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Q8BLR9

- HIF1N_MOUSE

UniProt

Q8BLR9 - HIF1N_MOUSE

Protein

Hypoxia-inducible factor 1-alpha inhibitor

Gene

Hif1an

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Hydroxylates HIF-1 alpha at 'Asp-799' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation By similarity. Positively regulates ASB4 activity, promoting vascular differentiation.By similarity1 Publication

    Catalytic activityi

    Hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 = hypoxia-inducible factor-(3S)-3-hydroxy-L-asparagine + succinate + CO2.
    Ankyrin-repeat-L-histidine + 2-oxoglutarate + O2 = ankyrin-repeat-(3S)-3-hydroxy-L-histidine + succinate + CO2.

    Cofactori

    Fe2+ ion.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei145 – 14512-oxoglutarateBy similarity
    Binding sitei152 – 1521SubstrateBy similarity
    Binding sitei196 – 19612-oxoglutarateBy similarity
    Metal bindingi199 – 1991Iron; via tele nitrogen; catalyticBy similarity
    Metal bindingi201 – 2011Iron; via tele nitrogen; catalyticBy similarity
    Binding sitei205 – 20512-oxoglutarateBy similarity
    Binding sitei214 – 21412-oxoglutarateBy similarity
    Metal bindingi279 – 2791Iron; via tele nitrogen; catalyticBy similarity
    Binding sitei294 – 29412-oxoglutarateBy similarity
    Binding sitei300 – 3001Substrate; via amide nitrogenBy similarity
    Binding sitei321 – 3211SubstrateBy similarity
    Sitei340 – 3401Important for dimer formationBy similarity

    GO - Molecular functioni

    1. ankyrin repeat binding Source: UniProtKB
    2. carboxylic acid binding Source: Ensembl
    3. cofactor binding Source: Ensembl
    4. iron ion binding Source: Ensembl
    5. Notch binding Source: UniProtKB
    6. peptidyl-asparagine 3-dioxygenase activity Source: UniProtKB
    7. peptidyl-histidine dioxygenase activity Source: UniProtKB
    8. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. negative regulation of Notch signaling pathway Source: UniProtKB
    2. negative regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
    3. oxidation-reduction process Source: UniProtKB
    4. peptidyl-asparagine hydroxylation Source: UniProtKB
    5. peptidyl-aspartic acid hydroxylation Source: UniProtKB
    6. peptidyl-histidine hydroxylation Source: UniProtKB
    7. positive regulation of myoblast differentiation Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_199104. Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hypoxia-inducible factor 1-alpha inhibitor (EC:1.14.11.30, EC:1.14.11.n4)
    Alternative name(s):
    Hypoxia-inducible factor asparagine hydroxylase
    Gene namesi
    Name:Hif1an
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:2442345. Hif1an.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 349348Hypoxia-inducible factor 1-alpha inhibitorPRO_0000083975Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ8BLR9.
    PRIDEiQ8BLR9.

    PTM databases

    PhosphoSiteiQ8BLR9.

    Expressioni

    Gene expression databases

    BgeeiQ8BLR9.
    GenevestigatoriQ8BLR9.

    Interactioni

    Subunit structurei

    Homodimer; homodimerization is essential for catalytic activity. Interacts with VHL and HIF1A. Part of a complex with VHL, HIF1A and HDAC1 or HDAC2 or HDAC3. Interacts with NFKB1 and NFKBIA. Interacts with NOTCH1, NOTCH2 and NOTCH3 but not with NOTCH4. Interacts with ABPA3. Interacts with TNKS2. Interacts with PPP1R12A By similarity. Interacts with UBE3A By similarity. Interacts with ASB4.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi235386. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BLR9.
    SMRiQ8BLR9. Positions 22-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini142 – 307166JmjCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 125124Interaction with VHLBy similarityAdd
    BLAST
    Regioni181 – 1833Substrate bindingBy similarity
    Regioni201 – 2033Substrate bindingBy similarity
    Regioni238 – 2392Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 JmjC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG71927.
    GeneTreeiENSGT00530000062914.
    HOGENOMiHOG000008146.
    HOVERGENiHBG051903.
    InParanoidiQ8BLR9.
    KOiK18055.
    OMAiMIKGRYD.
    OrthoDBiEOG72NRQ4.
    PhylomeDBiQ8BLR9.
    TreeFamiTF329609.

    Family and domain databases

    Gene3Di1.10.287.1010. 1 hit.
    InterProiIPR027445. FIH-1.
    IPR027452. FIH-1_domII.
    IPR003347. JmjC_dom.
    [Graphical view]
    PANTHERiPTHR12461:SF19. PTHR12461:SF19. 1 hit.
    SMARTiSM00558. JmjC. 1 hit.
    [Graphical view]
    PROSITEiPS51184. JMJC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BLR9-1) [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

    MAATAAEVAA SGSGEAREEA EAPGPAWDES QLRSYSFPTR PIPRLSQSDP    50
    RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF 100
    LYYDEKKMGN FQNFKPRSNR EEIKFHEFVE KLQAIQQRGG EERLYLQQTL 150
    NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY 200
    DEQQNFFAQI KGHKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE 250
    RFPNFRNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA 300
    PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN 349
    Length:349
    Mass (Da):40,241
    Last modified:March 7, 2006 - v2
    Checksum:iED5C2B875EBCE76E
    GO
    Isoform 2 (identifier: Q8BLR9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         241-263: QVDFDNPDYERFPNFRNVVGYET → GVKRRDQAKRETIAKEKYTKQNK
         264-349: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:263
    Mass (Da):30,424
    Checksum:iF7386262A6C77954
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti177 – 1771R → L in AAI30014. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei241 – 26323QVDFD…VGYET → GVKRRDQAKRETIAKEKYTK QNK in isoform 2. 1 PublicationVSP_017537Add
    BLAST
    Alternative sequencei264 – 34986Missing in isoform 2. 1 PublicationVSP_017538Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK043636 mRNA. Translation: BAC31602.1.
    AK154774 mRNA. Translation: BAE32822.1.
    BC130013 mRNA. Translation: AAI30014.1.
    CCDSiCCDS29852.1. [Q8BLR9-1]
    RefSeqiNP_795932.2. NM_176958.3. [Q8BLR9-1]
    UniGeneiMm.145278.

    Genome annotation databases

    EnsembliENSMUST00000040455; ENSMUSP00000035326; ENSMUSG00000036450. [Q8BLR9-1]
    GeneIDi319594.
    KEGGimmu:319594.
    UCSCiuc008hpx.1. mouse. [Q8BLR9-2]
    uc008hpy.1. mouse. [Q8BLR9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK043636 mRNA. Translation: BAC31602.1 .
    AK154774 mRNA. Translation: BAE32822.1 .
    BC130013 mRNA. Translation: AAI30014.1 .
    CCDSi CCDS29852.1. [Q8BLR9-1 ]
    RefSeqi NP_795932.2. NM_176958.3. [Q8BLR9-1 ]
    UniGenei Mm.145278.

    3D structure databases

    ProteinModelPortali Q8BLR9.
    SMRi Q8BLR9. Positions 22-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 235386. 2 interactions.

    PTM databases

    PhosphoSitei Q8BLR9.

    Proteomic databases

    PaxDbi Q8BLR9.
    PRIDEi Q8BLR9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040455 ; ENSMUSP00000035326 ; ENSMUSG00000036450 . [Q8BLR9-1 ]
    GeneIDi 319594.
    KEGGi mmu:319594.
    UCSCi uc008hpx.1. mouse. [Q8BLR9-2 ]
    uc008hpy.1. mouse. [Q8BLR9-1 ]

    Organism-specific databases

    CTDi 55662.
    MGIi MGI:2442345. Hif1an.

    Phylogenomic databases

    eggNOGi NOG71927.
    GeneTreei ENSGT00530000062914.
    HOGENOMi HOG000008146.
    HOVERGENi HBG051903.
    InParanoidi Q8BLR9.
    KOi K18055.
    OMAi MIKGRYD.
    OrthoDBi EOG72NRQ4.
    PhylomeDBi Q8BLR9.
    TreeFami TF329609.

    Enzyme and pathway databases

    Reactomei REACT_199104. Oxygen-dependent asparagine hydroxylation of Hypoxia-inducible Factor Alpha.

    Miscellaneous databases

    NextBioi 395052.
    PROi Q8BLR9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BLR9.
    Genevestigatori Q8BLR9.

    Family and domain databases

    Gene3Di 1.10.287.1010. 1 hit.
    InterProi IPR027445. FIH-1.
    IPR027452. FIH-1_domII.
    IPR003347. JmjC_dom.
    [Graphical view ]
    PANTHERi PTHR12461:SF19. PTHR12461:SF19. 1 hit.
    SMARTi SM00558. JmjC. 1 hit.
    [Graphical view ]
    PROSITEi PS51184. JMJC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Brain cortex.
    2. "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).
    3. "ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism."
      Ferguson J.E. III, Wu Y., Smith K., Charles P., Powers K., Wang H., Patterson C.
      Mol. Cell. Biol. 27:6407-6419(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ASB4.

    Entry informationi

    Entry nameiHIF1N_MOUSE
    AccessioniPrimary (citable) accession number: Q8BLR9
    Secondary accession number(s): A1L3B7, Q3U3G4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2003
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3