Full text data of S100A6
S100A6
(CACY)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Protein S100-A6 (Calcyclin; Growth factor-inducible protein 2A9; MLN 4; Prolactin receptor-associated protein; PRA; S100 calcium-binding protein A6)
Protein S100-A6 (Calcyclin; Growth factor-inducible protein 2A9; MLN 4; Prolactin receptor-associated protein; PRA; S100 calcium-binding protein A6)
hRBCD
IPI00027463
IPI00027463 Calcyclin calcium binding, protein binding, associates with the prolactin receptor soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band between 38 - 49 kdDa
IPI00027463 Calcyclin calcium binding, protein binding, associates with the prolactin receptor soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band between 38 - 49 kdDa
UniProt
P06703
ID S10A6_HUMAN Reviewed; 90 AA.
AC P06703; D3DV39; Q5RHS4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1988, sequence version 1.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Protein S100-A6;
DE AltName: Full=Calcyclin;
DE AltName: Full=Growth factor-inducible protein 2A9;
DE AltName: Full=MLN 4;
DE AltName: Full=Prolactin receptor-associated protein;
DE Short=PRA;
DE AltName: Full=S100 calcium-binding protein A6;
GN Name=S100A6; Synonyms=CACY;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=3755724;
RA Calabretta B., Battini R., Kaczmarek L., de Riel J.K., Baserga R.;
RT "Molecular cloning of the cDNA for a growth factor-inducible gene with
RT strong homology to S-100, a calcium-binding protein.";
RL J. Biol. Chem. 261:12628-12632(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036810;
RA Ferrari S., Calabretta B., Deriel J.K., Battini R., Ghezzo F.,
RA Lauret E., Griffin C., Emanuel B.S., Gurrieri F., Baserga R.;
RT "Structural and functional analysis of a growth-regulated gene, the
RT human calcyclin.";
RL J. Biol. Chem. 262:8325-8332(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2448309;
RA Murphy L.C., Murphy L.J., Tsuyuki D., Duckworth M.L., Shiu R.P.C.;
RT "Cloning and characterization of a cDNA encoding a highly conserved,
RT putative calcium binding protein, identified by an anti-prolactin
RT receptor antiserum.";
RL J. Biol. Chem. 263:2397-2401(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wu J., Liu W., Zhou Y., Zhao Z., Peng X., Yuan J., Qiang B.;
RT "Cloning of human calcyclin and calcyclin binding protein (CacyBP).";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 27-31 AND 48-89.
RC TISSUE=Platelet;
RX PubMed=1482346; DOI=10.1016/0006-291X(92)90216-8;
RA Tomida Y., Terasawa M., Kobayashi R., Hidaka H.;
RT "Calcyclin and calvasculin exist in human platelets.";
RL Biochem. Biophys. Res. Commun. 189:1310-1316(1992).
RN [10]
RP PROTEIN SEQUENCE OF 57-74.
RX PubMed=2775283; DOI=10.1016/0006-291X(89)92166-9;
RA Gabius H.J., Bardosi A., Gabius S., Hellmann K.P., Karas M.,
RA Kratzin H.;
RT "Identification of a cell cycle-dependent gene product as a sialic
RT acid-binding protein.";
RL Biochem. Biophys. Res. Commun. 163:506-512(1989).
RN [11]
RP INTERACTION WITH SUGT1.
RX PubMed=12746458; DOI=10.1074/jbc.M211518200;
RA Nowotny M., Spiechowicz M., Jastrzebska B., Filipek A., Kitagawa K.,
RA Kuznicki J.;
RT "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and
RT other S100 proteins.";
RL J. Biol. Chem. 278:26923-26928(2003).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=12601007; DOI=10.1074/jbc.M212669200;
RA Tomas A., Moss S.E.;
RT "Calcium- and cell cycle-dependent association of annexin 11 with the
RT nuclear envelope.";
RL J. Biol. Chem. 278:20210-20216(2003).
RN [13]
RP INTERACTION WITH ANXA2; ANXA11 AND TROPOMYOSIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19724273; DOI=10.1038/sj.bjc.6605289;
RA Nedjadi T., Kitteringham N., Campbell F., Jenkins R.E., Park B.K.,
RA Navarro P., Ashcroft F., Tepikin A., Neoptolemos J.P., Costello E.;
RT "S100A6 binds to annexin 2 in pancreatic cancer cells and promotes
RT pancreatic cancer cell motility.";
RL Br. J. Cancer 101:1145-1154(2009).
