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[1]
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PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
TISSUE=Bone;
DOI=10.1126/science.1137614; PubMed=17431180 [NCBI, ExPASy, EBI, Israel, Japan]
Asara J.M.,
Schweitzer M.H.,
Freimark L.M.,
Phillips M.,
Cantley L.C.;
"Protein sequences from Mastodon and Tyrannosaurus rex revealed by mass spectrometry.";
Science 316:280-285(2007).
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[2]
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COMMENTS ON INTERPRETATION OF POTENTIAL HYDROXYLATION SITES.
DOI=10.1126/science.317.5843.1324; PubMed=17823333 [NCBI, ExPASy, EBI, Israel, Japan]
Asara J.M.,
Garavelli J.S.,
Slatter D.A.,
Schweitzer M.H.,
Freimark L.M.,
Phillips M.,
Cantley L.C.;
"Interpreting sequences from mastodon and T. rex.";
Science 317:1324-1325(2007).
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- FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains (By similarity).
- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity).
- PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains (By similarity).
- MISCELLANEOUS: These protein fragments where extracted from a 68 millions years old fossil. The tryptic peptides required multiple purification steps in order to eliminate contaminants and to increase the concentration of peptidic material.
- SIMILARITY: Belongs to the fibrillar collagen family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 18 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 1579 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: 47D5FA729AE23B19 [This is a checksum on the sequence] |
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