIRKRSFGNPFEGS -> VRRAGPLTKNKNRESPRQG (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012150"
FT   VAR_SEQ         498
FT                   /note="N -> T (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012151"
FT   VAR_SEQ         499..507
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012152"
FT   VAR_SEQ         504..588
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012153"
FT   VAR_SEQ         508..588
FT                   /note="RSLSAPGNLLTKKPTREWEPLSEPKEARQRRQPPGPRAGPCGGGGSALVKGG
FT                   PCVESWGAPAPGSPPRMPPLQPEEVMEPE -> RSKVAAGRNVPCQRLETCSRSKAAKT
FT                   APGAQSRPLWGRRKCSCERWSLRGKLGGSGPWLPTTHASTAARGGDGAGVAAWTT (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012154"
FT   VAR_SEQ         520..588
FT                   /note="KPTREWEPLSEPKEARQRRQPPGPRAGPCGGGGSALVKGGPCVESWGAPAPG
FT                   SPPRMPPLQPEEVMEPE -> QGSEDSPRGPEPAPVGEEEVLL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012155"
FT   VAR_SEQ         533..588
FT                   /note="EARQRRQPPGPRAGPCGGGGSALVKGGPCVESWGAPAPGSPPRMPPLQPEEV
FT                   MEPE -> VNACLPACAIASPPLGPGGGQLQSKHVGISSRQDVPSAGAAVPGSLRASGF
FT                   PARGIQGLGSHGVSCMRAGLRCMALHPECLRTYPGSSGPLDG (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_012156"
FT   CONFLICT        176
FT                   /note="Y -> F (in Ref. 2; BAC32023)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="R -> H (in Ref. 2; BAC27681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        396..398
FT                   /note="MCL -> IWR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="K -> R (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q8C078-2:522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   588 AA;  64618 MW;  AED7433ADB3477A5 CRC64;
     MSSCVSSQPT SDRVAPQDEL GSGGGSREGQ KPCEALRGLS SLSIHLGMES FIVVTECEPG
     RGVDLNLARD QPPEADGQEL PLEASDPESR SPLSGRKMSL QEPSQGGPAS SSNSLDMNGR
     CICPSLSYSP ASSPQSSPRM PRRPTVESHH VSITGLQDCV QLNQYTLKDE IGKGSYGVVK
     LAYNENDNTY YAMKVLSKKK LIRQAGFPRR PPPRGARPAP GGCIQPRGPI EQVYQEIAIL
     KKLDHPNVVK LVEVLDDPNE DHLYMVFELV NQGPVMEVPT LKPLSEDQAR FYFQDLIKGI
     EYLHYQKIIH RDIKPSNLLV GEDGHIKIAD FGVSNEFKGS DALLSNTVGT PAFMAPESLS
     ETRKIFSGKA LDVWAMGVTL YCFVFGQCPF MDERIMCLHS KIKSQALEFP DQPDIAEDLK
     DLITRMLDKN PESRIVVPEI KLHPWVTRHG AEPLPSEDEN CTLVEVTEEE VENSVKHIPS
     LATVILVKTM IRKRSFGNPF EGSRREERSL SAPGNLLTKK PTREWEPLSE PKEARQRRQP
     PGPRAGPCGG GGSALVKGGP CVESWGAPAP GSPPRMPPLQ PEEVMEPE
//