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Protein S100-A6 (Calcyclin) (Growth factor-inducible protein 2A9) (MLN 4) (Prolactin receptor-associated protein) (PRA) (S100 calcium-binding protein A6)

 S10A6_HUMAN             Reviewed;          90 AA.
P06703; D3DV39; Q5RHS4;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
05-DEC-2018, entry version 190.
RecName: Full=Protein S100-A6;
AltName: Full=Calcyclin;
AltName: Full=Growth factor-inducible protein 2A9;
AltName: Full=MLN 4;
AltName: Full=Prolactin receptor-associated protein;
Short=PRA;
AltName: Full=S100 calcium-binding protein A6;
Name=S100A6; Synonyms=CACY;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=3755724;
Calabretta B., Battini R., Kaczmarek L., de Riel J.K., Baserga R.;
"Molecular cloning of the cDNA for a growth factor-inducible gene with
strong homology to S-100, a calcium-binding protein.";
J. Biol. Chem. 261:12628-12632(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3036810;
Ferrari S., Calabretta B., Deriel J.K., Battini R., Ghezzo F.,
Lauret E., Griffin C., Emanuel B.S., Gurrieri F., Baserga R.;
"Structural and functional analysis of a growth-regulated gene, the
human calcyclin.";
J. Biol. Chem. 262:8325-8332(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2448309;
Murphy L.C., Murphy L.J., Tsuyuki D., Duckworth M.L., Shiu R.P.C.;
"Cloning and characterization of a cDNA encoding a highly conserved,
putative calcium binding protein, identified by an anti-prolactin
receptor antiserum.";
J. Biol. Chem. 263:2397-2401(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Wu J., Liu W., Zhou Y., Zhao Z., Peng X., Yuan J., Qiang B.;
"Cloning of human calcyclin and calcyclin binding protein (CacyBP).";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 27-31 AND 48-89.
TISSUE=Platelet;
PubMed=1482346; DOI=10.1016/0006-291X(92)90216-8;
Tomida Y., Terasawa M., Kobayashi R., Hidaka H.;
"Calcyclin and calvasculin exist in human platelets.";
Biochem. Biophys. Res. Commun. 189:1310-1316(1992).
[10]
PROTEIN SEQUENCE OF 57-74.
PubMed=2775283; DOI=10.1016/0006-291X(89)92166-9;
Gabius H.J., Bardosi A., Gabius S., Hellmann K.P., Karas M.,
Kratzin H.;
"Identification of a cell cycle-dependent gene product as a sialic
acid-binding protein.";
Biochem. Biophys. Res. Commun. 163:506-512(1989).
[11]
INTERACTION WITH SUGT1.
PubMed=12746458; DOI=10.1074/jbc.M211518200;
Nowotny M., Spiechowicz M., Jastrzebska B., Filipek A., Kitagawa K.,
Kuznicki J.;
"Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and
other S100 proteins.";
J. Biol. Chem. 278:26923-26928(2003).
[12]
SUBCELLULAR LOCATION.
PubMed=12601007; DOI=10.1074/jbc.M212669200;
Tomas A., Moss S.E.;
"Calcium- and cell cycle-dependent association of annexin 11 with the
nuclear envelope.";
J. Biol. Chem. 278:20210-20216(2003).
[13]
INTERACTION WITH ANXA2; ANXA11 AND TROPOMYOSIN, AND SUBCELLULAR
LOCATION.
PubMed=19724273; DOI=10.1038/sj.bjc.6605289;
Nedjadi T., Kitteringham N., Campbell F., Jenkins R.E., Park B.K.,
Navarro P., Ashcroft F., Tepikin A., Neoptolemos J.P., Costello E.;
"S100A6 binds to annexin 2 in pancreatic cancer cells and promotes
pancreatic cancer cell motility.";
Br. J. Cancer 101:1145-1154(2009).
[14]
INTERACTION WITH TP53.
PubMed=19819244; DOI=10.1016/j.jmb.2009.10.002;
van Dieck J., Teufel D.P., Jaulent A.M., Fernandez-Fernandez M.R.,
Rutherford T.J., Wyslouch-Cieszynska A., Fersht A.R.;
"Posttranslational modifications affect the interaction of S100
proteins with tumor suppressor p53.";
J. Mol. Biol. 394:922-930(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
INTERACTION WITH FKBP4.
PubMed=20188096; DOI=10.1016/j.febslet.2010.02.055;
Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.;
"S100 proteins regulate the interaction of Hsp90 with cyclophilin 40
and FKBP52 through their tetratricopeptide repeats.";
FEBS Lett. 584:1119-1125(2010).
[17]
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).
[18]
FUNCTION, INTERACTION WITH PPP5C, AND SUBCELLULAR LOCATION.
PubMed=22399290; DOI=10.1074/jbc.M111.329771;
Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H.,
Tokuda M., Kobayashi R.;
"S100 proteins modulate protein phosphatase 5 function: a link between
CA2+ signal transduction and protein dephosphorylation.";
J. Biol. Chem. 287:13787-13798(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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]
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
INTERACTION WITH ANXA11.
PubMed=28469040; DOI=10.1126/scitranslmed.aad9157;
Smith B.N., Topp S.D., Fallini C., Shibata H., Chen H.J., Troakes C.,
King A., Ticozzi N., Kenna K.P., Soragia-Gkazi A., Miller J.W.,
Sato A., Dias D.M., Jeon M., Vance C., Wong C.H., de Majo M.,
Kattuah W., Mitchell J.C., Scotter E.L., Parkin N.W., Sapp P.C.,
Nolan M., Nestor P.J., Simpson M., Weale M., Lek M., Baas F.,
Vianney de Jong J.M., Ten Asbroek A.L.M.A., Redondo A.G.,
Esteban-Perez J., Tiloca C., Verde F., Duga S., Leigh N., Pall H.,
Morrison K.E., Al-Chalabi A., Shaw P.J., Kirby J., Turner M.R.,
Talbot K., Hardiman O., Glass J.D., De Belleroche J., Maki M.,
Moss S.E., Miller C., Gellera C., Ratti A., Al-Sarraj S.,
Brown R.H. Jr., Silani V., Landers J.E., Shaw C.E.;
"Mutations in the vesicular trafficking protein annexin A11 are
associated with amyotrophic lateral sclerosis.";
Sci. Transl. Med. 9:0-0(2017).
[23]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), SUBUNIT, AND CALCIUM-BINDING.
PubMed=11937060; DOI=10.1016/S0969-2126(02)00740-2;
Otterbein L.R., Kordowska J., Witte-Hoffmann C., Wang C.-L.A.,
Dominguez R.;
"Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound
states: the calcium sensor mechanism of S100 proteins revealed at
atomic resolution.";
Structure 10:557-567(2002).
-!- FUNCTION: May function as calcium sensor and modulator,
contributing to cellular calcium signaling. May function by
interacting with other proteins, such as TPR-containing proteins,
and indirectly play a role in many physiological processes such as
the reorganization of the actin cytoskeleton and in cell motility.
Binds 2 calcium ions. Calcium binding is cooperative.
{ECO:0000269|PubMed:22399290}.
-!- SUBUNIT: Homodimer; head to tail assembly of 2 subunits. Interacts
with CACYBP in a calcium-dependent manner. Interacts with ANXA2
and ANXA11 (via N-terminus). Interacts with SUGT1. Interacts with
TP53; has higher affinity for TP53 that is phosphorylated on its
N-terminal domain, and lower affinity for TP53 that is
phosphorylated on its C-terminal domain. Interacts with
tropomyosin. Interacts with FKBP4. Interacts with PPP5C (via TPR
repeats); the interaction is calcium-dependent and modulates PPP5C
activity. {ECO:0000269|PubMed:11937060,
ECO:0000269|PubMed:12746458, ECO:0000269|PubMed:19724273,
ECO:0000269|PubMed:19819244, ECO:0000269|PubMed:20188096,
ECO:0000269|PubMed:22399290, ECO:0000269|PubMed:28469040}.
-!- INTERACTION:
Q02790:FKBP4; NbExp=3; IntAct=EBI-352877, EBI-1047444;
P52292:KPNA2; NbExp=3; IntAct=EBI-352877, EBI-349938;
Q00987:MDM2; NbExp=2; IntAct=EBI-352877, EBI-389668;
P50542:PEX5; NbExp=3; IntAct=EBI-352877, EBI-597835;
P26882:PPID (xeno); NbExp=3; IntAct=EBI-352877, EBI-6477155;
P04271:S100B; NbExp=6; IntAct=EBI-352877, EBI-458391;
-!- SUBCELLULAR LOCATION: Nucleus envelope. Cytoplasm. Cell membrane;
Peripheral membrane protein; Cytoplasmic side.
-!- INDUCTION: Preferentially expressed when quiescent fibroblasts are
stimulated to proliferate. It is inducible by growth factors and
overexpressed in acute myeloid leukemias.
-!- PTM: The N-terminus is blocked.
-!- MISCELLANEOUS: This protein co-purified with the prolactin
receptor.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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EMBL; M14300; AAA35886.1; -; mRNA.
EMBL; J02763; AAA51905.1; -; Genomic_DNA.
EMBL; M18981; AAA51906.1; -; mRNA.
EMBL; AY034480; AAK59702.1; -; Genomic_DNA.
EMBL; BT006965; AAP35611.1; -; mRNA.
EMBL; BX470102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53318.1; -; Genomic_DNA.
EMBL; CH471121; EAW53320.1; -; Genomic_DNA.
EMBL; CH471121; EAW53321.1; -; Genomic_DNA.
EMBL; CH471121; EAW53322.1; -; Genomic_DNA.
EMBL; CH471121; EAW53323.1; -; Genomic_DNA.
EMBL; CH471121; EAW53324.1; -; Genomic_DNA.
EMBL; CH471121; EAW53325.1; -; Genomic_DNA.
EMBL; CH471121; EAW53326.1; -; Genomic_DNA.
EMBL; BC001431; AAH01431.1; -; mRNA.
EMBL; BC009017; AAH09017.1; -; mRNA.
CCDS; CCDS1040.1; -.
