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Q9HCY8

- S10AE_HUMAN

UniProt

Q9HCY8 - S10AE_HUMAN

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Protein

Protein S100-A14

Gene
S100A14, S100A15
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium.3 Publications

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. chemokine receptor binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. calcium ion homeostasis Source: UniProtKB
  3. defense response to bacterium Source: UniProtKB
  4. positive regulation of granulocyte chemotaxis Source: UniProtKB
  5. positive regulation of monocyte chemotaxis Source: UniProtKB
  6. response to lipopolysaccharide Source: UniProtKB
  7. toll-like receptor 4 signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-A14
Alternative name(s):
S100 calcium-binding protein A14
Short name:
S114
Gene namesi
Name:S100A14
Synonyms:S100A15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:18901. S100A14.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134905502.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 104104Protein S100-A14PRO_0000144021Add
BLAST

Proteomic databases

MaxQBiQ9HCY8.
PaxDbiQ9HCY8.
PeptideAtlasiQ9HCY8.
PRIDEiQ9HCY8.

PTM databases

PhosphoSiteiQ9HCY8.

Expressioni

Tissue specificityi

Expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiQ9HCY8.
CleanExiHS_S100A14.
GenevestigatoriQ9HCY8.

Organism-specific databases

HPAiHPA027613.

Interactioni

Subunit structurei

Homodimer. Interacts with AGER.2 Publications

Protein-protein interaction databases

BioGridi121504. 5 interactions.
IntActiQ9HCY8. 3 interactions.
MINTiMINT-5002007.
STRINGi9606.ENSP00000340463.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114
Helixi19 – 3214
Turni34 – 396
Helixi43 – 5311
Turni55 – 573
Helixi60 – 623
Helixi65 – 717
Helixi81 – 9414
Beta strandi98 – 1003

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M0RNMR-A/B1-104[»]
ProteinModelPortaliQ9HCY8.
SMRiQ9HCY8. Positions 1-104.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 6135EF-handAdd
BLAST

Sequence similaritiesi

Belongs to the S-100 family.
Contains 1 EF-hand domain.

Phylogenomic databases

eggNOGiNOG46731.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiQ9HCY8.
OMAiYPARNLA.
OrthoDBiEOG715Q6C.
PhylomeDBiQ9HCY8.
TreeFamiTF332727.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR013787. S100_Ca-bd_sub.
IPR028493. S100A14.
[Graphical view]
PANTHERiPTHR11639:SF4. PTHR11639:SF4. 1 hit.
PfamiPF01023. S_100. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HCY8-1 [UniParc]FASTAAdd to Basket

« Hide

MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV    50
TQQLPHLMPS NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP 100
VRGH 104
Length:104
Mass (Da):11,662
Last modified:March 1, 2001 - v1
Checksum:i97EF31A46B388E79
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY007220 mRNA. Translation: AAG01893.1.
AF426828 Genomic DNA. Translation: AAM19206.1.
BX470102 Genomic DNA. Translation: CAI14759.1.
BC005019 mRNA. Translation: AAH05019.1.
CCDSiCCDS1046.1.
RefSeqiNP_065723.1. NM_020672.2.
XP_005245419.1. XM_005245362.1.
XP_006711531.1. XM_006711468.1.
UniGeneiHs.288998.

Genome annotation databases

EnsembliENST00000344616; ENSP00000340463; ENSG00000189334.
ENST00000368701; ENSP00000357690; ENSG00000189334.
ENST00000368702; ENSP00000357691; ENSG00000189334.
ENST00000476873; ENSP00000420296; ENSG00000189334.
GeneIDi57402.
KEGGihsa:57402.
UCSCiuc001fce.3. human.

Polymorphism databases

DMDMi20178118.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY007220 mRNA. Translation: AAG01893.1 .
AF426828 Genomic DNA. Translation: AAM19206.1 .
BX470102 Genomic DNA. Translation: CAI14759.1 .
BC005019 mRNA. Translation: AAH05019.1 .
CCDSi CCDS1046.1.
RefSeqi NP_065723.1. NM_020672.2.
XP_005245419.1. XM_005245362.1.
XP_006711531.1. XM_006711468.1.
UniGenei Hs.288998.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M0R NMR - A/B 1-104 [» ]
ProteinModelPortali Q9HCY8.
SMRi Q9HCY8. Positions 1-104.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121504. 5 interactions.
IntActi Q9HCY8. 3 interactions.
MINTi MINT-5002007.
STRINGi 9606.ENSP00000340463.

PTM databases

PhosphoSitei Q9HCY8.

Polymorphism databases

DMDMi 20178118.

Proteomic databases

MaxQBi Q9HCY8.
PaxDbi Q9HCY8.
PeptideAtlasi Q9HCY8.
PRIDEi Q9HCY8.

Protocols and materials databases

DNASUi 57402.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344616 ; ENSP00000340463 ; ENSG00000189334 .
ENST00000368701 ; ENSP00000357690 ; ENSG00000189334 .
ENST00000368702 ; ENSP00000357691 ; ENSG00000189334 .
ENST00000476873 ; ENSP00000420296 ; ENSG00000189334 .
GeneIDi 57402.
KEGGi hsa:57402.
UCSCi uc001fce.3. human.

Organism-specific databases

CTDi 57402.
GeneCardsi GC01M153586.
HGNCi HGNC:18901. S100A14.
HPAi HPA027613.
MIMi 607986. gene.
neXtProti NX_Q9HCY8.
PharmGKBi PA134905502.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46731.
HOGENOMi HOG000246968.
HOVERGENi HBG001479.
InParanoidi Q9HCY8.
OMAi YPARNLA.
OrthoDBi EOG715Q6C.
PhylomeDBi Q9HCY8.
TreeFami TF332727.

Miscellaneous databases

ChiTaRSi S100A14. human.
GenomeRNAii 57402.
NextBioi 63504.
PROi Q9HCY8.
SOURCEi Search...

Gene expression databases

Bgeei Q9HCY8.
CleanExi HS_S100A14.
Genevestigatori Q9HCY8.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR013787. S100_Ca-bd_sub.
IPR028493. S100A14.
[Graphical view ]
PANTHERi PTHR11639:SF4. PTHR11639:SF4. 1 hit.
Pfami PF01023. S_100. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of the human S100A14 gene encoding a novel member of the S100 family."
    Pietas A., Schluns K., Marenholz I., Schafer B.W., Heizmann C.W., Petersen I.
    Genomics 79:513-522(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "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].
  3. "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: Pancreas.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "S100A14 stimulates cell proliferation and induces cell apoptosis at different concentrations via receptor for advanced glycation end products (RAGE)."
    Jin Q., Chen H., Luo A., Ding F., Liu Z.
    PLoS ONE 6:E19375-E19375(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AGER.
  6. "Involvement of S100A14 protein in cell invasion by affecting expression and function of matrix metalloproteinase (MMP)-2 via p53-dependent transcriptional regulation."
    Chen H., Yuan Y., Zhang C., Luo A., Ding F., Ma J., Yang S., Tian Y., Tong T., Zhan Q., Liu Z.
    J. Biol. Chem. 287:17109-17119(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "S100A14 inhibits proliferation of oral carcinoma derived cells through G1-arrest."
    Sapkota D., Costea D.E., Blo M., Bruland O., Lorens J.B., Vasstrand E.N., Ibrahim S.O.
    Oral Oncol. 48:219-225(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: STRUCTURE BY NMR, ABSENCE OF CALCIUM BINDING, SUBUNIT.

Entry informationi

Entry nameiS10AE_HUMAN
AccessioniPrimary (citable) accession number: Q9HCY8
Secondary accession number(s): Q5RHT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 109 of the entry and version 1 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

Caution

Part of the residues that are essential for calcium binding are not conserved, resulting in loss of calcium binding at physiological calcium concentrations (1 Publication).

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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