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P02457

- CO1A1_CHICK

UniProt

P02457 - CO1A1_CHICK

Protein

Collagen alpha-1(I) chain

Gene

COL1A1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (10 Jul 2007)
      Previous versions | rss
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    Functioni

    Type I collagen is a member of group I collagen (fibrillar forming collagen).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1022 – 10221Not glycosylated
    Sitei1085 – 10851Not glycosylated
    Metal bindingi1266 – 12661CalciumBy similarity
    Metal bindingi1268 – 12681CalciumBy similarity
    Metal bindingi1269 – 12691Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1271 – 12711Calcium; via carbonyl oxygenBy similarity
    Metal bindingi1274 – 12741CalciumBy similarity

    GO - Molecular functioni

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

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(I) chain
    Alternative name(s):
    Alpha-1 type I collagen
    Gene namesi
    Name:COL1A1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Propeptidei23 – 151129N-terminal propeptide1 PublicationPRO_0000005716Add
    BLAST
    Chaini152 – 12051054Collagen alpha-1(I) chainPRO_0000005717Add
    BLAST
    Propeptidei1206 – 1453248C-terminal propeptidePRO_0000005718Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei152 – 1521Pyrrolidone carboxylic acid
    Modified residuei160 – 1601AllysineBy similarity
    Modified residuei179 – 17914-hydroxyproline1 Publication
    Modified residuei182 – 18214-hydroxyproline1 Publication
    Modified residuei185 – 18514-hydroxyproline1 Publication
    Modified residuei194 – 19414-hydroxyproline1 Publication
    Modified residuei197 – 19714-hydroxyproline1 Publication
    Modified residuei200 – 20014-hydroxyproline1 Publication
    Modified residuei215 – 21514-hydroxyproline1 Publication
    Modified residuei230 – 23014-hydroxyproline1 Publication
    Modified residuei236 – 23614-hydroxyproline1 Publication
    Modified residuei245 – 24514-hydroxyproline1 Publication
    Modified residuei251 – 25114-hydroxyproline1 Publication
    Modified residuei254 – 25415-hydroxylysine1 Publication
    Glycosylationi254 – 2541O-linked (Gal...); partial1 Publication
    Modified residuei269 – 26914-hydroxyproline1 Publication
    Modified residuei278 – 27814-hydroxyproline1 Publication
    Modified residuei281 – 28114-hydroxyproline1 Publication
    Modified residuei287 – 28714-hydroxyproline1 Publication
    Modified residuei296 – 29614-hydroxyproline1 Publication
    Modified residuei302 – 30214-hydroxyproline1 Publication
    Modified residuei317 – 31714-hydroxyproline1 Publication
    Modified residuei323 – 32314-hydroxyproline1 Publication
    Modified residuei332 – 33214-hydroxyproline1 Publication
    Modified residuei335 – 33514-hydroxyproline1 Publication
    Modified residuei362 – 36214-hydroxyproline1 Publication
    Modified residuei365 – 36514-hydroxyproline1 Publication
    Modified residuei377 – 37714-hydroxyproline1 Publication
    Modified residuei383 – 38314-hydroxyproline1 Publication
    Modified residuei392 – 39214-hydroxyproline1 Publication
    Modified residuei398 – 39814-hydroxyproline1 Publication
    Modified residuei401 – 40114-hydroxyproline1 Publication
    Modified residuei416 – 41614-hydroxyproline1 Publication
    Modified residuei419 – 41915-hydroxylysine1 Publication
    Modified residuei425 – 42514-hydroxyproline1 Publication
    Modified residuei428 – 42814-hydroxyproline1 Publication
    Modified residuei440 – 44014-hydroxyproline1 Publication
    Modified residuei449 – 44914-hydroxyproline1 Publication
    Modified residuei464 – 46414-hydroxyproline1 Publication
    Modified residuei470 – 47014-hydroxyproline1 Publication
    Modified residuei479 – 47914-hydroxyproline1 Publication
    Modified residuei485 – 48514-hydroxyproline1 Publication
    Modified residuei494 – 49415-hydroxylysine1 Publication
    Modified residuei497 – 49714-hydroxyproline1 Publication
    Modified residuei503 – 50314-hydroxyproline1 Publication
    Modified residuei512 – 51214-hydroxyproline1 Publication
    Modified residuei518 – 51814-hydroxyproline1 Publication
    Modified residuei524 – 52414-hydroxyproline1 Publication
    Modified residuei533 – 53314-hydroxyproline1 Publication
    Modified residuei536 – 53614-hydroxyproline1 Publication
    Modified residuei545 – 54514-hydroxyproline1 Publication
    Modified residuei554 – 55414-hydroxyproline1 Publication
    Modified residuei560 – 56014-hydroxyproline1 Publication
    Modified residuei572 – 57214-hydroxyproline1 Publication
    Modified residuei581 – 58114-hydroxyproline1 Publication
    Modified residuei584 – 58414-hydroxyproline1 Publication
    Modified residuei590 – 59014-hydroxyproline1 Publication
    Modified residuei593 – 59314-hydroxyproline1 Publication
    Modified residuei611 – 61114-hydroxyproline1 Publication
    Modified residuei629 – 62914-hydroxyproline1 Publication
    Modified residuei635 – 63514-hydroxyproline1 Publication
    Modified residuei641 – 64114-hydroxyproline1 Publication
    Modified residuei647 – 64714-hydroxyproline1 Publication
    Modified residuei653 – 65314-hydroxyproline1 Publication
    Modified residuei659 – 65914-hydroxyproline1 Publication
    Modified residuei671 – 67114-hydroxyproline1 Publication
    Modified residuei680 – 68014-hydroxyproline1 Publication
    Modified residuei692 – 69214-hydroxyproline1 Publication
    Modified residuei704 – 70414-hydroxyproline1 Publication
    Modified residuei707 – 70714-hydroxyproline1 Publication
    Modified residuei713 – 71314-hydroxyproline1 Publication
    Modified residuei719 – 71914-hydroxyproline1 Publication
    Modified residuei728 – 72814-hydroxyproline1 Publication
    Modified residuei737 – 73714-hydroxyproline1 Publication
    Modified residuei740 – 74015-hydroxylysine1 Publication
    Modified residuei746 – 74614-hydroxyproline1 Publication
    Modified residuei761 – 76114-hydroxyproline1 Publication
    Modified residuei767 – 76714-hydroxyproline1 Publication
    Modified residuei776 – 77614-hydroxyproline1 Publication
    Modified residuei788 – 78814-hydroxyproline1 Publication
    Modified residuei794 – 79414-hydroxyproline1 Publication
    Modified residuei797 – 79714-hydroxyproline1 Publication
    Modified residuei806 – 80614-hydroxyproline1 Publication
    Modified residuei812 – 81214-hydroxyproline1 Publication
    Modified residuei830 – 83014-hydroxyproline1 Publication
    Modified residuei839 – 83914-hydroxyproline1 Publication
    Modified residuei848 – 84814-hydroxyproline1 Publication
    Modified residuei851 – 85115-hydroxylysine1 Publication
    Modified residuei860 – 86014-hydroxyproline1 Publication
    Modified residuei866 – 86614-hydroxyproline1 Publication
    Modified residuei875 – 87514-hydroxyproline1 Publication
    Modified residuei884 – 88414-hydroxyproline1 Publication
    Modified residuei887 – 88714-hydroxyproline1 Publication
    Modified residuei908 – 90814-hydroxyproline1 Publication
    Modified residuei911 – 91114-hydroxyproline1 Publication
    Modified residuei917 – 91714-hydroxyproline1 Publication
    Modified residuei920 – 92014-hydroxyproline1 Publication
    Modified residuei926 – 92614-hydroxyproline1 Publication
    Modified residuei935 – 93514-hydroxyproline1 Publication
    Modified residuei953 – 95314-hydroxyproline1 Publication
    Modified residuei962 – 96214-hydroxyproline1 Publication
    Modified residuei965 – 96514-hydroxyproline1 Publication
    Modified residuei971 – 97114-hydroxyproline1 Publication
    Modified residuei986 – 98614-hydroxyproline1 Publication
    Modified residuei992 – 99214-hydroxyproline1 Publication
    Modified residuei998 – 99814-hydroxyproline1 Publication
    Modified residuei1007 – 100714-hydroxyproline1 Publication
    Modified residuei1013 – 101314-hydroxyproline1 Publication
    Modified residuei1022 – 102215-hydroxylysine; partial1 Publication
    Modified residuei1034 – 103414-hydroxyproline1 Publication
    Modified residuei1037 – 103714-hydroxyproline1 Publication
    Modified residuei1040 – 104014-hydroxyproline1 Publication
    Modified residuei1067 – 106714-hydroxyproline1 Publication
    Modified residuei1085 – 108515-hydroxylysine; partial1 Publication
    Modified residuei1097 – 109715-hydroxylysine1 Publication
    Glycosylationi1097 – 10971O-linked (Gal...); partial1 Publication
    Modified residuei1109 – 110914-hydroxyproline1 Publication
    Modified residuei1112 – 111214-hydroxyproline1 Publication
    Modified residuei1115 – 111514-hydroxyproline1 Publication
    Modified residuei1133 – 113314-hydroxyproline1 Publication
    Modified residuei1148 – 114814-hydroxyproline1 Publication
    Modified residuei1153 – 115313-hydroxyproline1 Publication
    Modified residuei1154 – 115414-hydroxyproline1 Publication
    Modified residuei1169 – 116914-hydroxyproline1 Publication
    Modified residuei1172 – 117214-hydroxyproline1 Publication
    Modified residuei1175 – 117514-hydroxyproline1 Publication
    Modified residuei1178 – 117814-hydroxyproline1 Publication
    Disulfide bondi1248 ↔ 1280PROSITE-ProRule annotation
    Disulfide bondi1254 – 1254Interchain (with C-1271)PROSITE-ProRule annotation
    Disulfide bondi1271 – 1271Interchain (with C-1254)PROSITE-ProRule annotation
    Disulfide bondi1288 ↔ 1451PROSITE-ProRule annotation
    Glycosylationi1354 – 13541N-linked (GlcNAc...)By similarity
    Disulfide bondi1359 ↔ 1404PROSITE-ProRule annotation

    Post-translational modificationi

    Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are 4-hydroxylated in some or all of the chains. Pro-1153 is the only 3-hydroxyproline and the only hydroxylated proline in position X.1 Publication
    Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
    O-linked glycans consist of Glc-Gal disaccharide bound to the hydroxyl group of 5-hydroxylysine.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

    Proteomic databases

    PRIDEiP02457.

    Expressioni

    Tissue specificityi

    Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

    Interactioni

    Subunit structurei

    Trimers of one alpha 2(I) and two alpha 1(I) chains.

    Protein-protein interaction databases

    IntActiP02457. 1 interaction.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 8959VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1218 – 1453236Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    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

    HOVERGENiHBG004933.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 12 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.

    P02457-1 [UniParc]FASTAAdd to Basket

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    MFSFVDSRLL LLIAATVLLT RGEGEEDIQT GSCVQDGLTY NDKDVWKPEP     50
    CQICVCDSGN ILCDEVICED TSDCPNAEIP FGECCPICPD VDASPVYPES 100
    AGVEGPKGDT GPRGDRGLPG PPGRDGIPGQ PGLPGPPGPP GPPGLGGNFA 150
    PQMSYGYDEK SAGVAVPGPM GPAGPRGLPG PPGAPGPQGF QGPPGEPGEP 200
    GASGPMGPRG PAGPPGKNGD DGEAGKPGRP GQRGPPGPQG ARGLPGTAGL 250
    PGMKGHRGFS GLDGAKGQPG PAGPKGEPGS PGENGAPGQM GPRGLPGERG 300
    RPGPSGPAGA RGNDGAPGAA GPPGPTGPAG PPGFPGAAGA KGETGPQGAR 350
    GSEGPQGSRG EPGPPGPAGA AGPAGNPGAD GQPGAKGATG APGIAGAPGF 400
    PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG 450
    PAGEEGKRGA RGEPGPAGLP GPAGERGAPG SRGFPGADGI AGPKGPPGER 500
    GSPGAVGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ 550
    DGRPGPAGPP GARGQAGVMG FPGPKGAAGE PGKPGERGAP GPPGAVGAAG 600
    KDGEAGAQGP PGPTGPAGER GEQGPAGAPG FQGLPGPAGP PGEAGKPGEQ 650
    GVPGNAGAPG PAGARGERGF PGERGVQGPP GPQGPRGANG APGNDGAKGD 700
    AGAPGAPGNE GPPGLEGMPG ERGAAGLPGA KGDRGDPGPK GADGAPGKDG 750
    LRGLTGPIGP PGPAGAPGDK GEAGPPGPAG PTGARGAPGD RGEPGPPGPA 800
    GFAGPPGADG QPGAKGETGD AGAKGDAGPP GPAGPTGAPG PAGZVGAPGP 850
    KGARGSAGPP GATGFPGAAG RVGPPGPSGN IGLPGPPGPA GKZGSKGPRG 900
    ETGPAGRPGE PGPAGPPGPP GEKGSPGADG PIGAPGTPGP QGIAGQRGVV 950
    GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE 1000
    AGREGAPGAE GAPGRDGAAG PKGDRGETGP AGPPGAPGAP GAPGPVGPAG 1050
    KNGDRGETGP AGPAGPPGPA GARGPAGPQG PRGDKGETGE QGDRGMKGHR 1100
    GFSGLQGPPG PPGAPGEQGP SGASGPAGPR GPPGSAGAAG KDGLNGLPGP 1150
    IGPPGPRGRT GEVGPVGPPG PPGPPGPPGP PSGGFDLSFL PQPPQEKAHD 1200
    GGRYYRADDA NVMRDRDLEV DTTLKSLSQQ IENIRSPEGT RKNPARTCRD 1250
    LKMCHGDWKS GEYWIDPNQG CNLDAIKVYC NMETGETCVY PTQATIAQKN 1300
    WYLSKNPKEK KHVWFGETMS DGFQFEYGGE GSNPADVAIQ LTFLRLMSTE 1350
    ATQNVTYHCK NSVAYMDHDT GNLKKALLLQ GANEIEIRAE GNSRFTYGVT 1400
    EDGCTSHTGA WGKTVIEYKT TKTSRLPIID LAPMDVGAPD QEFGIDIGPV 1450
    CFL 1453
    Length:1,453
    Mass (Da):137,755
    Last modified:July 10, 2007 - v3
    Checksum:i61C617239E271A82
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1441 – 14411Q → H in AAA48671. (PubMed:6987088)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17839, M17838 Genomic DNA. Translation: AAA48704.1.
    V00401 mRNA. Translation: CAA23695.1.
    M10571 mRNA. Translation: AAA48671.1. Sequence problems.
    M17607 mRNA. Translation: AAA48672.1.
    PIRiA27179.
    A90458. CGCH1S.
    I50629.
    S07234.
    UniGeneiGga.2073.
    Gga.43371.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17839 , M17838 Genomic DNA. Translation: AAA48704.1 .
    V00401 mRNA. Translation: CAA23695.1 .
    M10571 mRNA. Translation: AAA48671.1 . Sequence problems.
    M17607 mRNA. Translation: AAA48672.1 .
    PIRi A27179.
    A90458. CGCH1S.
    I50629.
    S07234.
    UniGenei Gga.2073.
    Gga.43371.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P02457. 1 interaction.

    Proteomic databases

    PRIDEi P02457.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG004933.

    Miscellaneous databases

    PROi P02457.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 12 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. "Construction and characterization of cDNA clones encoding the 5' end of the chicken pro alpha 1(I) collagen mRNA."
      Finer M.H., Boedtker H., Doty P.
      Gene 56:71-78(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
    2. "Unusual DNA sequences located within the promoter region and the first intron of the chicken pro-alpha 1(I) collagen gene."
      Finer M.H., Aho S., Gerstenfeld L.C., Boedtker H., Doty P.
      J. Biol. Chem. 262:13323-13332(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-144.
    3. "Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skicollagen."
      Kang A.H., Gross J.
      Biochemistry 9:796-804(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 152-206, HYDROXYLATION AT PRO-179; PRO-182; PRO-185; PRO-194; PRO-197 AND PRO-200.
    4. "The covalent structure of collagen. Amino acid sequence of alpha1-CB5 glycopeptide and alpha1-CB4 from chick skin collagen."
      Kang A.H., Dixit S.N., Corbett C., Gross J.
      J. Biol. Chem. 250:7428-7434(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 207-290, HYDROXYLATION AT PRO-215; PRO-230; PRO-236; PRO-245; PRO-251; LYS-254; PRO-269; PRO-278; PRO-281 AND PRO-287, GLYCOSYLATION AT LYS-254.
    5. "Amino acid sequence of chick skin collagen alpha 1(I)-CB8 and the complete primary structure of the helical portion of the chick skin collagen alpha 1(I) chain."
      Highberger J.H., Corbett C., Dixit S.N., Yu W., Seyer J.M., Kang A.H., Gross J.
      Biochemistry 21:2048-2055(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 291-569, HYDROXYLATION AT PRO-296; PRO-302; PRO-317; PRO-323; PRO-332; PRO-335; PRO-362; PRO-365; PRO-377; PRO-383; PRO-392; PRO-398; PRO-401; PRO-416; LYS-419; PRO-425; PRO-428; PRO-440; PRO-449; PRO-464; PRO-470; PRO-479; PRO-485; LYS-494; PRO-497; PRO-503; PRO-512; PRO-518; PRO-524; PRO-533; PRO-536; PRO-545; PRO-554 AND PRO-560.
    6. "Covalent structure of collagen: amino acid sequence of alpha1-CB3 of chick skin collagen."
      Dixit S.N., Kang A.H., Gross J.
      Biochemistry 14:1929-1933(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 570-718, HYDROXYLATION AT PRO-572; PRO-581; PRO-584; PRO-590; PRO-593; PRO-611; PRO-629; PRO-635; PRO-641; PRO-647; PRO-653; PRO-659; PRO-671; PRO-680; PRO-692; PRO-704; PRO-707 AND PRO-713.
    7. "The amino acid sequence of chick skin collagen alpha1-CB7."
      Highberger J.H., Corbett C., Kang A.H., Gross J.
      Biochemistry 14:2872-2881(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 719-989, HYDROXYLATION AT PRO-719; PRO-728; PRO-737; LYS-740; PRO-746; PRO-761; PRO-767; PRO-776; PRO-788; PRO-794; PRO-797; PRO-806; PRO-812; PRO-830; PRO-839; PRO-848; LYS-851; PRO-860; PRO-866; PRO-875; PRO-884; PRO-887; PRO-908; PRO-911; PRO-917; PRO-920; PRO-926; PRO-935; PRO-953; PRO-962; PRO-965; PRO-971 AND PRO-986.
    8. "Covalent structure of collagen: amino acid sequence of alpha1-CB6A of chick skin collagen."
      Dixit S.N., Seyer J.M., Oronsky A.O., Corbett C., Kang A.H., Gross J.
      Biochemistry 14:1933-1938(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 990-1096, HYDROXYLATION AT PRO-992; PRO-998; PRO-1007; PRO-1013; LYS-1022; PRO-1034; PRO-1037; PRO-1040; PRO-1067 AND LYS-1085, ABSENCE OF GLYCOSYLATION AT LYS-1022 AND LYS-1085.
    9. "Covalent structure of collagen: amino acid sequence of chick skin collagen alpha1(1)-CB6B."
      Dixit S.N., Seyer J.M., Kang A.H., Gross J.
      Biochemistry 17:5719-5722(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1097-1187, HYDROXYLATION AT LYS-1097; PRO-1109; PRO-1112; PRO-1115; PRO-1133; PRO-1148; PRO-1153; PRO-1154; PRO-1169; PRO-1172; PRO-1175 AND PRO-1178, GLYCOSYLATION AT LYS-1097.
    10. "Evidence for a previously undetected sequence at the carboxyterminus of the alpha 1 chain of chicken bone collagen."
      Eyre D.R., Glimcher M.J.
      Biochem. Biophys. Res. Commun. 48:720-726(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1200-1205.
    11. "Sequence determination and analysis of the 3' region of chicken pro-alpha 1(I) and pro-alpha 2(I) collagen messenger ribonucleic acids including the carboxy-terminal propeptide sequences."
      Fuller F., Boedtker H.
      Biochemistry 20:996-1006(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 981-1453.
    12. "Nucleotide sequence of a collagen cDNA-fragment coding for the carboxyl end of pro alpha 1(I)-chains."
      Showalter A.M., Pesciotta D.M., Eikenberry E.F., Yamamoto T., Pastan I., Decrombrugghe B., Fietzek P.P., Olsen B.R.
      FEBS Lett. 111:61-65(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1453.

    Entry informationi

    Entry nameiCO1A1_CHICK
    AccessioniPrimary (citable) accession number: P02457
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 101 of the entry and version 3 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