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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 II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces (By similarity).
- SUBUNIT: Homotrimers of alpha 1(II) chains (By similarity).
- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity).
- PTM: Prolines 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.
- SIMILARITY: Contains 1 VWFC domain.
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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: 14 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 1292 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: 3D7835BEF84F9C28 [This is a checksum on the sequence] |
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