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O75151

- PHF2_HUMAN

UniProt

O75151 - PHF2_HUMAN

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Protein

Lysine-specific demethylase PHF2

Gene
PHF2, KIAA0662
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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; catalytic
Metal bindingi251 – 2511Iron; catalytic
Binding sitei259 – 2591Alpha-ketoglutarate
Binding sitei266 – 2661Alpha-ketoglutarate
Metal bindingi321 – 3211Iron; catalytic
Binding sitei321 – 3211Alpha-ketoglutarate
Binding sitei323 – 3231Alpha-ketoglutarate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri5 – 5652PHD-typeAdd
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
Complete GO annotation...

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
Complete GO annotation...

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 – 4741Phosphoserine1 Publication
Modified residuei479 – 4791Phosphothreonine1 Publication
Modified residuei539 – 5391Phosphoserine1 Publication
Modified residuei705 – 7051Phosphoserine2 Publications
Modified residuei720 – 7201N6-acetyllysine By similarity
Modified residuei882 – 8821Phosphoserine3 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.1 Publication

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 NR1H4.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiO75151.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 353157JmjCAdd
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.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri5 – 5652PHD-typeAdd
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

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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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 4123FMIEC…VEEEE → PRAARPPARPGPTRAAQRRG RAT in BAA31637. 1 PublicationAdd
BLAST
Sequence conflicti75 – 762QA → PT in AAD21791. 1 Publication
Sequence conflicti100 – 1001S → R in BAA31637. 1 Publication
Sequence conflicti106 – 1061A → S in AAD21791. 1 Publication
Sequence conflicti115 – 1151L → V in AAD21791. 1 Publication
Sequence conflicti621 – 6211K → R in AAD21791. 1 Publication
Sequence conflicti633 – 6331Missing in AAD21791. 1 Publication
Sequence conflicti642 – 6421K → R in AAD21791. 1 Publication
Sequence conflicti654 – 6541T → S in AAD21791. 1 Publication
Sequence conflicti664 – 6641N → S in AAD21791. 1 Publication
Sequence conflicti670 – 6701P → A in AAD21791. 1 Publication
Sequence conflicti698 – 6981N → S in AAD21791. 1 Publication
Sequence conflicti712 – 7198AVLPTPVT → EALLMPTS in AAD21791. 1 Publication
Sequence conflicti727 – 7271A → V in AAD21791. 1 Publication
Sequence conflicti752 – 7521R → K in AAD21791. 1 Publication
Sequence conflicti782 – 7821S → N in AAD21791. 1 Publication
Sequence conflicti817 – 8171A → T in AAD21791. 1 Publication
Sequence conflicti823 – 8231S → G in AAD21791. 1 Publication
Sequence conflicti833 – 8331N → I in AAD21791. 1 Publication
Sequence conflicti837 – 8415SGKSA → NKGT in AAD21791. 1 Publication
Sequence conflicti849 – 8491A → T in AAD21791. 1 Publication
Sequence conflicti857 – 8571D → E in AAD21791. 1 Publication
Sequence conflicti862 – 8621Missing in AAD21791. 1 Publication
Sequence conflicti888 – 8881I → V in AAD21791. 1 Publication
Sequence conflicti949 – 9502SK → NR in AAD21791. 1 Publication
Sequence conflicti954 – 9552SA → NT in AAD21791. 1 Publication
Sequence conflicti959 – 9602LT → PA in AAD21791. 1 Publication
Sequence conflicti964 – 9641T → A in AAD21791. 1 Publication
Sequence conflicti968 – 9681T → I in AAD21791. 1 Publication
Sequence conflicti972 – 9721I → ASASTGTT in AAD21791. 1 Publication
Sequence conflicti975 – 9751G → S in AAD21791. 1 Publication
Sequence conflicti978 – 9792ST → PA in AAD21791. 1 Publication
Sequence conflicti996 – 9961T → TTPAST in BAA31637. 1 Publication
Sequence conflicti996 – 9961T → TTPAST in CAD38938. 1 Publication
Sequence conflicti1033 – 10353TGA → SGS in AAD21791. 1 Publication
Sequence conflicti1040 – 10401T → A in AAD21791. 1 Publication
Sequence conflicti1063 – 10631Missing in AAD21791. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 111 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 (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

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