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O75151 (PHF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysine-specific demethylase PHF2

EC=1.14.11.-
Alternative name(s):
GRC5
PHD finger protein 2
Gene names
Name:PHF2
Synonyms:KIAA0662
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1096 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.14 Ref.15

Enzyme regulation

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

Subunit structure

Component of the PHF2-ARID5B complex, at least composed of PHF2 and ARID5B. Interacts with HNF4A and NR1H4. Ref.12

Subcellular location

Nucleusnucleolus Ref.14.

Tissue specificity

Widely expressed, including in liver (at protein level). Ref.12

Domain

The PHD-type zinc finger mediates the binding to H3K4me2 and H3K4me3. Ref.14

Post-translational modification

Phosphorylated by PKA on specific serine residues, leading to the formation of an active lysine demethylase complex. Ref.12

Sequence similarities

Belongs to the JHDM1 histone demethylase family. JHDM1D subfamily.

Contains 1 JmjC domain.

Contains 1 PHD-type zinc finger.

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 (Ref.15).

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10961096Lysine-specific demethylase PHF2
PRO_0000059290

Regions

Domain197 – 353157JmjC
Zinc finger5 – 5652PHD-type
Compositional bias472 – 51847Pro-rich
Compositional bias487 – 648162Lys-rich
Compositional bias960 – 102061Ser/Thr-rich

Sites

Metal binding2491Iron; catalytic
Metal binding2511Iron; catalytic
Metal binding3211Iron; catalytic
Binding site1931Alpha-ketoglutarate
Binding site2461Alpha-ketoglutarate
Binding site2591Alpha-ketoglutarate
Binding site2661Alpha-ketoglutarate
Binding site3211Alpha-ketoglutarate
Binding site3231Alpha-ketoglutarate

Amino acid modifications

Modified residue4741Phosphoserine Ref.11
Modified residue4791Phosphothreonine Ref.11
Modified residue5391Phosphoserine Ref.8
Modified residue7051Phosphoserine Ref.11 Ref.13
Modified residue7201N6-acetyllysine By similarity
Modified residue8821Phosphoserine Ref.8 Ref.10 Ref.11
Modified residue10561Phosphoserine; by PKA Ref.12

Natural variations

Natural variant561T → P.
Corresponds to variant rs34279404 [ dbSNP | Ensembl ].
VAR_047553
Natural variant10581S → L.
Corresponds to variant rs35236745 [ dbSNP | Ensembl ].
VAR_051598

Experimental info

Mutagenesis71Y → A: Abolishes binding to H3K4me2 and H3K4me3. Ref.14
Mutagenesis291W → A: Abolishes binding to H3K4me2 and H3K4me3. Ref.14
Mutagenesis2491H → A: Abolishes demethylase activity. Ref.12
Mutagenesis3211Y → H: Does not alter iron-binding nor activates histone demethylase activity. Ref.15
Mutagenesis7571S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-899; A-954 and A-1056. Ref.12
Mutagenesis8991S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-954 and A-1056. Ref.12
Mutagenesis9541S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-1056. Ref.12
Mutagenesis10561S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-954. Ref.12
Sequence conflict19 – 4123FMIEC…VEEEE → PRAARPPARPGPTRAAQRRG RAT in BAA31637. Ref.2
Sequence conflict75 – 762QA → PT in AAD21791. Ref.1
Sequence conflict1001S → R in BAA31637. Ref.2
Sequence conflict1061A → S in AAD21791. Ref.1
Sequence conflict1151L → V in AAD21791. Ref.1
Sequence conflict6211K → R in AAD21791. Ref.1
Sequence conflict6331Missing in AAD21791. Ref.1
Sequence conflict6421K → R in AAD21791. Ref.1
Sequence conflict6541T → S in AAD21791. Ref.1
Sequence conflict6641N → S in AAD21791. Ref.1
Sequence conflict6701P → A in AAD21791. Ref.1
Sequence conflict6981N → S in AAD21791. Ref.1
Sequence conflict712 – 7198AVLPTPVT → EALLMPTS in AAD21791. Ref.1
Sequence conflict7271A → V in AAD21791. Ref.1
Sequence conflict7521R → K in AAD21791. Ref.1
Sequence conflict7821S → N in AAD21791. Ref.1
Sequence conflict8171A → T in AAD21791. Ref.1
Sequence conflict8231S → G in AAD21791. Ref.1
Sequence conflict8331N → I in AAD21791. Ref.1
Sequence conflict837 – 8415SGKSA → NKGT in AAD21791. Ref.1
Sequence conflict8491A → T in AAD21791. Ref.1
Sequence conflict8571D → E in AAD21791. Ref.1
Sequence conflict8621Missing in AAD21791. Ref.1
Sequence conflict8881I → V in AAD21791. Ref.1
Sequence conflict949 – 9502SK → NR in AAD21791. Ref.1
Sequence conflict954 – 9552SA → NT in AAD21791. Ref.1
Sequence conflict959 – 9602LT → PA in AAD21791. Ref.1
Sequence conflict9641T → A in AAD21791. Ref.1
Sequence conflict9681T → I in AAD21791. Ref.1
Sequence conflict9721I → ASASTGTT in AAD21791. Ref.1
Sequence conflict9751G → S in AAD21791. Ref.1
Sequence conflict978 – 9792ST → PA in AAD21791. Ref.1
Sequence conflict9961T → TTPAST in BAA31637. Ref.2
Sequence conflict9961T → TTPAST in CAD38938. Ref.6
Sequence conflict1033 – 10353TGA → SGS in AAD21791. Ref.1
Sequence conflict10401T → A in AAD21791. Ref.1
Sequence conflict10631Missing in AAD21791. Ref.1

