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P06703

- S10A6_HUMAN

UniProt

P06703 - S10A6_HUMAN

Protein

Protein S100-A6

Gene

S100A6

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

    May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi20 – 33141Add
    BLAST
    Calcium bindingi61 – 72122Add
    BLAST

    GO - Molecular functioni

    1. calcium-dependent protein binding Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. ion transmembrane transporter activity Source: Ensembl
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. S100 protein binding Source: UniProtKB
    7. tropomyosin binding Source: UniProtKB
    8. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. axonogenesis Source: UniProtKB
    2. positive regulation of fibroblast proliferation Source: UniProtKB
    3. signal transduction Source: UniProtKB

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein S100-A6
    Alternative name(s):
    Calcyclin
    Growth factor-inducible protein 2A9
    MLN 4
    Prolactin receptor-associated protein
    Short name:
    PRA
    S100 calcium-binding protein A6
    Gene namesi
    Name:S100A6
    Synonyms:CACY
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10496. S100A6.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    5. nuclear envelope Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB
    8. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34908.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9090Protein S100-A6PRO_0000143984Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401N6-acetyllysine1 Publication
    Modified residuei47 – 471N6-acetyllysine; alternateBy similarity
    Modified residuei47 – 471N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP06703.
    PaxDbiP06703.
    PeptideAtlasiP06703.
    PRIDEiP06703.

    2D gel databases

    DOSAC-COBS-2DPAGEP06703.

    PTM databases

    PhosphoSiteiP06703.

    Expressioni

    Inductioni

    Preferentially expressed when quiescent fibroblasts are stimulated to proliferate. It is inducible by growth factors and overexpressed in acute myeloid leukemias.

    Gene expression databases

    BgeeiP06703.
    CleanExiHS_S100A6.
    GenevestigatoriP06703.

    Organism-specific databases

    HPAiCAB002601.
    CAB040549.
    HPA007575.

    Interactioni

    Subunit structurei

    Homodimer; head to tail assembly of 2 subunits. Interacts with CACYBP in a calcium-dependent manner. Interacts with ANXA2 and ANXA11 (via N-terminus). Interacts with SUGT1. Interacts with TP53; has higher affinity for TP53 that is phosphorylated on its N-terminal domain, and lower affinity for TP53 that is phosphorylated on its C-terminal domain. Interacts with tropomyosin. Interacts with FKBP4. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FKBP4Q027903EBI-352877,EBI-1047444
    KPNA2P522923EBI-352877,EBI-349938
    MDM2Q009872EBI-352877,EBI-389668
    PPIDP268823EBI-352877,EBI-6477155From a different organism.
    S100BP042715EBI-352877,EBI-458391

    Protein-protein interaction databases

    BioGridi112185. 19 interactions.
    IntActiP06703. 10 interactions.
    MINTiMINT-3005220.
    STRINGi9606.ENSP00000357708.

    Structurei

    Secondary structure

    1
    90
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 2017
    Beta strandi22 – 243
    Beta strandi28 – 303
    Helixi31 – 4111
    Helixi45 – 473
    Helixi51 – 6212
    Turni63 – 653
    Beta strandi67 – 693
    Helixi70 – 8415
    Helixi86 – 883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K8UX-ray1.15A1-90[»]
    1K96X-ray1.44A1-90[»]
    1K9KX-ray1.76A/B1-90[»]
    1K9PX-ray1.90A1-90[»]
    ProteinModelPortaliP06703.
    SMRiP06703. Positions 2-90.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06703.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 4736EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini48 – 8336EF-hand 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the S-100 family.Curated
    Contains 2 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG40006.
    HOGENOMiHOG000246968.
    HOVERGENiHBG001479.
    InParanoidiP06703.
    OMAiCHLIRIS.
    OrthoDBiEOG78WKVD.
    PhylomeDBiP06703.
    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.
    IPR001751. S100/CaBP-9k_CS.
    IPR013787. S100_Ca-bd_sub.
    [Graphical view]
    PfamiPF01023. 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.

    P06703-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD   50
    AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG 90
    Length:90
    Mass (Da):10,180
    Last modified:January 1, 1988 - v1
    Checksum:i860CBB1416ACBCA1
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti27 – 271H → R.
    Corresponds to variant rs11974 [ dbSNP | Ensembl ].
    VAR_011982
    Natural varianti69 – 691N → S.
    Corresponds to variant rs1802581 [ dbSNP | Ensembl ].
    VAR_011983
    Natural varianti83 – 831I → T.
    Corresponds to variant rs1802582 [ dbSNP | Ensembl ].
    VAR_011984
    Natural varianti90 – 901G → D.
    Corresponds to variant rs2228293 [ dbSNP | Ensembl ].
    VAR_029281

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14300 mRNA. Translation: AAA35886.1.
    J02763 Genomic DNA. Translation: AAA51905.1.
    M18981 mRNA. Translation: AAA51906.1.
    AY034480 Genomic DNA. Translation: AAK59702.1.
    BT006965 mRNA. Translation: AAP35611.1.
    BX470102 Genomic DNA. Translation: CAI14752.1.
    CH471121 Genomic DNA. Translation: EAW53318.1.
    CH471121 Genomic DNA. Translation: EAW53320.1.
    CH471121 Genomic DNA. Translation: EAW53321.1.
    CH471121 Genomic DNA. Translation: EAW53322.1.
    CH471121 Genomic DNA. Translation: EAW53323.1.
    CH471121 Genomic DNA. Translation: EAW53324.1.
    CH471121 Genomic DNA. Translation: EAW53325.1.
    CH471121 Genomic DNA. Translation: EAW53326.1.
    BC001431 mRNA. Translation: AAH01431.1.
    BC009017 mRNA. Translation: AAH09017.1.
    CCDSiCCDS1040.1.
    PIRiA28363. BCHUY.
    RefSeqiNP_055439.1. NM_014624.3.
    UniGeneiHs.275243.

    Genome annotation databases

    EnsembliENST00000368719; ENSP00000357708; ENSG00000197956.
    ENST00000368720; ENSP00000357709; ENSG00000197956.
    ENST00000496817; ENSP00000473589; ENSG00000197956.
    GeneIDi6277.
    KEGGihsa:6277.
    UCSCiuc001fbw.1. human.

    Polymorphism databases

    DMDMi116509.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14300 mRNA. Translation: AAA35886.1 .
    J02763 Genomic DNA. Translation: AAA51905.1 .
    M18981 mRNA. Translation: AAA51906.1 .
    AY034480 Genomic DNA. Translation: AAK59702.1 .
    BT006965 mRNA. Translation: AAP35611.1 .
    BX470102 Genomic DNA. Translation: CAI14752.1 .
    CH471121 Genomic DNA. Translation: EAW53318.1 .
    CH471121 Genomic DNA. Translation: EAW53320.1 .
    CH471121 Genomic DNA. Translation: EAW53321.1 .
    CH471121 Genomic DNA. Translation: EAW53322.1 .
    CH471121 Genomic DNA. Translation: EAW53323.1 .
    CH471121 Genomic DNA. Translation: EAW53324.1 .
    CH471121 Genomic DNA. Translation: EAW53325.1 .
    CH471121 Genomic DNA. Translation: EAW53326.1 .
    BC001431 mRNA. Translation: AAH01431.1 .
    BC009017 mRNA. Translation: AAH09017.1 .
    CCDSi CCDS1040.1.
    PIRi A28363. BCHUY.
    RefSeqi NP_055439.1. NM_014624.3.
    UniGenei Hs.275243.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K8U X-ray 1.15 A 1-90 [» ]
    1K96 X-ray 1.44 A 1-90 [» ]
    1K9K X-ray 1.76 A/B 1-90 [» ]
    1K9P X-ray 1.90 A 1-90 [» ]
    ProteinModelPortali P06703.
    SMRi P06703. Positions 2-90.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112185. 19 interactions.
    IntActi P06703. 10 interactions.
    MINTi MINT-3005220.
    STRINGi 9606.ENSP00000357708.

    PTM databases

    PhosphoSitei P06703.

    Polymorphism databases

    DMDMi 116509.

    2D gel databases

    DOSAC-COBS-2DPAGE P06703.

    Proteomic databases

    MaxQBi P06703.
    PaxDbi P06703.
    PeptideAtlasi P06703.
    PRIDEi P06703.

    Protocols and materials databases

    DNASUi 6277.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368719 ; ENSP00000357708 ; ENSG00000197956 .
    ENST00000368720 ; ENSP00000357709 ; ENSG00000197956 .
    ENST00000496817 ; ENSP00000473589 ; ENSG00000197956 .
    GeneIDi 6277.
    KEGGi hsa:6277.
    UCSCi uc001fbw.1. human.

    Organism-specific databases

    CTDi 6277.
    GeneCardsi GC01M153507.
    HGNCi HGNC:10496. S100A6.
    HPAi CAB002601.
    CAB040549.
    HPA007575.
    MIMi 114110. gene.
    neXtProti NX_P06703.
    PharmGKBi PA34908.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40006.
    HOGENOMi HOG000246968.
    HOVERGENi HBG001479.
    InParanoidi P06703.
    OMAi CHLIRIS.
    OrthoDBi EOG78WKVD.
    PhylomeDBi P06703.
    TreeFami TF332727.

    Miscellaneous databases

    ChiTaRSi S100A6. human.
    EvolutionaryTracei P06703.
    GeneWikii S100A6.
    GenomeRNAii 6277.
    NextBioi 24365.
    PROi P06703.
    SOURCEi Search...

    Gene expression databases

    Bgeei P06703.
    CleanExi HS_S100A6.
    Genevestigatori P06703.

    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.
    IPR001751. S100/CaBP-9k_CS.
    IPR013787. S100_Ca-bd_sub.
    [Graphical view ]
    Pfami 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

    1. "Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein."
      Calabretta B., Battini R., Kaczmarek L., de Riel J.K., Baserga R.
      J. Biol. Chem. 261:12628-12632(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibroblast.
    2. "Structural and functional analysis of a growth-regulated gene, the human calcyclin."
      Ferrari S., Calabretta B., Deriel J.K., Battini R., Ghezzo F., Lauret E., Griffin C., Emanuel B.S., Gurrieri F., Baserga R.
      J. Biol. Chem. 262:8325-8332(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning and characterization of a cDNA encoding a highly conserved, putative calcium binding protein, identified by an anti-prolactin receptor antiserum."
      Murphy L.C., Murphy L.J., Tsuyuki D., Duckworth M.L., Shiu R.P.C.
      J. Biol. Chem. 263:2397-2401(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Cloning of human calcyclin and calcyclin binding protein (CacyBP)."
      Wu J., Liu W., Zhou Y., Zhao Z., Peng X., Yuan J., Qiang B.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 and Placenta.
    9. Cited for: PROTEIN SEQUENCE OF 27-31 AND 48-89.
      Tissue: Platelet.
    10. "Identification of a cell cycle-dependent gene product as a sialic acid-binding protein."
      Gabius H.J., Bardosi A., Gabius S., Hellmann K.P., Karas M., Kratzin H.
      Biochem. Biophys. Res. Commun. 163:506-512(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 57-74.
    11. "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins."
      Nowotny M., Spiechowicz M., Jastrzebska B., Filipek A., Kitagawa K., Kuznicki J.
      J. Biol. Chem. 278:26923-26928(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUGT1.
    12. "Calcium- and cell cycle-dependent association of annexin 11 with the nuclear envelope."
      Tomas A., Moss S.E.
      J. Biol. Chem. 278:20210-20216(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. "S100A6 binds to annexin 2 in pancreatic cancer cells and promotes pancreatic cancer cell motility."
      Nedjadi T., Kitteringham N., Campbell F., Jenkins R.E., Park B.K., Navarro P., Ashcroft F., Tepikin A., Neoptolemos J.P., Costello E.
      Br. J. Cancer 101:1145-1154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANXA2; ANXA11 AND TROPOMYOSIN, SUBCELLULAR LOCATION.
    14. "Posttranslational modifications affect the interaction of S100 proteins with tumor suppressor p53."
      van Dieck J., Teufel D.P., Jaulent A.M., Fernandez-Fernandez M.R., Rutherford T.J., Wyslouch-Cieszynska A., Fersht A.R.
      J. Mol. Biol. 394:922-930(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53.
    15. "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-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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, SUBCELLULAR LOCATION.
    19. "Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution."
      Otterbein L.R., Kordowska J., Witte-Hoffmann C., Wang C.-L.A., Dominguez R.
      Structure 10:557-567(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), SUBUNIT, CALCIUM-BINDING.

    Entry informationi

    Entry nameiS10A6_HUMAN
    AccessioniPrimary (citable) accession number: P06703
    Secondary accession number(s): D3DV39, Q5RHS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 151 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

    Miscellaneous

    This protein co-purified with the prolactin receptor.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3