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Protein

Protein S100-A10

Gene

S100A10

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

Functioni

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.

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • ion channel binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • establishment of protein localization to plasma membrane Source: UniProtKB
  • membrane budding Source: UniProtKB
  • membrane raft assembly Source: UniProtKB
  • positive regulation of binding Source: Ensembl
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • positive regulation of GTPase activity Source: UniProtKB
  • positive regulation of stress fiber assembly Source: UniProtKB
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • protein heterotetramerization Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_641. Dissolution of Fibrin Clot.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:S100A10
Synonyms:ANX2LG, CAL1L, CLP11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10487. S100A10.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extrinsic component of plasma membrane Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34899.

Polymorphism and mutation databases

BioMutaiS100A10.
DMDMi46397706.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 9796Protein S100-A10PRO_0000144002Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231N6-acetyllysine1 Publication
Modified residuei28 – 281N6-acetyllysine1 Publication
Modified residuei37 – 371N6-acetyllysine1 Publication
Modified residuei54 – 541N6-acetyllysine1 Publication
Modified residuei57 – 571N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP60903.
PaxDbiP60903.
PeptideAtlasiP60903.
PRIDEiP60903.

2D gel databases

SWISS-2DPAGEP60903.

PTM databases

PhosphoSiteiP60903.

Expressioni

Gene expression databases

BgeeiP60903.
CleanExiHS_S100A10.
GenevisibleiP60903. HS.

Organism-specific databases

HPAiCAB025484.
HPA003340.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
HLTFQ145272EBI-717048,EBI-1045161

Protein-protein interaction databases

BioGridi112189. 42 interactions.
IntActiP60903. 7 interactions.
MINTiMINT-1178035.
STRINGi9606.ENSP00000357799.

Structurei

Secondary structure

1
97
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2017Combined sources
Helixi21 – 233Combined sources
Beta strandi24 – 263Combined sources
Helixi28 – 3811Combined sources
Helixi42 – 454Combined sources
Helixi51 – 577Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 653Combined sources
Helixi69 – 9022Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP60903.
SMRiP60903. Positions 2-93.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60903.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 7112Ancestral calcium siteAdd
BLAST

Sequence similaritiesi

Belongs to the S-100 family.Curated

Phylogenomic databases

eggNOGiNOG26977.
GeneTreeiENSGT00760000119034.
HOVERGENiHBG001479.
InParanoidiP60903.
KOiK17274.
OMAiAMETLMF.
OrthoDBiEOG7R833W.
PhylomeDBiP60903.
TreeFamiTF332727.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR028476. S100-A10.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR11639:SF56. PTHR11639:SF56. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
PROSITEiPS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60903-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSQMEHAME TMMFTFHKFA GDKGYLTKED LRVLMEKEFP GFLENQKDPL
60 70 80 90
AVDKIMKDLD QCRDGKVGFQ SFFSLIAGLT IACNDYFVVH MKQKGKK
Length:97
Mass (Da):11,203
Last modified:January 23, 2007 - v2
Checksum:i3E8E03A6E7DD7A8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1008.1.
PIRiJC1139.
RefSeqiNP_002957.1. NM_002966.2.
UniGeneiHs.143873.

Genome annotation databases

EnsembliENST00000368809; ENSP00000357799; ENSG00000197747.
ENST00000368811; ENSP00000357801; ENSG00000197747.
GeneIDi6281.
KEGGihsa:6281.
UCSCiuc001ezl.3. 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
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.
CCDSiCCDS1008.1.
PIRiJC1139.
RefSeqiNP_002957.1. NM_002966.2.
UniGeneiHs.143873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP60903.
SMRiP60903. Positions 2-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112189. 42 interactions.
IntActiP60903. 7 interactions.
MINTiMINT-1178035.
STRINGi9606.ENSP00000357799.

Chemistry

ChEMBLiCHEMBL2111435.

PTM databases

PhosphoSiteiP60903.

Polymorphism and mutation databases

BioMutaiS100A10.
DMDMi46397706.

2D gel databases

SWISS-2DPAGEP60903.

Proteomic databases

MaxQBiP60903.
PaxDbiP60903.
PeptideAtlasiP60903.
PRIDEiP60903.

Protocols and materials databases

DNASUi6281.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368809; ENSP00000357799; ENSG00000197747.
ENST00000368811; ENSP00000357801; ENSG00000197747.
GeneIDi6281.
KEGGihsa:6281.
UCSCiuc001ezl.3. human.

Organism-specific databases

CTDi6281.
GeneCardsiGC01M151955.
HGNCiHGNC:10487. S100A10.
HPAiCAB025484.
HPA003340.
MIMi114085. gene.
neXtProtiNX_P60903.
PharmGKBiPA34899.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG26977.
GeneTreeiENSGT00760000119034.
HOVERGENiHBG001479.
InParanoidiP60903.
KOiK17274.
OMAiAMETLMF.
OrthoDBiEOG7R833W.
PhylomeDBiP60903.
TreeFamiTF332727.

Enzyme and pathway databases

ReactomeiREACT_641. Dissolution of Fibrin Clot.

Miscellaneous databases

ChiTaRSiS100A10. human.
EvolutionaryTraceiP60903.
GeneWikiiS100A10.
GenomeRNAii6281.
NextBioi24381.
PROiP60903.
SOURCEiSearch...

Gene expression databases

BgeeiP60903.
CleanExiHS_S100A10.
GenevisibleiP60903. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR028476. S100-A10.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR11639:SF56. PTHR11639:SF56. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]
PROSITEiPS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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).

Entry informationi

Entry nameiS10AA_HUMAN
AccessioniPrimary (citable) accession number: P60903
Secondary accession number(s): A8K4V8, P08206, Q5T1C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 121 of the entry and version 2 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

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

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

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 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.