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P23297

- S10A1_HUMAN

UniProt

P23297 - S10A1_HUMAN

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Protein

Protein S100-A1

Gene
S100A1, S100A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi20 – 33141; low affinityAdd
BLAST
Calcium bindingi63 – 74122; high affinityAdd
BLAST

GO - Molecular functioni

  1. ATPase binding Source: UniProtKB
  2. calcium ion binding Source: ProtInc
  3. identical protein binding Source: IntAct
  4. protein binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. S100 protein binding Source: UniProtKB

GO - Biological processi

  1. intracellular signal transduction Source: UniProtKB
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. positive regulation of voltage-gated calcium channel activity Source: Ensembl
  4. regulation of heart contraction Source: UniProtKB
  5. substantia nigra development Source: UniProt
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-A1
Alternative name(s):
S-100 protein alpha chain
S-100 protein subunit alpha
S100 calcium-binding protein A1
Gene namesi
Name:S100A1
Synonyms:S100A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10486. S100A1.

Subcellular locationi

GO - Cellular componenti

  1. M band Source: Ensembl
  2. neuron projection Source: Ensembl
  3. nucleus Source: UniProtKB
  4. protein complex Source: UniProtKB
  5. sarcoplasmic reticulum Source: UniProtKB
  6. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34898.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 9493Protein S100-A1PRO_0000143961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861S-nitrosocysteine1 Publication

Keywords - PTMi

S-nitrosylation

Proteomic databases

MaxQBiP23297.
PaxDbiP23297.
PRIDEiP23297.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP23297.
BgeeiP23297.
CleanExiHS_S100A1.
GenevestigatoriP23297.

Organism-specific databases

HPAiCAB002599.
HPA006462.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-743686,EBI-743686
MDM2Q009872EBI-743686,EBI-389668
S100BP042717EBI-743686,EBI-458391
S100PP258157EBI-743686,EBI-743700
TP53P046372EBI-743686,EBI-366083

Protein-protein interaction databases

BioGridi112179. 18 interactions.
IntActiP23297. 8 interactions.
MINTiMINT-1543322.
STRINGi9606.ENSP00000292169.

Structurei

Secondary structure

1
94
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2017
Beta strandi22 – 243
Beta strandi26 – 305
Helixi31 – 4111
Helixi45 – 484
Helixi52 – 6413
Turni65 – 673
Beta strandi68 – 703
Helixi72 – 8716
Turni88 – 903

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP23297.
SMRiP23297. Positions 2-94.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 4836EF-hand 1Add
BLAST
Domaini50 – 8536EF-hand 2Add
BLAST

Sequence similaritiesi

Belongs to the S-100 family.
Contains 2 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG277258.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP23297.
PhylomeDBiP23297.
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.
IPR028486. S100-A1.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PANTHERiPTHR11639:SF66. PTHR11639:SF66. 1 hit.
PfamiPF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P23297-1 [UniParc]FASTAAdd to Basket

« Hide

MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK   50
DVDAVDKVMK ELDENGDGEV DFQEYVVLVA ALTVACNNFF WENS 94
Length:94
Mass (Da):10,546
Last modified:January 23, 2007 - v2
Checksum:iAD5E53AF326B25D2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1047.1.
PIRiA44470. BCHUIA.
RefSeqiNP_006262.1. NM_006271.1.
UniGeneiHs.515715.

Genome annotation databases

EnsembliENST00000292169; ENSP00000292169; ENSG00000160678.
GeneIDi6271.
KEGGihsa:6271.
UCSCiuc001fck.1. human.

Polymorphism databases

DMDMi134136.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1047.1.
PIRi A44470. BCHUIA.
RefSeqi NP_006262.1. NM_006271.1.
UniGenei Hs.515715.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2L0P NMR - A/B 1-94 [» ]
2LHL NMR - A/B 2-94 [» ]
2LLS NMR - A/B 2-94 [» ]
2LLT NMR - A/B 2-94 [» ]
2LLU NMR - A/B 2-94 [» ]
2LP2 NMR - A/B 2-94 [» ]
2LP3 NMR - A/B 2-94 [» ]
2LUX NMR - A/B 2-94 [» ]
2M3W NMR - A/B 2-94 [» ]
ProteinModelPortali P23297.
SMRi P23297. Positions 2-94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112179. 18 interactions.
IntActi P23297. 8 interactions.
MINTi MINT-1543322.
STRINGi 9606.ENSP00000292169.

Chemistry

DrugBanki DB00768. Olopatadine.

Polymorphism databases

DMDMi 134136.

Proteomic databases

MaxQBi P23297.
PaxDbi P23297.
PRIDEi P23297.

Protocols and materials databases

DNASUi 6271.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000292169 ; ENSP00000292169 ; ENSG00000160678 .
GeneIDi 6271.
KEGGi hsa:6271.
UCSCi uc001fck.1. human.

Organism-specific databases

CTDi 6271.
GeneCardsi GC01P153600.
HGNCi HGNC:10486. S100A1.
HPAi CAB002599.
HPA006462.
MIMi 176940. gene.
neXtProti NX_P23297.
PharmGKBi PA34898.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG277258.
HOGENOMi HOG000246968.
HOVERGENi HBG001479.
InParanoidi P23297.
PhylomeDBi P23297.
TreeFami TF332727.

Miscellaneous databases

GeneWikii S100_calcium-binding_protein_A1.
GenomeRNAii 6271.
NextBioi 24339.
PROi P23297.
SOURCEi Search...

Gene expression databases

ArrayExpressi P23297.
Bgeei P23297.
CleanExi HS_S100A1.
Genevestigatori P23297.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. 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 ]
PANTHERi PTHR11639:SF66. PTHR11639:SF66. 1 hit.
Pfami PF00036. EF-hand_1. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiS10A1_HUMAN
AccessioniPrimary (citable) accession number: P23297
Secondary accession number(s): B2R5D9, Q5T7Y3
Entry historyi
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 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

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

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