RN [14]
RP INTERACTION WITH TP53.
RX PubMed=19819244; DOI=10.1016/j.jmb.2009.10.002;
RA van Dieck J., Teufel D.P., Jaulent A.M., Fernandez-Fernandez M.R.,
RA Rutherford T.J., Wyslouch-Cieszynska A., Fersht A.R.;
RT "Posttranslational modifications affect the interaction of S100
RT proteins with tumor suppressor p53.";
RL J. Mol. Biol. 394:922-930(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP INTERACTION WITH FKBP4.
RX PubMed=20188096; DOI=10.1016/j.febslet.2010.02.055;
RA Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.;
RT "S100 proteins regulate the interaction of Hsp90 with cyclophilin 40
RT and FKBP52 through their tetratricopeptide repeats.";
RL FEBS Lett. 584:1119-1125(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, INTERACTION WITH PPP5C, AND SUBCELLULAR LOCATION.
RX PubMed=22399290; DOI=10.1074/jbc.M111.329771;
RA Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H.,
RA Tokuda M., Kobayashi R.;
RT "S100 proteins modulate protein phosphatase 5 function: a link between
RT CA2+ signal transduction and protein dephosphorylation.";
RL J. Biol. Chem. 287:13787-13798(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), SUBUNIT, AND CALCIUM-BINDING.
RX PubMed=11937060; DOI=10.1016/S0969-2126(02)00740-2;
RA Otterbein L.R., Kordowska J., Witte-Hoffmann C., Wang C.-L.A.,
RA Dominguez R.;
RT "Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound
RT states: the calcium sensor mechanism of S100 proteins revealed at
RT atomic resolution.";
RL Structure 10:557-567(2002).
CC -!- FUNCTION: May function as calcium sensor and modulator,
CC contributing to cellular calcium signaling. May function by
CC interacting with other proteins, such as TPR-containing proteins,
CC and indirectly play a role in many physiological processes such as
CC the reorganization of the actin cytoskeleton and in cell motility.
CC Binds 2 calcium ions. Calcium binding is cooperative.
CC -!- SUBUNIT: Homodimer; head to tail assembly of 2 subunits. Interacts
CC with CACYBP in a calcium-dependent manner. Interacts with ANXA2
CC and ANXA11 (via N-terminus). Interacts with SUGT1. Interacts with
CC TP53; has higher affinity for TP53 that is phosphorylated on its
CC N-terminal domain, and lower affinity for TP53 that is
CC phosphorylated on its C-terminal domain. Interacts with
CC tropomyosin. Interacts with FKBP4. Interacts with PPP5C (via TPR
CC repeats); the interaction is calcium-dependent and modulates PPP5C
CC activity.
CC -!- INTERACTION:
CC Q02790:FKBP4; NbExp=3; IntAct=EBI-352877, EBI-1047444;
CC P52292:KPNA2; NbExp=3; IntAct=EBI-352877, EBI-349938;
CC Q00987:MDM2; NbExp=2; IntAct=EBI-352877, EBI-389668;
CC P26882:PPID (xeno); NbExp=3; IntAct=EBI-352877, EBI-6477155;
CC P04271:S100B; NbExp=5; IntAct=EBI-352877, EBI-458391;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope. Cytoplasm. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- INDUCTION: Preferentially expressed when quiescent fibroblasts are
CC stimulated to proliferate. It is inducible by growth factors and
CC overexpressed in acute myeloid leukemias.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: This protein co-purified with the prolactin
CC receptor.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M14300; AAA35886.1; -; mRNA.
DR EMBL; J02763; AAA51905.1; -; Genomic_DNA.
DR EMBL; M18981; AAA51906.1; -; mRNA.
DR EMBL; AY034480; AAK59702.1; -; Genomic_DNA.
DR EMBL; BT006965; AAP35611.1; -; mRNA.
DR EMBL; BX470102; CAI14752.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53318.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53320.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53321.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53322.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53323.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53324.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53325.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53326.1; -; Genomic_DNA.
DR EMBL; BC001431; AAH01431.1; -; mRNA.
DR EMBL; BC009017; AAH09017.1; -; mRNA.
DR PIR; A28363; BCHUY.
DR RefSeq; NP_055439.1; NM_014624.3.
DR UniGene; Hs.275243; -.
DR PDB; 1K8U; X-ray; 1.15 A; A=1-90.
DR PDB; 1K96; X-ray; 1.44 A; A=1-90.
DR PDB; 1K9K; X-ray; 1.76 A; A/B=1-90.
DR PDB; 1K9P; X-ray; 1.90 A; A=1-90.
DR PDBsum; 1K8U; -.
DR PDBsum; 1K96; -.
DR PDBsum; 1K9K; -.
DR PDBsum; 1K9P; -.
DR ProteinModelPortal; P06703; -.
DR SMR; P06703; 2-90.
DR IntAct; P06703; 10.
DR MINT; MINT-3005220; -.
DR STRING; 9606.ENSP00000357708; -.
DR PhosphoSite; P06703; -.
DR DMDM; 116509; -.
DR DOSAC-COBS-2DPAGE; P06703; -.
DR PaxDb; P06703; -.
DR PeptideAtlas; P06703; -.
DR PRIDE; P06703; -.
DR DNASU; 6277; -.
DR Ensembl; ENST00000368719; ENSP00000357708; ENSG00000197956.
DR Ensembl; ENST00000368720; ENSP00000357709; ENSG00000197956.
DR Ensembl; ENST00000496817; ENSP00000473589; ENSG00000197956.
DR GeneID; 6277; -.
DR KEGG; hsa:6277; -.
DR UCSC; uc001fbw.1; human.
DR CTD; 6277; -.
DR GeneCards; GC01M153507; -.
DR HGNC; HGNC:10496; S100A6.
DR HPA; CAB002601; -.
DR HPA; CAB040549; -.
DR HPA; HPA007575; -.
DR MIM; 114110; gene.
DR neXtProt; NX_P06703; -.
DR PharmGKB; PA34908; -.
DR eggNOG; NOG40006; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR InParanoid; P06703; -.
DR OMA; VVNFQEY; -.
DR OrthoDB; EOG78WKVD; -.
DR PhylomeDB; P06703; -.
DR ChiTaRS; S100A6; human.
DR EvolutionaryTrace; P06703; -.
DR GeneWiki; S100A6; -.
DR GenomeRNAi; 6277; -.
DR NextBio; 24365; -.
DR PRO; PR:P06703; -.
DR Bgee; P06703; -.
DR CleanEx; HS_S100A6; -.
DR Genevestigator; P06703; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic to cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0015075; F:ion transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005523; F:tropomyosin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028497; S100-A5/S100-A6.
DR InterPro; IPR001751; S100/CaBP-9k_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF14; PTHR11639:SF14; 1.
DR Pfam; PF01023; S_100; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cell membrane; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Membrane; Metal-binding;
KW Nucleus; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 90 Protein S100-A6.
FT /FTId=PRO_0000143984.
FT DOMAIN 12 47 EF-hand 1.
FT DOMAIN 48 83 EF-hand 2.
FT CA_BIND 20 33 1.
FT CA_BIND 61 72 2.
FT MOD_RES 40 40 N6-acetyllysine.
FT VARIANT 27 27 H -> R (in dbSNP:rs11974).
FT /FTId=VAR_011982.
FT VARIANT 69 69 N -> S (in dbSNP:rs1802581).
FT /FTId=VAR_011983.
FT VARIANT 83 83 I -> T (in dbSNP:rs1802582).
FT /FTId=VAR_011984.
FT VARIANT 90 90 G -> D (in dbSNP:rs2228293).
FT /FTId=VAR_029281.
FT HELIX 4 20
FT STRAND 22 24
FT STRAND 28 30
FT HELIX 31 41
FT HELIX 45 47
FT HELIX 51 62
FT TURN 63 65
FT STRAND 67 69
FT HELIX 70 84
FT HELIX 86 88
SQ SEQUENCE 90 AA; 10180 MW; 860CBB1416ACBCA1 CRC64;
MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL
DRNKDQEVNF QEYVTFLGAL ALIYNEALKG
//
ID S10A6_HUMAN Reviewed; 90 AA.
AC P06703; D3DV39; Q5RHS4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1988, sequence version 1.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Protein S100-A6;
DE AltName: Full=Calcyclin;
DE AltName: Full=Growth factor-inducible protein 2A9;
DE AltName: Full=MLN 4;
DE AltName: Full=Prolactin receptor-associated protein;
DE Short=PRA;
DE AltName: Full=S100 calcium-binding protein A6;
GN Name=S100A6; Synonyms=CACY;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=3755724;
RA Calabretta B., Battini R., Kaczmarek L., de Riel J.K., Baserga R.;
RT "Molecular cloning of the cDNA for a growth factor-inducible gene with
RT strong homology to S-100, a calcium-binding protein.";
RL J. Biol. Chem. 261:12628-12632(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036810;
RA Ferrari S., Calabretta B., Deriel J.K., Battini R., Ghezzo F.,
RA Lauret E., Griffin C., Emanuel B.S., Gurrieri F., Baserga R.;
RT "Structural and functional analysis of a growth-regulated gene, the
RT human calcyclin.";
RL J. Biol. Chem. 262:8325-8332(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2448309;
RA Murphy L.C., Murphy L.J., Tsuyuki D., Duckworth M.L., Shiu R.P.C.;
RT "Cloning and characterization of a cDNA encoding a highly conserved,
RT putative calcium binding protein, identified by an anti-prolactin
RT receptor antiserum.";
RL J. Biol. Chem. 263:2397-2401(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wu J., Liu W., Zhou Y., Zhao Z., Peng X., Yuan J., Qiang B.;
RT "Cloning of human calcyclin and calcyclin binding protein (CacyBP).";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 27-31 AND 48-89.
RC TISSUE=Platelet;
RX PubMed=1482346; DOI=10.1016/0006-291X(92)90216-8;
RA Tomida Y., Terasawa M., Kobayashi R., Hidaka H.;
RT "Calcyclin and calvasculin exist in human platelets.";
RL Biochem. Biophys. Res. Commun. 189:1310-1316(1992).
RN [10]
RP PROTEIN SEQUENCE OF 57-74.
RX PubMed=2775283; DOI=10.1016/0006-291X(89)92166-9;
RA Gabius H.J., Bardosi A., Gabius S., Hellmann K.P., Karas M.,
RA Kratzin H.;
RT "Identification of a cell cycle-dependent gene product as a sialic
RT acid-binding protein.";
RL Biochem. Biophys. Res. Commun. 163:506-512(1989).
RN [11]
RP INTERACTION WITH SUGT1.
RX PubMed=12746458; DOI=10.1074/jbc.M211518200;
RA Nowotny M., Spiechowicz M., Jastrzebska B., Filipek A., Kitagawa K.,
RA Kuznicki J.;
RT "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and
RT other S100 proteins.";
RL J. Biol. Chem. 278:26923-26928(2003).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=12601007; DOI=10.1074/jbc.M212669200;
RA Tomas A., Moss S.E.;
RT "Calcium- and cell cycle-dependent association of annexin 11 with the
RT nuclear envelope.";
RL J. Biol. Chem. 278:20210-20216(2003).
RN [13]
RP INTERACTION WITH ANXA2; ANXA11 AND TROPOMYOSIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19724273; DOI=10.1038/sj.bjc.6605289;
RA Nedjadi T., Kitteringham N., Campbell F., Jenkins R.E., Park B.K.,
RA Navarro P., Ashcroft F., Tepikin A., Neoptolemos J.P., Costello E.;
RT "S100A6 binds to annexin 2 in pancreatic cancer cells and promotes
RT pancreatic cancer cell motility.";
RL Br. J. Cancer 101:1145-1154(2009).
RN [14]
RP INTERACTION WITH TP53.
RX PubMed=19819244; DOI=10.1016/j.jmb.2009.10.002;
RA van Dieck J., Teufel D.P., Jaulent A.M., Fernandez-Fernandez M.R.,
RA Rutherford T.J., Wyslouch-Cieszynska A., Fersht A.R.;
RT "Posttranslational modifications affect the interaction of S100
RT proteins with tumor suppressor p53.";
RL J. Mol. Biol. 394:922-930(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP INTERACTION WITH FKBP4.
RX PubMed=20188096; DOI=10.1016/j.febslet.2010.02.055;
RA Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.;
RT "S100 proteins regulate the interaction of Hsp90 with cyclophilin 40
RT and FKBP52 through their tetratricopeptide repeats.";
RL FEBS Lett. 584:1119-1125(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, INTERACTION WITH PPP5C, AND SUBCELLULAR LOCATION.
RX PubMed=22399290; DOI=10.1074/jbc.M111.329771;
RA Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H.,
RA Tokuda M., Kobayashi R.;
RT "S100 proteins modulate protein phosphatase 5 function: a link between
RT CA2+ signal transduction and protein dephosphorylation.";
RL J. Biol. Chem. 287:13787-13798(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), SUBUNIT, AND CALCIUM-BINDING.
