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Protein

Histone lysine demethylase PHF8

Gene

PHF8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Only has activity toward H4K20Me1 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 H3K4me3.10 Publications

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

Fe2+2 PublicationsNote: Binds 1 Fe2+ ion per subunit.2 Publications

Kineticsi

  1. KM=134 µM for histone H3 H3K9Me21 Publication
  2. KM=8 µM for histone H3 H3K4me3 and H3K9Me21 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei280 – 2801Substrate
    Metal bindingi283 – 2831Iron; catalyticPROSITE-ProRule annotation2 Publications
    Metal bindingi285 – 2851Iron; catalyticPROSITE-ProRule annotation2 Publications
    Binding sitei300 – 3001Substrate
    Metal bindingi355 – 3551Iron; catalyticPROSITE-ProRule annotation2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri41 – 9252PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    • chromatin binding Source: UniProtKB
    • histone demethylase activity Source: UniProtKB
    • histone demethylase activity (H3-K27 specific) Source: UniProtKB
    • histone demethylase activity (H3-K36 specific) Source: UniProtKB
    • histone demethylase activity (H3-K9 specific) Source: UniProtKB
    • histone demethylase activity (H4-K20 specific) Source: UniProtKB
    • iron ion binding Source: UniProtKB
    • methylated histone binding Source: UniProtKB
    • 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
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • brain development Source: UniProtKB
    • chromatin organization Source: Reactome
    • G1/S transition of mitotic cell cycle Source: UniProtKB
    • histone H3-K27 demethylation Source: UniProtKB
    • histone H3-K36 demethylation Source: UniProtKB
    • histone H3-K9 demethylation Source: UniProtKB
    • histone H4-K20 demethylation Source: UniProtKB
    • mitotic cell cycle Source: Reactome
    • negative regulation of chromatin silencing at rDNA Source: UniProtKB
    • positive regulation of transcription, DNA-templated Source: UniProtKB
    • positive regulation of transcription from RNA polymerase I promoter Source: UniProtKB
    • transcription, DNA-templated Source: UniProtKB-KW
    Complete GO annotation...

    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_263961. HDMs demethylate histones.
    REACT_264303. 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, ZNF422
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:20672. PHF8.

    Subcellular locationi

    • Nucleus
    • Nucleusnucleolus

    • Note: Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis.

    GO - Cellular componenti

    • nuclear membrane Source: HPA
    • nucleolus Source: UniProtKB
    • nucleoplasm Source: Reactome
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked, syndromic, Siderius type (MRXSSD)2 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA syndrome characterized by mild to borderline mental retardation with or without cleft lip/cleft palate.

    See also OMIM:300263
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti315 – 3151F → S in MRXSSD; abolishes histone methyltransferase activity. 8 Publications
    VAR_062250

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431Y → A: Abolishes binding to H3K4me3; when associated with A-50. 2 Publications
    Mutagenesisi50 – 501Y → A: Abolishes binding to H3K4me3; when associated with A-43. Abolishes binding to H3K4me3; when associated with A-65. 1 Publication
    Mutagenesisi65 – 651W → A: Abolishes binding to H3K4me3; when associated with A-50. 1 Publication
    Mutagenesisi69 – 691S → A: Impairs phosphorylation by CDK1 and dissociation from chromatin when cells enter mitosis; when associated with A-120. 1 Publication
    Mutagenesisi120 – 1201S → A: Impairs phosphorylation by CDK1 and dissociation from chromatin when cells enter mitosis; when associated with A-69. 1 Publication
    Mutagenesisi283 – 2853HID → AAA: Abolishes histone methyltransferase activity. 1 Publication
    Mutagenesisi283 – 2831H → A: Abolishes histone methyltransferase activity. 3 Publications

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300263. phenotype.
    Orphaneti85287. X-linked intellectual disability, Siderius type.
    PharmGKBiPA134889361.

    Polymorphism and mutation databases

    BioMutaiPHF8.
    DMDMi73620986.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10601060Histone lysine demethylase PHF8PRO_0000059295Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691Phosphoserine; by CDK11 Publication
    Modified residuei120 – 1201Phosphoserine; by CDK11 Publication
    Modified residuei651 – 6511Phosphoserine1 Publication
    Modified residuei705 – 7051Phosphothreonine2 Publications
    Modified residuei706 – 7061Phosphothreonine2 Publications
    Modified residuei804 – 8041Phosphoserine1 Publication
    Modified residuei854 – 8541Phosphoserine3 Publications
    Modified residuei857 – 8571Phosphoserine5 Publications
    Modified residuei880 – 8801Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylation at Ser-69 and Ser-120 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UPP1.
    PaxDbiQ9UPP1.
    PRIDEiQ9UPP1.

    PTM databases

    PhosphoSiteiQ9UPP1.

    Expressioni

    Gene expression databases

    BgeeiQ9UPP1.
    CleanExiHS_PHF8.
    ExpressionAtlasiQ9UPP1. baseline and differential.
    GenevisibleiQ9UPP1. HS.

    Organism-specific databases

    HPAiHPA038779.
    HPA062015.

    Interactioni

    Subunit structurei

    Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and ZNF711.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PML-RARQ151566EBI-6601215,EBI-867256
    RARAP102762EBI-6601215,EBI-413374

    Protein-protein interaction databases

    BioGridi116751. 32 interactions.
    DIPiDIP-38913N.
    IntActiQ9UPP1. 4 interactions.
    MINTiMINT-4651164.
    STRINGi9606.ENSP00000350676.

    Structurei

    Secondary structure

    1
    1060
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni44 – 474Combined sources
    Beta strandi56 – 583Combined sources
    Turni60 – 623Combined sources
    Beta strandi65 – 673Combined sources
    Helixi68 – 714Combined sources
    Helixi75 – 784Combined sources
    Beta strandi81 – 833Combined sources
    Helixi87 – 937Combined sources
    Helixi121 – 1299Combined sources
    Turni136 – 1383Combined sources
    Turni144 – 1463Combined sources
    Helixi149 – 1557Combined sources
    Beta strandi161 – 1655Combined sources
    Turni167 – 1704Combined sources
    Helixi180 – 1878Combined sources
    Beta strandi192 – 1976Combined sources
    Turni198 – 2014Combined sources
    Beta strandi202 – 2076Combined sources
    Helixi208 – 2158Combined sources
    Beta strandi224 – 2307Combined sources
    Helixi235 – 2384Combined sources
    Helixi244 – 2496Combined sources
    Helixi251 – 2555Combined sources
    Beta strandi270 – 2745Combined sources
    Beta strandi278 – 2836Combined sources
    Helixi286 – 2883Combined sources
    Beta strandi290 – 30516Combined sources
    Helixi309 – 31911Combined sources
    Helixi324 – 3263Combined sources
    Helixi329 – 3313Combined sources
    Beta strandi332 – 3343Combined sources
    Beta strandi337 – 3426Combined sources
    Beta strandi346 – 3494Combined sources
    Beta strandi354 – 37017Combined sources
    Beta strandi373 – 3753Combined sources
    Helixi376 – 38914Combined sources
    Helixi393 – 3953Combined sources
    Helixi400 – 42021Combined sources
    Helixi427 – 44418Combined sources
    Turni446 – 4483Combined sources
    Helixi449 – 4513Combined sources
    Helixi453 – 4553Combined sources
    Helixi462 – 47716Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WWUX-ray2.15A115-483[»]
    3K3NX-ray2.40A122-483[»]
    3K3OX-ray2.10A122-483[»]
    3KV4X-ray2.19A37-483[»]
    4DO0X-ray2.55A115-483[»]
    ProteinModelPortaliQ9UPP1.
    SMRiQ9UPP1. Positions 39-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UPP1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini231 – 387157JmjCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni101 – 11515LinkerAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi769 – 80739Ser-richAdd
    BLAST

    Domaini

    The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 promotes its access to H3K9me2.
    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.

    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 fingeri41 – 9252PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG290496.
    GeneTreeiENSGT00550000074396.
    HOGENOMiHOG000231232.
    HOVERGENiHBG045631.
    InParanoidiQ9UPP1.
    KOiK11445.
    OMAiLGTCFKD.
    PhylomeDBiQ9UPP1.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9UPP1-1) [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

            10         20         30         40         50
    MNRSRAIVQR GRVLPPPAPL DTTNLAGRRT LQGRAKMASV PVYCLCRLPY
    60 70 80 90 100
    DVTRFMIECD MCQDWFHGSC VGVEEEKAAD IDLYHCPNCE VLHGPSIMKK
    110 120 130 140 150
    RRGSSKGHDT HKGKPVKTGS PTFVRELRSR TFDSSDEVIL KPTGNQLTVE
    160 170 180 190 200
    FLEENSFSVP ILVLKKDGLG MTLPSPSFTV RDVEHYVGSD KEIDVIDVTR
    210 220 230 240 250
    QADCKMKLGD FVKYYYSGKR EKVLNVISLE FSDTRLSNLV ETPKIVRKLS
    260 270 280 290 300
    WVENLWPEEC VFERPNVQKY CLMSVRDSYT DFHIDFGGTS VWYHVLKGEK
    310 320 330 340 350
    IFYLIRPTNA NLTLFECWSS SSNQNEMFFG DQVDKCYKCS VKQGQTLFIP
    360 370 380 390 400
    TGWIHAVLTP VDCLAFGGNF LHSLNIEMQL KAYEIEKRLS TADLFRFPNF
    410 420 430 440 450
    ETICWYVGKH ILDIFRGLRE NRRHPASYLV HGGKALNLAF RAWTRKEALP
    460 470 480 490 500
    DHEDEIPETV RTVQLIKDLA REIRLVEDIF QQNVGKTSNI FGLQRIFPAG
    510 520 530 540 550
    SIPLTRPAHS TSVSMSRLSL PSKNGSKKKG LKPKELFKKA ERKGKESSAL
    560 570 580 590 600
    GPAGQLSYNL MDTYSHQALK TGSFQKAKFN ITGACLNDSD DDSPDLDLDG
    610 620 630 640 650
    NESPLALLMS NGSTKRVKSL SKSRRTKIAK KVDKARLMAE QVMEDEFDLD
    660 670 680 690 700
    SDDELQIDER LGKEKATLII RPKFPRKLPR AKPCSDPNRV REPGEVEFDI
    710 720 730 740 750
    EEDYTTDEDM VEGVEGKLGN GSGAGGILDL LKASRQVGGP DYAALTEAPA
    760 770 780 790 800
    SPSTQEAIQG MLCMANLQSS SSSPATSSLQ AWWTGGQDRS SGSSSSGLGT
    810 820 830 840 850
    VSNSPASQRT PGKRPIKRPA YWRTESEEEE ENASLDEQDS LGACFKDAEY
    860 870 880 890 900
    IYPSLESDDD DPALKSRPKK KKNSDDAPWS PKARVTPTLP KQDRPVREGT
    910 920 930 940 950
    RVASIETGLA AAAAKLAQQE LQKAQKKKYI KKKPLLKEVE QPRPQDSNLS
    960 970 980 990 1000
    LTVPAPTVAA TPQLVTSSSP LPPPEPKQEA LSGSLADHEY TARPNAFGMA
    1010 1020 1030 1040 1050
    QANRSTTPMA PGVFLTQRRP SVGSQSNQAG QGKRPKKGLA TAKQRLGRIL
    1060
    KIHRNGKLLL
    Length:1,060
    Mass (Da):117,864
    Last modified:August 16, 2005 - v3
    Checksum:i04C83D7C5E9E56B8
    GO
    Isoform 2 (identifier: Q9UPP1-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: Missing.

    Show »
    Length:1,024
    Mass (Da):113,913
    Checksum:i75773C0918578FB0
    GO
    Isoform 3 (identifier: Q9UPP1-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         478-578: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:959
    Mass (Da):106,902
    Checksum:iF54BE8A814BF1701
    GO
    Isoform 4 (identifier: Q9UPP1-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: Missing.
         478-578: Missing.
         1060-1060: L → LRQVIVQAECRQAIHEPKLKRRDAHP

    Note: No experimental confirmation available.
    Show »
    Length:948
    Mass (Da):105,913
    Checksum:iF32740CB7A2CE3F6
    GO
    Isoform 5 (identifier: Q9UPP1-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-36: Missing.
         717-746: KLGNGSGAGGILDLLKASRQVGGPDYAALT → YQTATPAPAQGAS
         920-931: ELQKAQKKKYIK → VKKMKLSLTDSG
         932-1060: Missing.

    Show »
    Length:878
    Mass (Da):98,290
    Checksum:i690CE764C0C28D28
    GO

    Sequence cautioni

    The sequence BAA83063.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAB13877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAI45929.1 differs from that shown. Reason: Erroneous termination at position 419. Translated as Arg.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti232 – 2321S → P in BAB13877 (PubMed:12168954).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti315 – 3151F → S in MRXSSD; abolishes histone methyltransferase activity. 8 Publications
    VAR_062250

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3636Missing in isoform 2, isoform 4 and isoform 5. 3 PublicationsVSP_014964Add
    BLAST
    Alternative sequencei478 – 578101Missing in isoform 3 and isoform 4. 1 PublicationVSP_014965Add
    BLAST
    Alternative sequencei717 – 74630KLGNG…YAALT → YQTATPAPAQGAS in isoform 5. 1 PublicationVSP_054019Add
    BLAST
    Alternative sequencei920 – 93112ELQKA…KKYIK → VKKMKLSLTDSG in isoform 5. 1 PublicationVSP_054020Add
    BLAST
    Alternative sequencei932 – 1060129Missing in isoform 5. 1 PublicationVSP_054021Add
    BLAST
    Alternative sequencei1060 – 10601L → LRQVIVQAECRQAIHEPKLK RRDAHP in isoform 4. 1 PublicationVSP_043640

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB029034 mRNA. Translation: BAA83063.1. Different initiation.
    CR933612 mRNA. Translation: CAI45929.1. Sequence problems.
    AK021696 mRNA. Translation: BAB13877.1. Different initiation.
    AK022788 mRNA. Translation: BAG51116.1.
    AK304272 mRNA. Translation: BAH14147.1.
    AL589872 Genomic DNA. No translation available.
    AL732374 Genomic DNA. No translation available.
    Z98051 Genomic DNA. No translation available.
    BC042108 mRNA. No translation available.
    BC053861 mRNA. Translation: AAH53861.1.
    CCDSiCCDS14355.1. [Q9UPP1-2]
    CCDS55418.1. [Q9UPP1-4]
    CCDS55419.1. [Q9UPP1-5]
    CCDS55420.1. [Q9UPP1-1]
    RefSeqiNP_001171825.1. NM_001184896.1. [Q9UPP1-1]
    NP_001171826.1. NM_001184897.1. [Q9UPP1-4]
    NP_055922.1. NM_015107.2. [Q9UPP1-2]
    UniGeneiHs.133352.

    Genome annotation databases

    EnsembliENST00000322659; ENSP00000319473; ENSG00000172943. [Q9UPP1-5]
    ENST00000338154; ENSP00000338868; ENSG00000172943. [Q9UPP1-2]
    ENST00000338946; ENSP00000340051; ENSG00000172943. [Q9UPP1-4]
    ENST00000357988; ENSP00000350676; ENSG00000172943.
    GeneIDi23133.
    KEGGihsa:23133.
    UCSCiuc004dst.3. human. [Q9UPP1-1]
    uc004dsw.3. human. [Q9UPP1-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB029034 mRNA. Translation: BAA83063.1. Different initiation.
    CR933612 mRNA. Translation: CAI45929.1. Sequence problems.
    AK021696 mRNA. Translation: BAB13877.1. Different initiation.
    AK022788 mRNA. Translation: BAG51116.1.
    AK304272 mRNA. Translation: BAH14147.1.
    AL589872 Genomic DNA. No translation available.
    AL732374 Genomic DNA. No translation available.
    Z98051 Genomic DNA. No translation available.
    BC042108 mRNA. No translation available.
    BC053861 mRNA. Translation: AAH53861.1.
    CCDSiCCDS14355.1. [Q9UPP1-2]
    CCDS55418.1. [Q9UPP1-4]
    CCDS55419.1. [Q9UPP1-5]
    CCDS55420.1. [Q9UPP1-1]
    RefSeqiNP_001171825.1. NM_001184896.1. [Q9UPP1-1]
    NP_001171826.1. NM_001184897.1. [Q9UPP1-4]
    NP_055922.1. NM_015107.2. [Q9UPP1-2]
    UniGeneiHs.133352.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WWUX-ray2.15A115-483[»]
    3K3NX-ray2.40A122-483[»]
    3K3OX-ray2.10A122-483[»]
    3KV4X-ray2.19A37-483[»]
    4DO0X-ray2.55A115-483[»]
    ProteinModelPortaliQ9UPP1.
    SMRiQ9UPP1. Positions 39-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116751. 32 interactions.
    DIPiDIP-38913N.
    IntActiQ9UPP1. 4 interactions.
    MINTiMINT-4651164.
    STRINGi9606.ENSP00000350676.

    Chemistry

    BindingDBiQ9UPP1.
    ChEMBLiCHEMBL1938212.
    GuidetoPHARMACOLOGYi2698.

    PTM databases

    PhosphoSiteiQ9UPP1.

    Polymorphism and mutation databases

    BioMutaiPHF8.
    DMDMi73620986.

    Proteomic databases

    MaxQBiQ9UPP1.
    PaxDbiQ9UPP1.
    PRIDEiQ9UPP1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000322659; ENSP00000319473; ENSG00000172943. [Q9UPP1-5]
    ENST00000338154; ENSP00000338868; ENSG00000172943. [Q9UPP1-2]
    ENST00000338946; ENSP00000340051; ENSG00000172943. [Q9UPP1-4]
    ENST00000357988; ENSP00000350676; ENSG00000172943.
    GeneIDi23133.
    KEGGihsa:23133.
    UCSCiuc004dst.3. human. [Q9UPP1-1]
    uc004dsw.3. human. [Q9UPP1-4]

    Organism-specific databases

    CTDi23133.
    GeneCardsiGC0XM053979.
    HGNCiHGNC:20672. PHF8.
    HPAiHPA038779.
    HPA062015.
    MIMi300263. phenotype.
    300560. gene.
    neXtProtiNX_Q9UPP1.
    Orphaneti85287. X-linked intellectual disability, Siderius type.
    PharmGKBiPA134889361.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG290496.
    GeneTreeiENSGT00550000074396.
    HOGENOMiHOG000231232.
    HOVERGENiHBG045631.
    InParanoidiQ9UPP1.
    KOiK11445.
    OMAiLGTCFKD.
    PhylomeDBiQ9UPP1.
    TreeFamiTF106480.

    Enzyme and pathway databases

    ReactomeiREACT_263961. HDMs demethylate histones.
    REACT_264303. Condensation of Prophase Chromosomes.

    Miscellaneous databases

    ChiTaRSiPHF8. human.
    EvolutionaryTraceiQ9UPP1.
    GeneWikiiPHF8.
    GenomeRNAii23133.
    NextBioi35468941.
    PROiQ9UPP1.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9UPP1.
    CleanExiHS_PHF8.
    ExpressionAtlasiQ9UPP1. baseline and differential.
    GenevisibleiQ9UPP1. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-927 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 515-1060 (ISOFORM 1).
      Tissue: Embryo, Teratocarcinoma and Trachea.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Endometrial tumor.
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 2 AND 5).
      Tissue: Brain and Cervix.
    7. Cited for: INVOLVEMENT IN MRXSSD.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-705; THR-706; SER-854; SER-857 AND SER-880, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; THR-705; THR-706; SER-854 AND SER-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis."
      Zhu Z., Wang Y., Li X., Wang Y., Xu L., Wang X., Sun T., Dong X., Chen L., Mao H., Yu Y., Li J., Chen P.A., Chen C.D.
      Cell Res. 20:794-801(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-283.
    13. "The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation."
      Qiu J., Shi G., Jia Y., Li J., Wu M., Li J., Dong S., Wong J.
      Cell Res. 20:908-918(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF VARIANT MRXSSD SER-315.
    14. "PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase."
      Loenarz C., Ge W., Coleman M.L., Rose N.R., Cooper C.D.O., Klose R.J., Ratcliffe P.J., Schofield C.J.
      Hum. Mol. Genet. 19:217-222(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
    15. "A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation."
      Kleine-Kohlbrecher D., Christensen J., Vandamme J., Abarrategui I., Bak M., Tommerup N., Shi X., Gozani O., Rappsilber J., Salcini A.E., Helin K.
      Mol. Cell 38:165-178(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN PHD-FINGER, INTERACTION WITH ZNF711, CHARACTERIZATION OF VARIANT MRXSSD SER-315, MUTAGENESIS OF HIS-283.
    16. "PHF8 targets histone methylation and RNA polymerase II to activate transcription."
      Fortschegger K., de Graaf P., Outchkourov N.S., van Schaik F.M., Timmers H.T., Shiekhattar R.
      Mol. Cell. Biol. 30:3286-3298(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN PHD-FINGER, CHARACTERIZATION OF VARIANT MRXSSD SER-315.
    17. "PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation."
      Feng W., Yonezawa M., Ye J., Jenuwein T., Grummt I.
      Nat. Struct. Mol. Biol. 17:445-450(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POLR1B AND UBTF, CHARACTERIZATION OF VARIANT MRXSSD SER-315, MUTAGENESIS OF TYR-43 AND 283-HIS--ASP-285.
    18. Cited for: FUNCTION, DOMAIN PHD-FINGER, CHARACTERIZATION OF VARIANT MRXSSD SER-315, MUTAGENESIS OF TYR-43; TYR-50 AND TRP-65.
    19. Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN PHD-FINGER, INTERACTION WITH SETD1A; HCFC1 AND E2F1, CHARACTERIZATION OF VARIANT MRXSSD SER-315, PHOSPHORYLATION AT SER-69 AND SER-120, MUTAGENESIS OF SER-69; SER-120 AND HIS-283.
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-804; SER-857 AND SER-880, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854; SER-857 AND SER-880, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Structural insights into a novel histone demethylase PHF8."
      Yu L., Wang Y., Huang S., Wang J., Deng Z., Zhang Q., Wu W., Zhang X., Liu Z., Gong W., Chen Z.
      Cell Res. 20:166-173(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 122-483 IN COMPLEX WITH IRON AND ALPHA-KETOGLUTARATE, FUNCTION, CHARACTERIZATION OF VARIANT MRXSSD SER-315.
    24. "Crystal structure of the PHF8 Jumonji domain, an N(epsilon)-methyl lysine demethylase."
      Yue W.W., Hozjan V., Ge W., Loenarz C., Cooper C.D., Schofield C.J., Kavanagh K.L., Oppermann U., McDonough M.A.
      FEBS Lett. 584:825-830(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 115-483.
    25. "Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases."
      Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X.
      Nat. Struct. Mol. Biol. 17:38-43(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-447 IN COMPLEX WITH IRON AND N-OXALYLGLYCINE, ZINC-BINDING, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DOMAIN LINKER AND PHD-FINGER.
    26. "Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate."
      Koivisto A.M., Ala-Mello S., Lemmelae S., Komu H.A., Rautio J., Jaervelae I.
      Clin. Genet. 72:145-149(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MRXSSD SER-315.

    Entry informationi

    Entry nameiPHF8_HUMAN
    AccessioniPrimary (citable) accession number: Q9UPP1
    Secondary accession number(s): B3KMV4
    , B7Z911, Q5H9U5, Q5JPR9, Q5JPS0, Q5JPS2, Q5JPS3, Q5VUJ4, Q7Z6D4, Q9HAH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: August 16, 2005
    Last modified: July 22, 2015
    This is version 128 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.