Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02459

- CO2A1_BOVIN

UniProt

P02459 - CO2A1_BOVIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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-endopeptidaseBy similarity
Sitei1241 – 12422Cleavage; by procollagen C-endopeptidaseBy similarity
Metal bindingi1301 – 13011CalciumBy similarity
Metal bindingi1303 – 13031CalciumBy similarity
Metal bindingi1304 – 13041Calcium; via carbonyl oxygenBy similarity
Metal bindingi1306 – 13061Calcium; via carbonyl oxygenBy similarity
Metal bindingi1309 – 13091CalciumBy 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

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

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 – 2525Sequence AnalysisAdd
BLAST
Propeptidei26 – 181156N-terminal propeptideBy similarityPRO_0000401210Add
BLAST
Chaini182 – 14871306Collagen alpha-1(II) chainPRO_0000005725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 19015-hydroxylysineBy similarity
Glycosylationi190 – 1901O-linked (Gal...)By similarity
Modified residuei212 – 2121Hydroxyproline1 Publication
Modified residuei218 – 2181Hydroxyproline1 Publication
Modified residuei230 – 2301Hydroxyproline1 Publication
Modified residuei233 – 2331Hydroxyproline1 Publication
Modified residuei245 – 2451Hydroxyproline1 Publication
Modified residuei248 – 2481Hydroxyproline1 Publication
Modified residuei251 – 2511Hydroxyproline1 Publication
Modified residuei260 – 2601Hydroxyproline1 Publication
Modified residuei269 – 2691Hydroxyproline1 Publication
Modified residuei278 – 2781Hydroxyproline1 Publication
Modified residuei281 – 2811Hydroxyproline1 Publication
Modified residuei284 – 2841Hydroxyproline1 Publication
Modified residuei287 – 28715-hydroxylysine1 Publication
Glycosylationi287 – 2871O-linked (Gal...)1 Publication
Modified residuei293 – 2931Hydroxyproline1 Publication
Modified residuei299 – 29915-hydroxylysine1 Publication
Glycosylationi299 – 2991O-linked (Gal...)1 Publication
Modified residuei305 – 3051Hydroxyproline1 Publication
Modified residuei308 – 30815-hydroxylysine1 Publication
Glycosylationi308 – 3081O-linked (Gal...)1 Publication
Modified residuei314 – 3141Hydroxyproline1 Publication
Modified residuei320 – 3201Hydroxyproline1 Publication
Modified residuei329 – 3291Hydroxyproline2 Publications
Modified residuei350 – 3501Hydroxyproline3 Publications
Modified residuei356 – 3561Hydroxyproline3 Publications
Modified residuei365 – 3651Hydroxyproline1 Publication
Modified residuei368 – 3681Hydroxyproline1 Publication
Modified residuei371 – 3711Hydroxyproline1 Publication
Modified residuei374 – 37415-hydroxylysine1 Publication
Glycosylationi374 – 3741O-linked (Gal...)By similarity
Modified residuei395 – 3951Hydroxyproline1 Publication
Modified residuei398 – 3981Hydroxyproline1 Publication
Modified residuei401 – 4011Hydroxyproline1 Publication
Modified residuei410 – 4101Hydroxyproline1 Publication
Modified residuei416 – 4161Hydroxyproline1 Publication
Modified residuei419 – 41915-hydroxylysine1 Publication
