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Plasma membrane calcium-transporting ATPase 1 (PMCA1) (EC 3.6.3.8) (Plasma membrane calcium ATPase isoform 1) (Plasma membrane calcium pump isoform 1)

 AT2B1_HUMAN             Reviewed;        1220 AA.
P20020; Q12992; Q12993; Q13819; Q13820; Q13821; Q16504; Q93082;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
12-SEP-2018, sequence version 4.
05-DEC-2018, entry version 207.
RecName: Full=Plasma membrane calcium-transporting ATPase 1;
Short=PMCA1;
EC=3.6.3.8;
AltName: Full=Plasma membrane calcium ATPase isoform 1;
AltName: Full=Plasma membrane calcium pump isoform 1;
Name=ATP2B1; Synonyms=PMCA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Erythrocyte;
PubMed=2844759;
Verma A.K., Filoteo A.G., Stanford D.R., Wieben E.D., Penniston J.T.,
Strehler E.E., Fischer R., Heim R., Vogel G., Mathews S.,
Strehler-Page M.-A., James P., Vorherr T.E., Krebs J., Carafoli E.;
"Complete primary structure of a human plasma membrane Ca2+ pump.";
J. Biol. Chem. 263:14152-14159(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Osteoblast;
PubMed=8386431; DOI=10.1002/jbmr.5650080415;
Kumar R., Haugen J.D., Penniston J.T.;
"Molecular cloning of a plasma membrane calcium pump from human
osteoblasts.";
J. Bone Miner. Res. 8:505-513(1993).
[3]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
TISSUE=Leukocyte;
PubMed=8396145;
Hilfiker H., Strehler-Page M.-A., Stauffer T.P., Carafoli E.,
Strehler E.E.;
"Structure of the gene encoding the human plasma membrane calcium pump
isoform 1.";
J. Biol. Chem. 268:19717-19725(1993).
[4]
SEQUENCE REVISION.
Strehler E.E., Strehler-Page M.-A.;
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[5]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A; C AND D).
TISSUE=Fetal skeletal muscle;
PubMed=2528729; DOI=10.1073/pnas.86.18.6908;
Strehler E.E., Strehler-Page M.-A., Vogel G., Carafoli E.;
"mRNAs for plasma membrane calcium pump isoforms differing in their
regulatory domain are generated by alternative splicing that involves
two internal donor sites in a single exon.";
Proc. Natl. Acad. Sci. U.S.A. 86:6908-6912(1989).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), REGION, AND
ALTERNATIVE SPLICING.
TISSUE=Fetal brain;
PubMed=1332771; DOI=10.1021/bi00162a016;
Kessler F., Falchetto R., Heim R., Meili R., Vorherr T.E.,
Strehler E.E., Carafoli E.;
"Study of calmodulin binding to the alternatively spliced C-terminal
domain of the plasma membrane Ca2+ pump.";
Biochemistry 31:11785-11792(1992).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND E).
TISSUE=Brain cortex;
PubMed=8245032;
Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.;
"Quantitative analysis of alternative splicing options of human plasma
membrane calcium pump genes.";
J. Biol. Chem. 268:25993-26003(1993).
[8]
ERRATUM.
PubMed=7989379;
Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.;
J. Biol. Chem. 269:32022-32022(1994).
[9]
ALTERNATIVE SPLICING (ISOFORM K).
TISSUE=Small intestine mucosa;
PubMed=7694502;
Howard A., Legon S., Walters J.R.;
"Human and rat intestinal plasma membrane calcium pump isoforms.";
Am. J. Physiol. 265:G917-G925(1993).
[10]
PHOSPHORYLATION BY CAMP KINASE.
PubMed=2548572; DOI=10.1021/bi00436a020;
James P.H., Pruschy M., Vorherr T.E., Penniston J.T., Carafoli E.;
"Primary structure of the cAMP-dependent phosphorylation site of the
plasma membrane calcium pump.";
Biochemistry 28:4253-4258(1989).
[11]
PHOSPHORYLATION AT THR-1116 BY PROTEIN KINASE C.
PubMed=1827443;
Wang K.K.W., Wright L.C., Machan C.L., Allen B.G., Conigrave A.D.,
Roufogalis B.D.;
"Protein kinase C phosphorylates the carboxyl terminus of the plasma
membrane Ca(2+)-ATPase from human erythrocytes.";
J. Biol. Chem. 266:9078-9085(1991).
[12]
INTERACTION WITH PDZD11.
PubMed=12763866; DOI=10.1111/j.1749-6632.2003.tb07230.x;
Goellner G.M., DeMarco S.J., Strehler E.E.;
"Characterization of PISP, a novel single-PDZ protein that binds to
all plasma membrane Ca2+-ATPase b-splice variants.";
Ann. N. Y. Acad. Sci. 986:461-471(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155 AND SER-1182, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-1155; THR-1165;
SER-1178 AND SER-1182, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-1155 AND THR-1165, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
INTERACTION WITH SLC35G1 AND STIM1.
PubMed=22084111; DOI=10.1073/pnas.1117231108;
Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.;
"POST, partner of stromal interaction molecule 1 (STIM1), targets
STIM1 to multiple transporters.";
Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155; SER-1178 AND
SER-1182, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-17; SER-1155 AND
THR-1165, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
VARIANT ARG-267.
PubMed=9020386; DOI=10.1007/s001090050088;
Benkwitz C., Kubsisch C., Kraft K., Neyses L.;
"Investigation of the Met-267 Arg exchange in isoform 1 of the human
plasma membrane calcium pump in patients with essential hypertension
by the amplification-created restriction site technique.";
J. Mol. Med. 75:62-66(1997).
-!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis
of ATP coupled with the transport of calcium out of the cell.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) +
phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.3.8;
-!- SUBUNIT: Interacts with PDZD11. Interacts with SLC35G1 and STIM1.
{ECO:0000269|PubMed:12763866, ECO:0000269|PubMed:22084111}.
-!- INTERACTION:
Q14160:SCRIB; NbExp=2; IntAct=EBI-5279998, EBI-357345;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=B; Synonyms=CI, hPMCA1b {ECO:0000303|PubMed:1332771};
IsoId=P20020-3; Sequence=Displayed;
Name=D; Synonyms=CIV, hPMCA1d {ECO:0000303|PubMed:1332771};
IsoId=P20020-1; Sequence=VSP_059773;
Name=A; Synonyms=CII, hPMCA1a {ECO:0000303|PubMed:1332771};
IsoId=P20020-2; Sequence=VSP_059774, VSP_059775;
Name=C; Synonyms=CIII, hPMCA1c {ECO:0000303|PubMed:1332771};
IsoId=P20020-4; Sequence=VSP_059772;
Name=E; Synonyms=CV;
IsoId=P20020-5; Sequence=VSP_059774, VSP_059776;
Name=K;
IsoId=P20020-6; Sequence=VSP_059771;
-!- TISSUE SPECIFICITY: Isoform B: Ubiquitously expressed. Isoform C:
Found in brain cortex, skeletal muscle and heart muscle. Isoform
D: Has only been found in fetal skeletal muscle. Isoform K: Found
in small intestine and liver.
-!- DOMAIN: Isoforms A, C, D and E contain and additional calmodulin-
binding subdomain B which is different in the different splice
variants and shows pH dependent calmodulin binding properties.
{ECO:0000269|PubMed:1332771}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIB subfamily. {ECO:0000305}.
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EMBL; J04027; AAA74511.1; -; mRNA.
EMBL; M95541; AAA35999.1; -; mRNA.
EMBL; M95542; AAA36000.1; -; mRNA.
EMBL; L14561; AAD09924.1; -; Genomic_DNA.
EMBL; L14561; AAD09925.1; -; Genomic_DNA.
EMBL; M25824; AAA58383.1; -; Genomic_DNA.
EMBL; M25824; AAA58382.1; -; Genomic_DNA.
EMBL; M25824; AAA58381.1; -; Genomic_DNA.
EMBL; S49852; AAB24324.1; -; mRNA.
EMBL; U15686; AAA60983.1; -; mRNA.
EMBL; U15687; AAA60984.1; -; mRNA.
CCDS; CCDS41817.1; -. [P20020-2]
CCDS; CCDS9035.1; -. [P20020-3]
PIR; A30802; A30802.
PIR; E49570; E49570.
PIR; I55491; I55491.
PIR; I70165; I70165.
RefSeq; NP_001001323.1; NM_001001323.1. [P20020-2]
RefSeq; NP_001673.2; NM_001682.2. [P20020-3]
RefSeq; XP_011536709.1; XM_011538407.2. [P20020-4]
RefSeq; XP_016874847.1; XM_017019358.1.
UniGene; Hs.506276; -.
PDB; 6A69; EM; 4.11 A; A=1-1220.
PDBsum; 6A69; -.
ProteinModelPortal; P20020; -.
SMR; P20020; -.
BioGrid; 106980; 47.
IntAct; P20020; 33.
MINT; P20020; -.
STRING; 9606.ENSP00000261173; -.
TCDB; 3.A.3.2.25; the p-type atpase (p-atpase) superfamily.
iPTMnet; P20020; -.
PhosphoSitePlus; P20020; -.
SwissPalm; P20020; -.
BioMuta; ATP2B1; -.
DMDM; 14286104; -.
EPD; P20020; -.
MaxQB; P20020; -.
PaxDb; P20020; -.
PeptideAtlas; P20020; -.
PRIDE; P20020; -.
ProteomicsDB; 53706; -.
ProteomicsDB; 53707; -. [P20020-2]
ProteomicsDB; 53708; -. [P20020-3]
ProteomicsDB; 53709; -. [P20020-4]
ProteomicsDB; 53710; -. [P20020-5]
ProteomicsDB; 53711; -. [P20020-6]
Ensembl; ENST00000261173; ENSP00000261173; ENSG00000070961. [P20020-3]
Ensembl; ENST00000359142; ENSP00000352054; ENSG00000070961. [P20020-2]
Ensembl; ENST00000428670; ENSP00000392043; ENSG00000070961. [P20020-3]
GeneID; 490; -.
KEGG; hsa:490; -.
UCSC; uc001tbg.4; human. [P20020-3]
CTD; 490; -.
DisGeNET; 490; -.
EuPathDB; HostDB:ENSG00000070961.15; -.
GeneCards; ATP2B1; -.
HGNC; HGNC:814; ATP2B1.
HPA; CAB005605; -.
HPA; HPA011166; -.
HPA; HPA012945; -.
MIM; 108731; gene.
neXtProt; NX_P20020; -.
OpenTargets; ENSG00000070961; -.
PharmGKB; PA25107; -.
eggNOG; KOG0204; Eukaryota.
eggNOG; ENOG410XNNC; LUCA.
GeneTree; ENSGT00940000158686; -.
HOVERGEN; HBG061286; -.
InParanoid; P20020; -.
KO; K05850; -.
OMA; HYKKIPE; -.
PhylomeDB; P20020; -.
TreeFam; TF300330; -.
BRENDA; 3.6.3.8; 2681.
Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
ChiTaRS; ATP2B1; human.
GeneWiki; ATP2B1; -.
GenomeRNAi; 490; -.
PRO; PR:P20020; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000070961; Expressed in 234 organ(s), highest expression level in putamen.
CleanEx; HS_ATP2B1; -.
ExpressionAtlas; P20020; baseline and differential.
Genevisible; P20020; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0032591; C:dendritic spine membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0099059; C:integral component of presynaptic active zone membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0032809; C:neuronal cell body membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:SynGO-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0015085; F:calcium ion transmembrane transporter activity; IDA:SynGO-UCL.
GO; GO:0005388; F:calcium-transporting ATPase activity; IBA:GO_Central.
GO; GO:1905056; F:calcium-transporting ATPase activity involved in regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; IBA:GO_Central.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:1990034; P:calcium ion export across plasma membrane; IDA:SynGO-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
GO; GO:0071386; P:cellular response to corticosterone stimulus; IEA:Ensembl.
GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0003407; P:neural retina development; IEA:Ensembl.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:SynGO-UCL.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030320; ATP2B1.
InterPro; IPR022141; ATP_Ca_trans_C.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006408; P-type_ATPase_IIB.
InterPro; IPR001757; P_typ_ATPase.
PANTHER; PTHR24093:SF245; PTHR24093:SF245; 1.
Pfam; PF12424; ATP_Ca_trans_C; 1.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 1.
TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding; Calcium;
Calcium transport; Calmodulin-binding; Cell membrane;
Complete proteome; Hydrolase; Ion transport; Magnesium; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231}.
CHAIN 2 1220 Plasma membrane calcium-transporting
ATPase 1.
/FTId=PRO_0000046209.
TOPO_DOM 2 97 Cytoplasmic. {ECO:0000255}.
TRANSMEM 98 118 Helical. {ECO:0000255}.
TOPO_DOM 119 154 Extracellular. {ECO:0000255}.
TRANSMEM 155 175 Helical. {ECO:0000255}.
TOPO_DOM 176 366 Cytoplasmic. {ECO:0000255}.
TRANSMEM 367 386 Helical. {ECO:0000255}.
TOPO_DOM 387 419 Extracellular. {ECO:0000255}.
TRANSMEM 420 437 Helical. {ECO:0000255}.
TOPO_DOM 438 852 Cytoplasmic. {ECO:0000255}.
TRANSMEM 853 872 Helical. {ECO:0000255}.
TOPO_DOM 873 882 Extracellular. {ECO:0000255}.
TRANSMEM 883 903 Helical. {ECO:0000255}.
TOPO_DOM 904 923 Cytoplasmic. {ECO:0000255}.
TRANSMEM 924 946 Helical. {ECO:0000255}.
TOPO_DOM 947 964 Extracellular. {ECO:0000255}.
TRANSMEM 965 986 Helical. {ECO:0000255}.
TOPO_DOM 987 1005 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1006 1027 Helical. {ECO:0000255}.
TOPO_DOM 1028 1037 Extracellular. {ECO:0000255}.
TRANSMEM 1038 1059 Helical. {ECO:0000255}.
TOPO_DOM 1060 1220 Cytoplasmic. {ECO:0000255}.
REGION 1100 1117 Calmodulin-binding subdomain A.
{ECO:0000305|PubMed:1332771}.
COMPBIAS 296 299 Poly-Glu.
ACT_SITE 475 475 4-aspartylphosphate intermediate.
METAL 797 797 Magnesium. {ECO:0000250}.
METAL 801 801 Magnesium. {ECO:0000250}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000250|UniProtKB:G5E829}.
MOD_RES 1116 1116 Phosphothreonine; by PKC.
{ECO:0000269|PubMed:1827443}.
MOD_RES 1140 1140 Phosphoserine.
{ECO:0000250|UniProtKB:P11505}.
MOD_RES 1155 1155 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1165 1165 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1178 1178 Phosphoserine; by PKA.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1182 1182 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
VAR_SEQ 1021 1056 Missing (in isoform K).
/FTId=VSP_059771.
VAR_SEQ 1117 1117 Q -> QMDVVNAFQSGSSIQGALRRQPSIASQHHD (in
isoform C).
/FTId=VSP_059772.
VAR_SEQ 1117 1117 Q -> QMDVVNAFQSGSSIQGALRRQPSIASQHHDVTNIST
PTH (in isoform D).
/FTId=VSP_059773.
VAR_SEQ 1118 1119 IR -> MD (in isoform A and isoform E).
/FTId=VSP_059774.
VAR_SEQ 1125 1220 RSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLIDDT
DAEDDAPTKRNSSPPPSPNKNNNAVDSGIHLTIEMNKSATS
SSPGSPLHSLETSL -> QSGSSIQGALRRQPSIASQHHDV
TNISTPTHVVFSSSTASTTVGYSSGECIS (in isoform
A).
/FTId=VSP_059775.
VAR_SEQ 1125 1220 RSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLIDDT
DAEDDAPTKRNSSPPPSPNKNNNAVDSGIHLTIEMNKSATS
SSPGSPLHSLETSL -> QSGSSIQGALRRQPSIASQHHDV
TNISTPTHVVFSSSTASTTVGFEW (in isoform E).
/FTId=VSP_059776.
VARIANT 267 267 M -> R (rare polymorphism).
{ECO:0000269|PubMed:9020386}.
/FTId=VAR_000698.
CONFLICT 259 262 LLLS -> MSAT (in Ref. 2; AAA36000).
{ECO:0000305}.
SEQUENCE 1220 AA; 134685 MW; 7E75C19B1A501423 CRC64;
MGDMANNSVA YSGVKNSLKE ANHDGDFGIT LAELRALMEL RSTDALRKIQ ESYGDVYGIC
TKLKTSPNEG LSGNPADLER REAVFGKNFI PPKKPKTFLQ LVWEALQDVT LIILEIAAIV
SLGLSFYQPP EGDNALCGEV SVGEEEGEGE TGWIEGAAIL LSVVCVVLVT AFNDWSKEKQ
FRGLQSRIEQ EQKFTVIRGG QVIQIPVADI TVGDIAQVKY GDLLPADGIL IQGNDLKIDE
SSLTGESDHV KKSLDKDPLL LSGTHVMEGS GRMVVTAVGV NSQTGIIFTL LGAGGEEEEK
KDEKKKEKKN KKQDGAIENR NKAKAQDGAA MEMQPLKSEE GGDGDEKDKK KANLPKKEKS
VLQGKLTKLA VQIGKAGLLM SAITVIILVL YFVIDTFWVQ KRPWLAECTP IYIQYFVKFF
IIGVTVLVVA VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL
TMNRMTVVQA YINEKHYKKV PEPEAIPPNI LSYLVTGISV NCAYTSKILP PEKEGGLPRH
VGNKTECALL GLLLDLKRDY QDVRNEIPEE ALYKVYTFNS VRKSMSTVLK NSDGSYRIFS
KGASEIILKK CFKILSANGE AKVFRPRDRD DIVKTVIEPM ASEGLRTICL AFRDFPAGEP
EPEWDNENDI VTGLTCIAVV GIEDPVRPEV PDAIKKCQRA GITVRMVTGD NINTARAIAT
KCGILHPGED FLCLEGKDFN RRIRNEKGEI EQERIDKIWP KLRVLARSSP TDKHTLVKGI
IDSTVSDQRQ VVAVTGDGTN DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFTSIVK
AVMWGRNVYD SISKFLQFQL TVNVVAVIVA FTGACITQDS PLKAVQMLWV NLIMDTLASL
ALATEPPTES LLLRKPYGRN KPLISRTMMK NILGHAFYQL VVVFTLLFAG EKFFDIDSGR
NAPLHAPPSE HYTIVFNTFV LMQLFNEINA RKIHGERNVF EGIFNNAIFC TIVLGTFVVQ
IIIVQFGGKP FSCSELSIEQ WLWSIFLGMG TLLWGQLIST IPTSRLKFLK EAGHGTQKEE
IPEEELAEDV EEIDHAEREL RRGQILWFRG LNRIQTQIRV VNAFRSSLYE GLEKPESRSS
IHNFMTHPEF RIEDSEPHIP LIDDTDAEDD APTKRNSSPP PSPNKNNNAV DSGIHLTIEM
NKSATSSSPG SPLHSLETSL


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