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P0C2W2

- CO1A1_TYREX

UniProt

P0C2W2 - CO1A1_TYREX

Protein

Collagen alpha-1(I) chain

Gene

COL1A1

Organism
Tyrannosaurus rex (Tyrant lizard king)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 21 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(I) chain
    Alternative name(s):
    Alpha-1 type I collagen
    Gene namesi
    Name:COL1A1
    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 – ›570›570Collagen alpha-1(I) chainPRO_0000286177Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 614-hydroxyproline1 Publication
    Modified residuei12 – 1214-hydroxyproline1 Publication
    Modified residuei15 – 1514-hydroxyproline1 Publication
    Modified residuei30 – 3014-hydroxyproline1 Publication
    Modified residuei294 – 29414-hydroxyproline1 Publication
    Modified residuei474 – 47414-hydroxyproline1 Publication
    Modified residuei480 – 48014-hydroxyproline1 Publication
    Modified residuei567 – 56714-hydroxyproline1 Publication

    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.1 Publication

    Keywords - PTMi

    Hydroxylation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP0C2W2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.Curated

    Keywords - Domaini

    Collagen, Repeat

    Sequencei

    Sequence statusi: Fragments.

    P0C2W2-1 [UniParc]FASTAAdd to Basket

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    GATGAPGIAG APGFPGARGA PGPQGPSGAP GPKXXXXXXX XXXXXXXXXX    50
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 100
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 150
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 200
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 250
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGV QGPPGPQGPR 300
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 350
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 400
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 450
    XXXXXXXXXX XXXXXXXXGS AGPPGATGFP GAAGRXXXXX XXXXXXXXXX 500
    XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX 550
    XXXXXXXXXX XGVVGLPGQR 570
    Length:570
    Mass (Da):61,737
    Last modified:November 13, 2007 - v2
    Checksum:iFE4DE139C463BEBF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei570 – 5701

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P0C2W2.
    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, HYDROXYLATION AT PRO-6; PRO-12; PRO-15; PRO-30; PRO-294; PRO-474; PRO-480 AND PRO-567.
      Tissue: Bone.
    2. Asara J.M.
      Submitted (SEP-2007) to UniProtKB
      Cited for: SEQUENCE REVISION TO 27 AND 470.
      Tissue: Bone.
    3. Cited for: COMMENTS ON INTERPRETATION OF POTENTIAL HYDROXYLATION SITES.
    4. Cited for: COMMENTS ON INTERPRETATION OF IDENTIFICATION BY MASS SPECTROMETRY.
    5. "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.
    6. "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.
    7. "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.
    8. "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 nameiCO1A1_TYREX
    AccessioniPrimary (citable) accession number: P0C2W2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 21 of the entry and version 2 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