Full text data of S100A2
S100A2
(S100L)
[Confidence: low (only semi-automatic identification from reviews)]
Protein S100-A2 (CAN19; Protein S-100L; S100 calcium-binding protein A2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein S100-A2 (CAN19; Protein S-100L; S100 calcium-binding protein A2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P29034
ID S10A2_HUMAN Reviewed; 98 AA.
AC P29034; O00266; Q3KRB9; Q5RHS8; Q9BU83;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-SEP-2006, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Protein S100-A2;
DE AltName: Full=CAN19;
DE AltName: Full=Protein S-100L;
DE AltName: Full=S100 calcium-binding protein A2;
GN Name=S100A2; Synonyms=S100L;
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], FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Mammary epithelium;
RX PubMed=1372446; DOI=10.1073/pnas.89.6.2504;
RA Lee S.W., Tomasetto C., Swisshelm K., Keyomarsi K., Sager R.;
RT "Down-regulation of a member of the S100 gene family in mammary
RT carcinoma cells and reexpression by azadeoxycytidine treatment.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2504-2508(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=9481475; DOI=10.1016/S0143-4160(97)90063-4;
RA Wicki R., Franz C., Scholl F.A., Heizmann C.W., Schaefer B.W.;
RT "Repression of the candidate tumor suppressor gene S100A2 in breast
RT cancer is mediated by site-specific hypermethylation.";
RL Cell Calcium 22:243-254(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [5]
RP PROTEIN SEQUENCE OF 37-40 AND 42-49.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [6]
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 [7]
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 [8]
RP FUNCTION IN CALCIUM SIGNALING, AND INTERACTION WITH PPP5C.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=18394645; DOI=10.1016/j.jmb.2008.03.019;
RA Koch M., Diez J., Fritz G.;
RT "Crystal structure of Ca2+ -free S100A2 at 1.6-A resolution.";
RL J. Mol. Biol. 378:933-942(2008).
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. May
CC also play a role in suppressing tumor cell growth.
CC -!- SUBUNIT: Homodimer. Interacts with FKBP4. Interacts with PPP5C
CC (via TPR repeats); the interaction is calcium-dependent and
CC modulates PPP5C activity.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-752230, EBI-752230;
CC Q02790:FKBP4; NbExp=3; IntAct=EBI-752230, EBI-1047444;
CC P52292:KPNA2; NbExp=5; IntAct=EBI-752230, EBI-349938;
CC P52293:Kpna2 (xeno); NbExp=2; IntAct=EBI-752230, EBI-3043908;
CC Q00987:MDM2; NbExp=2; IntAct=EBI-752230, EBI-389668;
CC P26882:PPID (xeno); NbExp=3; IntAct=EBI-752230, EBI-6477155;
CC P04637:TP53; NbExp=2; IntAct=EBI-752230, EBI-366083;
CC -!- TISSUE SPECIFICITY: A subset of epithelial cells including normal
CC human mammary epithelial cells and keratinocytes.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in normal human
CC mammary epithelial cells as opposed to tumor-derived ones. The
CC level of S100L was shown to correlate inversely with tumor
CC progression.
CC -!- INDUCTION: By growth factors in early G1 phase and probably by
CC cell-cycle regulation in S phase. DNA methylation probably plays a
CC direct negative role in suppressing S100L gene expression in tumor
CC cells.
CC -!- MISCELLANEOUS: This protein binds two calcium ions (By
CC similarity).
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA69033.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/S100A2ID42191ch1q21.html";
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; M87068; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Y07755; CAA69033.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX470102; CAI14756.1; -; Genomic_DNA.
DR EMBL; BC002829; AAH02829.3; -; mRNA.
DR EMBL; BC105787; AAI05788.1; -; mRNA.
DR PIR; A41988; A41988.
DR RefSeq; NP_005969.1; NM_005978.3.
DR UniGene; Hs.516484; -.
DR PDB; 2RGI; X-ray; 1.60 A; A/B=1-98.
DR PDB; 4DUQ; X-ray; 1.30 A; A/B=1-98.
DR PDBsum; 2RGI; -.
DR PDBsum; 4DUQ; -.
DR ProteinModelPortal; P29034; -.
DR SMR; P29034; 4-92.
DR IntAct; P29034; 9.
DR MINT; MINT-7256670; -.
DR STRING; 9606.ENSP00000357697; -.
DR PhosphoSite; P29034; -.
DR DMDM; 114152869; -.
DR PaxDb; P29034; -.
DR PRIDE; P29034; -.
DR Ensembl; ENST00000368708; ENSP00000357697; ENSG00000196754.
