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P0C2W2

- CO1A1_TYREX

UniProt

P0C2W2 - CO1A1_TYREX

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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

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-KW
Complete GO annotation...

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

« Hide

        10         20         30         40         50
GATGAPGIAG APGFPGARGA PGPQGPSGAP GPKXXXXXXX XXXXXXXXXX
60 70 80 90 100
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
110 120 130 140 150
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
160 170 180 190 200
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
210 220 230 240 250
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
260 270 280 290 300
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXGV QGPPGPQGPR
310 320 330 340 350
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
360 370 380 390 400
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
410 420 430 440 450
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
460 470 480 490 500
XXXXXXXXXX XXXXXXXXGS AGPPGATGFP GAAGRXXXXX XXXXXXXXXX
510 520 530 540 550
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
560 570
XXXXXXXXXX XGVVGLPGQR
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 29, 2014
This is version 22 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