CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004906
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Collagen alpha-1(V) chain 
Protein Synonyms/Alias
  
Gene Name
 COL5A1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1391GPSGPPGKRGPPGPAubiquitination[1]
1686TCVFPDKKSEGARITacetylation[2]
1697ARITSWPKENPGSWFacetylation[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. 
Sequence Annotation
 DOMAIN 72 244 Laminin G-like.
 DOMAIN 1609 1837 Fibrillar collagen NC1.
 REGION 231 443 Nonhelical region.
 REGION 444 558 Interrupted collagenous region.
 REGION 559 1570 Triple-helical region.
 REGION 1571 1605 Nonhelical region.
 METAL 1657 1657 Calcium (By similarity).
 METAL 1659 1659 Calcium (By similarity).
 METAL 1660 1660 Calcium; via carbonyl oxygen (By
 METAL 1662 1662 Calcium; via carbonyl oxygen (By
 METAL 1665 1665 Calcium (By similarity).
 MOD_RES 234 234 Sulfotyrosine (Potential).
 MOD_RES 236 236 Sulfotyrosine (Potential).
 MOD_RES 240 240 Sulfotyrosine (Potential).
 MOD_RES 262 262 Sulfotyrosine (Potential).
 MOD_RES 263 263 Sulfotyrosine (Potential).
 MOD_RES 338 338 Sulfotyrosine (Potential).
 MOD_RES 340 340 Sulfotyrosine (Potential).
 MOD_RES 346 346 Sulfotyrosine (Potential).
 MOD_RES 347 347 Sulfotyrosine (Potential).
 MOD_RES 416 416 Sulfotyrosine (Potential).
 MOD_RES 417 417 Sulfotyrosine (Potential).
 MOD_RES 420 420 Sulfotyrosine (Potential).
 MOD_RES 421 421 Sulfotyrosine (Potential).
 MOD_RES 570 570 Hydroxyproline.
 MOD_RES 576 576 Hydroxyproline.
 MOD_RES 621 621 Hydroxyproline.
 MOD_RES 627 627 5-hydroxylysine.
 MOD_RES 639 639 Hydroxyproline.
 MOD_RES 642 642 5-hydroxylysine.
 MOD_RES 648 648 Hydroxyproline.
 MOD_RES 654 654 Hydroxyproline.
 MOD_RES 657 657 Hydroxyproline.
 MOD_RES 675 675 Hydroxyproline.
 MOD_RES 678 678 Hydroxyproline.
 MOD_RES 680 680 Hydroxyproline.
 MOD_RES 686 686 Hydroxyproline.
 MOD_RES 690 690 Hydroxyproline.
 MOD_RES 696 696 Hydroxyproline.
 MOD_RES 705 705 Hydroxyproline.
 MOD_RES 708 708 5-hydroxylysine.
 MOD_RES 717 717 Hydroxyproline.
 MOD_RES 720 720 Hydroxyproline.
 MOD_RES 726 726 Hydroxyproline.
 MOD_RES 732 732 Hydroxyproline.
 MOD_RES 744 744 5-hydroxylysine.
 MOD_RES 750 750 Hydroxyproline.
 MOD_RES 756 756 Hydroxyproline.
 MOD_RES 762 762 Hydroxyproline.
 MOD_RES 765 765 Hydroxyproline.
 MOD_RES 771 771 Hydroxyproline.
 MOD_RES 774 774 5-hydroxylysine.
 MOD_RES 780 780 Hydroxyproline.
 MOD_RES 789 789 Hydroxyproline.
 MOD_RES 795 795 5-hydroxylysine.
 MOD_RES 804 804 5-hydroxylysine.
 MOD_RES 807 807 5-hydroxylysine.
 MOD_RES 810 810 5-hydroxylysine.
 MOD_RES 816 816 Hydroxyproline.
 MOD_RES 819 819 5-hydroxylysine.
 MOD_RES 834 834 Hydroxyproline.
 MOD_RES 846 846 5-hydroxylysine.
 MOD_RES 861 861 Hydroxyproline.
 MOD_RES 864 864 5-hydroxylysine.
 MOD_RES 870 870 Hydroxyproline.
 MOD_RES 873 873 Hydroxyproline.
 MOD_RES 876 876 Hydroxyproline.
 MOD_RES 882 882 5-hydroxylysine.
 MOD_RES 888 888 Hydroxyproline.
 MOD_RES 891 891 Hydroxyproline.
 MOD_RES 897 897 5-hydroxylysine.
 MOD_RES 903 903 Hydroxyproline.
 MOD_RES 906 906 Hydroxyproline.
 MOD_RES 930 930 Hydroxyproline.
 MOD_RES 945 945 Hydroxyproline.
 MOD_RES 1017 1017 Hydroxyproline.
 MOD_RES 1020 1020 Hydroxyproline.
 MOD_RES 1023 1023 Hydroxyproline.
 MOD_RES 1029 1029 Hydroxyproline.
 MOD_RES 1221 1221 Hydroxyproline.
 MOD_RES 1224 1224 Hydroxyproline.
 MOD_RES 1467 1467 Hydroxyproline.
 MOD_RES 1470 1470 Hydroxyproline.
 MOD_RES 1601 1601 Sulfotyrosine (Potential).
 MOD_RES 1604 1604 Sulfotyrosine (Potential).
 DISULFID 1639 1671 By similarity.
 DISULFID 1645 1645 Interchain (with C-1662) (By similarity).
 DISULFID 1662 1662 Interchain (with C-1645) (By similarity).
 DISULFID 1680 1835 By similarity.
 DISULFID 1746 1789 By similarity.  
Keyword
 3D-structure; Calcium; Collagen; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Ehlers-Danlos syndrome; Extracellular matrix; Heparin-binding; Hydroxylation; Metal-binding; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Sulfation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1838 AA 
Protein Sequence
MDVHTRWKAR SALRPGAPLL PPLLLLLLWA PPPSRAAQPA DLLKVLDFHN LPDGITKTTG 60
FCATRRSSKG PDVAYRVTKD AQLSAPTKQL YPASAFPEDF SILTTVKAKK GSQAFLVSIY 120
NEQGIQQIGL ELGRSPVFLY EDHTGKPGPE DYPLFRGINL SDGKWHRIAL SVHKKNVTLI 180
LDCKKKTTKF LDRSDHPMID INGIIVFGTR ILDEEVFEGD IQQLLFVSDH RAAYDYCEHY 240
SPDCDTAVPD TPQSQDPNPD EYYTEGDGEG ETYYYEYPYY EDPEDLGKEP TPSKKPVEAA 300
KETTEVPEEL TPTPTEAAPM PETSEGAGKE EDVGIGDYDY VPSEDYYTPS PYDDLTYGEG 360
EENPDQPTDP GAGAEIPTST ADTSNSSNPA PPPGEGADDL EGEFTEETIR NLDENYYDPY 420
YDPTSSPSEI GPGMPANQDT IYEGIGGPRG EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP 480
GPPGTMGPTG QVGDPGERGP PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS 540
AQESQAQAIL QQARLALRGP AGPMGLTGRP GPVGPPGSGG LKGEPGDVGP QGPRGVQGPP 600
GPAGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP SGPPGPPGDD 660
GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG MDGQPGPKGN VGPQGEPGPP 720
GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP GLPGMPGADG PPGHPGKEGP PGEKGGQGPP 780
GPQGPIGYPG PRGVKGADGI RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED 840
GPEGPKGRGG PNGDPGPLGP PGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR 900
GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP NGPQGPTGFP 960
GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG PQGPTGETGP MGERGHPGPP 1020
GPPGEQGLPG LAGKEGTKGD PGPAGLPGKD GPPGLRGFPG DRGLPGPVGA LGLKGNEGPP 1080
GPPGPAGSPG ERGPAGAAGP IGIPGRPGPQ GPPGPAGEKG APGEKGPQGP AGRDGLQGPV 1140
GLPGPAGPVG PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP 1200
GPRGQQGLFG QKGDEGPRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP PGPPGPRGPS 1260
GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GEPGLPGEGG PPGPKGERGE KGESGPSGAA 1320
GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT 1380
GEPGPSGPPG KRGPPGPAGP EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR 1440
GIPGPVGEQG LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK 1500
GDRGLPGPQG SSGPKGEQGI TGPSGPIGPP GPPGLPGPPG PKGAKGSSGP TGPKGEAGHP 1560
GPPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGNGEN YVDYADGMEE IFGSLNSLKL 1620
EIEQMKRPLG TQQNPARTCK DLQLCHPDFP DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC 1680
VFPDKKSEGA RITSWPKENP GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ 1740
NVTYHCYQSV AWQDAATGSY DKALRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL 1800
EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFMG 1838 
Gene Ontology
 GO:0005604; C:basement membrane; IEA:Compara.
 GO:0005588; C:collagen type V; IMP:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0005201; F:extracellular matrix structural constituent; IEA:Compara.
 GO:0008201; F:heparin binding; IDA:UniProtKB.
 GO:0005178; F:integrin binding; NAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0001568; P:blood vessel development; IEA:Compara.
 GO:0007155; P:cell adhesion; IMP:UniProtKB.
 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:0043206; P:extracellular fibril organization; IMP:UniProtKB.
 GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
 GO:0048592; P:eye morphogenesis; IMP:UniProtKB.
 GO:0003007; P:heart morphogenesis; IEA:Compara.
 GO:0045112; P:integrin biosynthetic process; IMP:UniProtKB.
 GO:0051128; P:regulation of cellular component organization; IEA:Compara.
 GO:0043588; P:skin development; IMP:UniProtKB.
 GO:0035313; P:wound healing, spreading of epidermal cells; IMP:UniProtKB. 
Interpro
 IPR008160; Collagen.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR000885; Fib_collagen_C.
 IPR001791; Laminin_G. 
Pfam
 PF01410; COLFI
 PF01391; Collagen
 PF02210; Laminin_G_2 
SMART
 SM00038; COLFI
 SM00282; LamG
 SM00210; TSPN 
PROSITE
 PS50025; LAM_G_DOMAIN
 PS51461; NC1_FIB 
PRINTS