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P63316

- TNNC1_HUMAN

UniProt

P63316 - TNNC1_HUMAN

Protein

Troponin C, slow skeletal and cardiac muscles

Gene

TNNC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi65 – 76121Add
    BLAST
    Calcium bindingi105 – 116122Add
    BLAST
    Calcium bindingi141 – 152123Add
    BLAST

    GO - Molecular functioni

    1. actin filament binding Source: BHF-UCL
    2. calcium-dependent protein binding Source: UniProtKB
    3. calcium ion binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: BHF-UCL
    6. troponin I binding Source: UniProtKB
    7. troponin T binding Source: UniProtKB

    GO - Biological processi

    1. cardiac muscle contraction Source: BHF-UCL
    2. diaphragm contraction Source: Ensembl
    3. muscle filament sliding Source: Reactome
    4. regulation of ATPase activity Source: BHF-UCL
    5. regulation of muscle contraction Source: UniProtKB
    6. regulation of muscle filament sliding speed Source: BHF-UCL
    7. response to metal ion Source: Ensembl
    8. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_16969. Striated Muscle Contraction.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Troponin C, slow skeletal and cardiac muscles
    Short name:
    TN-C
    Gene namesi
    Name:TNNC1
    Synonyms:TNNC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11943. TNNC1.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. cytosol Source: Reactome
    3. mitochondrion Source: HPA
    4. nucleus Source: HPA
    5. troponin complex Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Cardiomyopathy, dilated 1Z (CMD1Z) [MIM:611879]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti159 – 1591G → R in CMD1Z. 1 Publication
    VAR_043988
    Cardiomyopathy, familial hypertrophic 13 (CMH13) [MIM:613243]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81A → V in CMH13; increases calcium sensitivity of the myofilaments. 1 Publication
    VAR_063070
    Natural varianti29 – 291L → Q in CMH13; impairs protein kinase A dependent signaling from cardiac troponin I to troponin C. 1 Publication
    VAR_019776
    Natural varianti84 – 841C → Y in CMH13; increases calcium sensitivity of the myofilaments. 1 Publication
    VAR_063071
    Natural varianti134 – 1341E → D in CMH13; no changes in calcium sensitivity of the myofilaments. 1 Publication
    VAR_063072
    Natural varianti145 – 1451D → E in CMH13; increases calcium sensitivity of the myofilaments. 1 Publication
    VAR_063073

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation

    Organism-specific databases

    MIMi611879. phenotype.
    613243. phenotype.
    Orphaneti154. Familial isolated dilated cardiomyopathy.
    155. Familial isolated hypertrophic cardiomyopathy.
    PharmGKBiPA36632.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 161161Troponin C, slow skeletal and cardiac musclesPRO_0000073697Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP63316.
    PaxDbiP63316.
    PRIDEiP63316.

    PTM databases

    PhosphoSiteiP63316.

    Expressioni

    Gene expression databases

    ArrayExpressiP63316.
    BgeeiP63316.
    CleanExiHS_TNNC1.
    GenevestigatoriP63316.

    Organism-specific databases

    HPAiCAB002450.
    HPA044848.

    Interactioni

    Protein-protein interaction databases

    BioGridi112988. 13 interactions.
    IntActiP63316. 6 interactions.
    STRINGi9606.ENSP00000232975.

    Structurei

    Secondary structure

    1
    161
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 97
    Helixi14 – 2512
    Turni30 – 323
    Beta strandi35 – 373
    Helixi38 – 4710
    Beta strandi51 – 533
    Helixi54 – 6411
    Beta strandi66 – 683
    Beta strandi71 – 733
    Helixi74 – 8512
    Beta strandi90 – 923
    Helixi94 – 10411
    Beta strandi106 – 1083
    Beta strandi109 – 1135
    Helixi114 – 12310
    Beta strandi124 – 1263
    Helixi130 – 14011
    Beta strandi145 – 1484
    Helixi150 – 1578
    Turni158 – 1603

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AP4NMR-A1-89[»]
    1IH0NMR-A91-161[»]
    1J1DX-ray2.61A/D1-161[»]
    1J1EX-ray3.30A/D1-161[»]
    1LXFNMR-C1-89[»]
    1MXLNMR-C1-89[»]
    1OZSNMR-A90-161[»]
    1SPYNMR-A1-89[»]
    1WRKX-ray2.15A/B1-88[»]
    1WRLX-ray2.60A/B/C/D/E/F1-88[»]
    2JT0NMR-A1-161[»]
    2JT3NMR-A1-161[»]
    2JT8NMR-A1-161[»]
    2JTZNMR-A1-161[»]
    2JXLNMR-A1-89[»]
    2KDHNMR-A91-161[»]
    2KFXNMR-T1-89[»]
    2KGBNMR-C1-89[»]
    2KRDNMR-C1-89[»]
    2L1RNMR-A1-89[»]
    2L98NMR-A91-161[»]
    2MKPNMR-C1-89[»]
    2MLENMR-C91-161[»]
    2MLFNMR-C91-161[»]
    3RV5X-ray2.20A/B/C/D1-89[»]
    3SD6X-ray1.37A1-89[»]
    3SWBX-ray1.67A1-89[»]
    4GJEX-ray1.60A1-89[»]
    4GJFX-ray1.90A1-89[»]
    4GJGX-ray2.00A1-89[»]
    ProteinModelPortaliP63316.
    SMRiP63316. Positions 1-161.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63316.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 5136EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini52 – 8736EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini92 – 12736EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini128 – 16134EF-hand 4PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the troponin C family.Curated
    Contains 4 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5126.
    HOGENOMiHOG000233018.
    HOVERGENiHBG012180.
    InParanoidiP63316.
    KOiK05865.
    OMAiMNDIYKA.
    OrthoDBiEOG76X61W.
    PhylomeDBiP63316.
    TreeFamiTF318191.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 4 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 3 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P63316-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ    50
    NPTPEELQEM IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKSEEELSDL 100
    FRMFDKNADG YIDLDELKIM LQATGETITE DDIEELMKDG DKNNDGRIDY 150
    DEFLEFMKGV E 161
    Length:161
    Mass (Da):18,403
    Last modified:October 11, 2004 - v1
    Checksum:i34DCCC46D503A312
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961Missing in AAB91994. 1 PublicationCurated
    Sequence conflicti115 – 1151D → E AA sequence (PubMed:3951483)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81A → V in CMH13; increases calcium sensitivity of the myofilaments. 1 Publication
    VAR_063070
    Natural varianti29 – 291L → Q in CMH13; impairs protein kinase A dependent signaling from cardiac troponin I to troponin C. 1 Publication
    VAR_019776
    Natural varianti84 – 841C → Y in CMH13; increases calcium sensitivity of the myofilaments. 1 Publication
    VAR_063071
    Natural varianti134 – 1341E → D in CMH13; no changes in calcium sensitivity of the myofilaments. 1 Publication
    VAR_063072
    Natural varianti145 – 1451D → E in CMH13; increases calcium sensitivity of the myofilaments. 1 Publication
    VAR_063073
    Natural varianti159 – 1591G → R in CMD1Z. 1 Publication
    VAR_043988

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07897 mRNA. Translation: CAA30736.1.
    M37984 Genomic DNA. Translation: AAA36772.1.
    AF020769 mRNA. Translation: AAB91994.1.
    BC030244 mRNA. Translation: AAH30244.1.
    CCDSiCCDS2857.1.
    RefSeqiNP_003271.1. NM_003280.2.
    UniGeneiHs.118845.

    Genome annotation databases

    EnsembliENST00000232975; ENSP00000232975; ENSG00000114854.
    GeneIDi7134.
    KEGGihsa:7134.
    UCSCiuc003deb.3. human.

    Polymorphism databases

    DMDMi54042075.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07897 mRNA. Translation: CAA30736.1 .
    M37984 Genomic DNA. Translation: AAA36772.1 .
    AF020769 mRNA. Translation: AAB91994.1 .
    BC030244 mRNA. Translation: AAH30244.1 .
    CCDSi CCDS2857.1.
    RefSeqi NP_003271.1. NM_003280.2.
    UniGenei Hs.118845.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AP4 NMR - A 1-89 [» ]
    1IH0 NMR - A 91-161 [» ]
    1J1D X-ray 2.61 A/D 1-161 [» ]
    1J1E X-ray 3.30 A/D 1-161 [» ]
    1LXF NMR - C 1-89 [» ]
    1MXL NMR - C 1-89 [» ]
    1OZS NMR - A 90-161 [» ]
    1SPY NMR - A 1-89 [» ]
    1WRK X-ray 2.15 A/B 1-88 [» ]
    1WRL X-ray 2.60 A/B/C/D/E/F 1-88 [» ]
    2JT0 NMR - A 1-161 [» ]
    2JT3 NMR - A 1-161 [» ]
    2JT8 NMR - A 1-161 [» ]
    2JTZ NMR - A 1-161 [» ]
    2JXL NMR - A 1-89 [» ]
    2KDH NMR - A 91-161 [» ]
    2KFX NMR - T 1-89 [» ]
    2KGB NMR - C 1-89 [» ]
    2KRD NMR - C 1-89 [» ]
    2L1R NMR - A 1-89 [» ]
    2L98 NMR - A 91-161 [» ]
    2MKP NMR - C 1-89 [» ]
    2MLE NMR - C 91-161 [» ]
    2MLF NMR - C 91-161 [» ]
    3RV5 X-ray 2.20 A/B/C/D 1-89 [» ]
    3SD6 X-ray 1.37 A 1-89 [» ]
    3SWB X-ray 1.67 A 1-89 [» ]
    4GJE X-ray 1.60 A 1-89 [» ]
    4GJF X-ray 1.90 A 1-89 [» ]
    4GJG X-ray 2.00 A 1-89 [» ]
    ProteinModelPortali P63316.
    SMRi P63316. Positions 1-161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112988. 13 interactions.
    IntActi P63316. 6 interactions.
    STRINGi 9606.ENSP00000232975.

    Chemistry

    ChEMBLi CHEMBL2095202.
    DrugBanki DB01244. Bepridil.
    DB01375. Dihydroxyaluminium.
    DB00922. Levosimendan.

    PTM databases

    PhosphoSitei P63316.

    Polymorphism databases

    DMDMi 54042075.

    Proteomic databases

    MaxQBi P63316.
    PaxDbi P63316.
    PRIDEi P63316.

    Protocols and materials databases

    DNASUi 7134.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000232975 ; ENSP00000232975 ; ENSG00000114854 .
    GeneIDi 7134.
    KEGGi hsa:7134.
    UCSCi uc003deb.3. human.

    Organism-specific databases

    CTDi 7134.
    GeneCardsi GC03M052485.
    GeneReviewsi TNNC1.
    HGNCi HGNC:11943. TNNC1.
    HPAi CAB002450.
    HPA044848.
    MIMi 191040. gene.
    611879. phenotype.
    613243. phenotype.
    neXtProti NX_P63316.
    Orphaneti 154. Familial isolated dilated cardiomyopathy.
    155. Familial isolated hypertrophic cardiomyopathy.
    PharmGKBi PA36632.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5126.
    HOGENOMi HOG000233018.
    HOVERGENi HBG012180.
    InParanoidi P63316.
    KOi K05865.
    OMAi MNDIYKA.
    OrthoDBi EOG76X61W.
    PhylomeDBi P63316.
    TreeFami TF318191.

    Enzyme and pathway databases

    Reactomei REACT_16969. Striated Muscle Contraction.

    Miscellaneous databases

    ChiTaRSi TNNC1. human.
    EvolutionaryTracei P63316.
    GeneWikii Troponin_C_type_1.
    GenomeRNAii 7134.
    NextBioi 27913.
    PROi P63316.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63316.
    Bgeei P63316.
    CleanExi HS_TNNC1.
    Genevestigatori P63316.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 4 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 3 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The amino acid sequence of human cardiac troponin-C."
      Roher A., Lieska N., Spitz W.
      Muscle Nerve 9:73-77(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, ACETYLATION AT MET-1.
      Tissue: Heart muscle.
    2. "Differential expression of slow and fast skeletal muscle troponin C. Slow skeletal muscle troponin C is expressed in human fibroblasts."
      Gahlmann R., Wade R., Gunning R., Kedes L.
      J. Mol. Biol. 201:379-391(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Slow skeletal muscle.
    3. "Cloning, structural analysis, and expression of the human slow twitch skeletal muscle/cardiac troponin C gene."
      Schreier T., Kedes L., Gahlmann R.
      J. Biol. Chem. 265:21247-21253(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Slow skeletal muscle.
    4. "H. sapiens mRNA for cardiac ventricular troponin C in idiopathic dilated cardiomyopathy."
      Margossian S.S., Yang F., Umeda P.K., Sciaky D., Anderson P.A.W.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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: Blood.
    6. "Calcium-induced structural transition in the regulatory domain of human cardiac troponin C."
      Spyracopoulos L., Li M.X., Sia S.K., Gagne S.M., Chandra M., Solaro R.J., Sykes B.D.
      Biochemistry 36:12138-12146(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-89.
      Tissue: Heart muscle.
    7. "Structural and functional domains of the troponin complex revealed by limited digestion."
      Takeda S., Kobayashi T., Taniguchi H., Hayashi H., Maeda Y.
      Eur. J. Biochem. 246:611-617(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).
    8. "Structure and dynamics of the C-domain of human cardiac troponin C in complex with the inhibitory region of human cardiac troponin I."
      Lindhout D.A., Sykes B.D.
      J. Biol. Chem. 278:27024-27034(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 89-161.
      Tissue: Heart muscle.
    9. "First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy."
      Hoffmann B., Schmidt-Traub H., Perrot A., Osterziel K.J., Gessner R.
      Hum. Mutat. 17:524-524(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMH13 GLN-29.
    10. "Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy."
      Mogensen J., Murphy R.T., Shaw T., Bahl A., Redwood C., Watkins H., Burke M., Elliott P.M., McKenna W.J.
      J. Am. Coll. Cardiol. 44:2033-2040(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMD1Z ARG-159.
    11. "Cardiac troponin C-L29Q, related to hypertrophic cardiomyopathy, hinders the transduction of the protein kinase A dependent phosphorylation signal from cardiac troponin I to C."
      Schmidtmann A., Lindow C., Villard S., Heuser A., Mugge A., Gessner R., Granier C., Jaquet K.
      FEBS J. 272:6087-6097(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT CMH13 GLN-29.
    12. "Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C."
      Landstrom A.P., Parvatiyar M.S., Pinto J.R., Marquardt M.L., Bos J.M., Tester D.J., Ommen S.R., Potter J.D., Ackerman M.J.
      J. Mol. Cell. Cardiol. 45:281-288(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145, CHARACTERIZATION OF VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145.
    13. "A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy."
      Pinto J.R., Parvatiyar M.S., Jones M.A., Liang J., Ackerman M.J., Potter J.D.
      J. Biol. Chem. 284:19090-19100(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145.

    Entry informationi

    Entry nameiTNNC1_HUMAN
    AccessioniPrimary (citable) accession number: P63316
    Secondary accession number(s): O14800, P02590, P04463
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 111 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

    Cardiac muscle Tn-C can bind 3 calcium ions per molecule. Domain I does not bind calcium.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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