RX PubMed=11937060; DOI=10.1016/S0969-2126(02)00740-2;
RA Otterbein L.R., Kordowska J., Witte-Hoffmann C., Wang C.-L.A.,
RA Dominguez R.;
RT "Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound
RT states: the calcium sensor mechanism of S100 proteins revealed at
RT atomic resolution.";
RL Structure 10:557-567(2002).
CC -!- FUNCTION: May function as calcium sensor and modulator,
CC contributing to cellular calcium signaling. May function by
CC interacting with other proteins, such as TPR-containing proteins,
CC and indirectly play a role in many physiological processes such as
CC the reorganization of the actin cytoskeleton and in cell motility.
CC Binds 2 calcium ions. Calcium binding is cooperative.
CC -!- SUBUNIT: Homodimer; head to tail assembly of 2 subunits. Interacts
CC with CACYBP in a calcium-dependent manner. Interacts with ANXA2
CC and ANXA11 (via N-terminus). Interacts with SUGT1. Interacts with
CC TP53; has higher affinity for TP53 that is phosphorylated on its
CC N-terminal domain, and lower affinity for TP53 that is
CC phosphorylated on its C-terminal domain. Interacts with
CC tropomyosin. Interacts with FKBP4. Interacts with PPP5C (via TPR
CC repeats); the interaction is calcium-dependent and modulates PPP5C
CC activity.
CC -!- INTERACTION:
CC Q02790:FKBP4; NbExp=3; IntAct=EBI-352877, EBI-1047444;
CC P52292:KPNA2; NbExp=3; IntAct=EBI-352877, EBI-349938;
CC Q00987:MDM2; NbExp=2; IntAct=EBI-352877, EBI-389668;
CC P26882:PPID (xeno); NbExp=3; IntAct=EBI-352877, EBI-6477155;
CC P04271:S100B; NbExp=5; IntAct=EBI-352877, EBI-458391;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope. Cytoplasm. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- INDUCTION: Preferentially expressed when quiescent fibroblasts are
CC stimulated to proliferate. It is inducible by growth factors and
CC overexpressed in acute myeloid leukemias.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: This protein co-purified with the prolactin
CC receptor.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M14300; AAA35886.1; -; mRNA.
DR EMBL; J02763; AAA51905.1; -; Genomic_DNA.
DR EMBL; M18981; AAA51906.1; -; mRNA.
DR EMBL; AY034480; AAK59702.1; -; Genomic_DNA.
DR EMBL; BT006965; AAP35611.1; -; mRNA.
DR EMBL; BX470102; CAI14752.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53318.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53320.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53321.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53322.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53323.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53324.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53325.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53326.1; -; Genomic_DNA.
DR EMBL; BC001431; AAH01431.1; -; mRNA.
DR EMBL; BC009017; AAH09017.1; -; mRNA.
DR PIR; A28363; BCHUY.
DR RefSeq; NP_055439.1; NM_014624.3.
DR UniGene; Hs.275243; -.
DR PDB; 1K8U; X-ray; 1.15 A; A=1-90.
DR PDB; 1K96; X-ray; 1.44 A; A=1-90.
DR PDB; 1K9K; X-ray; 1.76 A; A/B=1-90.
DR PDB; 1K9P; X-ray; 1.90 A; A=1-90.
DR PDBsum; 1K8U; -.
DR PDBsum; 1K96; -.
DR PDBsum; 1K9K; -.
DR PDBsum; 1K9P; -.
DR ProteinModelPortal; P06703; -.
DR SMR; P06703; 2-90.
DR IntAct; P06703; 10.
DR MINT; MINT-3005220; -.
DR STRING; 9606.ENSP00000357708; -.
DR PhosphoSite; P06703; -.
DR DMDM; 116509; -.
DR DOSAC-COBS-2DPAGE; P06703; -.
DR PaxDb; P06703; -.
DR PeptideAtlas; P06703; -.
DR PRIDE; P06703; -.
DR DNASU; 6277; -.
DR Ensembl; ENST00000368719; ENSP00000357708; ENSG00000197956.
DR Ensembl; ENST00000368720; ENSP00000357709; ENSG00000197956.
DR Ensembl; ENST00000496817; ENSP00000473589; ENSG00000197956.
DR GeneID; 6277; -.
DR KEGG; hsa:6277; -.
DR UCSC; uc001fbw.1; human.
DR CTD; 6277; -.
DR GeneCards; GC01M153507; -.
DR HGNC; HGNC:10496; S100A6.
DR HPA; CAB002601; -.
