| Tag | Content |
|---|
| CPLM ID | CPLM-000083 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 |
Protein Synonyms/Alias | Lysyl hydroxylase 2; LH2 |
Gene Name | PLOD2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 341 | NKEVYHEKDIKVFFD | ubiquitination | [1] | | 344 | VYHEKDIKVFFDKAK | ubiquitination | [1] |
|
Reference | [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [ PMID: 21890473] |
Functional Description | Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. |
Sequence Annotation | DOMAIN 644 737 Fe2OG dioxygenase.
ACT_SITE 728 728 Potential.
METAL 666 666 Iron (By similarity).
METAL 668 668 Iron (By similarity).
METAL 718 718 Iron (By similarity).
MOD_RES 320 320 Phosphothreonine.
MOD_RES 323 323 Phosphotyrosine.
CARBOHYD 63 63 N-linked (GlcNAc...) (Potential).
CARBOHYD 209 209 N-linked (GlcNAc...).
CARBOHYD 297 297 N-linked (GlcNAc...) (Potential).
CARBOHYD 365 365 N-linked (GlcNAc...) (Potential).
CARBOHYD 522 522 N-linked (GlcNAc...).
CARBOHYD 696 696 N-linked (GlcNAc...) (Potential).
CARBOHYD 725 725 N-linked (GlcNAc...) (Potential). |
Keyword | Alternative splicing; Complete proteome; Dioxygenase; Disease mutation; Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding; Osteogenesis imperfecta; Oxidoreductase; Phosphoprotein; Reference proteome; Signal; Vitamin C. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 737 AA |
Protein Sequence | MGGCTVKPQL LLLALVLHPW NPCLGADSEK PSSIPTDKLL VITVATKESD GFHRFMQSAK 60
YFNYTVKVLG QGEEWRGGDG INSIGGGQKV RLMKEVMEHY ADQDDLVVMF TECFDVIFAG 120
GPEEVLKKFQ KANHKVVFAA DGILWPDKRL ADKYPVVHIG KRYLNSGGFI GYAPYVNRIV 180
QQWNLQDNDD DQLFYTKVYI DPLKREAINI TLDHKCKIFQ TLNGAVDEVV LKFENGKARA 240
KNTFYETLPV AINGNGPTKI LLNYFGNYVP NSWTQDNGCT LCEFDTVDLS AVDVHPNVSI 300
GVFIEQPTPF LPRFLDILLT LDYPKEALKL FIHNKEVYHE KDIKVFFDKA KHEIKTIKIV 360
GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP RTLKILIEQN RKIIAPLVTR 420
HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG NRVGVWNVPY MANVYLIKGK TLRSEMNERN 480
YFVRDKLDPD MALCRNAREM GVFMYISNRH EFGRLLSTAN YNTSHYNNDL WQIFENPVDW 540
KEKYINRDYS KIFTENIVEQ PCPDVFWFPI FSEKACDELV EEMEHYGKWS GGKHHDSRIS 600
GGYENVPTDD IHMKQVDLEN VWLHFIREFI APVTLKVFAG YYTKGFALLN FVVKYSPERQ 660
RSLRPHHDAS TFTINIALNN VGEDFQGGGC KFLRYNCSIE SPRKGWSFMH PGRLTHLHEG 720
LPVKNGTRYI AVSFIDP 737 |
Gene Ontology | GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0005506; F:iron ion binding; IEA:InterPro. GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. GO:0008475; F:procollagen-lysine 5-dioxygenase activity; TAS:ProtInc. GO:0006464; P:cellular protein modification process; TAS:ProtInc. GO:0030198; P:extracellular matrix organization; TAS:Reactome. GO:0001666; P:response to hypoxia; IEP:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |