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Protein

Protein S100-A2

Gene

S100A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. May also play a role in suppressing tumor cell growth.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi21 – 34141; low affinityPROSITE-ProRule annotationAdd
BLAST
Calcium bindingi64 – 75122; high affinityPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • identical protein binding Source: IntAct

GO - Biological processi

  • endothelial cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-A2
Alternative name(s):
CAN19
Protein S-100L
S100 calcium-binding protein A2
Gene namesi
Name:S100A2
Synonyms:S100L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10492. S100A2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34904.

Chemistry

DrugBankiDB00768. Olopatadine.

Polymorphism and mutation databases

BioMutaiS100A2.
DMDMi114152869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9898Protein S100-A2PRO_0000143971Add
BLAST

Proteomic databases

EPDiP29034.
MaxQBiP29034.
PaxDbiP29034.
PRIDEiP29034.

PTM databases

iPTMnetiP29034.
PhosphoSiteiP29034.

Expressioni

Tissue specificityi

A subset of epithelial cells including normal human mammary epithelial cells and keratinocytes.1 Publication

Developmental stagei

Preferentially expressed in normal human mammary epithelial cells as opposed to tumor-derived ones. The level of S100L was shown to correlate inversely with tumor progression.1 Publication

Inductioni

By growth factors in early G1 phase and probably by cell-cycle regulation in S phase. DNA methylation probably plays a direct negative role in suppressing S100L gene expression in tumor cells.2 Publications

Gene expression databases

BgeeiP29034.
CleanExiHS_S100A2.
ExpressionAtlasiP29034. baseline and differential.
GenevisibleiP29034. HS.

Organism-specific databases

HPAiCAB002600.
CAB047339.
CAB047340.
HPA062451.

Interactioni

Subunit structurei

Homodimer. Interacts with FKBP4. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-752230,EBI-752230
FKBP4Q027903EBI-752230,EBI-1047444
KPNA2P522925EBI-752230,EBI-349938
Kpna2P522932EBI-752230,EBI-3043908From a different organism.
MDM2Q009872EBI-752230,EBI-389668
PPIDP268823EBI-752230,EBI-6477155From a different organism.
S100A1P232973EBI-752230,EBI-743686
S100BP042713EBI-752230,EBI-458391
TP53P046372EBI-752230,EBI-366083

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi112181. 13 interactions.
IntActiP29034. 12 interactions.
MINTiMINT-7256670.
STRINGi9606.ENSP00000357697.

Structurei

Secondary structure

1
98
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2117Combined sources
Beta strandi23 – 264Combined sources
Helixi32 – 4211Combined sources
Helixi44 – 474Combined sources
Helixi53 – 6311Combined sources
Beta strandi67 – 715Combined sources
Helixi73 – 8917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RGIX-ray1.60A/B1-98[»]
4DUQX-ray1.30A/B1-98[»]
ProteinModelPortaliP29034.
SMRiP29034. Positions 4-92.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29034.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 4836EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini51 – 8636EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the S-100 family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IYI7. Eukaryota.
ENOG41115QW. LUCA.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP29034.
OrthoDBiEOG7R833W.
PhylomeDBiP29034.
TreeFamiTF332727.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29034-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMCSSLEQAL AVLVTTFHKY SCQEGDKFKL SKGEMKELLH KELPSFVGEK
60 70 80 90
VDEEGLKKLM GSLDENSDQQ VDFQEYAVFL ALITVMCNDF FQGCPDRP
Length:98
Mass (Da):11,117
Last modified:September 5, 2006 - v3
Checksum:i56D09548450142A9
GO

Sequence cautioni

The sequence CAA69033.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621S → N in M87068 (PubMed:1372446).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87068 mRNA. No translation available.
Y07755 Genomic DNA. Translation: CAA69033.1. Different initiation.
BX470102 Genomic DNA. Translation: CAI14756.1.
BC002829 mRNA. Translation: AAH02829.3.
BC105787 mRNA. Translation: AAI05788.1.
PIRiA41988.
RefSeqiNP_005969.1. NM_005978.3.
UniGeneiHs.516484.