DR Ensembl; ENST00000368709; ENSP00000357698; ENSG00000196754.
DR Ensembl; ENST00000368710; ENSP00000357699; ENSG00000196754.
DR Ensembl; ENST00000487430; ENSP00000473260; ENSG00000196754.
DR GeneID; 6273; -.
DR KEGG; hsa:6273; -.
DR UCSC; uc001fcb.3; human.
DR CTD; 6273; -.
DR GeneCards; GC01M153533; -.
DR H-InvDB; HIX0001083; -.
DR HGNC; HGNC:10492; S100A2.
DR HPA; CAB002600; -.
DR HPA; CAB047340; -.
DR MIM; 176993; gene.
DR neXtProt; NX_P29034; -.
DR PharmGKB; PA34904; -.
DR eggNOG; NOG132073; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR OrthoDB; EOG7R833W; -.
DR ChiTaRS; S100A2; human.
DR EvolutionaryTrace; P29034; -.
DR GeneWiki; S100A2; -.
DR GenomeRNAi; 6273; -.
DR NextBio; 24347; -.
DR PRO; PR:P29034; -.
DR Bgee; P29034; -.
DR CleanEx; HS_S100A2; -.
DR Genevestigator; P29034; -.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; IMP: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; IPR028496; S100-A2/S100-A4.
DR InterPro; IPR001751; S100/CaBP-9k_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF15; PTHR11639:SF15; 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; Calcium; Complete proteome; Direct protein sequencing;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1 98 Protein S100-A2.
FT /FTId=PRO_0000143971.
FT DOMAIN 13 48 EF-hand 1.
FT DOMAIN 51 86 EF-hand 2.
FT CA_BIND 21 34 1; low affinity (Potential).
FT CA_BIND 64 75 2; high affinity (Potential).
FT CONFLICT 62 62 S -> N (in Ref. 1; M87068).
FT HELIX 5 21
FT STRAND 23 26
FT HELIX 32 42
FT HELIX 44 47
FT HELIX 53 63
FT STRAND 67 71
FT HELIX 73 89
SQ SEQUENCE 98 AA; 11117 MW; 56D09548450142A9 CRC64;
MMCSSLEQAL AVLVTTFHKY SCQEGDKFKL SKGEMKELLH KELPSFVGEK VDEEGLKKLM
GSLDENSDQQ VDFQEYAVFL ALITVMCNDF FQGCPDRP
//
ID S10A2_HUMAN Reviewed; 98 AA.
AC P29034; O00266; Q3KRB9; Q5RHS8; Q9BU83;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-SEP-2006, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Protein S100-A2;
DE AltName: Full=CAN19;
DE AltName: Full=Protein S-100L;
DE AltName: Full=S100 calcium-binding protein A2;
GN Name=S100A2; Synonyms=S100L;
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], FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Mammary epithelium;
RX PubMed=1372446; DOI=10.1073/pnas.89.6.2504;
RA Lee S.W., Tomasetto C., Swisshelm K., Keyomarsi K., Sager R.;
RT "Down-regulation of a member of the S100 gene family in mammary
RT carcinoma cells and reexpression by azadeoxycytidine treatment.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2504-2508(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=9481475; DOI=10.1016/S0143-4160(97)90063-4;
RA Wicki R., Franz C., Scholl F.A., Heizmann C.W., Schaefer B.W.;
RT "Repression of the candidate tumor suppressor gene S100A2 in breast
RT cancer is mediated by site-specific hypermethylation.";
RL Cell Calcium 22:243-254(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [5]
RP PROTEIN SEQUENCE OF 37-40 AND 42-49.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [6]
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 [7]
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 [8]
RP FUNCTION IN CALCIUM SIGNALING, AND INTERACTION WITH PPP5C.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=18394645; DOI=10.1016/j.jmb.2008.03.019;
RA Koch M., Diez J., Fritz G.;
RT "Crystal structure of Ca2+ -free S100A2 at 1.6-A resolution.";
RL J. Mol. Biol. 378:933-942(2008).
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. May
CC also play a role in suppressing tumor cell growth.
