P29034 (S10A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein S100-A2

Alternative name(s):
CAN19
Protein S-100L
S100 calcium-binding protein A2

Gene names

Name:	S100A2
Synonyms:	S100L

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	98 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May act as a modulator against excess calcium accumulation in normal human mammary epithelial cells. May also play a role in suppressing tumor cell growth. Ref.1
Subunit structure	Homomultimeric Probable. Interacts with FKBP4. Ref.6
Tissue specificity	A subset of epithelial cells including normal human mammary epithelial cells and keratinocytes. Ref.1
Developmental stage	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. Ref.2
Induction	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. Ref.1 Ref.2
Miscellaneous	This protein binds two calcium ions By similarity.
Sequence similarities	Belongs to the S-100 family. Contains 2 EF-hand domains.
Caution	It is uncertain whether Met-1 or Met-2 is the initiator.
Sequence caution	The sequence CAA69033.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Domain	Repeat
Ligand	Calcium
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	endothelial cell migration Inferred from mutant phenotype. Source: UniProtKB
Molecular function	calcium ion binding Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 98

98

Protein S100-A2

PRO_0000143971

Regions

Domain

13 – 48

36

EF-hand 1

Domain

51 – 86

36

EF-hand 2

Calcium binding

21 – 34

14

1; low affinity Potential

Calcium binding

64 – 75

12

2; high affinity Potential

Experimental info

Sequence conflict

62

1

S → N in M87068. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

98

Helix Strand Turn

Details...

Helix

5 – 21

17

Helix

32 – 42

11

Helix

53 – 65

13

Turn

66 – 68

3

Beta strand

69 – 71

3

Helix

73 – 87

15

Helix

89 – 92

4

Sequences

	Sequence		Length	Mass (Da)
	P29034 [UniParc]. Last modified September 5, 2006. Version 3. Checksum: 56D09548450142A9	FASTA	98	11,117
	10 20 30 40 50 60 MMCSSLEQAL AVLVTTFHKY SCQEGDKFKL SKGEMKELLH KELPSFVGEK VDEEGLKKLM 70 80 90 GSLDENSDQQ VDFQEYAVFL ALITVMCNDF FQGCPDRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1372446] [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: 9481475] [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: 16710414] [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: 15489334] [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: 1286667] [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: 20188096] [Abstract] Cited for: INTERACTION WITH FKBP4.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00019869.

PIR

A41988.

RefSeq

NP_005969.1. NM_005978.3.

UniGene

Hs.516484.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RGI	X-ray	1.60	A/B	1-98	[»]
3N22	X-ray	1.30	A/B	1-98	[»]

ProteinModelPortal

P29034.

SMR

P29034. Positions 4-92.

ModBase

Search...

Protein-protein interaction databases

IntAct

P29034. 1 interaction.

MINT

MINT-7256670.

STRING

P29034.

PTM databases

PhosphoSite

P29034.

Polymorphism databases

DMDM

114152869.

2D gel databases

Aarhus/Ghent-2DPAGE

9027. IEF.
9051. IEF.

Proteomic databases

PRIDE

P29034.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368711; ENSP00000357700; ENSG00000196754.

GeneID

6273.

KEGG

hsa:6273.

UCSC

uc001fcb.1. human.

Organism-specific databases

CTD

6273.

GeneCards

GC01M153533.

H-InvDB

HIX0001083.

HGNC

HGNC:10492. S100A2.

HPA

CAB002600.
CAB047340.

MIM

176993. gene.

neXtProt

NX_P29034.

PharmGKB

PA34904.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00600000084162.

HOVERGEN

HBG001479.

Gene expression databases

ArrayExpress

P29034.

Bgee

P29034.

CleanEx

HS_S100A2.

Genevestigator

P29034.

GermOnline

ENSG00000196754. Homo sapiens.

Family and domain databases

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF01023. S_100. 1 hit.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

24347.

SOURCE

Search...

Entry information

Entry name

S10A2_HUMAN

Accession

Primary (citable) accession number: P29034
Secondary accession number(s): O00266 , Q3KRB9, Q5RHS8, Q9BU83

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.