Secondary structure

................................................................................. 1096
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75151 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: DD088363DB76674D

FASTA1,096120,775
        10         20         30         40         50         60 
MATVPVYCVC RLPYDVTRFM IECDACKDWF HGSCVGVEEE EAPDIDIYHC PNCEKTHGKS 

        70         80         90        100        110        120 
TLKKKRTWHK HGPGQAPDVK PVQNGSQLFI KELRSRTFPS AEDVVARVPG SQLTLGYMEE 

       130        140        150        160        170        180 
HGFTEPILVP KKDGLGLAVP APTFYVSDVE NYVGPERSVD VTDVTKQKDC KMKLKEFVDY 

       190        200        210        220        230        240 
YYSTNRKRVL NVTNLEFSDT RMSSFVEPPD IVKKLSWVEN YWPDDALLAK PKVTKYCLIC 

       250        260        270        280        290        300 
VKDSYTDFHI DSGGASAWYH VLKGEKTFYL IRPASANISL YERWRSASNH SEMFFADQVD 

       310        320        330        340        350        360 
KCYKCIVKQG QTLFIPSGWI YATLTPVDCL AFAGHFLHSL SVEMQMRAYE VERRLKLGSL 

       370        380        390        400        410        420 
TQFPNFETAC WYMGKHLLEA FKGSHKSGKQ LPPHLVQGAK ILNGAFRSWT KKQALAEHED 

       430        440        450        460        470        480 
ELPEHFKPSQ LIKDLAKEIR LSENASKAVR PEVNTVASSD EVCDGDREKE EPPSPIEATP 

       490        500        510        520        530        540 
PQSLLEKVSK KKTPKTVKMP KPSKIPKPPK PPKPPRPPKT LKLKDGGKKK GKKSRESASP 

       550        560        570        580        590        600 
TIPNLDLLEA HTKEALTKME PPKKGKATKS VLSVPNKDVV HMQNDVERLE IREQTKSKSE 

       610        620        630        640        650        660 
AKWKYKNSKP DSLLKMEEEQ KLEKSPLAGN KDNKFSFSFS NKKLLGSKAL RPPTSPGVFG 

       670        680        690        700        710        720 
ALQNFKEDKP KPVRDEYEYV SDDGELKIDE FPIRRKKNAP KRDLSFLLDK KAVLPTPVTK 

       730        740        750        760        770        780 
PKLDSAAYKS DDSSDEGSLH IDTDTKPGRN ARVKKESGSS AAGILDLLQA SEEVGALEYN 

       790        800        810        820        830        840 
PSSQPPASPS TQEAIQGMLS MANLQASDSC LQTTWGAGQA KGSSLAAHGA RKNGGGSGKS 

       850        860        870        880        890        900 
AGKRLLKRAA KNSVDLDDYE EEQDHLDACF KDSDYVYPSL ESDEDNPIFK SRSKKRKGSD 

       910        920        930        940        950        960 
DAPYSPTARV GPSVPRQDRP VREGTRVASI ETGLAAAAAK LSQQEEQKSK KKKSAKRKLT 

       970        980        990       1000       1010       1020 
PNTTSPSTST SISAGTTSTS TTPASTTPAS TTPASTSTAS SQASQEGSSP EPPPESHSSS 

      1030       1040       1050       1060       1070       1080 
LADHEYTAAG TFTGAQAGRT SQPMAPGVFL TQRRPSASSP NNNTAAKGKR TKKGMATAKQ 

      1090 
RLGKILKIHR NGKLLL 

« Hide

References

« Hide 'large scale' references
[1]"PHF2, a novel PHD finger gene located on human chromosome 9q22."
Hasenpusch-Theil K., Chadwick B.P., Theil T., Heath S.K., Wilkinson D.G., Frischauf A.M.
Mamm. Genome 10:294-298(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT00369.
RefSeqNP_005383.3. NM_005392.3.
UniGeneHs.211441.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO75151.
SMRO75151. Positions 1-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111272. 3 interactions.
STRING9606.ENSP00000352185.

PTM databases

PhosphoSiteO75151.

Proteomic databases

PaxDbO75151.
PRIDEO75151.

Protocols and materials databases

DNASU5253.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359246; ENSP00000352185; ENSG00000197724.
GeneID5253.
KEGGhsa:5253.
UCSCuc004aub.3. human.

Organism-specific databases

CTD5253.
GeneCardsGC09P096338.
H-InvDBHIX0008184.
HGNCHGNC:8920. PHF2.
HPAHPA010831.
MIM604351. gene.
neXtProtNX_O75151.
PharmGKBPA33260.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290496.
HOGENOMHOG000231232.
HOVERGENHBG045631.
InParanoidO75151.
KOK11445.
OMAKYKNSKP.
OrthoDBEOG73JKV9.
PhylomeDBO75151.
TreeFamTF106480.

Gene expression databases

ArrayExpressO75151.
BgeeO75151.
CleanExHS_PHF2.
GenevestigatorO75151.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR003347. 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]
PfamPF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTSM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75151.
GenomeRNAi5253.
NextBio20296.
PROO75151.
SOURCESearch...

Entry information

Entry namePHF2_HUMAN
AccessionPrimary (citable) accession number: O75151
Secondary accession number(s): Q4VXG0, Q8N3K2, Q9Y6N4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 108 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM