Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23297 (S10A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. 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-A1
Alternative name(s):
S-100 protein alpha chain
S-100 protein subunit alpha
S100 calcium-binding protein A1
Gene names
Name:S100A1
Synonyms:S100A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length94 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity. Ref.13

Subunit structure

Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain. Also forms heterodimers with S100P. Interacts with AGER and CAPZA1. Interacts with FKBP4. Interacts with RYR1 and RYR2. Interacts with CACYBP in a calcium-dependent manner. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14

Subcellular location

Cytoplasm.

Tissue specificity

Highly prevalent in heart. Also found in lesser quantities in skeletal muscle and brain.

Sequence similarities

Belongs to the S-100 family.

Contains 2 EF-hand domains.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
   LigandCalcium
Metal-binding
Zinc
   PTMS-nitrosylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular signal transduction

Non-traceable author statement PubMed 12804600. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of voltage-gated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

regulation of heart contraction

Non-traceable author statement PubMed 12804600. Source: UniProtKB

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentM band

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 12118070. Source: UniProtKB

protein complex

Non-traceable author statement PubMed 14638689. Source: UniProtKB

sarcoplasmic reticulum

Inferred from direct assay PubMed 12804600. Source: UniProtKB

   Molecular_functionATPase binding

Inferred from physical interaction PubMed 12804600. Source: UniProtKB

S100 protein binding

Inferred from physical interaction PubMed 10913138. Source: UniProtKB

calcium ion binding

Traceable author statement PubMed 1998503. Source: ProtInc

identical protein binding

Inferred from physical interaction PubMed 10913138Ref.9PubMed 16189514Ref.14. Source: IntAct

protein binding

Inferred from physical interaction PubMed 10913138. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 10913138. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 9493Protein S100-A1
PRO_0000143961

Regions

Domain13 – 4836EF-hand 1
Domain50 – 8536EF-hand 2
Calcium binding20 – 33141; low affinity
Calcium binding63 – 74122; high affinity

Amino acid modifications

Modified residue861S-nitrosocysteine Ref.15

Secondary structure

................. 94
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23297 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AD5E53AF326B25D2

FASTA9410,546
        10         20         30         40         50         60 
MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK DVDAVDKVMK 

        70         80         90 
ELDENGDGEV DFQEYVVLVA ALTVACNNFF WENS 

« Hide

References

« Hide 'large scale' references
[1]"S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart."
Engelkamp D., Schaefer B.W., Erne P., Heizmann C.W.
Biochemistry 31:10258-10264(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"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].
Tissue: Caudate nucleus.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Skin.
[8]"CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family."
Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.
J. Biol. Chem. 277:28848-28852(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CACYBP.
[9]"Heterodimeric interaction and interfaces of S100A1 and S100P."
Wang G., Zhang S., Fernig D.G., Spiller D., Martin-Fernandez M., Zhang H., Ding Y., Rao Z., Rudland P.S., Barraclough R.
Biochem. J. 382:375-383(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH S100P.
[10]"S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RYR1 AND RYR2.
[11]"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.
[12]"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].
[13]"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, INTERACTION WITH PPP5C.
[14]"Solution NMR structure and dynamics of human apo-S100A1 protein."
Nowakowski M., Jaremko L., Jaremko M., Zhukov I., Belczyk A., Bierzynski A., Ejchart A.
J. Struct. Biol. 174:391-399(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, SUBUNIT.
[15]"Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein."
Lenarcic Zivkovic M., Zareba-Koziol M., Zhukova L., Poznanski J., Zhukov I., Wyslouch-Cieszynska A.
J. Biol. Chem. 287:40457-40470(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-94, S-NITROSYLATION AT CYS-86.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58079 mRNA. Translation: CAA41107.1.
AK312152 mRNA. Translation: BAG35086.1.
BT006938 mRNA. Translation: AAP35584.1.
AB451316 mRNA. Translation: BAG70130.1.
AB451446 mRNA. Translation: BAG70260.1.
AL162258 Genomic DNA. Translation: CAI19677.1.
CH471121 Genomic DNA. Translation: EAW53302.1.
BC014392 mRNA. Translation: AAH14392.1.
CCDSCCDS1047.1.
PIRBCHUIA. A44470.
RefSeqNP_006262.1. NM_006271.1.
UniGeneHs.515715.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L0PNMR-A/B1-94[»]
2LHLNMR-A/B2-94[»]
2LLSNMR-A/B2-94[»]
2LLTNMR-A/B2-94[»]
2LLUNMR-A/B2-94[»]
2LP2NMR-A/B2-94[»]
2LP3NMR-A/B2-94[»]
2LUXNMR-A/B2-94[»]
2M3WNMR-A/B2-94[»]
ProteinModelPortalP23297.
SMRP23297. Positions 2-94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112179. 18 interactions.
IntActP23297. 8 interactions.
MINTMINT-1543322.
STRING9606.ENSP00000292169.

Chemistry

DrugBankDB00768. Olopatadine.

Polymorphism databases

DMDM134136.

Proteomic databases

MaxQBP23297.
PaxDbP23297.
PRIDEP23297.

Protocols and materials databases

DNASU6271.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292169; ENSP00000292169; ENSG00000160678.
GeneID6271.
KEGGhsa:6271.
UCSCuc001fck.1. human.

Organism-specific databases

CTD6271.
GeneCardsGC01P153600.
HGNCHGNC:10486. S100A1.
HPACAB002599.
HPA006462.
MIM176940. gene.
neXtProtNX_P23297.
PharmGKBPA34898.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277258.
HOGENOMHOG000246968.
HOVERGENHBG001479.
InParanoidP23297.
PhylomeDBP23297.
TreeFamTF332727.

Gene expression databases

ArrayExpressP23297.
BgeeP23297.
CleanExHS_S100A1.
GenevestigatorP23297.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028486. S100-A1.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERPTHR11639:SF66. PTHR11639:SF66. 1 hit.
PfamPF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiS100_calcium-binding_protein_A1.
GenomeRNAi6271.
NextBio24339.
PROP23297.
SOURCESearch...

Entry information

Entry nameS10A1_HUMAN
AccessionPrimary (citable) accession number: P23297
Secondary accession number(s): B2R5D9, Q5T7Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 143 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