KKCC2_MOUSE
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 03-AUG-2022, entry version 166.
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; 9.
DR IntAct; Q8C078; 4.
DR MINT; Q8C078; -.
DR STRING; 10090.ENSMUSP00000107297; -.
DR BindingDB; Q8C078; -.
DR ChEMBL; CHEMBL4295888; -.
DR iPTMnet; Q8C078; -.
DR PhosphoSitePlus; Q8C078; -.
DR EPD; Q8C078; -.
DR jPOST; Q8C078; -.
DR MaxQB; Q8C078; -.
DR PaxDb; Q8C078; -.
DR PeptideAtlas; Q8C078; -.
DR PRIDE; 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 Antibodypedia; 19059; 395 antibodies from 35 providers.
DR DNASU; 207565; -.
DR Ensembl; ENSMUST00000111668; ENSMUSP00000107297; ENSMUSG00000029471. [Q8C078-1]
DR Ensembl; ENSMUST00000200109; ENSMUSP00000143732; ENSMUSG00000029471. [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 CTD; 10645; -.
DR MGI; MGI:2444812; Camkk2.
DR VEuPathDB; HostDB:ENSMUSG00000029471; -.
DR eggNOG; KOG0585; Eukaryota.
DR GeneTree; ENSGT00940000161828; -.
DR InParanoid; Q8C078; -.
DR OMA; NGRCVHP; -.
DR OrthoDB; 856506at2759; -.
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 73 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 252 other tissues.
DR ExpressionAtlas; Q8C078; baseline and differential.
DR Genevisible; Q8C078; MM.
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:0032147; P:activation of protein kinase activity; ISO:MGI.
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 GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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 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
