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Protein

Collagen alpha-2(I) chain

Gene

COL1A2

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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaTyrannosauridaeTyrannosaurus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

        10 
GLPGESGAVG PAGPIGSR
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

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

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: February 4, 2015
This is version 21 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.