CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000459
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prolyl 4-hydroxylase subunit alpha-2 
Protein Synonyms/Alias
 4-PH alpha-2; Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2 
Gene Name
 P4HA2 
Gene Synonyms/Alias
 UNQ290/PRO330 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45KELVQSLKEYILVEEubiquitination[1]
64KIKSWANKMEALTSKubiquitination[1]
134EDEIGAAKALMRLQDubiquitination[1, 2, 3, 4, 5]
206GEEATTTKSQVLDYLubiquitination[1]
300LCRGEGVKLTPRRQKubiquitination[1]
328QLLIAPFKEEDEWDSubiquitination[1]
383VASYRVSKSSWLEEDubiquitination[1, 6, 7]
443NDERDTFKHLGTGNRubiquitination[1]
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] 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]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. 
Sequence Annotation
 REPEAT 207 240 TPR.
 DOMAIN 412 520 Fe2OG dioxygenase.
 METAL 430 430 Iron (By similarity).
 METAL 432 432 Iron (By similarity).
 METAL 501 501 Iron (By similarity).
 BINDING 511 511 2-oxoglutarate (Potential).
 CARBOHYD 115 115 N-linked (GlcNAc...) (Potential).
 CARBOHYD 264 264 N-linked (GlcNAc...) (Potential).  
Keyword
 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
 535 AA 
Protein Sequence
MKLWVSALLM AWFGVLSCVQ AEFFTSIGHM TDLIYAEKEL VQSLKEYILV EEAKLSKIKS 60
WANKMEALTS KSAADAEGYL AHPVNAYKLV KRLNTDWPAL EDLVLQDSAA GFIANLSVQR 120
QFFPTDEDEI GAAKALMRLQ DTYRLDPGTI SRGELPGTKY QAMLSVDDCF GMGRSAYNEG 180
DYYHTVLWME QVLKQLDAGE EATTTKSQVL DYLSYAVFQL GDLHRALELT RRLLSLDPSH 240
ERAGGNLRYF EQLLEEEREK TLTNQTEAEL ATPEGIYERP VDYLPERDVY ESLCRGEGVK 300
LTPRRQKRLF CRYHHGNRAP QLLIAPFKEE DEWDSPHIVR YYDVMSDEEI ERIKEIAKPK 360
LARATVRDPK TGVLTVASYR VSKSSWLEED DDPVVARVNR RMQHITGLTV KTAELLQVAN 420
YGVGGQYEPH FDFSRNDERD TFKHLGTGNR VATFLNYMSD VEAGGATVFP DLGAAIWPKK 480
GTAVFWYNLL RSGEGDYRTR HAACPVLVGC KWVSNKWFHE RGQEFLRPCG STEVD 535 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; TAS:UniProtKB.
 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: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