CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001962
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Collagen alpha-1(I) chain 
Protein Synonyms/Alias
 Alpha-1 type I collagen 
Gene Name
 Col1a1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
266FSGLDGAKGDTGPAGacetylation[1]
575VMGFPGPKGTAGEPGglycation[2]
601GAVGPAGKDGEAGAQglycation[2]
646GPPGEAGKPGEQGVPglycation[2]
698APGNDGAKGDTGAPGglycation[2]
748GADGSPGKDGVRGLTacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Nonenzymatic glycation of type I collagen. The effects of aging on preferential glycation sites.
 Reiser KM, Amigable MA, Last JA.
 J Biol Chem. 1992 Dec 5;267(34):24207-16. [PMID: 1447170] 
Functional Description
 Type I collagen is a member of group I collagen (fibrillar forming collagen). 
Sequence Annotation
 DOMAIN 29 87 VWFC.
 DOMAIN 1218 1453 Fibrillar collagen NC1.
 REGION 152 167 Nonhelical region (N-terminal).
 REGION 168 1181 Triple-helical region.
 REGION 1176 1186 Major antigenic determinant (of neutral
 REGION 1182 1207 Nonhelical region (C-terminal).
 MOTIF 734 736 Cell attachment site (Potential).
 MOTIF 1082 1084 Cell attachment site (Potential).
 METAL 1266 1266 Calcium (By similarity).
 METAL 1268 1268 Calcium (By similarity).
 METAL 1269 1269 Calcium; via carbonyl oxygen (By
 METAL 1271 1271 Calcium; via carbonyl oxygen (By
 METAL 1274 1274 Calcium (By similarity).
 MOD_RES 152 152 Pyrrolidone carboxylic acid (Probable).
 MOD_RES 160 160 Allysine.
 MOD_RES 179 179 4-hydroxyproline (Probable).
 MOD_RES 182 182 4-hydroxyproline (Probable).
 MOD_RES 185 185 4-hydroxyproline (Probable).
 MOD_RES 194 194 4-hydroxyproline (Probable).
 MOD_RES 197 197 4-hydroxyproline (Probable).
 MOD_RES 200 200 4-hydroxyproline (Probable).
 MOD_RES 254 254 5-hydroxylysine.
 MOD_RES 575 575 5-hydroxylysine (Probable).
 MOD_RES 698 698 5-hydroxylysine (Probable).
 MOD_RES 1153 1153 3-hydroxyproline (By similarity).
 CARBOHYD 56 56 N-linked (GlcNAc...) (Potential).
 CARBOHYD 254 254 O-linked (Gal...).
 CARBOHYD 1354 1354 N-linked (GlcNAc...) (Potential).
 DISULFID 1248 1280 By similarity.
 DISULFID 1254 1254 Interchain (with C-1271) (By similarity).
 DISULFID 1271 1271 Interchain (with C-1254) (By similarity).
 DISULFID 1288 1451 By similarity.
 DISULFID 1359 1404 By similarity.  
Keyword
 3D-structure; Calcium; Collagen; Complete proteome; Direct protein sequencing; Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding; Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1453 AA 
Protein Sequence
MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPDVCL ICICHNGTAV 60
CDGVLCKEDL DCPNPQKREG ECCPFCPEEY VSPDAEVIGV EGPKGDPGPQ GPRGPVGPPG 120
QDGIPGQPGL PGPPGPPGPP GPPGLGGNFA SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG 180
PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG 240
ARGLPGTAGL PGMKGHRGFS GLDGAKGDTG PAGPKGEPGS PGENGAPGQM GPRGLPGERG 300
RPGPPGSAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAAGA KGEAGPQGAR GSEGPQGVRG 360
EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF PGARGPSGPQ GPSGAPGPKG 420
NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG PAGEEGKRGA RGEPGPSGLP GPPGERGGPG 480
SRGFPGADGV AGPKGPAGER GSPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG 540
KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGVP GPPGAVGPAG 600
KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ GVPGDLGAPG 660
PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD TGAPGAPGSQ GAPGLQGMPG 720
ERGAAGLPGP KGDRGDAGPK GADGSPGKDG VRGLTGPIGP PGPAGAPGDK GETGPSGPAG 780
PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG 840
PIGNVGAPGP KGSRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG 900
ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV GLPGQRGERG 960
FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE SGREGSPGAE GSPGRDGAPG 1020
AKGDRGETGP AGPPGAPGAP GAPGPVGPAG KNGDRGETGP AGPAGPIGPA GARGPAGPQG 1080
PRGDKGETGE QGDRGIKGHR GFSGLQGPPG SPGSPGEQGP SGASGPAGPR GPPGSAGSPG 1140
KDGLNGLPGP IGPPGPRGRT GDSGPAGPPG PPGPPGPPGP PSGGYDFSFL PQPPQEKSQD 1200
GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD LKMCHSDWKS 1260
GEYWIDPNQG CNLDAIKVYC NMETGQTCVF PTQPSVPQKN WYISPNPKEK KHVWFGESMT 1320
DGFQFEYGSE GSDPADVAIQ LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKSLLLQ 1380
GSNEIELRGE GNSRFTYSTL VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD 1440
QEFGMDIGPA CFV 1453 
Gene Ontology
 GO:0005584; C:collagen type I; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:RGD.
 GO:0005201; F:extracellular matrix structural constituent; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0001568; P:blood vessel development; IEA:Compara.
 GO:0060346; P:bone trabecula formation; IEA:Compara.
 GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Compara.
 GO:0071230; P:cellular response to amino acid stimulus; IEA:Compara.
 GO:0071260; P:cellular response to mechanical stimulus; IEA:Compara.
 GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
 GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
 GO:0032964; P:collagen biosynthetic process; IEA:Compara.
 GO:0030199; P:collagen fibril organization; IEA:Compara.
 GO:0048706; P:embryonic skeletal system development; IEA:Compara.
 GO:0001958; P:endochondral ossification; IEA:Compara.
 GO:0060325; P:face morphogenesis; IEA:Compara.
 GO:0001957; P:intramembranous ossification; IEA:Compara.
 GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Compara.
 GO:0001503; P:ossification; IEP:RGD.
 GO:0001649; P:osteoblast differentiation; IEA:Compara.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IEA:Compara.
 GO:0030335; P:positive regulation of cell migration; IEA:Compara.
 GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Compara.
 GO:0070208; P:protein heterotrimerization; IEA:Compara.
 GO:0034504; P:protein localization to nucleus; IEA:Compara.
 GO:0015031; P:protein transport; IEA:Compara.
 GO:0051591; P:response to cAMP; IEP:RGD.
 GO:0031960; P:response to corticosteroid stimulus; IEP:RGD.
 GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
 GO:0009612; P:response to mechanical stimulus; IEP:RGD.
 GO:0007584; P:response to nutrient; IEP:RGD.
 GO:0043434; P:response to peptide hormone stimulus; IEP:RGD.
 GO:0007605; P:sensory perception of sound; IEA:Compara.
 GO:0043589; P:skin morphogenesis; IEA:Compara.
 GO:0034505; P:tooth mineralization; IEA:Compara.
 GO:0007601; P:visual perception; IEA:Compara.
 GO:0042060; P:wound healing; IMP:RGD. 
Interpro
 IPR008160; Collagen.
 IPR000885; Fib_collagen_C.
 IPR001007; VWF_C. 
Pfam
 PF01410; COLFI
 PF01391; Collagen
 PF00093; VWC 
SMART
 SM00038; COLFI
 SM00214; VWC 
PROSITE
 PS51461; NC1_FIB
 PS01208; VWFC_1
 PS50184; VWFC_2 
PRINTS