PIR; A28363; BCHUY.
RefSeq; NP_055439.1; NM_014624.3.
RefSeq; XP_016857522.1; XM_017002033.1.
UniGene; Hs.275243; -.
PDB; 1K8U; X-ray; 1.15 A; A=1-90.
PDB; 1K96; X-ray; 1.44 A; A=1-90.
PDB; 1K9K; X-ray; 1.76 A; A/B=1-90.
PDB; 1K9P; X-ray; 1.90 A; A=1-90.
PDB; 2M1K; NMR; -; B/D=1-90.
PDB; 4YBH; X-ray; 2.40 A; B=1-90.
PDBsum; 1K8U; -.
PDBsum; 1K96; -.
PDBsum; 1K9K; -.
PDBsum; 1K9P; -.
PDBsum; 2M1K; -.
PDBsum; 4YBH; -.
ProteinModelPortal; P06703; -.
SMR; P06703; -.
BioGrid; 112185; 32.
CORUM; P06703; -.
IntAct; P06703; 21.
MINT; P06703; -.
STRING; 9606.ENSP00000357708; -.
iPTMnet; P06703; -.
PhosphoSitePlus; P06703; -.
SwissPalm; P06703; -.
BioMuta; S100A6; -.
DMDM; 116509; -.
DOSAC-COBS-2DPAGE; P06703; -.
EPD; P06703; -.
MaxQB; P06703; -.
PaxDb; P06703; -.
PeptideAtlas; P06703; -.
PRIDE; P06703; -.
ProteomicsDB; 51911; -.
TopDownProteomics; P06703; -.
DNASU; 6277; -.
Ensembl; ENST00000368719; ENSP00000357708; ENSG00000197956.
Ensembl; ENST00000368720; ENSP00000357709; ENSG00000197956.
Ensembl; ENST00000496817; ENSP00000473589; ENSG00000197956.
GeneID; 6277; -.
KEGG; hsa:6277; -.
UCSC; uc001fbw.2; human.
CTD; 6277; -.
DisGeNET; 6277; -.
EuPathDB; HostDB:ENSG00000197956.9; -.
GeneCards; S100A6; -.
HGNC; HGNC:10496; S100A6.
HPA; CAB002601; -.
HPA; CAB040549; -.
HPA; CAB047354; -.
HPA; HPA007575; -.
MIM; 114110; gene.
neXtProt; NX_P06703; -.
OpenTargets; ENSG00000197956; -.
PharmGKB; PA34908; -.
eggNOG; ENOG410IYT5; Eukaryota.
eggNOG; ENOG410Z6I6; LUCA.
GeneTree; ENSGT00940000161896; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P06703; -.
OMA; QVVNFQE; -.
OrthoDB; EOG091G10JX; -.
PhylomeDB; P06703; -.
TreeFam; TF332727; -.
SIGNOR; P06703; -.
ChiTaRS; S100A6; human.
EvolutionaryTrace; P06703; -.
GeneWiki; S100A6; -.
GenomeRNAi; 6277; -.
PRO; PR:P06703; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000197956; Expressed in 225 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_S100A6; -.
ExpressionAtlas; P06703; baseline and differential.
Genevisible; P06703; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
GO; GO:0015075; F:ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:0005523; F:tropomyosin binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
CDD; cd05029; S-100A6; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR034118; S-100A6.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
Pfam; PF01023; S_100; 1.
SMART; SM00054; EFh; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Cell membrane; Complete proteome;
Cytoplasm; Direct protein sequencing; Membrane; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 90 Protein S100-A6.
/FTId=PRO_0000143984.
DOMAIN 12 47 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 48 83 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 20 33 1.
CA_BIND 61 72 2.
MOD_RES 40 40 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 47 47 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P14069}.
MOD_RES 47 47 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P14069}.
VARIANT 27 27 H -> R (in dbSNP:rs11974).
/FTId=VAR_011982.
VARIANT 69 69 N -> S (in dbSNP:rs1802581).
/FTId=VAR_011983.
VARIANT 83 83 I -> T (in dbSNP:rs1802582).
/FTId=VAR_011984.
VARIANT 90 90 G -> D (in dbSNP:rs2228293).
/FTId=VAR_029281.
HELIX 4 20 {ECO:0000244|PDB:1K8U}.
STRAND 22 24 {ECO:0000244|PDB:1K8U}.
STRAND 28 30 {ECO:0000244|PDB:1K8U}.
HELIX 31 41 {ECO:0000244|PDB:1K8U}.
HELIX 45 47 {ECO:0000244|PDB:1K8U}.
HELIX 51 62 {ECO:0000244|PDB:1K8U}.
TURN 63 65 {ECO:0000244|PDB:1K8U}.
STRAND 67 69 {ECO:0000244|PDB:1K8U}.
HELIX 70 84 {ECO:0000244|PDB:1K8U}.
HELIX 86 88 {ECO:0000244|PDB:1K8U}.
SEQUENCE 90 AA; 10180 MW; 860CBB1416ACBCA1 CRC64;
MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL
DRNKDQEVNF QEYVTFLGAL ALIYNEALKG


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