CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001960
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1310TQPSVAQKNWYISKNubiquitination[1]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Type I collagen is a member of group I collagen (fibrillar forming collagen). 
Sequence Annotation
 DOMAIN 38 96 VWFC.
 DOMAIN 1229 1464 Fibrillar collagen NC1.
 REGION 162 178 Nonhelical region (N-terminal).
 REGION 179 1192 Triple-helical region.
 REGION 1193 1218 Nonhelical region (C-terminal).
 MOTIF 745 747 Cell attachment site (Potential).
 MOTIF 1093 1095 Cell attachment site (Potential).
 METAL 1277 1277 Calcium (By similarity).
 METAL 1279 1279 Calcium (By similarity).
 METAL 1280 1280 Calcium; via carbonyl oxygen (By
 METAL 1282 1282 Calcium; via carbonyl oxygen (By
 METAL 1285 1285 Calcium (By similarity).
 MOD_RES 162 162 Pyrrolidone carboxylic acid.
 MOD_RES 170 170 Allysine.
 MOD_RES 265 265 5-hydroxylysine.
 MOD_RES 1108 1108 5-hydroxylysine (By similarity).
 MOD_RES 1164 1164 3-hydroxyproline (By similarity).
 MOD_RES 1208 1208 Allysine (By similarity).
 CARBOHYD 265 265 O-linked (Gal...).
 CARBOHYD 1108 1108 O-linked (Gal...) (By similarity).
 CARBOHYD 1365 1365 N-linked (GlcNAc...).
 DISULFID 1259 1291 By similarity.
 DISULFID 1265 1265 Interchain (By similarity).
 DISULFID 1282 1282 Interchain (By similarity).
 DISULFID 1299 1462 By similarity.
 DISULFID 1370 1415 By similarity.  
Keyword
 3D-structure; Calcium; Chromosomal rearrangement; Collagen; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Dwarfism; Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding; Osteogenesis imperfecta; Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1464 AA 
Protein Sequence
MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR DVWKPEPCRI 60
CVCDNGKVLC DDVICDETKN CPGAEVPEGE CCPVCPDGSE SPTDQETTGV EGPKGDTGPR 120
GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGGISVPGP 180
MGPSGPRGLP GPPGAPGPQG FQGPPGEPGE PGASGPMGPR GPPGPPGKNG DDGEAGKPGR 240
PGERGPPGPQ GARGLPGTAG LPGMKGHRGF SGLDGAKGDA GPAGPKGEPG SPGENGAPGQ 300
MGPRGLPGER GRPGAPGPAG ARGNDGATGA AGPPGPTGPA GPPGFPGAVG AKGEAGPQGP 360
RGSEGPQGVR GEPGPPGPAG AAGPAGNPGA DGQPGAKGAN GAPGIAGAPG FPGARGPSGP 420
QGPGGPPGPK GNSGEPGAPG SKGDTGAKGE PGPVGVQGPP GPAGEEGKRG ARGEPGPTGL 480
PGPPGERGGP GSRGFPGADG VAGPKGPAGE RGSPGPAGPK GSPGEAGRPG EAGLPGAKGL 540
TGSPGSPGPD GKTGPPGPAG QDGRPGPPGP PGARGQAGVM GFPGPKGAAG EPGKAGERGV 600
PGPPGAVGPA GKDGEAGAQG PPGPAGPAGE RGEQGPAGSP GFQGLPGPAG PPGEAGKPGE 660
QGVPGDLGAP GPSGARGERG FPGERGVQGP PGPAGPRGAN GAPGNDGAKG DAGAPGAPGS 720
QGAPGLQGMP GERGAAGLPG PKGDRGDAGP KGADGSPGKD GVRGLTGPIG PPGPAGAPGD 780
KGESGPSGPA GPTGARGAPG DRGEPGPPGP AGFAGPPGAD GQPGAKGEPG DAGAKGDAGP 840
PGPAGPAGPP GPIGNVGAPG AKGARGSAGP PGATGFPGAA GRVGPPGPSG NAGPPGPPGP 900
AGKEGGKGPR GETGPAGRPG EVGPPGPPGP AGEKGSPGAD GPAGAPGTPG PQGIAGQRGV 960
VGLPGQRGER GFPGLPGPSG EPGKQGPSGA SGERGPPGPM GPPGLAGPPG ESGREGAPGA 1020
EGSPGRDGSP GAKGDRGETG PAGPPGAPGA PGAPGPVGPA GKSGDRGETG PAGPTGPVGP 1080
VGARGPAGPQ GPRGDKGETG EQGDRGIKGH RGFSGLQGPP GPPGSPGEQG PSGASGPAGP 1140
RGPPGSAGAP GKDGLNGLPG PIGPPGPRGR TGDAGPVGPP GPPGPPGPPG PPSAGFDFSF 1200
LPQPPQEKAH DGGRYYRADD ANVVRDRDLE VDTTLKSLSQ QIENIRSPEG SRKNPARTCR 1260
DLKMCHSDWK SGEYWIDPNQ GCNLDAIKVF CNMETGETCV YPTQPSVAQK NWYISKNPKD 1320
KRHVWFGESM TDGFQFEYGG QGSDPADVAI QLTFLRLMST EASQNITYHC KNSVAYMDQQ 1380
TGNLKKALLL QGSNEIEIRA EGNSRFTYSV TVDGCTSHTG AWGKTVIEYK TTKTSRLPII 1440
DVAPLDVGAP DQEFGFDVGP VCFL 1464 
Gene Ontology
 GO:0005584; C:collagen type I; IMP:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0005615; C:extracellular space; IDA:BHF-UCL.
 GO:0005201; F:extracellular matrix structural constituent; IEA:Compara.
 GO:0042802; F:identical protein binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
 GO:0001568; P:blood vessel development; IMP:UniProtKB.
 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; IEA:Compara.
 GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Compara.
 GO:0032964; P:collagen biosynthetic process; IMP:UniProtKB.
 GO:0030574; P:collagen catabolic process; TAS:Reactome.
 GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
 GO:0048706; P:embryonic skeletal system development; IMP:UniProtKB.
 GO:0001958; P:endochondral ossification; IEA:Compara.
 GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
 GO:0060325; P:face morphogenesis; IEA:Compara.
 GO:0001957; P:intramembranous ossification; IEA:Compara.
 GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Compara.
 GO:0001649; P:osteoblast differentiation; IEA:Compara.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IDA:UniProtKB.
 GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
 GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0070208; P:protein heterotrimerization; IEA:Compara.
 GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
 GO:0015031; P:protein transport; IEA:Compara.
 GO:0051591; P:response to cAMP; IEA:Compara.
 GO:0031960; P:response to corticosteroid stimulus; IEA:Compara.
 GO:0042542; P:response to hydrogen peroxide; IEA:Compara.
 GO:0007584; P:response to nutrient; IEA:Compara.
 GO:0043434; P:response to peptide hormone stimulus; IEA:Compara.
 GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
 GO:0043589; P:skin morphogenesis; IMP:UniProtKB.
 GO:0034505; P:tooth mineralization; IMP:UniProtKB.
 GO:0007601; P:visual perception; IMP:UniProtKB. 
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