Variant position: 9 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1487 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human MIRLGAPQ TLVLLT---LLVAAVLRCQGQ-DVQ
Mouse MIRLGAPQ SLVLLT---LLIAAVLRCQGQ
Rat MIRLGAPQ SLVLLT---LLIATVLQCQGQ
Bovine MIRLGAPQ TLVLLT---LLVAAVLRCHGQ
Xenopus laevis MFSFVDSR TLVLFAATQVILLAVVRCQDE
Xenopus tropicalis MFSFVDSR TLVLFAATQVILLAVVRCQDE
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 25
1 – 1219 Missing. In isoform 3.
Nucleotide sequence of the full length cDNA encoding for human type II procollagen.
Su M.W.; Lee B.; Ramirez F.; Machado M.A.; Horton W.A.;
Nucleic Acids Res. 17:9473-9473(1989)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS SER-9 AND LEU-158;
Conservation of the sizes of 53 introns and over 100 intronic sequences for the binding of common transcription factors in the human and mouse genes for type II procollagen (COL2A1).
Ala-Kokko L.; Kvist A.-P.; Metsaranta M.; Kivirikko K.I.; de Crombrugghe B.; Prockop D.J.; Vuorio E.;
Biochem. J. 308:923-929(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2); VARIANT SER-9;
Structure of cDNA clones coding for human type II procollagen. The alpha 1(II) chain is more similar to the alpha 1(I) chain than two other alpha chains of fibrillar collagens.
Baldwin C.T.; Reginato A.M.; Smith C.; Jimenez S.A.; Prockop D.J.;
Biochem. J. 262:521-528(1989)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1229 (ISOFORM 1); VARIANT SER-9;
Organization of the exons coding for pro alpha 1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes.
Su M.W.; Benson-Chanda V.; Vissing H.; Ramirez F.;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236 (ISOFORM 1); VARIANT SER-9;
The human type II procollagen gene: identification of an additional protein-coding domain and location of potential regulatory sequences in the promoter and first intron.
Ryan M.C.; Sieraski M.; Sandell L.J.;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103 (ISOFORM 2); VARIANT SER-9;
A COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in cartilage.
Chan D.; Cole W.G.; Chow C.W.; Mundlos S.; Bateman J.F.;
J. Biol. Chem. 270:1747-1753(1995)
Cited for: VARIANT ACG2 SER-969;
Widely distributed mutations in the COL2A1 gene produce achondrogenesis type II/hypochondrogenesis.
Koerkkoe J.; Cohn D.H.; Ala-Kokko L.; Krakow D.; Prockop D.J.;
Am. J. Med. Genet. 92:95-100(2000)
Cited for: VARIANTS ACG2 VAL-453; ASP-453; ASP-771; ARG-780; ARG-795; GLU-894; ASP-948; SER-981; VAL-1065 AND ARG-1119; VARIANT HYPOCHONDROGENESIS 1017-GLY--VAL-1022 DEL; VARIANT ILE-1331;
Natural variation in four human collagen genes across an ethnically diverse population.
Chan T.F.; Poon A.; Basu A.; Addleman N.R.; Chen J.; Phong A.; Byers P.H.; Klein T.E.; Kwok P.Y.;
Cited for: VARIANTS SER-9; ASP-142; ILE-638; THR-1051; ILE-1331 AND SER-1405;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.