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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 – 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
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

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. proteinaceous extracellular matrix Source: UniProtKB-KW
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 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.
InParanoidiP02457.

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

« Hide

        10         20         30         40         50
MFSFVDSRLL LLIAATVLLT RGEGEEDIQT GSCVQDGLTY NDKDVWKPEP
60 70 80 90 100
CQICVCDSGN ILCDEVICED TSDCPNAEIP FGECCPICPD VDASPVYPES
110 120 130 140 150
AGVEGPKGDT GPRGDRGLPG PPGRDGIPGQ PGLPGPPGPP GPPGLGGNFA
160 170 180 190 200
PQMSYGYDEK SAGVAVPGPM GPAGPRGLPG PPGAPGPQGF QGPPGEPGEP
210 220 230 240 250
GASGPMGPRG PAGPPGKNGD DGEAGKPGRP GQRGPPGPQG ARGLPGTAGL
260 270 280 290 300
PGMKGHRGFS GLDGAKGQPG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
310 320 330 340 350
RPGPSGPAGA RGNDGAPGAA GPPGPTGPAG PPGFPGAAGA KGETGPQGAR
360 370 380 390 400
GSEGPQGSRG EPGPPGPAGA AGPAGNPGAD GQPGAKGATG APGIAGAPGF
410 420 430 440 450
PGARGPSGPQ GPSGAPGPKG NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG
460 470 480 490 500
PAGEEGKRGA RGEPGPAGLP GPAGERGAPG SRGFPGADGI AGPKGPPGER
510 520 530 540 550
GSPGAVGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ
560 570 580 590 600
DGRPGPAGPP GARGQAGVMG FPGPKGAAGE PGKPGERGAP GPPGAVGAAG
610 620 630 640 650
KDGEAGAQGP PGPTGPAGER GEQGPAGAPG FQGLPGPAGP PGEAGKPGEQ
660 670 680 690 700
GVPGNAGAPG PAGARGERGF PGERGVQGPP GPQGPRGANG APGNDGAKGD
710 720 730 740 750
AGAPGAPGNE GPPGLEGMPG ERGAAGLPGA KGDRGDPGPK GADGAPGKDG
760 770 780 790 800
LRGLTGPIGP PGPAGAPGDK GEAGPPGPAG PTGARGAPGD RGEPGPPGPA
810 820 830 840 850
GFAGPPGADG QPGAKGETGD AGAKGDAGPP GPAGPTGAPG PAGZVGAPGP
860 870 880 890 900
KGARGSAGPP GATGFPGAAG RVGPPGPSGN IGLPGPPGPA GKZGSKGPRG
910 920 930 940 950
ETGPAGRPGE PGPAGPPGPP GEKGSPGADG PIGAPGTPGP QGIAGQRGVV
960 970 980 990 1000
GLPGQRGERG FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE
1010 1020 1030 1040 1050
AGREGAPGAE GAPGRDGAAG PKGDRGETGP AGPPGAPGAP GAPGPVGPAG
1060 1070 1080 1090 1100
KNGDRGETGP AGPAGPPGPA GARGPAGPQG PRGDKGETGE QGDRGMKGHR
1110 1120 1130 1140 1150
GFSGLQGPPG PPGAPGEQGP SGASGPAGPR GPPGSAGAAG KDGLNGLPGP
1160 1170 1180 1190 1200
IGPPGPRGRT GEVGPVGPPG PPGPPGPPGP PSGGFDLSFL PQPPQEKAHD
1210 1220 1230 1240 1250
GGRYYRADDA NVMRDRDLEV DTTLKSLSQQ IENIRSPEGT RKNPARTCRD
1260 1270 1280 1290 1300
LKMCHGDWKS GEYWIDPNQG CNLDAIKVYC NMETGETCVY PTQATIAQKN
1310 1320 1330 1340 1350
WYLSKNPKEK KHVWFGETMS DGFQFEYGGE GSNPADVAIQ LTFLRLMSTE
1360 1370 1380 1390 1400
ATQNVTYHCK NSVAYMDHDT GNLKKALLLQ GANEIEIRAE GNSRFTYGVT
1410 1420 1430 1440 1450
EDGCTSHTGA WGKTVIEYKT TKTSRLPIID LAPMDVGAPD QEFGIDIGPV

CFL
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.
InParanoidi P02457.

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 29, 2014
This is version 102 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