DR HPA; CAB040549; -.
DR HPA; HPA007575; -.
DR MIM; 114110; gene.
DR neXtProt; NX_P06703; -.
DR PharmGKB; PA34908; -.
DR eggNOG; NOG40006; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR InParanoid; P06703; -.
DR OMA; VVNFQEY; -.
DR OrthoDB; EOG78WKVD; -.
DR PhylomeDB; P06703; -.
DR ChiTaRS; S100A6; human.
DR EvolutionaryTrace; P06703; -.
DR GeneWiki; S100A6; -.
DR GenomeRNAi; 6277; -.
DR NextBio; 24365; -.
DR PRO; PR:P06703; -.
DR Bgee; P06703; -.
DR CleanEx; HS_S100A6; -.
DR Genevestigator; P06703; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic to cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0015075; F:ion transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005523; F:tropomyosin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028497; S100-A5/S100-A6.
DR InterPro; IPR001751; S100/CaBP-9k_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF14; PTHR11639:SF14; 1.
DR Pfam; PF01023; S_100; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cell membrane; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Membrane; Metal-binding;
KW Nucleus; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 90 Protein S100-A6.
FT /FTId=PRO_0000143984.
FT DOMAIN 12 47 EF-hand 1.
FT DOMAIN 48 83 EF-hand 2.
FT CA_BIND 20 33 1.
FT CA_BIND 61 72 2.
FT MOD_RES 40 40 N6-acetyllysine.
FT VARIANT 27 27 H -> R (in dbSNP:rs11974).
FT /FTId=VAR_011982.
FT VARIANT 69 69 N -> S (in dbSNP:rs1802581).
FT /FTId=VAR_011983.
FT VARIANT 83 83 I -> T (in dbSNP:rs1802582).
FT /FTId=VAR_011984.
FT VARIANT 90 90 G -> D (in dbSNP:rs2228293).
FT /FTId=VAR_029281.
FT HELIX 4 20
FT STRAND 22 24
FT STRAND 28 30
FT HELIX 31 41
FT HELIX 45 47
FT HELIX 51 62
FT TURN 63 65
FT STRAND 67 69
FT HELIX 70 84
FT HELIX 86 88
SQ SEQUENCE 90 AA; 10180 MW; 860CBB1416ACBCA1 CRC64;
MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL
DRNKDQEVNF QEYVTFLGAL ALIYNEALKG
//
MIM
114110
*RECORD*
*FIELD* NO
114110
*FIELD* TI
*114110 S100 CALCIUM-BINDING PROTEIN A6; S100A6
;;CALCYCLIN; CACY
*FIELD* TX
DESCRIPTION
read more
S100 proteins, such as S100A6, are small, acidic Ca(2+)-binding proteins
that transduce Ca(2+)-signals via interaction with intracellular target
proteins (Mandinova et al., 1998).
CLONING
Ferrari et al. (1987) noted that S100A6, which they called calcyclin,
was originally defined as a cDNA clone (2A9) whose cognate RNA was found
to be growth-regulated and whose sequence showed strong similarities to
that of the S100 protein (see S100A1; 176940) and to a subunit of the
major cellular substrate for tyrosine kinase.
Using Northern blot analysis, Engelkamp et al. (1992) found ubiquitous
expression of a CACY transcript of about 550 bp. Highest expression was
detected in kidney, lung, and thymus.
Using immunofluorescence analysis and confocal laser scanning
microscopy, Mandinova et al. (1998) showed that S100A1, S100A2 (176993),
S100A4 (114210), and S100A6 localized to distinct intracellular
compartments in cultured human vascular and intestinal smooth muscle
cells. S100A6 localized predominantly with the sarcoplasmic reticulum.
GENE FUNCTION
Mandinova et al. (1998) showed that elevated cytosolic Ca(2+) led to
relocalization of S100A1, S100A4, and S100A6 from sarcoplasmic reticulum
to vesicle-like structures around the nucleus in human vascular smooth
muscle cells.
GENE STRUCTURE
Using a full-length cDNA, Ferrari et al. (1987) isolated the entire
calcyclin gene plus extensive flanking sequences. They found that the
calcyclin gene is present in single copy and has 3 exons. The 5-prime
flanking sequence contains a TATA box, GC boxes, and a sequence with a
strong homology to the enhancer core of the SV40 promoter. Other
enhancer-like elements are scattered in both the 5-prime and 3-prime
flanking regions.
MAPPING
By in situ hybridization, Ferrari et al. (1987) determined that the CACY
gene maps to chromosome 1q21-q25. Using cDNA probes for CACY, van
Heyningen et al. (1989) and Dorin et al. (1990) showed that the CACY
gene cosegregates with CAGA (S100A8; 123885) and CAGB (S100A9; 123886),
which are located on chromosome 1q12-q21. In the course of constructing
a physical map of human 1q21-q23, Oakey et al. (1992) determined that
the CACY gene is located at the centromeric end of that segment,
proximal to SPTA1 (182860).
Schafer et al. (1995) isolated a YAC from chromosome 1q21 on which 9
different genes coding for S100 calcium-binding proteins could be
localized. The clustered organization of S100 genes allowed introduction
of a new logical nomenclature based on their physical arrangement on the
chromosome with S100A1 being closest to the telomere and S100A9 being
closest to the centromere. In the new nomenclature, CACY became S100A6.
By linkage studies of interspecific backcrosses of Mus spretus and Mus
musculus domesticus, Seldin (1989) demonstrated that the Cacy gene is
located on mouse chromosome 3.
*FIELD* RF
1. Dorin, J. R.; Emslie, E.; van Heyningen, V.: Related calcium-binding
proteins map to the same subregion of chromosome 1q and to an extended
region of synteny on mouse chromosome 3. Genomics 8: 420-426, 1990.
2. Engelkamp, D.; Schafer, B. W.; Erne, P.; Heizmann, C. W.: S100-alpha,
CAPL, and CACY: molecular cloning and expression analysis of three
calcium-binding proteins from human heart. Biochemistry 31: 10258-10264,
1992.
3. 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.
4. Mandinova, A.; Atar, D.; Schafer, B. W.; Spiess, M.; Aebi, U.;
Heizmann, C. W.: Distinct subcellular localization of calcium binding
S100 proteins in human smooth muscle cells and their relocation in
response to rises in intracellular calcium. J. Cell Sci. 111: 2043-2054,
1998.
5. Oakey, R. J.; Watson, M. L.; Seldin, M. F.: Construction of a
physical map on mouse and human chromosome 1: comparison of 13 Mb
of mouse and 11 Mb of human DNA. Hum. Molec. Genet. 1: 613-620,
1992.
6. Schafer, B. W.; Wicki, R.; Engelkamp, D.; Mattei, M.-G.; Heizmann,
C. W.: Isolation of a YAC clone covering a cluster of nine S100 genes
on human chromosome 1q21: rationale for a new nomenclature of the
S100 calcium-binding protein family. Genomics 25: 638-643, 1995.
7. Seldin, M. F.: Personal Communication. Durham, N. C. 3/13/1989.
8. van Heyningen, V.; Emslie, E.; Dorin, J. R.: Related calcium binding
proteins map to the same sub-region of chromosome 1q and to an extended
region of synteny on mouse chromosome 3. (Abstract) Cytogenet. Cell
Genet. 51: 1095 only, 1989.
*FIELD* CN
Matthew B. Gross - updated: 08/19/2009
Patricia A. Hartz - updated: 7/17/2009
*FIELD* CD
Victor A. McKusick: 6/30/1987
*FIELD* ED
mgross: 08/19/2009
terry: 7/17/2009
mark: 12/21/1996
mark: 6/15/1995
carol: 1/23/1995
carol: 10/21/1993
carol: 2/9/1993
supermim: 3/16/1992
carol: 11/28/1990
*RECORD*
*FIELD* NO
114110
*FIELD* TI
*114110 S100 CALCIUM-BINDING PROTEIN A6; S100A6
;;CALCYCLIN; CACY
*FIELD* TX
DESCRIPTION
read more
S100 proteins, such as S100A6, are small, acidic Ca(2+)-binding proteins
that transduce Ca(2+)-signals via interaction with intracellular target
proteins (Mandinova et al., 1998).
CLONING
Ferrari et al. (1987) noted that S100A6, which they called calcyclin,
was originally defined as a cDNA clone (2A9) whose cognate RNA was found
to be growth-regulated and whose sequence showed strong similarities to
that of the S100 protein (see S100A1; 176940) and to a subunit of the
major cellular substrate for tyrosine kinase.
Using Northern blot analysis, Engelkamp et al. (1992) found ubiquitous
expression of a CACY transcript of about 550 bp. Highest expression was
detected in kidney, lung, and thymus.
Using immunofluorescence analysis and confocal laser scanning
microscopy, Mandinova et al. (1998) showed that S100A1, S100A2 (176993),
S100A4 (114210), and S100A6 localized to distinct intracellular
compartments in cultured human vascular and intestinal smooth muscle
cells. S100A6 localized predominantly with the sarcoplasmic reticulum.
GENE FUNCTION
Mandinova et al. (1998) showed that elevated cytosolic Ca(2+) led to
relocalization of S100A1, S100A4, and S100A6 from sarcoplasmic reticulum
to vesicle-like structures around the nucleus in human vascular smooth
muscle cells.
GENE STRUCTURE
Using a full-length cDNA, Ferrari et al. (1987) isolated the entire
calcyclin gene plus extensive flanking sequences. They found that the
calcyclin gene is present in single copy and has 3 exons. The 5-prime
flanking sequence contains a TATA box, GC boxes, and a sequence with a
strong homology to the enhancer core of the SV40 promoter. Other
enhancer-like elements are scattered in both the 5-prime and 3-prime
flanking regions.
MAPPING
By in situ hybridization, Ferrari et al. (1987) determined that the CACY
gene maps to chromosome 1q21-q25. Using cDNA probes for CACY, van
Heyningen et al. (1989) and Dorin et al. (1990) showed that the CACY
gene cosegregates with CAGA (S100A8; 123885) and CAGB (S100A9; 123886),
which are located on chromosome 1q12-q21. In the course of constructing
a physical map of human 1q21-q23, Oakey et al. (1992) determined that
the CACY gene is located at the centromeric end of that segment,
proximal to SPTA1 (182860).
Schafer et al. (1995) isolated a YAC from chromosome 1q21 on which 9
different genes coding for S100 calcium-binding proteins could be
localized. The clustered organization of S100 genes allowed introduction
of a new logical nomenclature based on their physical arrangement on the
chromosome with S100A1 being closest to the telomere and S100A9 being
closest to the centromere. In the new nomenclature, CACY became S100A6.
By linkage studies of interspecific backcrosses of Mus spretus and Mus
musculus domesticus, Seldin (1989) demonstrated that the Cacy gene is
located on mouse chromosome 3.
*FIELD* RF
1. Dorin, J. R.; Emslie, E.; van Heyningen, V.: Related calcium-binding
proteins map to the same subregion of chromosome 1q and to an extended
region of synteny on mouse chromosome 3. Genomics 8: 420-426, 1990.
2. Engelkamp, D.; Schafer, B. W.; Erne, P.; Heizmann, C. W.: S100-alpha,
CAPL, and CACY: molecular cloning and expression analysis of three
calcium-binding proteins from human heart. Biochemistry 31: 10258-10264,
1992.
3. 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.
4. Mandinova, A.; Atar, D.; Schafer, B. W.; Spiess, M.; Aebi, U.;
Heizmann, C. W.: Distinct subcellular localization of calcium binding
S100 proteins in human smooth muscle cells and their relocation in
response to rises in intracellular calcium. J. Cell Sci. 111: 2043-2054,
1998.
5. Oakey, R. J.; Watson, M. L.; Seldin, M. F.: Construction of a
physical map on mouse and human chromosome 1: comparison of 13 Mb
of mouse and 11 Mb of human DNA. Hum. Molec. Genet. 1: 613-620,
1992.
6. Schafer, B. W.; Wicki, R.; Engelkamp, D.; Mattei, M.-G.; Heizmann,
C. W.: Isolation of a YAC clone covering a cluster of nine S100 genes
on human chromosome 1q21: rationale for a new nomenclature of the
S100 calcium-binding protein family. Genomics 25: 638-643, 1995.
7. Seldin, M. F.: Personal Communication. Durham, N. C. 3/13/1989.
8. van Heyningen, V.; Emslie, E.; Dorin, J. R.: Related calcium binding
proteins map to the same sub-region of chromosome 1q and to an extended
region of synteny on mouse chromosome 3. (Abstract) Cytogenet. Cell
Genet. 51: 1095 only, 1989.
*FIELD* CN
Matthew B. Gross - updated: 08/19/2009
Patricia A. Hartz - updated: 7/17/2009
*FIELD* CD
Victor A. McKusick: 6/30/1987
*FIELD* ED
mgross: 08/19/2009
terry: 7/17/2009
mark: 12/21/1996
mark: 6/15/1995
carol: 1/23/1995
carol: 10/21/1993
carol: 2/9/1993
supermim: 3/16/1992
carol: 11/28/1990