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P0C2W4

- CO1A2_TYREX

UniProt

P0C2W4 - CO1A2_TYREX

Protein

Collagen alpha-2(I) chain

Gene

COL1A2

Organism
Tyrannosaurus rex (Tyrant lizard king)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Type I collagen is a member of group I collagen (fibrillar forming collagen).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-2(I) chain
    Alternative name(s):
    Alpha-2 type I collagen
    Gene namesi
    Name:COL1A2
    OrganismiTyrannosaurus rex (Tyrant lizard king)
    Taxonomic identifieri436495 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaTyrannosauridaeTyrannosaurus

    Subcellular locationi

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›18›18Collagen alpha-2(I) chainPRO_0000286185Add
    BLAST

    Post-translational modificationi

    Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

    Interactioni

    Subunit structurei

    Trimers of one alpha 2(I) and two alpha 1(I) chains.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.Curated

    Keywords - Domaini

    Collagen, Repeat

    Sequencei

    Sequence statusi: Fragment.

    P0C2W4-1 [UniParc]FASTAAdd to Basket

    « Hide

    GLPGESGAVG PAGPIGSR                                      18
    Length:18
    Mass (Da):1,579
    Last modified:May 1, 2007 - v1
    Checksum:i47D5FA729AE23B19
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei18 – 181

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Protein sequences from Mastodon and Tyrannosaurus rex revealed by mass spectrometry."
      Asara J.M., Schweitzer M.H., Freimark L.M., Phillips M., Cantley L.C.
      Science 316:280-285(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Bone.
    2. Cited for: COMMENTS ON INTERPRETATION OF POTENTIAL HYDROXYLATION SITES.
    3. Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
    4. "Response to comment on 'Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry'."
      Asara J.M., Schweitzer M.H., Cantley L.C., Cottrell J.S.
      Science 319:33-33(2008)
      Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
    5. "Comment on 'Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry'."
      Pevzner P.A., Kim S., Ng J.
      Science 321:1040-1040(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Response to comment on 'Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry'."
      Asara J.M., Schweitzer M.H., Cantley L.C., Cottrell J.S.
      Science 321:1040-1040(2008)
      Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Reanalysis of Tyrannosaurus rex mass spectra."
      Bern M., Phinney B.S., Goldberg D.
      J. Proteome Res. 8:4328-4332(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCO1A2_TYREX
    AccessioniPrimary (citable) accession number: P0C2W4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 18 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    These protein fragments where extracted from a 68-million-year-old fossil. The tryptic peptides required multiple purification steps in order to eliminate contaminants and to increase the concentration of peptidic material.

    Keywords - Technical termi

    Direct protein sequencing, Extinct organism protein

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3