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P02457

- CO1A1_CHICK

UniProt

P02457 - CO1A1_CHICK

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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

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 – 12661Calcium By similarity
Metal bindingi1268 – 12681Calcium By similarity
Metal bindingi1269 – 12691Calcium; via carbonyl oxygen By similarity
Metal bindingi1271 – 12711Calcium; via carbonyl oxygen By similarity
Metal bindingi1274 – 12741Calcium By similarity

GO - Molecular functioni

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

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Propeptidei23 – 151129N-terminal propeptidePRO_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 – 1601Allysine By 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 ↔ 1280 By similarity
Disulfide bondi1254 – 1254Interchain (with C-1271) By similarity
Disulfide bondi1271 – 1271Interchain (with C-1254) By similarity
Disulfide bondi1288 ↔ 1451 By similarity
Glycosylationi1354 – 13541N-linked (GlcNAc...) By similarity
Disulfide bondi1359 ↔ 1404 By similarity

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.
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.

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 – 8959VWFCAdd
BLAST
Domaini1218 – 1453236Fibrillar collagen NC1Add
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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1441 – 14411Q → H in AAA48671. 1 Publication

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: July 9, 2014
This is version 100 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

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