Prolyl 3-hydroxylase OGFOD1

Details

Name
Prolyl 3-hydroxylase OGFOD1
Synonyms
  • 1.14.11.-
  • 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1
  • KIAA1612
  • Termination and polyadenylation 1 homolog
  • TPA1
Gene Name
OGFOD1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0004337|Prolyl 3-hydroxylase OGFOD1
MNGKRPAEPGPARVGKKGKKEVMAEFSDAVTEETLKKQVAEAWSRRTPFSHEVIVMDMDP
FLHCVIPNFIQSQDFLEGLQKELMNLDFHEKYNDLYKFQQSDDLKKRREPHISTLRKILF
EDFRSWLSDISKIDLESTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPPWDRSMGG
TLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSPVSFHQVSEVLSEEKSRLSISGWFHGP
SLTRPPNYFEPPIPRSPHIPQDHEILYDWINPTYLDMDYQVQIQEEFEESSEILLKEFLK
PEKFTKVCEALEHGHVEWSSRGPPNKRFYEKAEESKLPEILKECMKLFRSEALFLLLSNF
TGLKLHFLAPSEEDEMNDKKEAETTDITEEGTSHSPPEPENNQMAISNNSQQSNEQTDPE
PEENETKKESSVPMCQGELRHWKTGHYTLIHDHSKAEFALDLILYCGCEGWEPEYGGFTS
YIAKGEDEELLTVNPESNSLALVYRDRETLKFVKHINHRSLEQKKTFPNRTGFWDFSFIY
YE
Number of residues
542
Molecular Weight
63245.655
Theoretical pI
4.77
GO Classification
Functions
iron ion binding / L-ascorbic acid binding / peptidyl-proline 3-dioxygenase activity / peptidyl-proline dioxygenase activity
Processes
cell proliferation / peptidyl-proline hydroxylation / protein hydroxylation / regulation of translational termination / stress granule assembly
Components
cytoplasm / cytoplasmic stress granule / nucleus
General Function
Peptidyl-proline dioxygenase activity
Specific Function
Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit RPS23, thereby regulating protein translation termination efficiency. Involved in stress granule formation.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011597|Prolyl 3-hydroxylase OGFOD1 (OGFOD1)
ATGAATGGGAAGCGGCCAGCGGAGCCCGGCCCAGCCCGGGTGGGAAAAAAGGGAAAGAAG
GAGGTGATGGCGGAGTTTTCGGACGCTGTTACGGAAGAAACCTTGAAAAAGCAGGTGGCT
GAGGCCTGGAGCCGCAGGACGCCGTTCAGTCACGAAGTCATTGTCATGGACATGGACCCT
TTTCTTCACTGTGTGATCCCAAACTTCATCCAAAGCCAAGACTTCTTAGAAGGGCTTCAG
AAGGAACTGATGAACTTGGACTTCCATGAGAAGTATAATGATTTATATAAGTTCCAGCAG
TCTGATGATTTGAAGAAGAGAAGAGAGCCTCACATCTCCACTTTAAGGAAAATTCTGTTT
GAAGATTTCCGGTCCTGGCTTTCTGATATTTCTAAAATTGACCTGGAATCAACCATTGAC
ATGTCCTGTGCTAAATATGAATTCACTGATGCCCTGCTGTGCCATGATGATGAGCTGGAA
GGGCGCCGGATTGCCTTCATCCTGTACCTGGTTCCTCCCTGGGACAGGAGCATGGGTGGT
ACCCTGGACCTGTACAGCATTGATGAACACTTTCAGCCGAAGCAGATTGTCAAGTCTCTT
ATCCCTTCGTGGAACAAACTGGTTTTCTTTGAAGTATCTCCTGTGTCCTTTCACCAGGTG
TCTGAAGTGCTGTCTGAAGAAAAGTCACGTTTGTCTATAAGTGGCTGGTTTCATGGTCCA
TCATTGACTCGGCCTCCCAACTACTTTGAACCCCCCATACCTCGGAGCCCTCACATCCCA
CAAGATCATGAGATTTTGTATGATTGGATCAACCCTACTTATCTGGACATGGATTACCAA
GTTCAAATTCAAGAAGAGTTTGAAGAAAGTTCTGAAATTCTCCTGAAGGAGTTTCTTAAG
CCTGAGAAATTCACGAAAGTCTGTGAGGCCTTGGAGCATGGACATGTGGAATGGAGCAGC
CGAGGTCCCCCTAACAAAAGGTTTTATGAGAAAGCTGAGGAGAGTAAGCTTCCTGAGATA
TTGAAGGAGTGCATGAAGTTATTTCGCTCTGAGGCACTATTCTTGCTGCTCTCCAACTTC
ACAGGCCTGAAGCTTCATTTCTTGGCCCCTTCGGAAGAAGATGAGATGAATGATAAAAAA
GAGGCAGAAACCACTGATATCACTGAAGAAGGGACTAGCCATAGTCCTCCTGAGCCAGAG
AATAATCAGATGGCCATCAGCAACAACAGCCAACAGAGCAATGAGCAGACAGACCCAGAG
CCAGAGGAAAATGAAACAAAGAAAGAATCAAGTGTTCCCATGTGCCAAGGGGAACTGAGG
CATTGGAAGACCGGTCACTACACTTTAATTCATGACCATAGCAAGGCTGAATTTGCCCTA
GACTTAATTCTGTACTGTGGCTGTGAAGGCTGGGAGCCAGAATATGGCGGTTTTACTTCT
TACATTGCCAAAGGTGAAGATGAAGAGCTGCTAACAGTGAATCCAGAAAGCAATTCTTTG
GCATTGGTCTACAGAGACAGAGAGACTCTGAAATTTGTCAAGCATATTAACCACCGAAGC
CTGGAACAAAAGAAAACCTTCCCAAACAGAACAGGTTTCTGGGACTTTTCATTCATCTAT
TATGAATGA
Chromosome Location
16
Locus
16q13
External Identifiers
ResourceLink
UniProtKB IDQ8N543
UniProtKB Entry NameOGFD1_HUMAN
GenBank Protein ID21410525
GenBank Gene IDBC032919
GenAtlas IDOGFOD1
HGNC IDHGNC:25585
General References
  1. Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [Article]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Saito K, Adachi N, Koyama H, Matsushita M: OGFOD1, a member of the 2-oxoglutarate and iron dependent dioxygenase family, functions in ischemic signaling. FEBS Lett. 2010 Aug 4;584(15):3340-7. doi: 10.1016/j.febslet.2010.06.015. Epub 2010 Jun 18. [Article]
  6. Wehner KA, Schutz S, Sarnow P: OGFOD1, a novel modulator of eukaryotic translation initiation factor 2alpha phosphorylation and the cellular response to stress. Mol Cell Biol. 2010 Apr;30(8):2006-16. doi: 10.1128/MCB.01350-09. Epub 2010 Feb 12. [Article]
  7. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  8. Ahmad Y, Boisvert FM, Lundberg E, Uhlen M, Lamond AI: Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization. Mol Cell Proteomics. 2012 Mar;11(3):M111.013680. doi: 10.1074/mcp.M111.013680. Epub 2011 Oct 16. [Article]
  9. Loenarz C, Sekirnik R, Thalhammer A, Ge W, Spivakovsky E, Mackeen MM, McDonough MA, Cockman ME, Kessler BM, Ratcliffe PJ, Wolf A, Schofield CJ: Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy. Proc Natl Acad Sci U S A. 2014 Mar 18;111(11):4019-24. doi: 10.1073/pnas.1311750111. Epub 2014 Feb 18. [Article]
  10. Singleton RS, Liu-Yi P, Formenti F, Ge W, Sekirnik R, Fischer R, Adam J, Pollard PJ, Wolf A, Thalhammer A, Loenarz C, Flashman E, Yamamoto A, Coleman ML, Kessler BM, Wappner P, Schofield CJ, Ratcliffe PJ, Cockman ME: OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation. Proc Natl Acad Sci U S A. 2014 Mar 18;111(11):4031-6. doi: 10.1073/pnas.1314482111. Epub 2014 Feb 18. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00126Ascorbic acidapproved, nutraceuticalunknowncofactorDetails