Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8N543

- OGFD1_HUMAN

UniProt

Q8N543 - OGFD1_HUMAN

Protein

Prolyl 3-hydroxylase OGFOD1

Gene

OGFOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.3 Publications

    Catalytic activityi

    Peptidyl L-proline + 2-oxoglutarate + O2 = peptidyl trans-3-hydroxy-L-proline + succinate + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.PROSITE-ProRule annotation
    Ascorbate.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi155 – 1551IronCurated
    Metal bindingi157 – 1571IronCurated
    Metal bindingi218 – 2181IronPROSITE-ProRule annotation
    Binding sitei228 – 22812-oxoglutaratePROSITE-ProRule annotation

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. L-ascorbic acid binding Source: UniProtKB-KW
    3. peptidyl-proline 3-dioxygenase activity Source: UniProtKB
    4. peptidyl-proline dioxygenase activity Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. peptidyl-proline hydroxylation Source: GOC
    3. protein hydroxylation Source: UniProtKB
    4. regulation of translational termination Source: UniProtKB
    5. stress granule assembly Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:OGFOD1
    Synonyms:KIAA1612, TPA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:25585. OGFOD1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic stress granule Source: UniProtKB
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi155 – 1551H → A: Loss of function. 1 Publication
    Mutagenesisi157 – 1571D → A: Loss of function. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485568.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 542542Prolyl 3-hydroxylase OGFOD1PRO_0000288974Add
    BLAST

    Proteomic databases

    MaxQBiQ8N543.
    PaxDbiQ8N543.
    PRIDEiQ8N543.

    PTM databases

    PhosphoSiteiQ8N543.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8N543.
    BgeeiQ8N543.
    CleanExiHS_OGFOD1.
    GenevestigatoriQ8N543.

    Organism-specific databases

    HPAiHPA003215.

    Interactioni

    Protein-protein interaction databases

    BioGridi120532. 33 interactions.
    STRINGi9606.ENSP00000337196.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N543.
    SMRiQ8N543. Positions 72-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 239106Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi4 – 2017Nuclear localization signalCuratedAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TPA1 family.Curated
    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3751.
    HOGENOMiHOG000007015.
    HOVERGENiHBG056995.
    InParanoidiQ8N543.
    OMAiFSFVYYE.
    OrthoDBiEOG7FBRHW.
    PhylomeDBiQ8N543.
    TreeFamiTF105920.

    Family and domain databases

    InterProiIPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR019601. Oxoglutarate/Fe-dep_Oase_C.
    IPR006620. Pro_4_hyd_alph.
    [Graphical view]
    PfamiPF13640. 2OG-FeII_Oxy_3. 1 hit.
    PF10637. Ofd1_CTDD. 1 hit.
    [Graphical view]
    SMARTiSM00702. P4Hc. 1 hit.
    [Graphical view]
    PROSITEiPS51471. FE2OG_OXY. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N543-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MNGKRPAEPG PARVGKKGKK EVMAEFSDAV TEETLKKQVA EAWSRRTPFS    50
    HEVIVMDMDP FLHCVIPNFI QSQDFLEGLQ KELMNLDFHE KYNDLYKFQQ 100
    SDDLKKRREP HISTLRKILF EDFRSWLSDI SKIDLESTID MSCAKYEFTD 150
    ALLCHDDELE GRRIAFILYL VPPWDRSMGG TLDLYSIDEH FQPKQIVKSL 200
    IPSWNKLVFF EVSPVSFHQV SEVLSEEKSR LSISGWFHGP SLTRPPNYFE 250
    PPIPRSPHIP QDHEILYDWI NPTYLDMDYQ VQIQEEFEES SEILLKEFLK 300
    PEKFTKVCEA LEHGHVEWSS RGPPNKRFYE KAEESKLPEI LKECMKLFRS 350
    EALFLLLSNF TGLKLHFLAP SEEDEMNDKK EAETTDITEE GTSHSPPEPE 400
    NNQMAISNNS QQSNEQTDPE PEENETKKES SVPMCQGELR HWKTGHYTLI 450
    HDHSKAEFAL DLILYCGCEG WEPEYGGFTS YIAKGEDEEL LTVNPESNSL 500
    ALVYRDRETL KFVKHINHRS LEQKKTFPNR TGFWDFSFIY YE 542
    Length:542
    Mass (Da):63,246
    Last modified:October 1, 2002 - v1
    Checksum:i8834BB200D5D8D85
    GO
    Isoform 2 (identifier: Q8N543-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-140: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:402
    Mass (Da):46,861
    Checksum:i8309970C9ED3AEB8
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501S → G in BAB13967. (PubMed:14702039)Curated
    Sequence conflicti112 – 1121I → V in BAB14226. (PubMed:14702039)Curated
    Sequence conflicti343 – 3431E → G in BAB14880. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti173 – 1731P → S.1 Publication
    Corresponds to variant rs34883368 [ dbSNP | Ensembl ].
    VAR_032545

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 140140Missing in isoform 2. 1 PublicationVSP_025852Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10761.2. [Q8N543-1]
    RefSeqiNP_060703.3. NM_018233.3.
    UniGeneiHs.231883.

    Genome annotation databases

    EnsembliENST00000566157; ENSP00000457258; ENSG00000087263. [Q8N543-1]
    GeneIDi55239.
    KEGGihsa:55239.
    UCSCiuc002ejb.3. human. [Q8N543-1]

    Polymorphism databases

    DMDMi74728942.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS10761.2. [Q8N543-1 ]
    RefSeqi NP_060703.3. NM_018233.3.
    UniGenei Hs.231883.

    3D structure databases

    ProteinModelPortali Q8N543.
    SMRi Q8N543. Positions 72-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120532. 33 interactions.
    STRINGi 9606.ENSP00000337196.

    Chemistry

    DrugBanki DB00126. Vitamin C.

    PTM databases

    PhosphoSitei Q8N543.

    Polymorphism databases

    DMDMi 74728942.

    Proteomic databases

    MaxQBi Q8N543.
    PaxDbi Q8N543.
    PRIDEi Q8N543.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000566157 ; ENSP00000457258 ; ENSG00000087263 . [Q8N543-1 ]
    GeneIDi 55239.
    KEGGi hsa:55239.
    UCSCi uc002ejb.3. human. [Q8N543-1 ]

    Organism-specific databases

    CTDi 55239.
    GeneCardsi GC16P056488.
    HGNCi HGNC:25585. OGFOD1.
    HPAi HPA003215.
    MIMi 615857. gene.
    neXtProti NX_Q8N543.
    PharmGKBi PA143485568.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3751.
    HOGENOMi HOG000007015.
    HOVERGENi HBG056995.
    InParanoidi Q8N543.
    OMAi FSFVYYE.
    OrthoDBi EOG7FBRHW.
    PhylomeDBi Q8N543.
    TreeFami TF105920.

    Miscellaneous databases

    ChiTaRSi OGFOD1. human.
    GeneWikii OGFOD1.
    GenomeRNAii 55239.
    NextBioi 35527560.
    PROi Q8N543.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N543.
    Bgeei Q8N543.
    CleanExi HS_OGFOD1.
    Genevestigatori Q8N543.

    Family and domain databases

    InterProi IPR005123. Oxoglu/Fe-dep_dioxygenase.
    IPR019601. Oxoglutarate/Fe-dep_Oase_C.
    IPR006620. Pro_4_hyd_alph.
    [Graphical view ]
    Pfami PF13640. 2OG-FeII_Oxy_3. 1 hit.
    PF10637. Ofd1_CTDD. 1 hit.
    [Graphical view ]
    SMARTi SM00702. P4Hc. 1 hit.
    [Graphical view ]
    PROSITEi PS51471. FE2OG_OXY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: FUNCTION, CATALYTIC ACTIVITY.
    10. Cited for: FUNCTION, MUTAGENESIS OF ASP-157.

    Entry informationi

    Entry nameiOGFD1_HUMAN
    AccessioniPrimary (citable) accession number: Q8N543
    Secondary accession number(s): H3BUQ2
    , Q9H7U5, Q9H9J9, Q9HA87, Q9HCG0, Q9NVB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3