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)

Q80TJ7

- PHF8_MOUSE

UniProt

Q80TJ7 - PHF8_MOUSE

Protein

Histone lysine demethylase PHF8

Gene

Phf8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (16 Aug 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3 By similarity.By similarity

    Catalytic activityi

    Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.
    Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei244 – 2441SubstrateBy similarity
    Metal bindingi247 – 2471Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi249 – 2491Iron; catalyticPROSITE-ProRule annotation
    Binding sitei264 – 2641SubstrateBy similarity
    Metal bindingi319 – 3191Iron; catalyticPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri5 – 5652PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. histone demethylase activity Source: UniProtKB
    3. histone demethylase activity (H3-K27 specific) Source: UniProtKB
    4. histone demethylase activity (H3-K36 specific) Source: UniProtKB
    5. histone demethylase activity (H3-K9 specific) Source: UniProtKB
    6. histone demethylase activity (H4-K20 specific) Source: UniProtKB
    7. iron ion binding Source: UniProtKB
    8. methylated histone binding Source: UniProtKB
    9. 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 Source: UniProtKB
    10. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. brain development Source: UniProtKB
    2. G1/S transition of mitotic cell cycle Source: UniProtKB
    3. histone H3-K27 demethylation Source: UniProtKB
    4. histone H3-K36 demethylation Source: UniProtKB
    5. histone H3-K9 demethylation Source: UniProtKB
    6. histone H4-K20 demethylation Source: UniProtKB
    7. negative regulation of chromatin silencing at rDNA Source: UniProtKB
    8. positive regulation of transcription, DNA-templated Source: UniProtKB
    9. positive regulation of transcription from RNA polymerase I promoter Source: UniProtKB
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_196580. Condensation of Prophase Chromosomes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone lysine demethylase PHF8 (EC:1.14.11.27)
    Alternative name(s):
    PHD finger protein 8
    Gene namesi
    Name:Phf8
    Synonyms:Kiaa1111
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:2444341. Phf8.

    Subcellular locationi

    Nucleus By similarity. Nucleusnucleolus By similarity
    Note: Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis By similarity.By similarity

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10231023Histone lysine demethylase PHF8PRO_0000059296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei33 – 331Phosphoserine; by CDK1By similarity
    Modified residuei84 – 841Phosphoserine; by CDK1By similarity
    Modified residuei615 – 6151Phosphoserine1 Publication
    Modified residuei669 – 6691PhosphothreonineBy similarity
    Modified residuei670 – 6701PhosphothreonineBy similarity
    Modified residuei768 – 7681PhosphoserineBy similarity
    Modified residuei817 – 8171PhosphoserineBy similarity
    Modified residuei820 – 8201Phosphoserine2 Publications
    Modified residuei843 – 8431PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation at Ser-33 and Ser-84 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ80TJ7.
    PRIDEiQ80TJ7.

    PTM databases

    PhosphoSiteiQ80TJ7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ80TJ7.
    BgeeiQ80TJ7.
    CleanExiMM_PHF8.
    GenevestigatoriQ80TJ7.

    Interactioni

    Subunit structurei

    Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and ZNF711.By similarity

    Structurei

    Secondary structure

    1
    1023
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 183
    Beta strandi20 – 234
    Turni24 – 263
    Beta strandi29 – 313
    Helixi32 – 354
    Helixi39 – 424
    Beta strandi46 – 483
    Turni51 – 566

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WEPNMR-A1-63[»]
    ProteinModelPortaliQ80TJ7.
    SMRiQ80TJ7. Positions 3-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ80TJ7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini195 – 351157JmjCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 7915LinkerBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi733 – 77139Ser-richAdd
    BLAST

    Domaini

    The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 promotes its access to H3K9me2 By similarity.By similarity
    The linker region is a critical determinant of demethylase specificity. It enables the active site of JmjC to reach the target H3K9me2 when the PHD-type zinc finger binds to H3K4me3 By similarity.By similarity

    Sequence similaritiesi

    Contains 1 JmjC domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri5 – 5652PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG290496.
    GeneTreeiENSGT00550000074396.
    HOVERGENiHBG045631.
    InParanoidiA2ABU8.
    KOiK11445.
    OMAiEIDLYHC.
    OrthoDBiEOG73JKV9.
    PhylomeDBiQ80TJ7.
    TreeFamiTF106480.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR003347. JmjC_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF02373. JmjC. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS51184. JMJC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q80TJ7-1) [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

    MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC     50
    PNCEVLHGPS IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD 100
    EVILKPTGSQ LTVEFLEENS FSVPILVLKK DGLGMTLPSP SFTVRDVEHY 150
    VGSDKEIDVI DVARQADCKM KLGDFVKYYY SGKREKVLNV ISLEFSDTRL 200
    SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR DSYTDFHIDF 250
    GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC 300
    YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE 350
    KRLSTADLFK FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL 400
    NLAFRAWTKK EALPDHEDEI PETVRTVQLI KDLAREIRLV EDIFQQNVGK 450
    TSNIFGLQRI FPAGSIPLTK PAHSTSVSMS KLSLPSKNGS KKKGLKPKDI 500
    FKKAERKGKQ SSALGPAGQL SYNLMDPYSH QALKTGPSQK AKFNMSGTSL 550
    NDSDDDSADM DLDGSENPLA LLMANGSTKR MKSVSKSRRA KIAKKVDSAR 600
    LVAEQVMGDE FDLDSDDELQ IDERLGKEKA NLLIRSKFPR KLPRAKPCSD 650
    PNRIREPGEV EFDIEEDYTT DEDMVEGVES KLGNGSGAGG ILDLLKASRQ 700
    VGGPDYAALT EAPASPSTQE AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG 750
    QERSSGSSSS GLGTVSSSPA SQRTPGKRPI KRPAYWKNES EEEENASLDE 800
    QDSLGACFKD AEYIYPSLES DDDDPALKSR PKKKKNSDDA PWSPKARVTP 850
    TLPKQDRPVR EGTRVASIET GLAAAAAKLA QQELQKAQKK KYIKKKPLLK 900
    EVEQPRPQDS NPIMTMPAPT VATTPQPDTS SSPQPPPEPK QEALSGSLAD 950
    HEYTARPNAF GMAQANRSTT PMAPGVFLTQ RRPSVGSQSS QAGQGKRPKK 1000
    GLATAKQRLG RILKIHRNGK LLL 1023
    Length:1,023
    Mass (Da):113,553
    Last modified:August 16, 2005 - v2
    Checksum:i7B9351944C000487
    GO
    Isoform 2 (identifier: Q80TJ7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         442-542: Missing.
         883-896: ELQKAQKKKYIKKK → VRVDTQLVALLLMT
         897-1023: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:795
    Mass (Da):88,919
    Checksum:iE14CF1810F1D3492
    GO
    Isoform 3 (identifier: Q80TJ7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         442-464: DIFQQNVGKTSNIFGLQRIFPAG → VRSMGEGKAFGKGWRLKWQVRTL
         465-1023: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:464
    Mass (Da):53,421
    Checksum:iA0A47C4A877F9291
    GO

    Sequence cautioni

    The sequence CAM17163.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei442 – 542101Missing in isoform 2. 1 PublicationVSP_014966Add
    BLAST
    Alternative sequencei442 – 46423DIFQQ…IFPAG → VRSMGEGKAFGKGWRLKWQV RTL in isoform 3. 1 PublicationVSP_014967Add
    BLAST
    Alternative sequencei465 – 1023559Missing in isoform 3. 1 PublicationVSP_014968Add
    BLAST
    Alternative sequencei883 – 89614ELQKA…YIKKK → VRVDTQLVALLLMT in isoform 2. 1 PublicationVSP_014969Add
    BLAST
    Alternative sequencei897 – 1023127Missing in isoform 2. 1 PublicationVSP_014970Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK036609 mRNA. Translation: BAC29505.1.
    AK040943 mRNA. Translation: BAC30755.2.
    AK040969 mRNA. Translation: BAC30763.1.
    AL662922 Genomic DNA. Translation: CAM17161.1.
    AL840642, AL662922 Genomic DNA. Translation: CAM15464.1.
    AL662922, AL840642 Genomic DNA. Translation: CAM17159.1.
    AL662922 Genomic DNA. Translation: CAM17163.1. Sequence problems.
    AK122447 mRNA. Translation: BAC65729.1.
    AF528164 Genomic DNA. Translation: AAO17385.1. Sequence problems.
    CCDSiCCDS30470.1. [Q80TJ7-2]
    CCDS53223.1. [Q80TJ7-1]
    RefSeqiNP_001009544.1. NM_001009544.2.
    NP_001106825.1. NM_001113354.1. [Q80TJ7-1]
    NP_796175.1. NM_177201.5. [Q80TJ7-2]
    XP_006528938.1. XM_006528875.1. [Q80TJ7-1]
    XP_006528939.1. XM_006528876.1. [Q80TJ7-1]
    XP_006528940.1. XM_006528877.1. [Q80TJ7-1]
    XP_006528943.1. XM_006528880.1. [Q80TJ7-1]
    UniGeneiMm.17156.
    Mm.84774.

    Genome annotation databases

    EnsembliENSMUST00000024121; ENSMUSP00000024121; ENSMUSG00000023350.
    ENSMUST00000046950; ENSMUSP00000040765; ENSMUSG00000041229. [Q80TJ7-1]
    ENSMUST00000046962; ENSMUSP00000041312; ENSMUSG00000041229. [Q80TJ7-2]
    ENSMUST00000112662; ENSMUSP00000108281; ENSMUSG00000041229. [Q80TJ7-2]
    ENSMUST00000112666; ENSMUSP00000108285; ENSMUSG00000041229. [Q80TJ7-3]
    ENSMUST00000168501; ENSMUSP00000127653; ENSMUSG00000041229. [Q80TJ7-1]
    GeneIDi320595.
    74042.
    KEGGimmu:320595.
    mmu:74042.
    UCSCiuc009upd.1. mouse. [Q80TJ7-3]
    uc009upe.1. mouse. [Q80TJ7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK036609 mRNA. Translation: BAC29505.1 .
    AK040943 mRNA. Translation: BAC30755.2 .
    AK040969 mRNA. Translation: BAC30763.1 .
    AL662922 Genomic DNA. Translation: CAM17161.1 .
    AL840642 , AL662922 Genomic DNA. Translation: CAM15464.1 .
    AL662922 , AL840642 Genomic DNA. Translation: CAM17159.1 .
    AL662922 Genomic DNA. Translation: CAM17163.1 . Sequence problems.
    AK122447 mRNA. Translation: BAC65729.1 .
    AF528164 Genomic DNA. Translation: AAO17385.1 . Sequence problems.
    CCDSi CCDS30470.1. [Q80TJ7-2 ]
    CCDS53223.1. [Q80TJ7-1 ]
    RefSeqi NP_001009544.1. NM_001009544.2.
    NP_001106825.1. NM_001113354.1. [Q80TJ7-1 ]
    NP_796175.1. NM_177201.5. [Q80TJ7-2 ]
    XP_006528938.1. XM_006528875.1. [Q80TJ7-1 ]
    XP_006528939.1. XM_006528876.1. [Q80TJ7-1 ]
    XP_006528940.1. XM_006528877.1. [Q80TJ7-1 ]
    XP_006528943.1. XM_006528880.1. [Q80TJ7-1 ]
    UniGenei Mm.17156.
    Mm.84774.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WEP NMR - A 1-63 [» ]
    ProteinModelPortali Q80TJ7.
    SMRi Q80TJ7. Positions 3-447.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL3038497.

    PTM databases

    PhosphoSitei Q80TJ7.

    Proteomic databases

    PaxDbi Q80TJ7.
    PRIDEi Q80TJ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024121 ; ENSMUSP00000024121 ; ENSMUSG00000023350 .
    ENSMUST00000046950 ; ENSMUSP00000040765 ; ENSMUSG00000041229 . [Q80TJ7-1 ]
    ENSMUST00000046962 ; ENSMUSP00000041312 ; ENSMUSG00000041229 . [Q80TJ7-2 ]
    ENSMUST00000112662 ; ENSMUSP00000108281 ; ENSMUSG00000041229 . [Q80TJ7-2 ]
    ENSMUST00000112666 ; ENSMUSP00000108285 ; ENSMUSG00000041229 . [Q80TJ7-3 ]
    ENSMUST00000168501 ; ENSMUSP00000127653 ; ENSMUSG00000041229 . [Q80TJ7-1 ]
    GeneIDi 320595.
    74042.
    KEGGi mmu:320595.
    mmu:74042.
    UCSCi uc009upd.1. mouse. [Q80TJ7-3 ]
    uc009upe.1. mouse. [Q80TJ7-1 ]

    Organism-specific databases

    CTDi 23133.
    MGIi MGI:2444341. Phf8.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG290496.
    GeneTreei ENSGT00550000074396.
    HOVERGENi HBG045631.
    InParanoidi A2ABU8.
    KOi K11445.
    OMAi EIDLYHC.
    OrthoDBi EOG73JKV9.
    PhylomeDBi Q80TJ7.
    TreeFami TF106480.

    Enzyme and pathway databases

    Reactomei REACT_196580. Condensation of Prophase Chromosomes.

    Miscellaneous databases

    EvolutionaryTracei Q80TJ7.
    NextBioi 339610.
    PROi Q80TJ7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q80TJ7.
    Bgeei Q80TJ7.
    CleanExi MM_PHF8.
    Genevestigatori Q80TJ7.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR003347. JmjC_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF02373. JmjC. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    SM00249. PHD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS51184. JMJC. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 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 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-490 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Bone.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
      DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-1023 (ISOFORM 1).
      Tissue: Brain.
    4. "Gene content of the 750-kb critical region for mouse embryonic ectoderm lethal tcl-w5."
      Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P., Nagaraja R.
      Mamm. Genome 15:265-276(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-899.
      Strain: 129/Sv.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615 AND SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Solution structure of PHD domain in protein AA017385."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: STRUCTURE BY NMR OF 1-66.

    Entry informationi

    Entry nameiPHF8_MOUSE
    AccessioniPrimary (citable) accession number: Q80TJ7
    Secondary accession number(s): A2ABU8
    , A2ABV0, A2ABV2, Q8BLX8, Q8BLY0, Q8BZ61, Q8CG26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: August 16, 2005
    Last modified: October 1, 2014
    This is version 97 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

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3