CC -!- SUBUNIT: Homodimer. Interacts with FKBP4. Interacts with PPP5C
CC (via TPR repeats); the interaction is calcium-dependent and
CC modulates PPP5C activity.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-752230, EBI-752230;
CC Q02790:FKBP4; NbExp=3; IntAct=EBI-752230, EBI-1047444;
CC P52292:KPNA2; NbExp=5; IntAct=EBI-752230, EBI-349938;
CC P52293:Kpna2 (xeno); NbExp=2; IntAct=EBI-752230, EBI-3043908;
CC Q00987:MDM2; NbExp=2; IntAct=EBI-752230, EBI-389668;
CC P26882:PPID (xeno); NbExp=3; IntAct=EBI-752230, EBI-6477155;
CC P04637:TP53; NbExp=2; IntAct=EBI-752230, EBI-366083;
CC -!- TISSUE SPECIFICITY: A subset of epithelial cells including normal
CC human mammary epithelial cells and keratinocytes.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in normal human
CC mammary epithelial cells as opposed to tumor-derived ones. The
CC level of S100L was shown to correlate inversely with tumor
CC progression.
CC -!- INDUCTION: By growth factors in early G1 phase and probably by
CC cell-cycle regulation in S phase. DNA methylation probably plays a
CC direct negative role in suppressing S100L gene expression in tumor
CC cells.
CC -!- MISCELLANEOUS: This protein binds two calcium ions (By
CC similarity).
CC -!- SIMILARITY: Belongs to the S-100 family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA69033.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/S100A2ID42191ch1q21.html";
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; M87068; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Y07755; CAA69033.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX470102; CAI14756.1; -; Genomic_DNA.
DR EMBL; BC002829; AAH02829.3; -; mRNA.
DR EMBL; BC105787; AAI05788.1; -; mRNA.
DR PIR; A41988; A41988.
DR RefSeq; NP_005969.1; NM_005978.3.
DR UniGene; Hs.516484; -.
DR PDB; 2RGI; X-ray; 1.60 A; A/B=1-98.
DR PDB; 4DUQ; X-ray; 1.30 A; A/B=1-98.
DR PDBsum; 2RGI; -.
DR PDBsum; 4DUQ; -.
DR ProteinModelPortal; P29034; -.
DR SMR; P29034; 4-92.
DR IntAct; P29034; 9.
DR MINT; MINT-7256670; -.
DR STRING; 9606.ENSP00000357697; -.
DR PhosphoSite; P29034; -.
DR DMDM; 114152869; -.
DR PaxDb; P29034; -.
DR PRIDE; P29034; -.
DR Ensembl; ENST00000368708; ENSP00000357697; ENSG00000196754.
DR Ensembl; ENST00000368709; ENSP00000357698; ENSG00000196754.
DR Ensembl; ENST00000368710; ENSP00000357699; ENSG00000196754.
DR Ensembl; ENST00000487430; ENSP00000473260; ENSG00000196754.
DR GeneID; 6273; -.
DR KEGG; hsa:6273; -.
DR UCSC; uc001fcb.3; human.
DR CTD; 6273; -.
DR GeneCards; GC01M153533; -.
DR H-InvDB; HIX0001083; -.
DR HGNC; HGNC:10492; S100A2.
DR HPA; CAB002600; -.
DR HPA; CAB047340; -.
DR MIM; 176993; gene.
DR neXtProt; NX_P29034; -.
DR PharmGKB; PA34904; -.
DR eggNOG; NOG132073; -.
DR HOGENOM; HOG000246968; -.
DR HOVERGEN; HBG001479; -.
DR OrthoDB; EOG7R833W; -.
DR ChiTaRS; S100A2; human.
DR EvolutionaryTrace; P29034; -.
DR GeneWiki; S100A2; -.
DR GenomeRNAi; 6273; -.
DR NextBio; 24347; -.
DR PRO; PR:P29034; -.
DR Bgee; P29034; -.
DR CleanEx; HS_S100A2; -.
DR Genevestigator; P29034; -.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; IMP: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; IPR028496; S100-A2/S100-A4.
DR InterPro; IPR001751; S100/CaBP-9k_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF15; PTHR11639:SF15; 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; Calcium; Complete proteome; Direct protein sequencing;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1 98 Protein S100-A2.
FT /FTId=PRO_0000143971.
FT DOMAIN 13 48 EF-hand 1.
FT DOMAIN 51 86 EF-hand 2.
FT CA_BIND 21 34 1; low affinity (Potential).
FT CA_BIND 64 75 2; high affinity (Potential).
FT CONFLICT 62 62 S -> N (in Ref. 1; M87068).
FT HELIX 5 21
FT STRAND 23 26
FT HELIX 32 42
FT HELIX 44 47
FT HELIX 53 63
FT STRAND 67 71
FT HELIX 73 89
SQ SEQUENCE 98 AA; 11117 MW; 56D09548450142A9 CRC64;
MMCSSLEQAL AVLVTTFHKY SCQEGDKFKL SKGEMKELLH KELPSFVGEK VDEEGLKKLM
GSLDENSDQQ VDFQEYAVFL ALITVMCNDF FQGCPDRP
//
MIM
176993
*RECORD*
*FIELD* NO
176993
*FIELD* TI
*176993 S100 CALCIUM-BINDING PROTEIN A2; S100A2
;;S100L
*FIELD* TX
DESCRIPTION
S100 proteins, such as S100A2, are small, acidic Ca(2+)-binding proteins
read morethat transduce Ca(2+)-signals via interaction with intracellular target
proteins (Mandinova et al., 1998).
CLONING
Using immunofluorescence analysis and confocal laser scanning
microscopy, Mandinova et al. (1998) showed that S100A1 (176940), S100A2,
S100A4 (114210), and S100A6 (114110) localized to distinct intracellular
compartments in cultured human vascular and intestinal smooth muscle
cells. Unlike the other S100 proteins, S100A2 localized primarily in the
nucleus.
MAPPING
Engelkamp et al. (1993) established the physical linkage of 6 S100 genes
by pulsed field gel electrophoresis. They stated that 4 of the S100
genes represented 'the tightest mammalian gene cluster discovered so
far.' The cluster was assigned to 1p21 by in situ hybridization. The 2
other S100 genes, S100L and S100A, were located within 450 kb.
Schafer et al. (1995) isolated a YAC clone from 1q21 on which 9
different genes coding for S100 calcium-binding proteins could be
localized. The clustered organization of these genes allowed
introduction of a new logical nomenclature based on their physical
arrangement, with S100A1 being the gene closest to the telomere and
S100A9 the one nearest the centromere. In this nomenclature, S100L
became S100A2.
*FIELD* RF
1. Engelkamp, D.; Schafer, B. W.; Mattei, M. G.; Erne, P.; Heizmann,
C. W.: Six S100 genes are clustered on human chromosome 1q21: identification
of two genes coding for the two previously unreported calcium-binding
proteins S100D and S100E. Proc. Nat. Acad. Sci. 90: 6547-6551, 1993.
2. 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.
3. 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.
*FIELD* CN
Patricia A. Hartz - updated: 7/17/2009
*FIELD* CD
Victor A. McKusick: 9/15/1993
*FIELD* ED
mgross: 08/19/2009
terry: 7/17/2009
alopez: 10/12/1998
mark: 12/21/1996
mark: 6/15/1995
carol: 1/23/1995
carol: 9/15/1993
*RECORD*
*FIELD* NO
176993
*FIELD* TI
*176993 S100 CALCIUM-BINDING PROTEIN A2; S100A2
;;S100L
*FIELD* TX
DESCRIPTION
S100 proteins, such as S100A2, are small, acidic Ca(2+)-binding proteins
read morethat transduce Ca(2+)-signals via interaction with intracellular target
proteins (Mandinova et al., 1998).
CLONING
Using immunofluorescence analysis and confocal laser scanning
microscopy, Mandinova et al. (1998) showed that S100A1 (176940), S100A2,
S100A4 (114210), and S100A6 (114110) localized to distinct intracellular
compartments in cultured human vascular and intestinal smooth muscle
cells. Unlike the other S100 proteins, S100A2 localized primarily in the
nucleus.
MAPPING
Engelkamp et al. (1993) established the physical linkage of 6 S100 genes
by pulsed field gel electrophoresis. They stated that 4 of the S100
genes represented 'the tightest mammalian gene cluster discovered so
far.' The cluster was assigned to 1p21 by in situ hybridization. The 2
other S100 genes, S100L and S100A, were located within 450 kb.
Schafer et al. (1995) isolated a YAC clone from 1q21 on which 9
different genes coding for S100 calcium-binding proteins could be
localized. The clustered organization of these genes allowed
introduction of a new logical nomenclature based on their physical
arrangement, with S100A1 being the gene closest to the telomere and
S100A9 the one nearest the centromere. In this nomenclature, S100L
became S100A2.
*FIELD* RF
1. Engelkamp, D.; Schafer, B. W.; Mattei, M. G.; Erne, P.; Heizmann,
C. W.: Six S100 genes are clustered on human chromosome 1q21: identification
of two genes coding for the two previously unreported calcium-binding
proteins S100D and S100E. Proc. Nat. Acad. Sci. 90: 6547-6551, 1993.
2. 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.
3. 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.
*FIELD* CN
Patricia A. Hartz - updated: 7/17/2009
*FIELD* CD
Victor A. McKusick: 9/15/1993
*FIELD* ED
mgross: 08/19/2009
terry: 7/17/2009
alopez: 10/12/1998
mark: 12/21/1996
mark: 6/15/1995
carol: 1/23/1995
carol: 9/15/1993