Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P02459

- CO2A1_BOVIN

UniProt

P02459 - CO2A1_BOVIN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 4 (30 Nov 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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.

    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.
    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

    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 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

    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 1, 2014
    This is version 126 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