Modified residuei425 – 4251Hydroxyproline1 Publication
Modified residuei431 – 4311Hydroxyproline1 Publication
Modified residuei434 – 4341Hydroxyproline1 Publication
Modified residuei440 – 4401Hydroxyproline1 Publication
Modified residuei452 – 45215-hydroxylysine1 Publication
Modified residuei458 – 4581Hydroxyproline1 Publication
Modified residuei464 – 46415-hydroxylysine1 Publication
Modified residuei470 – 47015-hydroxylysine1 Publication
Modified residuei473 – 4731Hydroxyproline1 Publication
Modified residuei482 – 4821Hydroxyproline1 Publication
Modified residuei497 – 4971Hydroxyproline1 Publication
Modified residuei506 – 5061Hydroxyproline1 Publication
Modified residuei512 – 5121Hydroxyproline1 Publication
Modified residuei518 – 5181Hydroxyproline1 Publication
Modified residuei527 – 52715-hydroxylysine1 Publication
Modified residuei530 – 5301Hydroxyproline1 Publication
Modified residuei542 – 54215-hydroxylysine1 Publication
Modified residuei551 – 5511Hydroxyproline1 Publication
Modified residuei557 – 5571Hydroxyproline1 Publication
Modified residuei566 – 5661Hydroxyproline1 Publication
Modified residuei581 – 5811Hydroxyproline1 Publication
Modified residuei587 – 5871Hydroxyproline1 Publication
Modified residuei590 – 5901Hydroxyproline1 Publication
Modified residuei599 – 5991Hydroxyproline1 Publication
Modified residuei605 – 6051Hydroxyproline1 Publication
Modified residuei608 – 60815-hydroxylysine1 Publication
Glycosylationi608 – 6081O-linked (Gal...)1 Publication
Modified residuei614 – 6141Hydroxyproline1 Publication
Modified residuei620 – 62015-hydroxylysine1 Publication
Glycosylationi620 – 6201O-linked (Gal...)1 Publication
Modified residuei623 – 6231Hydroxyproline1 Publication
Modified residuei626 – 6261Hydroxyproline1 Publication
Modified residuei632 – 6321Hydroxyproline1 Publication
Modified residuei644 – 6441Hydroxyproline1 Publication
Modified residuei659 – 6591Hydroxyproline1 Publication
Modified residuei668 – 6681Hydroxyproline1 Publication
Modified residuei670 – 67013-hydroxyprolineBy similarity
Modified residuei671 – 6711Hydroxyproline1 Publication
Modified residuei674 – 6741Hydroxyproline1 Publication
Modified residuei907 – 90713-hydroxyprolineBy similarity
Modified residuei1130 – 113015-hydroxylysineBy similarity
Glycosylationi1130 – 11301O-linked (Gal...)By similarity
Modified residuei1144 – 114413-hydroxyprolineBy similarity
Modified residuei1186 – 118613-hydroxyprolineBy similarity
Modified residuei1201 – 120113-hydroxyprolineBy similarity
Modified residuei1207 – 120713-hydroxyprolineBy similarity
Modified residuei1213 – 121313-hydroxyprolineBy similarity
Disulfide bondi1283 ↔ 1315PROSITE-ProRule annotation
Disulfide bondi1289 – 1289Interchain (with C-1306)PROSITE-ProRule annotation
Disulfide bondi1306 – 1306Interchain (with C-1289)PROSITE-ProRule annotation
Disulfide bondi1323 ↔ 1485PROSITE-ProRule annotation
Glycosylationi1388 – 13881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1393 ↔ 1438PROSITE-ProRule annotation

