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Q8N543 (OGFD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prolyl 3-hydroxylase OGFOD1

EC=1.14.11.-
Alternative name(s):
2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1
Termination and polyadenylation 1 homolog
Gene names
Name:OGFOD1
Synonyms:KIAA1612, TPA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.9 Ref.10

Catalytic activity

Peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl trans-3-hydroxy-L-proline + succinate + CO2. Ref.9

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Ascorbate By similarity.

Subcellular location

Isoform 1: Cytoplasm. Nucleus. Note: Mainly nuclear. A portion relocalizes to cytoplasmic stress granules upon stress. Ref.5 Ref.6 Ref.8

Isoform 2: Cytoplasm Ref.5 Ref.6 Ref.8.

Sequence similarities

Belongs to the TPA1 family.

Contains 1 Fe2OG dioxygenase domain.

Caution

According to a report, it is incorporated into stress granules upon arsenite-induced stress and associates with heme-regulated kinase and eIF-2-alpha (EIF2S1) in regulating eIF-2-alpha phosphorylation (Ref.6). However, no effect in eIF-2-alpha phosphorylation have been observed by another study (Ref.10).

Sequence caution

The sequence BAB13438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB14880.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N543-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N543-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-140: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Prolyl 3-hydroxylase OGFOD1
PRO_0000288974

Regions

Domain134 – 239106Fe2OG dioxygenase
Motif4 – 2017Nuclear localization signal Probable

Sites

Metal binding1551Iron Probable
Metal binding1571Iron Probable
Metal binding2181Iron By similarity
Binding site22812-oxoglutarate Potential

Natural variations

Alternative sequence1 – 140140Missing in isoform 2.
VSP_025852
Natural variant1731P → S. Ref.2
Corresponds to variant rs34883368 [ dbSNP | Ensembl ].
VAR_032545

Experimental info

Mutagenesis1551H → A: Loss of function. Ref.5
Mutagenesis1571D → A: Loss of function. Ref.10
Sequence conflict501S → G in BAB13967. Ref.2
Sequence conflict1121I → V in BAB14226. Ref.2
Sequence conflict3431E → G in BAB14880. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 8834BB200D5D8D85

FASTA54263,246
        10         20         30         40         50         60 
MNGKRPAEPG PARVGKKGKK EVMAEFSDAV TEETLKKQVA EAWSRRTPFS HEVIVMDMDP 

        70         80         90        100        110        120 
FLHCVIPNFI QSQDFLEGLQ KELMNLDFHE KYNDLYKFQQ SDDLKKRREP HISTLRKILF 

       130        140        150        160        170        180 
EDFRSWLSDI SKIDLESTID MSCAKYEFTD ALLCHDDELE GRRIAFILYL VPPWDRSMGG 

       190        200        210        220        230        240 
TLDLYSIDEH FQPKQIVKSL IPSWNKLVFF EVSPVSFHQV SEVLSEEKSR LSISGWFHGP 

       250        260        270        280        290        300 
SLTRPPNYFE PPIPRSPHIP QDHEILYDWI NPTYLDMDYQ VQIQEEFEES SEILLKEFLK 

       310        320        330        340        350        360 
PEKFTKVCEA LEHGHVEWSS RGPPNKRFYE KAEESKLPEI LKECMKLFRS EALFLLLSNF 

       370        380        390        400        410        420 
TGLKLHFLAP SEEDEMNDKK EAETTDITEE GTSHSPPEPE NNQMAISNNS QQSNEQTDPE 

       430        440        450        460        470        480 
PEENETKKES SVPMCQGELR HWKTGHYTLI HDHSKAEFAL DLILYCGCEG WEPEYGGFTS 

       490        500        510        520        530        540 
YIAKGEDEEL LTVNPESNSL ALVYRDRETL KFVKHINHRS LEQKKTFPNR TGFWDFSFIY 


YE 

« Hide

Isoform 2 [UniParc].

Checksum: 8309970C9ED3AEB8
Show »

FASTA40246,861

References

« Hide 'large scale' references
[1]"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."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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 T.-O., 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT SER-173.
Tissue: Embryo, Ovary and Teratocarcinoma.
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"OGFOD1, a member of the 2-oxoglutarate and iron dependent dioxygenase family, functions in ischemic signaling."
Saito K., Adachi N., Koyama H., Matsushita M.
FEBS Lett. 584:3340-3347(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-155.
[6]"OGFOD1, a novel modulator of eukaryotic translation initiation factor 2alpha phosphorylation and the cellular response to stress."
Wehner K.A., Schutz S., Sarnow P.
Mol. Cell. Biol. 30:2006-2016(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy."
Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E., Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M., Ratcliffe P.J., Wolf A., Schofield C.J.
Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[10]"OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation."
Singleton R.S., Liu-Yi P., Formenti F., Ge W., Sekirnik R., Fischer R., Adam J., Pollard P.J., Wolf A., Thalhammer A., Loenarz C., Flashman E., Yamamoto A., Coleman M.L., Kessler B.M., Wappner P., Schofield C.J., Ratcliffe P.J., Cockman M.E.
Proc. Natl. Acad. Sci. U.S.A. 111:4031-4036(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-157.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046832 mRNA. Translation: BAB13438.1. Different initiation.
AK001688 mRNA. Translation: BAA91838.1.
AK022130 mRNA. Translation: BAB13967.1.
AK022752 mRNA. Translation: BAB14226.1.
AK024314 mRNA. Translation: BAB14880.1. Different initiation.
AC092140 Genomic DNA. No translation available.
BC032919 mRNA. Translation: AAH32919.1.
CCDSCCDS10761.2. [Q8N543-1]
RefSeqNP_060703.3. NM_018233.3.
UniGeneHs.231883.

3D structure databases

ProteinModelPortalQ8N543.
SMRQ8N543. Positions 72-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120532. 32 interactions.
STRING9606.ENSP00000337196.

Chemistry

DrugBankDB00126. Vitamin C.

PTM databases

PhosphoSiteQ8N543.

Polymorphism databases

DMDM74728942.

Proteomic databases

MaxQBQ8N543.
PaxDbQ8N543.
PRIDEQ8N543.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000566157; ENSP00000457258; ENSG00000087263. [Q8N543-1]
ENST00000568397; ENSP00000457746; ENSG00000087263.
GeneID55239.
KEGGhsa:55239.
UCSCuc002ejb.3. human. [Q8N543-1]

Organism-specific databases

CTD55239.
GeneCardsGC16P056488.
HGNCHGNC:25585. OGFOD1.
HPAHPA003215.
neXtProtNX_Q8N543.
PharmGKBPA143485568.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3751.
HOGENOMHOG000007015.
HOVERGENHBG056995.
InParanoidQ8N543.
OMAFSFVYYE.
OrthoDBEOG7FBRHW.
PhylomeDBQ8N543.
TreeFamTF105920.

Gene expression databases

ArrayExpressQ8N543.
BgeeQ8N543.
CleanExHS_OGFOD1.
GenevestigatorQ8N543.

Family and domain databases

InterProIPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR019601. Oxoglutarate/Fe-dep_Oase_C.
IPR006620. Pro_4_hyd_alph.
[Graphical view]
PfamPF13640. 2OG-FeII_Oxy_3. 1 hit.
PF10637. Ofd1_CTDD. 1 hit.
[Graphical view]
SMARTSM00702. P4Hc. 1 hit.
[Graphical view]
PROSITEPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOGFOD1. human.
GeneWikiOGFOD1.
GenomeRNAi55239.
NextBio35527560.
PROQ8N543.

Entry information

Entry nameOGFD1_HUMAN
AccessionPrimary (citable) accession number: Q8N543
Secondary accession number(s): H3BUQ2 expand/collapse secondary AC list , Q9H7U5, Q9H9J9, Q9HA87, Q9HCG0, Q9NVB6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM