CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022337
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transmembrane prolyl 4-hydroxylase 
Protein Synonyms/Alias
 P4H-TM; Hypoxia-inducible factor prolyl hydroxylase 4; HIF-PH4; HIF-prolyl hydroxylase 4; HPH-4 
Gene Name
 P4HTM 
Gene Synonyms/Alias
 PH4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
141FIRTLSLKPLLFEIPubiquitination[1]
265HKYMRSHKAESSELVubiquitination[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
Functional Description
 Catalyzes the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. 
Sequence Annotation
 DOMAIN 185 220 EF-hand 1.
 DOMAIN 224 259 EF-hand 2.
 DOMAIN 310 460 Fe2OG dioxygenase.
 METAL 328 328 Iron (By similarity).
 METAL 330 330 Iron (By similarity).
 METAL 374 374 Iron (By similarity).
 BINDING 451 451 2-oxoglutarate (Potential).
 CARBOHYD 348 348 N-linked (GlcNAc...) (Potential).
 CARBOHYD 368 368 N-linked (GlcNAc...) (Potential).
 CARBOHYD 382 382 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Calcium; Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase; Reference proteome; Repeat; Signal-anchor; Transmembrane; Transmembrane helix; Vitamin C. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 502 AA 
Protein Sequence
MAAAAVTGQR PETAAAEEAS RPQWAPPDHC QAQAAAGLGD GEDAPVRPLC KPRGICSRAY 60
FLVLMVFVHL YLGNVLALLL FVHYSNGDES SDPGPQHRAQ GPGPEPTLGP LTRLEGIKVG 120
HERKVQLVTD RDHFIRTLSL KPLLFEIPGF LTDEECRLII HLAQMKGLQR SQILPTEEYE 180
EAMSTMQVSQ LDLFRLLDQN RDGHLQLREV LAQTRLGNGW WMTPESIQEM YAAIKADPDG 240
DGVLSLQEFS NMDLRDFHKY MRSHKAESSE LVRNSHHTWL YQGEGAHHIM RAIRQRVLRL 300
TRLSPEIVEL SEPLQVVRYG EGGHYHAHVD SGPVYPETIC SHTKLVANES VPFETSCRYM 360
TVLFYLNNVT GGGETVFPVA DNRTYDEMSL IQDDVDLRDT RRHCDKGNLR VKPQQGTAVF 420
WYNYLPDGQG WVGDVDDYSL HGGCLVTRGT KWIANNWINV DPSRARQALF QQEMARLARE 480
GGTDSQPEWA LDRAYRDARV EL 502 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
 GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:InterPro.
 GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR005123; Oxoglu/Fe-dep_dioxygenase.
 IPR006620; Pro_4_hyd_alph. 
Pfam
 PF13640; 2OG-FeII_Oxy_3
 PF13202; EF_hand_3 
SMART
 SM00702; P4Hc 
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS51471; FE2OG_OXY 
PRINTS