Genome annotation databases

EnsembliENST00000368708; ENSP00000357697; ENSG00000196754.
ENST00000368709; ENSP00000357698; ENSG00000196754.
ENST00000368710; ENSP00000357699; ENSG00000196754.
ENST00000487430; ENSP00000473260; ENSG00000196754.
GeneIDi6273.
KEGGihsa:6273.
UCSCiuc001fcb.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87068 mRNA. No translation available.
Y07755 Genomic DNA. Translation: CAA69033.1. Different initiation.
BX470102 Genomic DNA. Translation: CAI14756.1.
BC002829 mRNA. Translation: AAH02829.3.
BC105787 mRNA. Translation: AAI05788.1.
PIRiA41988.
RefSeqiNP_005969.1. NM_005978.3.
UniGeneiHs.516484.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RGIX-ray1.60A/B1-98[»]
4DUQX-ray1.30A/B1-98[»]
ProteinModelPortaliP29034.
SMRiP29034. Positions 4-92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112181. 13 interactions.
IntActiP29034. 12 interactions.
MINTiMINT-7256670.
STRINGi9606.ENSP00000357697.

Chemistry

DrugBankiDB00768. Olopatadine.

PTM databases

iPTMnetiP29034.
PhosphoSiteiP29034.

Polymorphism and mutation databases

BioMutaiS100A2.
DMDMi114152869.

Proteomic databases

EPDiP29034.
MaxQBiP29034.
PaxDbiP29034.
PRIDEiP29034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368708; ENSP00000357697; ENSG00000196754.
ENST00000368709; ENSP00000357698; ENSG00000196754.
ENST00000368710; ENSP00000357699; ENSG00000196754.
ENST00000487430; ENSP00000473260; ENSG00000196754.
GeneIDi6273.
KEGGihsa:6273.
UCSCiuc001fcb.4. human.

Organism-specific databases

CTDi6273.
GeneCardsiS100A2.
H-InvDBHIX0001083.
HGNCiHGNC:10492. S100A2.
HPAiCAB002600.
CAB047339.
CAB047340.
HPA062451.
MIMi176993. gene.
neXtProtiNX_P29034.
PharmGKBiPA34904.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IYI7. Eukaryota.
ENOG41115QW. LUCA.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP29034.
OrthoDBiEOG7R833W.
PhylomeDBiP29034.
TreeFamiTF332727.

Miscellaneous databases

ChiTaRSiS100A2. human.
EvolutionaryTraceiP29034.
GeneWikiiS100A2.
GenomeRNAii6273.
NextBioi24347.
PROiP29034.
SOURCEiSearch...

Gene expression databases

BgeeiP29034.
CleanExiHS_S100A2.
ExpressionAtlasiP29034. baseline and differential.
GenevisibleiP29034. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment."
    Lee S.W., Tomasetto C., Swisshelm K., Keyomarsi K., Sager R.
    Proc. Natl. Acad. Sci. U.S.A. 89:2504-2508(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Tissue: Mammary epithelium.
  2. "Repression of the candidate tumor suppressor gene S100A2 in breast cancer is mediated by site-specific hypermethylation."
    Wicki R., Franz C., Scholl F.A., Heizmann C.W., Schaefer B.W.
    Cell Calcium 22:243-254(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, INDUCTION.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  5. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 37-40 AND 42-49.
    Tissue: Keratinocyte.
  6. "S100 proteins regulate the interaction of Hsp90 with cyclophilin 40 and FKBP52 through their tetratricopeptide repeats."
    Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.
    FEBS Lett. 584:1119-1125(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP4.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "S100 proteins modulate protein phosphatase 5 function: a link between CA2+ signal transduction and protein dephosphorylation."
    Yamaguchi F., Umeda Y., Shimamoto S., Tsuchiya M., Tokumitsu H., Tokuda M., Kobayashi R.
    J. Biol. Chem. 287:13787-13798(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CALCIUM SIGNALING, INTERACTION WITH PPP5C.
  9. "Crystal structure of Ca2+ -free S100A2 at 1.6-A resolution."
    Koch M., Diez J., Fritz G.
    J. Mol. Biol. 378:933-942(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiS10A2_HUMAN
AccessioniPrimary (citable) accession number: P29034
Secondary accession number(s): O00266
, Q3KRB9, Q5RHS8, Q9BU83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 5, 2006
Last modified: May 11, 2016
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

This protein binds two calcium ions.By similarity

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.