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O75151

- PHF2_HUMAN

UniProt

O75151 - PHF2_HUMAN

Protein

Lysine-specific demethylase PHF2

Gene

PHF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA.3 Publications

    Enzyme regulationi

    Enzymatically inactive by itself, and become active following phosphorylation by PKA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei193 – 1931Alpha-ketoglutarate
    Binding sitei246 – 2461Alpha-ketoglutarate
    Metal bindingi249 – 2491Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi251 – 2511Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Binding sitei259 – 2591Alpha-ketoglutarate
    Binding sitei266 – 2661Alpha-ketoglutarate
    Metal bindingi321 – 3211Iron; catalytic1 PublicationPROSITE-ProRule annotation
    Binding sitei321 – 3211Alpha-ketoglutarate
    Binding sitei323 – 3231Alpha-ketoglutarate

    Regions

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

    GO - Molecular functioni

    1. dioxygenase activity Source: UniProtKB-KW
    2. histone demethylase activity (H3-K9 specific) Source: UniProtKB
    3. iron ion binding Source: UniProtKB
    4. methylated histone binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. liver development Source: UniProtKB
    2. negative regulation of chromatin silencing at rDNA Source: UniProtKB
    3. protein demethylation Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysine-specific demethylase PHF2 (EC:1.14.11.-)
    Alternative name(s):
    GRC5
    PHD finger protein 2
    Gene namesi
    Name:PHF2
    Synonyms:KIAA0662
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8920. PHF2.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleolus Source: UniProtKB
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71Y → A: Abolishes binding to H3K4me2 and H3K4me3. 1 Publication
    Mutagenesisi29 – 291W → A: Abolishes binding to H3K4me2 and H3K4me3. 1 Publication
    Mutagenesisi249 – 2491H → A: Abolishes demethylase activity. 1 Publication
    Mutagenesisi321 – 3211Y → H: Does not alter iron-binding nor activates histone demethylase activity. 1 Publication
    Mutagenesisi757 – 7571S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-899; A-954 and A-1056. 1 Publication
    Mutagenesisi899 – 8991S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-954 and A-1056. 1 Publication
    Mutagenesisi954 – 9541S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-1056. 1 Publication
    Mutagenesisi1056 – 10561S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-954. 1 Publication

    Organism-specific databases

    PharmGKBiPA33260.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10961096Lysine-specific demethylase PHF2PRO_0000059290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei474 – 4741Phosphoserine2 Publications
    Modified residuei479 – 4791Phosphothreonine2 Publications
    Modified residuei539 – 5391Phosphoserine2 Publications
    Modified residuei705 – 7051Phosphoserine3 Publications
    Modified residuei720 – 7201N6-acetyllysineBy similarity
    Modified residuei882 – 8821Phosphoserine4 Publications
    Modified residuei1056 – 10561Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Phosphorylated by PKA on specific serine residues, leading to the formation of an active lysine demethylase complex.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75151.
    PaxDbiO75151.
    PRIDEiO75151.

    PTM databases

    PhosphoSiteiO75151.

    Expressioni

    Tissue specificityi

    Widely expressed, including in liver (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiO75151.
    BgeeiO75151.
    CleanExiHS_PHF2.
    GenevestigatoriO75151.

    Organism-specific databases

    HPAiHPA010831.

    Interactioni

    Subunit structurei

    Component of the PHF2-ARID5B complex, at least composed of PHF2 and ARID5B. Interacts with HNF4A and NR1H4.3 Publications

    Protein-protein interaction databases

    BioGridi111272. 3 interactions.
    STRINGi9606.ENSP00000352185.

    Structurei

    Secondary structure

    1
    1096
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 114
    Beta strandi20 – 223
    Turni24 – 263
    Beta strandi29 – 313
    Helixi32 – 354
    Turni39 – 413
    Helixi42 – 443
    Beta strandi45 – 473
    Helixi51 – 577
    Helixi87 – 959
    Helixi101 – 1033
    Beta strandi105 – 1073
    Helixi110 – 1123
    Helixi115 – 1217
    Beta strandi127 – 1315
    Turni133 – 1364
    Helixi146 – 1538
    Beta strandi158 – 1636
    Turni164 – 1663
    Beta strandi169 – 1735
    Helixi174 – 1818
    Beta strandi190 – 1967
    Helixi201 – 2055
    Helixi210 – 2156
    Helixi217 – 2215
    Beta strandi236 – 2405
    Beta strandi245 – 2495
    Helixi252 – 2543
    Beta strandi256 – 27116
    Helixi275 – 28612
    Helixi290 – 2923
    Helixi295 – 2984
    Beta strandi303 – 3086
    Beta strandi312 – 3154
    Beta strandi320 – 33617
    Helixi339 – 3413
    Helixi342 – 35514
    Beta strandi359 – 3613
    Helixi366 – 38722
    Helixi393 – 40917
    Turni412 – 4143
    Helixi415 – 4184
    Helixi419 – 4213
    Helixi428 – 44316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KQIX-ray1.78A1-70[»]
    3PTRX-ray1.95B60-451[»]
    3PU3X-ray1.95A/B60-451[»]
    3PU8X-ray1.94A/B60-451[»]
    3PUAX-ray1.89A60-451[»]
    3PUSX-ray2.08A/B60-451[»]
    ProteinModelPortaliO75151.
    SMRiO75151. Positions 1-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75151.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini197 – 353157JmjCPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi472 – 51847Pro-richAdd
    BLAST
    Compositional biasi487 – 648162Lys-richAdd
    BLAST
    Compositional biasi960 – 102061Ser/Thr-richAdd
    BLAST

    Domaini

    The PHD-type zinc finger mediates the binding to H3K4me2 and H3K4me3.1 Publication

    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.
    HOGENOMiHOG000231232.
    HOVERGENiHBG045631.
    InParanoidiO75151.
    KOiK11445.
    OMAiKYKNSKP.
    OrthoDBiEOG73JKV9.
    PhylomeDBiO75151.
    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]

    Sequencei

    Sequence statusi: Complete.

    O75151-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATVPVYCVC RLPYDVTRFM IECDACKDWF HGSCVGVEEE EAPDIDIYHC     50
    PNCEKTHGKS TLKKKRTWHK HGPGQAPDVK PVQNGSQLFI KELRSRTFPS 100
    AEDVVARVPG SQLTLGYMEE HGFTEPILVP KKDGLGLAVP APTFYVSDVE 150
    NYVGPERSVD VTDVTKQKDC KMKLKEFVDY YYSTNRKRVL NVTNLEFSDT 200
    RMSSFVEPPD IVKKLSWVEN YWPDDALLAK PKVTKYCLIC VKDSYTDFHI 250
    DSGGASAWYH VLKGEKTFYL IRPASANISL YERWRSASNH SEMFFADQVD 300
    KCYKCIVKQG QTLFIPSGWI YATLTPVDCL AFAGHFLHSL SVEMQMRAYE 350
    VERRLKLGSL TQFPNFETAC WYMGKHLLEA FKGSHKSGKQ LPPHLVQGAK 400
    ILNGAFRSWT KKQALAEHED ELPEHFKPSQ LIKDLAKEIR LSENASKAVR 450
    PEVNTVASSD EVCDGDREKE EPPSPIEATP PQSLLEKVSK KKTPKTVKMP 500
    KPSKIPKPPK PPKPPRPPKT LKLKDGGKKK GKKSRESASP TIPNLDLLEA 550
    HTKEALTKME PPKKGKATKS VLSVPNKDVV HMQNDVERLE IREQTKSKSE 600
    AKWKYKNSKP DSLLKMEEEQ KLEKSPLAGN KDNKFSFSFS NKKLLGSKAL 650
    RPPTSPGVFG ALQNFKEDKP KPVRDEYEYV SDDGELKIDE FPIRRKKNAP 700
    KRDLSFLLDK KAVLPTPVTK PKLDSAAYKS DDSSDEGSLH IDTDTKPGRN 750
    ARVKKESGSS AAGILDLLQA SEEVGALEYN PSSQPPASPS TQEAIQGMLS 800
    MANLQASDSC LQTTWGAGQA KGSSLAAHGA RKNGGGSGKS AGKRLLKRAA 850
    KNSVDLDDYE EEQDHLDACF KDSDYVYPSL ESDEDNPIFK SRSKKRKGSD 900
    DAPYSPTARV GPSVPRQDRP VREGTRVASI ETGLAAAAAK LSQQEEQKSK 950
    KKKSAKRKLT PNTTSPSTST SISAGTTSTS TTPASTTPAS TTPASTSTAS 1000
    SQASQEGSSP EPPPESHSSS LADHEYTAAG TFTGAQAGRT SQPMAPGVFL 1050
    TQRRPSASSP NNNTAAKGKR TKKGMATAKQ RLGKILKIHR NGKLLL 1096
    Length:1,096
    Mass (Da):120,775
    Last modified:November 25, 2008 - v4
    Checksum:iDD088363DB76674D
    GO

    Sequence cautioni

    The sequence BAA31637.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 4123FMIEC…VEEEE → PRAARPPARPGPTRAAQRRG RAT in BAA31637. (PubMed:9734811)CuratedAdd
    BLAST
    Sequence conflicti75 – 762QA → PT in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti100 – 1001S → R in BAA31637. (PubMed:9734811)Curated
    Sequence conflicti106 – 1061A → S in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti115 – 1151L → V in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti621 – 6211K → R in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti633 – 6331Missing in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti642 – 6421K → R in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti654 – 6541T → S in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti664 – 6641N → S in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti670 – 6701P → A in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti698 – 6981N → S in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti712 – 7198AVLPTPVT → EALLMPTS in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti727 – 7271A → V in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti752 – 7521R → K in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti782 – 7821S → N in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti817 – 8171A → T in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti823 – 8231S → G in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti833 – 8331N → I in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti837 – 8415SGKSA → NKGT in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti849 – 8491A → T in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti857 – 8571D → E in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti862 – 8621Missing in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti888 – 8881I → V in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti949 – 9502SK → NR in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti954 – 9552SA → NT in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti959 – 9602LT → PA in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti964 – 9641T → A in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti968 – 9681T → I in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti972 – 9721I → ASASTGTT in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti975 – 9751G → S in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti978 – 9792ST → PA in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti996 – 9961T → TTPAST in BAA31637. (PubMed:9734811)Curated
    Sequence conflicti996 – 9961T → TTPAST in CAD38938. (PubMed:17974005)Curated
    Sequence conflicti1033 – 10353TGA → SGS in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti1040 – 10401T → A in AAD21791. (PubMed:10051327)Curated
    Sequence conflicti1063 – 10631Missing in AAD21791. (PubMed:10051327)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561T → P.
    Corresponds to variant rs34279404 [ dbSNP | Ensembl ].
    VAR_047553
    Natural varianti1058 – 10581S → L.
    Corresponds to variant rs35236745 [ dbSNP | Ensembl ].
    VAR_051598

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043725 mRNA. Translation: AAD21791.1.
    AB014562 mRNA. Translation: BAA31637.2. Different initiation.
    AL353629, AL359181 Genomic DNA. Translation: CAI96110.1.
    AL359181, AL353629 Genomic DNA. Translation: CAI96111.1.
    CH471089 Genomic DNA. Translation: EAW62867.1.
    AL834263 mRNA. Translation: CAD38938.1.
    CCDSiCCDS35069.1.
    PIRiT00369.
    RefSeqiNP_005383.3. NM_005392.3.
    UniGeneiHs.211441.

    Genome annotation databases

    EnsembliENST00000359246; ENSP00000352185; ENSG00000197724.
    GeneIDi5253.
    KEGGihsa:5253.
    UCSCiuc004aub.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043725 mRNA. Translation: AAD21791.1 .
    AB014562 mRNA. Translation: BAA31637.2 . Different initiation.
    AL353629 , AL359181 Genomic DNA. Translation: CAI96110.1 .
    AL359181 , AL353629 Genomic DNA. Translation: CAI96111.1 .
    CH471089 Genomic DNA. Translation: EAW62867.1 .
    AL834263 mRNA. Translation: CAD38938.1 .
    CCDSi CCDS35069.1.
    PIRi T00369.
    RefSeqi NP_005383.3. NM_005392.3.
    UniGenei Hs.211441.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KQI X-ray 1.78 A 1-70 [» ]
    3PTR X-ray 1.95 B 60-451 [» ]
    3PU3 X-ray 1.95 A/B 60-451 [» ]
    3PU8 X-ray 1.94 A/B 60-451 [» ]
    3PUA X-ray 1.89 A 60-451 [» ]
    3PUS X-ray 2.08 A/B 60-451 [» ]
    ProteinModelPortali O75151.
    SMRi O75151. Positions 1-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111272. 3 interactions.
    STRINGi 9606.ENSP00000352185.

    PTM databases

    PhosphoSitei O75151.

    Proteomic databases

    MaxQBi O75151.
    PaxDbi O75151.
    PRIDEi O75151.

    Protocols and materials databases

    DNASUi 5253.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359246 ; ENSP00000352185 ; ENSG00000197724 .
    GeneIDi 5253.
    KEGGi hsa:5253.
    UCSCi uc004aub.3. human.

    Organism-specific databases

    CTDi 5253.
    GeneCardsi GC09P096338.
    H-InvDB HIX0008184.
    HGNCi HGNC:8920. PHF2.
    HPAi HPA010831.
    MIMi 604351. gene.
    neXtProti NX_O75151.
    PharmGKBi PA33260.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290496.
    HOGENOMi HOG000231232.
    HOVERGENi HBG045631.
    InParanoidi O75151.
    KOi K11445.
    OMAi KYKNSKP.
    OrthoDBi EOG73JKV9.
    PhylomeDBi O75151.
    TreeFami TF106480.

    Miscellaneous databases

    EvolutionaryTracei O75151.
    GenomeRNAii 5253.
    NextBioi 20296.
    PROi O75151.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75151.
    Bgeei O75151.
    CleanExi HS_PHF2.
    Genevestigatori O75151.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "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.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1096.
      Tissue: Amygdala.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-882, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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].
    10. "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-882, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-474; THR-479; SER-705 AND SER-882, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "PKA-dependent regulation of the histone lysine demethylase complex PHF2-ARID5B."
      Baba A., Ohtake F., Okuno Y., Yokota K., Okada M., Imai Y., Ni M., Meyer C.A., Igarashi K., Kanno J., Brown M., Kato S.
      Nat. Cell Biol. 13:668-675(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION BY PKA, PHOSPHORYLATION AT SER-1056, INTERACTION WITH ARID5B; HNF4A AND NR1H4, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, IDENTIFICATION IN THE PHF2-ARID5B COMPLEX, MUTAGENESIS OF HIS-249; SER-757; SER-899; SER-954 AND SER-1056.
    13. "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-705, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation."
      Wen H., Li J., Song T., Lu M., Kan P.Y., Lee M.G., Sha B., Shi X.
      J. Biol. Chem. 285:9322-9326(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 1-70 IN COMPLEX WITH ZINC, DOMAIN PHD-TYPE ZINC-FINGER, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-7 AND TRP-29.
    15. "Structural basis for human PHF2 Jumonji domain interaction with metal ions."
      Horton J.R., Upadhyay A.K., Hashimoto H., Zhang X., Cheng X.
      J. Mol. Biol. 406:1-8(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 60-451 IN COMPLEX WITH IRON AND N-OXALYLGLYCINE, FUNCTION, MUTAGENESIS OF TYR-321.

    Entry informationi

    Entry nameiPHF2_HUMAN
    AccessioniPrimary (citable) accession number: O75151
    Secondary accession number(s): Q4VXG0, Q8N3K2, Q9Y6N4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 112 of the entry and version 4 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

    Caution

    In contrast to the related histone demethylases JHDM1D and PHF8, the conserved active His in position 321 is replaced by a Tyr. However, the presence of a Tyr residue neither affects binding to the catalytic iron nor abolishes demethylase activity (PubMed:21167174).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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