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.By similarity4 Publications
O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PRIDEiP02459.

Miscellaneous databases

PMAP-CutDBP02459.

Expressioni

Gene expression databases

ExpressionAtlasiP02459. baseline.

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 – 9059VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1253 – 1487235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP02459.
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

        10         20         30         40         50
MIRLGAPQTL VLLTLLVAAV LRCHGQDVQK AGSCVQDGQR YNDKDVWKPE
60 70 80 90 100
PCRICVCDTG TVLCDDIICE DMKDCLSPET PFGECCPICS ADLPTASGQP
110 120 130 140 150
GPKGQKGEPG DIKDIVGPKG PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG
160 170 180 190 200
RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA AQMAGGFDEK AGGAQMGVMQ
210 220 230 240 250
GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG PRGPPGPPGK
260 270 280 290 300
PGDDGEAGKP GKSGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
310 320 330 340 350
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP
360 370 380 390 400
GPAGPPGPVG PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS
410 420 430 440 450
PGPAGAAGNP GTDGIPGAKG SAGAPGIAGA PGFPGPRGPP GPQGATGPLG
460 470 480 490 500
PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG APGPAGEEGK RGARGEPGGA
510 520 530 540 550
GPAGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG PKGANGDPGR
560 570 580 590 600
PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
610 620 630 640 650
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA
660 670 680 690 700
GERGEQGAPG PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE
710 720 730 740 750
RGFPGERGSP GSQGLQGARG LPGTPGTDGP KGAAGPAGPP GAQGPPGLQG
760 770 780 790 800
MPGERGAAGI AGPKGDRGDV GEKGPEGAPG KDGGRGLTGP IGPPGPAGAN
810 820 830 840 850
GEKGEVGPPG PAGTAGARGA PGERGETGPP GPAGFAGPPG ADGQPGAKGE
860 870 880 890 900
QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
910 920 930 940 950
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGDPGLQGPA
960 970 980 990 1000
GPPGEKGEPG DDGPSGPDGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP
1010 1020 1030 1040 1050
SGEPGKQGAP GASGDRGPPG PVGPPGLTGP AGEPGREGSP GADGPPGRDG
1060 1070 1080 1090 1100
AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG PIGKQGDRGE AGAQGPMGPA
1110 1120 1130 1140 1150
GPAGARGMPG PQGPRGDKGE TGEAGERGLK GHRGFTGLQG LPGPPGPSGD
1160 1170 1180 1190 1200
QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG
1210 1220 1230 1240 1250
PPGNPGPPGP PGPPGPGIDM SAFAGLGQRE KGPDPLQYMR ADEAAGNLRQ
1260 1270 1280 1290 1300
HDAEVDATLK SLNNQIESLR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI
1310 1320 1330 1340 1350
DPNQGCTLDA MKVFCNMETG ETCVYPNPAS VPKKNWWSSK SKDKKHIWFG
1360 1370 1380 1390 1400
ETINGGFHFS YGDDNLAPNT ANVQMTFLRL LSTEGSQNIT YHCKNSIAYL
1410 1420 1430 1440 1450
DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTVLKDGCTK HTGKWGKTMI
1460 1470 1480
EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL
Length:1,487
Mass (Da):141,828
Last modified:November 30, 2010 - v4
Checksum:iF99891F6FD1E47F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021P → V AA sequence (PubMed:782511)Curated
Sequence conflicti380 – 3801T → Q AA sequence (PubMed:2714276)Curated
Sequence conflicti400 – 4001S → A AA sequence (PubMed:2714276)Curated
Sequence conflicti412 – 4121T → A AA sequence (PubMed:2714276)Curated
Sequence conflicti436 – 4361P → A AA sequence (PubMed:2714276)Curated
Sequence conflicti443 – 4431Q → T AA sequence (PubMed:2714276)Curated
Sequence conflicti446 – 4461T → S AA sequence (PubMed:2714276)Curated
Sequence conflicti476 – 4761A → T in AAA30436. (PubMed:7511638)Curated
Sequence conflicti478 – 4781P → V AA sequence (PubMed:2714276)Curated
Sequence conflicti514 – 5141N → S AA sequence (PubMed:2714276)Curated
Sequence conflicti518 – 5181P → S in AAA30436. (PubMed:7511638)Curated
Sequence conflicti523 – 5231L → I AA sequence (PubMed:2714276)Curated
Sequence conflicti529 – 5291A → P AA sequence (PubMed:2714276)Curated
Sequence conflicti535 – 5395PSGLA → SPGAV AA sequence (PubMed:2714276)Curated
Sequence conflicti544 – 5485ANGDP → SPGEA AA sequence (PubMed:2714276)Curated
Sequence conflicti554 – 5541P → A AA sequence (PubMed:2714276)Curated
Sequence conflicti560 – 5601R → K AA sequence (PubMed:2714276)Curated
Sequence conflicti677 – 6771G → P AA sequence (PubMed:4857180)Curated
Sequence conflicti712 – 7121S → A in AAD42347. (PubMed:10479530)Curated
Sequence conflicti718 – 7181A → P in AAD42347. (PubMed:10479530)Curated
Sequence conflicti734 – 7341A → S in AAD42347. (PubMed:10479530)Curated
Sequence conflicti1372 – 13721N → D in CAA26269. (PubMed:2582365)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti349 – 3491Q → L.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 ENSGT00760000118776.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi P02459.
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.

Gene expression databases

ExpressionAtlasi P02459. baseline.

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: October 29, 2014
This is version 127 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