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P60903 (S10AA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein S100-A10
Alternative name(s):
Calpactin I light chain
Calpactin-1 light chain
Cellular ligand of annexin II
S100 calcium-binding protein A10
p10 protein
p11
Gene names
Name:S100A10
Synonyms:ANX2LG, CAL1L, CLP11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length97 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.

Subunit structure

Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36. Interacts with SCN10A By similarity.

Miscellaneous

Does not appear to bind calcium. Contains 2 ancestral calcium site related to EF-hand domains that have lost their ability to bind calcium.

Sequence similarities

Belongs to the S-100 family.

Ontologies

Keywords
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to acid

Inferred from electronic annotation. Source: Ensembl

establishment of protein localization to plasma membrane

Inferred from direct assay PubMed 12198146. Source: UniProt

membrane budding

Inferred from direct assay PubMed 23861394. Source: UniProt

membrane raft assembly

Inferred from direct assay PubMed 23861394. Source: UniProt

positive regulation of Rac GTPase activity

Inferred from mutant phenotype PubMed 23129259. Source: UniProt

positive regulation of binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of focal adhesion assembly

Inferred from mutant phenotype PubMed 23129259. Source: UniProt

positive regulation of stress fiber assembly

Inferred from mutant phenotype PubMed 23129259. Source: UniProt

positive regulation of substrate adhesion-dependent cell spreading

Inferred from mutant phenotype PubMed 23129259. Source: UniProt

protein heterotetramerization

Inferred from direct assay PubMed 23091277PubMed 23861394. Source: UniProt

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

extrinsic component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

ion channel binding

Inferred from physical interaction PubMed 12198146. Source: UniProt

protein homodimerization activity

Inferred from direct assay PubMed 23091277. Source: UniProt

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HLTFQ145272EBI-717048,EBI-1045161

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 9796Protein S100-A10
PRO_0000144002

Regions

Region60 – 7112Ancestral calcium site

Amino acid modifications

Modified residue231N6-acetyllysine Ref.7
Modified residue281N6-acetyllysine Ref.7
Modified residue371N6-acetyllysine Ref.7
Modified residue541N6-acetyllysine Ref.7
Modified residue571N6-acetyllysine Ref.7

Secondary structure

................. 97
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60903 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3E8E03A6E7DD7A8D

FASTA9711,203
        10         20         30         40         50         60 
MPSQMEHAME TMMFTFHKFA GDKGYLTKED LRVLMEKEFP GFLENQKDPL AVDKIMKDLD 

        70         80         90 
QCRDGKVGFQ SFFSLIAGLT IACNDYFVVH MKQKGKK 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of human, chicken, and Xenopus laevis p11, a cellular ligand of the Src-kinase substrate, annexin II."
Kube E., Weber K., Gerke V.
Gene 102:255-259(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and characterization of the human gene encoding p11: structural similarity to other members of the S-100 gene family."
Harder T., Kube E., Gerke V.
Gene 113:269-274(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"cDNA sequence of human p11 calpactin I light chain."
Dooley T.P., Weiland K.L., Simon M.
Genomics 13:866-868(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Keratinocyte.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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. expand/collapse author list , 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].
[6]"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: Brain.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-28; LYS-37; LYS-54 AND LYS-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The crystal structure of a complex of p11 with the annexin II N-terminal peptide."
Rety S., Sopkova J., Renouard M., Osterloh D., Gerke V., Tabaries S., Russo-Marie F., Lewit-Bentley A.
Nat. Struct. Biol. 6:89-95(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81457 mRNA. Translation: AAA58404.1.
M38591 mRNA. Translation: AAA58426.1.
M77483 Genomic DNA. No translation available.
AK291073 mRNA. Translation: BAF83762.1.
AL450992 Genomic DNA. Translation: CAI12164.1.
BC015973 mRNA. Translation: AAH15973.1.
BC105786 mRNA. Translation: AAI05787.1.
PIRJC1139.
RefSeqNP_002957.1. NM_002966.2.
UniGeneHs.143873.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4PX-ray2.25A/B2-97[»]
1BT6X-ray2.40A/B2-97[»]
4DRWX-ray3.50A/B/C/D1-93[»]
4FTGX-ray2.51A/B2-97[»]
4HREX-ray2.79E/F/I/J2-97[»]
4HRGX-ray2.00A/B1-93[»]
4HRHX-ray3.00A/B1-93[»]
ProteinModelPortalP60903.
SMRP60903. Positions 2-93.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112189. 35 interactions.
IntActP60903. 7 interactions.
MINTMINT-1178035.
STRING9606.ENSP00000357799.

Chemistry

BindingDBP60903.
ChEMBLCHEMBL2111435.

PTM databases

PhosphoSiteP60903.

Polymorphism databases

DMDM46397706.

2D gel databases

SWISS-2DPAGEP60903.

Proteomic databases

PaxDbP60903.
PeptideAtlasP60903.
PRIDEP60903.

Protocols and materials databases

DNASU6281.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368809; ENSP00000357799; ENSG00000197747.
ENST00000368811; ENSP00000357801; ENSG00000197747.
GeneID6281.
KEGGhsa:6281.
UCSCuc001ezl.3. human.

Organism-specific databases

CTD6281.
GeneCardsGC01M151955.
HGNCHGNC:10487. S100A10.
HPACAB025484.
HPA003340.
MIM114085. gene.
neXtProtNX_P60903.
PharmGKBPA34899.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26977.
HOVERGENHBG001479.
InParanoidP60903.
KOK17274.
OMAAMETLMF.
OrthoDBEOG7R833W.
PhylomeDBP60903.
TreeFamTF332727.

Gene expression databases

ArrayExpressP60903.
BgeeP60903.
CleanExHS_S100A10.
GenevestigatorP60903.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR028476. S100-A10.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERPTHR11639:SF8. PTHR11639:SF8. 1 hit.
PfamPF01023. S_100. 1 hit.
[Graphical view]
PROSITEPS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSS100A10. human.
EvolutionaryTraceP60903.
GeneWikiS100A10.
GenomeRNAi6281.
NextBio24381.
PROP60903.
SOURCESearch...

Entry information

Entry nameS10AA_HUMAN
AccessionPrimary (citable) accession number: P60903
Secondary accession number(s): A8K4V8, P08206, Q5T1C5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM