Tag | Content |
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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 |
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141 | FIRTLSLKPLLFEIP | ubiquitination | [1] | 265 | HKYMRSHKAESSELV | ubiquitination | [1] |
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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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |