CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004161
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prolyl 4-hydroxylase subunit alpha-1 
Protein Synonyms/Alias
 4-PH alpha-1; Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1 
Gene Name
 P4HA1 
Gene Synonyms/Alias
 P4HA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
43KDLVTSLKDYIKAEEubiquitination[1]
62QIKKWAEKLDRLTSTubiquitination[1]
72RLTSTATKDPEGFVGubiquitination[1]
132EDQVGAAKALLRLQDubiquitination[1]
150LDTDTISKGNLPGVKubiquitination[1]
230KALLLTKKLLELDPEubiquitination[1]
288DYLPERQKYEMLCRGubiquitination[1]
299LCRGEGIKMTPRRQKubiquitination[1]
382TVHYRISKSAWLSGYacetylation[2]
382TVHYRISKSAWLSGYubiquitination[1]
510CPVLVGNKWVSNKWLubiquitination[1]
515GNKWVSNKWLHERGQubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. 
Sequence Annotation
 REPEAT 205 238 TPR.
 DOMAIN 411 519 Fe2OG dioxygenase.
 METAL 429 429 Iron (By similarity).
 METAL 431 431 Iron (By similarity).
 METAL 500 500 Iron (By similarity).
 BINDING 510 510 2-oxoglutarate (Potential).
 CARBOHYD 113 113 N-linked (GlcNAc...).
 CARBOHYD 259 259 N-linked (GlcNAc...).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Metal-binding; Oxidoreductase; Reference proteome; Signal; TPR repeat; Vitamin C. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 534 AA 
Protein Sequence
MIWYILIIGI LLPQSLAHPG FFTSIGQMTD LIHTEKDLVT SLKDYIKAEE DKLEQIKKWA 60
EKLDRLTSTA TKDPEGFVGH PVNAFKLMKR LNTEWSELEN LVLKDMSDGF ISNLTIQRQY 120
FPNDEDQVGA AKALLRLQDT YNLDTDTISK GNLPGVKHKS FLTAEDCFEL GKVAYTEADY 180
YHTELWMEQA LRQLDEGEIS TIDKVSVLDY LSYAVYQQGD LDKALLLTKK LLELDPEHQR 240
ANGNLKYFEY IMAKEKDVNK SASDDQSDQK TTPKKKGVAV DYLPERQKYE MLCRGEGIKM 300
TPRRQKKLFC RYHDGNRNPK FILAPAKQED EWDKPRIIRF HDIISDAEIE IVKDLAKPRL 360
RRATISNPIT GDLETVHYRI SKSAWLSGYE NPVVSRINMR IQDLTGLDVS TAEELQVANY 420
GVGGQYEPHF DFARKDEPDA FKELGTGNRI ATWLFYMSDV SAGGATVFPE VGASVWPKKG 480
TAVFWYNLFA SGEGDYSTRH AACPVLVGNK WVSNKWLHER GQEFRRPCTL SELE 534 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:HPA.
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:HPA.
 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:0004656; F:procollagen-proline 4-dioxygenase activity; TAS:ProtInc.
 GO:0030199; P:collagen fibril organization; IEA:Compara.
 GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IEA:Compara. 
Interpro
 IPR005123; Oxoglu/Fe-dep_dioxygenase.
 IPR006620; Pro_4_hyd_alph.
 IPR013547; Pro_4_hyd_alph_N.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF03171; 2OG-FeII_Oxy
 PF08336; P4Ha_N 
SMART
 SM00702; P4Hc 
PROSITE
 PS51471; FE2OG_OXY
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS