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P02459

- CO2A1_BOVIN

UniProt

P02459 - CO2A1_BOVIN

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Protein
Collagen alpha-1(II) chain
Gene
COL2A1
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei181 – 1822Cleavage; by procollagen N-endopeptidase By similarity
Sitei1241 – 12422Cleavage; by procollagen C-endopeptidase By similarity
Metal bindingi1301 – 13011Calcium By similarity
Metal bindingi1303 – 13031Calcium By similarity
Metal bindingi1304 – 13041Calcium; via carbonyl oxygen By similarity
Metal bindingi1306 – 13061Calcium; via carbonyl oxygen By similarity
Metal bindingi1309 – 13091Calcium By similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cartilage condensation Source: Ensembl
  2. cartilage development involved in endochondral bone morphogenesis Source: Ensembl
  3. cellular response to BMP stimulus Source: Ensembl
  4. central nervous system development Source: Ensembl
  5. chondrocyte differentiation Source: Ensembl
  6. collagen fibril organization Source: Ensembl
  7. embryonic skeletal joint morphogenesis Source: Ensembl
  8. endochondral ossification Source: Ensembl
  9. heart morphogenesis Source: Ensembl
  10. inner ear morphogenesis Source: Ensembl
  11. limb bud formation Source: Ensembl
  12. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  13. notochord development Source: Ensembl
  14. otic vesicle development Source: Ensembl
  15. palate development Source: Ensembl
  16. proteoglycan metabolic process Source: Ensembl
  17. regulation of gene expression Source: Ensembl
  18. sensory perception of sound Source: Ensembl
  19. tissue homeostasis Source: Ensembl
  20. visual perception Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_202514. NCAM1 interactions.
REACT_204365. Signaling by PDGF.
REACT_207047. Integrin cell surface interactions.
REACT_215758. Collagen biosynthesis and modifying enzymes.
REACT_219927. Non-integrin membrane-ECM interactions.
REACT_222217. ECM proteoglycans.
REACT_222620. Collagen degradation.
REACT_223425. Extracellular matrix organization.
REACT_226104. Assembly of collagen fibrils and other multimeric structures.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen
Gene namesi
Name:COL2A1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. collagen type II trimer Source: Ensembl
  3. cytoplasm Source: Ensembl
  4. extracellular region Source: Reactome
  5. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed prediction
Add
BLAST
Propeptidei26 – 181156N-terminal propeptide By similarity
PRO_0000401210Add
BLAST
Chaini182 – 14871306Collagen alpha-1(II) chain
PRO_0000005725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 19015-hydroxylysine By similarity
Glycosylationi190 – 1901O-linked (Gal...) By similarity
Modified residuei212 – 2121Hydroxyproline
Modified residuei218 – 2181Hydroxyproline
Modified residuei230 – 2301Hydroxyproline
Modified residuei233 – 2331Hydroxyproline
Modified residuei245 – 2451Hydroxyproline
Modified residuei248 – 2481Hydroxyproline
Modified residuei251 – 2511Hydroxyproline
Modified residuei260 – 2601Hydroxyproline
Modified residuei269 – 2691Hydroxyproline
Modified residuei278 – 2781Hydroxyproline
Modified residuei281 – 2811Hydroxyproline
Modified residuei284 – 2841Hydroxyproline
Modified residuei287 – 28715-hydroxylysine1 Publication
Glycosylationi287 – 2871O-linked (Gal...)1 Publication
Modified residuei293 – 2931Hydroxyproline
Modified residuei299 – 29915-hydroxylysine1 Publication
Glycosylationi299 – 2991O-linked (Gal...)1 Publication
Modified residuei305 – 3051Hydroxyproline
Modified residuei308 – 30815-hydroxylysine1 Publication
Glycosylationi308 – 3081O-linked (Gal...)1 Publication
Modified residuei314 – 3141Hydroxyproline
Modified residuei320 – 3201Hydroxyproline
Modified residuei329 – 3291Hydroxyproline
Modified residuei350 – 3501Hydroxyproline
Modified residuei356 – 3561Hydroxyproline
Modified residuei365 – 3651Hydroxyproline
Modified residuei368 – 3681Hydroxyproline
Modified residuei371 – 3711Hydroxyproline
Modified residuei374 – 37415-hydroxylysine1 Publication
Glycosylationi374 – 3741O-linked (Gal...) By similarity
Modified residuei395 – 3951Hydroxyproline
Modified residuei398 – 3981Hydroxyproline
Modified residuei401 – 4011Hydroxyproline
Modified residuei410 – 4101Hydroxyproline
Modified residuei416 – 4161Hydroxyproline
Modified residuei419 – 41915-hydroxylysine1 Publication
Modified residuei425 – 4251Hydroxyproline
Modified residuei431 – 4311Hydroxyproline
Modified residuei434 – 4341Hydroxyproline
Modified residuei440 – 4401Hydroxyproline
Modified residuei452 – 45215-hydroxylysine1 Publication
Modified residuei458 – 4581Hydroxyproline
Modified residuei464 – 46415-hydroxylysine1 Publication
Modified residuei470 – 47015-hydroxylysine1 Publication
Modified residuei473 – 4731Hydroxyproline
Modified residuei482 – 4821Hydroxyproline
Modified residuei497 – 4971Hydroxyproline
Modified residuei506 – 5061Hydroxyproline
Modified residuei512 – 5121Hydroxyproline
Modified residuei518 – 5181Hydroxyproline
Modified residuei527 – 52715-hydroxylysine1 Publication
Modified residuei530 – 5301Hydroxyproline
Modified residuei542 – 54215-hydroxylysine1 Publication
Modified residuei551 – 5511Hydroxyproline
Modified residuei557 – 5571Hydroxyproline
Modified residuei566 – 5661Hydroxyproline
Modified residuei581 – 5811Hydroxyproline
Modified residuei587 – 5871Hydroxyproline
Modified residuei590 – 5901Hydroxyproline
Modified residuei599 – 5991Hydroxyproline
Modified residuei605 – 6051Hydroxyproline
Modified residuei608 – 60815-hydroxylysine1 Publication
Glycosylationi608 – 6081O-linked (Gal...)1 Publication
Modified residuei614 – 6141Hydroxyproline
Modified residuei620 – 62015-hydroxylysine1 Publication
Glycosylationi620 – 6201O-linked (Gal...)1 Publication
Modified residuei623 – 6231Hydroxyproline
Modified residuei626 – 6261Hydroxyproline
Modified residuei632 – 6321Hydroxyproline
Modified residuei644 – 6441Hydroxyproline
Modified residuei659 – 6591Hydroxyproline
Modified residuei668 – 6681Hydroxyproline
Modified residuei670 – 67013-hydroxyproline By similarity
Modified residuei671 – 6711Hydroxyproline
Modified residuei674 – 6741Hydroxyproline
Modified residuei907 – 90713-hydroxyproline By similarity
Modified residuei1130 – 113015-hydroxylysine By similarity
Glycosylationi1130 – 11301O-linked (Gal...) By similarity
Modified residuei1144 – 114413-hydroxyproline By similarity
Modified residuei1186 – 118613-hydroxyproline By similarity
Modified residuei1201 – 120113-hydroxyproline By similarity
Modified residuei1207 – 120713-hydroxyproline By similarity
Modified residuei1213 – 121313-hydroxyproline By similarity
Disulfide bondi1283 ↔ 1315 By similarity
Disulfide bondi1289 – 1289Interchain (with C-1306) By similarity
Disulfide bondi1306 – 1306Interchain (with C-1289) By similarity
Disulfide bondi1323 ↔ 1485 By similarity
Glycosylationi1388 – 13881N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1393 ↔ 1438 By similarity

Post-translational modificationi

Probably 3-hydroxylated on prolines by LEPREL1 By similarity. Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.
O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PRIDEiP02459.

Miscellaneous databases

PMAP-CutDBP02459.

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.

Protein-protein interaction databases

IntActiP02459. 1 interaction.
STRINGi9913.ENSBTAP00000017505.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 9059VWFC
Add
BLAST
Domaini1253 – 1487235Fibrillar collagen NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 12141014Triple-helical region By similarity
Add
BLAST
Regioni1215 – 124127Nonhelical region (C-terminal) By similarity
Add
BLAST

Domaini

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.

Sequence similaritiesi

Contains 1 VWFC domain.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00740000114967.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiQ9XT25.
KOiK06236.
OMAiPLQYMRA.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 10 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02459-1 [UniParc]FASTAAdd to Basket

« Hide

MIRLGAPQTL VLLTLLVAAV LRCHGQDVQK AGSCVQDGQR YNDKDVWKPE     50
PCRICVCDTG TVLCDDIICE DMKDCLSPET PFGECCPICS ADLPTASGQP 100
GPKGQKGEPG DIKDIVGPKG PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG 150
RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA AQMAGGFDEK AGGAQMGVMQ 200
GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG PRGPPGPPGK 250
PGDDGEAGKP GKSGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG 300
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP 350
GPAGPPGPVG PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS 400
PGPAGAAGNP GTDGIPGAKG SAGAPGIAGA PGFPGPRGPP GPQGATGPLG 450
PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG APGPAGEEGK RGARGEPGGA 500
GPAGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG PKGANGDPGR 550
PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG 600
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA 650
GERGEQGAPG PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE 700
RGFPGERGSP GSQGLQGARG LPGTPGTDGP KGAAGPAGPP GAQGPPGLQG 750
MPGERGAAGI AGPKGDRGDV GEKGPEGAPG KDGGRGLTGP IGPPGPAGAN 800
GEKGEVGPPG PAGTAGARGA PGERGETGPP GPAGFAGPPG ADGQPGAKGE 850
QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG 900
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGDPGLQGPA 950
GPPGEKGEPG DDGPSGPDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP 1000
SGEPGKQGAP GASGDRGPPG PVGPPGLTGP AGEPGREGSP GADGPPGRDG 1050
AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG PIGKQGDRGE AGAQGPMGPA 1100
GPAGARGMPG PQGPRGDKGE TGEAGERGLK GHRGFTGLQG LPGPPGPSGD 1150
QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG 1200
PPGNPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPLQYMR ADEAAGNLRQ 1250
HDAEVDATLK SLNNQIESLR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI 1300
DPNQGCTLDA MKVFCNMETG ETCVYPNPAS VPKKNWWSSK SKDKKHIWFG 1350
ETINGGFHFS YGDDNLAPNT ANVQMTFLRL LSTEGSQNIT YHCKNSIAYL 1400
DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTVLKDGCTK HTGKWGKTMI 1450
EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL 1487
Length:1,487
Mass (Da):141,828
Last modified:November 30, 2010 - v4
Checksum:iF99891F6FD1E47F9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti349 – 3491Q → L.1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021P → V AA sequence 1 Publication
Sequence conflicti380 – 3801T → Q AA sequence 1 Publication
Sequence conflicti400 – 4001S → A AA sequence 1 Publication
Sequence conflicti412 – 4121T → A AA sequence 1 Publication
Sequence conflicti436 – 4361P → A AA sequence 1 Publication
Sequence conflicti443 – 4431Q → T AA sequence 1 Publication
Sequence conflicti446 – 4461T → S AA sequence 1 Publication
Sequence conflicti476 – 4761A → T in AAA30436. 1 Publication
Sequence conflicti478 – 4781P → V AA sequence 1 Publication
Sequence conflicti514 – 5141N → S AA sequence 1 Publication
Sequence conflicti518 – 5181P → S in AAA30436. 1 Publication
Sequence conflicti523 – 5231L → I AA sequence 1 Publication
Sequence conflicti529 – 5291A → P AA sequence 1 Publication
Sequence conflicti535 – 5395PSGLA → SPGAV AA sequence 1 Publication
Sequence conflicti544 – 5485ANGDP → SPGEA AA sequence 1 Publication
Sequence conflicti554 – 5541P → A AA sequence 1 Publication
Sequence conflicti560 – 5601R → K AA sequence 1 Publication
Sequence conflicti677 – 6771G → P AA sequence 1 Publication
Sequence conflicti712 – 7121S → A in AAD42347. 1 Publication
Sequence conflicti718 – 7181A → P in AAD42347. 1 Publication
Sequence conflicti734 – 7341A → S in AAD42347. 1 Publication
Sequence conflicti1372 – 13721N → D in CAA26269. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAFC03017082 Genomic DNA. No translation available.
AAFC03017085 Genomic DNA. No translation available.
AAFC03056593 Genomic DNA. No translation available.
L28918 mRNA. Translation: AAA30436.2.
AF138883 mRNA. Translation: AAD42346.1.
AF138957 mRNA. Translation: AAD42347.1.
X02420 mRNA. Translation: CAA26269.1.
PIRiA90369. CGBO6C.
I45876.
RefSeqiNP_001001135.2. NM_001001135.2.
UniGeneiBt.21390.

Genome annotation databases

EnsembliENSBTAT00000017505; ENSBTAP00000017505; ENSBTAG00000013155.
GeneIDi407142.
KEGGibta:407142.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAFC03017082 Genomic DNA. No translation available.
AAFC03017085 Genomic DNA. No translation available.
AAFC03056593 Genomic DNA. No translation available.
L28918 mRNA. Translation: AAA30436.2 .
AF138883 mRNA. Translation: AAD42346.1 .
AF138957 mRNA. Translation: AAD42347.1 .
X02420 mRNA. Translation: CAA26269.1 .
PIRi A90369. CGBO6C.
I45876.
RefSeqi NP_001001135.2. NM_001001135.2.
UniGenei Bt.21390.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P02459. 1 interaction.
STRINGi 9913.ENSBTAP00000017505.

Proteomic databases

PRIDEi P02459.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000017505 ; ENSBTAP00000017505 ; ENSBTAG00000013155 .
GeneIDi 407142.
KEGGi bta:407142.

Organism-specific databases

CTDi 1280.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00740000114967.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi Q9XT25.
KOi K06236.
OMAi PLQYMRA.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_202514. NCAM1 interactions.
REACT_204365. Signaling by PDGF.
REACT_207047. Integrin cell surface interactions.
REACT_215758. Collagen biosynthesis and modifying enzymes.
REACT_219927. Non-integrin membrane-ECM interactions.
REACT_222217. ECM proteoglycans.
REACT_222620. Collagen degradation.
REACT_223425. Extracellular matrix organization.
REACT_226104. Assembly of collagen fibrils and other multimeric structures.

Miscellaneous databases

NextBioi 20818406.
PMAP-CutDB P02459.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 10 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of taurine cattle: a window to ruminant biology and evolution."
    The bovine genome sequencing and analysis consortium
    Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.
  2. "The covalent structure of cartilage collagen. Amino acid sequence of the NH2-terminal helical portion of the alpha 1 (II) chain."
    Butler W.T., Miller E.J., Finch J.E. Jr.
    Biochemistry 15:3000-3006(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 201-362, HYDROXYLATION AT PRO-212; PRO-218; PRO-230; PRO-233; PRO-245; PRO-248; PRO-251; PRO-260; PRO-269; PRO-278; PRO-281; PRO-284; LYS-287; PRO-293; LYS-299; PRO-305; LYS-308; PRO-314; PRO-320; PRO-329; PRO-350 AND PRO-356, GLYCOSYLATION AT LYS-287; LYS-299 AND LYS-308.
    Tissue: Cartilage.
  3. "The covalent structure of cartilage collagen. Evidence for sequence heterogeneity of bovine alpha1(II) chains."
    Butler W.T., Finch J.E. Jr., Miller E.J.
    J. Biol. Chem. 252:639-643(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 345-359, HYDROXYLATION AT PRO-350 AND PRO-356, VARIANT LEU-349.
    Tissue: Cartilage.
  4. "Covalent structure of collagen. Amino acid sequence of an arthritogenic cyanogen bromide peptide from type II collagen of bovine cartilage."
    Seyer J.M., Hasty K.A., Kang A.H.
    Eur. J. Biochem. 181:159-173(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 324-602, HYDROXYLATION AT PRO-329; PRO-350; PRO-356; PRO-365; PRO-368; PRO-371; LYS-374; PRO-395; PRO-398; PRO-401; PRO-410; PRO-416; LYS-419; PRO-425; PRO-431; PRO-434; PRO-440; LYS-452; PRO-458; LYS-464; LYS-470; PRO-473; PRO-482; PRO-497; PRO-506; PRO-512; PRO-518; LYS-527; PRO-530; LYS-542; PRO-551; PRO-557; PRO-566; PRO-581; PRO-587; PRO-590 AND PRO-599, GLYCOSYLATION AT LYS-374; LYS-419; LYS-452; LYS-464; LYS-470; LYS-527 AND LYS-542.
    Tissue: Cartilage.
  5. "Homologous regions of collagen alpha1(I) and alpha1(II) chains: apparent clustering of variable and invariant amino acid residues."
    Butler W.T., Miller E.J., Finch J.E. Jr., Inagami T.
    Biochem. Biophys. Res. Commun. 57:190-195(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 603-677, HYDROXYLATION AT PRO-605; LYS-608; PRO-614; LYS-620; PRO-623; PRO-626; PRO-632; PRO-644; PRO-659; PRO-668; PRO-671 AND PRO-674, GLYCOSYLATION AT LYS-608 AND LYS-620.
  6. "Characterization of the T cell determinants in the induction of autoimmune arthritis by bovine alpha 1(II)-CB11 in H-2q mice."
    Brand D.D., Myers L.K., Terato K., Whittington K.B., Stuart J.M., Kang A.H., Rosloniec E.F.
    J. Immunol. 152:3088-3097(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 323-602.
    Tissue: Chondrocyte.
  7. "Molecular definition and characterization of recombinant bovine CB8 and CB10: immunogenicity and arthritogenicity."
    Tang B., Chiang T.M., Brand D.D., Gumanovskaya M.L., Stuart J.M., Kang A.H., Myers L.K.
    Clin. Immunol. 92:256-264(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 602-751.
    Tissue: Chondrocyte.
  8. "Analysis of cDNA and genomic clones coding for the pro alpha 1 chain of calf type II collagen."
    Sangiorgi F.O., Benson-Chanda V., de Wet W.J., Sobel M.E., Ramirez F.
    Nucleic Acids Res. 13:2815-2826(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1307-1487.

Entry informationi

Entry nameiCO2A1_BOVIN
AccessioniPrimary (citable) accession number: P02459
Secondary accession number(s): Q28070, Q9XT24, Q9XT25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 30, 2010
Last modified: September 3, 2014
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi