CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000460
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
64KIKSWANKMEALTSKubiquitination[1]
71KMEALTSKSAADAEGubiquitination[1]
134EDEIGAAKALMRLQDubiquitination[1]
383VASYRVSKSSWLEEDubiquitination[1]
443RPFDSGLKTEGNRLAubiquitination[1, 2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
 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 FDFSRRPFDS GLKTEGNRLA TFLNYMSDVE AGGATVFPDL GAAIWPKKGT 480
AVFWYNLLRS GEGDYRTRHA ACPVLVGCKW VSNKWFHERG QEFLRPCGST EVD 533 
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