O75151 (PHF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysine-specific demethylase PHF2
EC=1.14.11.-

Alternative name(s):
GRC5
PHD finger protein 2

Gene names

Name:	PHF2
Synonyms:	KIAA0662

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1096 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11 Ref.13 Ref.14
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.11
Subcellular location	Nucleus › nucleolus Ref.13.
Tissue specificity	Widely expressed, including in liver (at protein level). Ref.11
Domain	The PHD-type zinc finger mediates the binding to H3K4me2 and H3K4me3. Ref.13
Post-translational modification	Phosphorylated by PKA on specific serine residues, leading to the formation of an active lysine demethylase complex. Ref.11
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.14).
Sequence caution	The sequence BAA31637.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Iron Metal-binding Zinc
Molecular function	Activator Chromatin regulator Dioxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	liver development Traceable author statement Ref.11. Source: UniProtKB negative regulation of chromatin silencing at rDNA Inferred from mutant phenotype Ref.13. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	histone demethylase activity (H3-K9 specific) Inferred from direct assay Ref.11. Source: UniProtKB iron ion binding Inferred from direct assay Ref.14. Source: UniProtKB methylated histone residue binding Inferred from direct assay Ref.13Ref.14. Source: UniProtKB oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1096

1096

Lysine-specific demethylase PHF2

PRO_0000059290

Regions

Domain

197 – 353

157

JmjC

Zinc finger

5 – 56

52

PHD-type

Compositional bias

472 – 518

47

Pro-rich

Compositional bias

487 – 648

162

Lys-rich

Compositional bias

960 – 1020

61

Ser/Thr-rich

Sites

Metal binding

249

1

Iron; catalytic

Metal binding

251

1

Iron; catalytic

Metal binding

321

1

Iron; catalytic

Binding site

193

1

Alpha-ketoglutarate

Binding site

246

1

Alpha-ketoglutarate

Binding site

259

1

Alpha-ketoglutarate

Binding site

266

1

Alpha-ketoglutarate

Binding site

321

1

Alpha-ketoglutarate

Binding site

323

1

Alpha-ketoglutarate

Amino acid modifications

Modified residue

458

1

Phosphoserine By similarity

Modified residue

459

1

Phosphoserine By similarity

Modified residue

474

1

Phosphoserine Ref.10

Modified residue

479

1

Phosphothreonine Ref.10

Modified residue

539

1

Phosphoserine Ref.8

Modified residue

681

1

Phosphoserine By similarity

Modified residue

705

1

Phosphoserine Ref.10 Ref.12

Modified residue

738

1

Phosphoserine By similarity

Modified residue

882

1

Phosphoserine Ref.8 Ref.9 Ref.10

Modified residue

1056

1

Phosphoserine; by PKA Ref.11

Natural variations

Natural variant

56

1

T → P.
Corresponds to variant rs34279404 [ dbSNP | Ensembl ].

VAR_047553

Natural variant

1058

1

S → L.
Corresponds to variant rs35236745 [ dbSNP | Ensembl ].

VAR_051598

Experimental info

Mutagenesis

7

1

Y → A: Abolishes binding to H3K4me2 and H3K4me3. Ref.13

Mutagenesis

29

1

W → A: Abolishes binding to H3K4me2 and H3K4me3. Ref.13

Mutagenesis

249

1

H → A: Abolishes demethylase activity. Ref.11

Mutagenesis

321

1

Y → H: Does not alter iron-binding nor activates histone demethylase activity. Ref.14

Mutagenesis

757

1

S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-899; A-954 and A-1056. Ref.11

Mutagenesis

899

1

S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-954 and A-1056. Ref.11

Mutagenesis

954

1

S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-1056. Ref.11

Mutagenesis

1056

1

S → A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-954. Ref.11

Sequence conflict

19 – 41

23

FMIEC…VEEEE → PRAARPPARPGPTRAAQRRG RAT in BAA31637. Ref.2

Sequence conflict

75 – 76

2

QA → PT in AAD21791. Ref.1

Sequence conflict

100

1

S → R in BAA31637. Ref.2

Sequence conflict

106

1

A → S in AAD21791. Ref.1

Sequence conflict

115

1

L → V in AAD21791. Ref.1

Sequence conflict

621

1

K → R in AAD21791. Ref.1

Sequence conflict

633

1

Missing in AAD21791. Ref.1

Sequence conflict

642

1

K → R in AAD21791. Ref.1

Sequence conflict

654

1

T → S in AAD21791. Ref.1

Sequence conflict

664

1

N → S in AAD21791. Ref.1

Sequence conflict

670

1

P → A in AAD21791. Ref.1

Sequence conflict

698

1

N → S in AAD21791. Ref.1

Sequence conflict

712 – 719

8

AVLPTPVT → EALLMPTS in AAD21791. Ref.1

Sequence conflict

727

1

A → V in AAD21791. Ref.1

Sequence conflict

752

1

R → K in AAD21791. Ref.1

Sequence conflict

782

1

S → N in AAD21791. Ref.1

Sequence conflict

817

1

A → T in AAD21791. Ref.1

Sequence conflict

823

1

S → G in AAD21791. Ref.1

Sequence conflict

833

1

N → I in AAD21791. Ref.1

Sequence conflict

837 – 841

5

SGKSA → NKGT in AAD21791. Ref.1

Sequence conflict

849

1

A → T in AAD21791. Ref.1

Sequence conflict

857

1

D → E in AAD21791. Ref.1

Sequence conflict

862

1

Missing in AAD21791. Ref.1

Sequence conflict

888

1

I → V in AAD21791. Ref.1

Sequence conflict

949 – 950

2

SK → NR in AAD21791. Ref.1

Sequence conflict

954 – 955

2

SA → NT in AAD21791. Ref.1

Sequence conflict

959 – 960

2

LT → PA in AAD21791. Ref.1

Sequence conflict

964

1

T → A in AAD21791. Ref.1

Sequence conflict

968

1

T → I in AAD21791. Ref.1

Sequence conflict

972

1

I → ASASTGTT in AAD21791. Ref.1

Sequence conflict

975

1

G → S in AAD21791. Ref.1

Sequence conflict

978 – 979

2

ST → PA in AAD21791. Ref.1

Sequence conflict

996

1

T → TTPAST in BAA31637. Ref.2

Sequence conflict

996

1

T → TTPAST in CAD38938. Ref.6

Sequence conflict

1033 – 1035

3

TGA → SGS in AAD21791. Ref.1

Sequence conflict

1040

1

T → A in AAD21791. Ref.1

Sequence conflict

1063

1

Missing in AAD21791. Ref.1

Secondary structure

1

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1096

Helix Strand Turn

Details...

Turn

8 – 11

4

Beta strand

20 – 22

3

Turn

24 – 26

3

Beta strand

29 – 31

3

Helix

32 – 35

4

Turn

39 – 41

3

Helix

42 – 44

3

Beta strand

45 – 47

3

Helix

51 – 57

7

Helix

87 – 95

9

Helix

101 – 103

3

Beta strand

105 – 107

3

Helix

110 – 112

3

Helix

115 – 121

7

Beta strand

127 – 131

5

Turn

133 – 136

4

Helix

146 – 153

8

Beta strand

158 – 163

6

Turn

164 – 166

3

Beta strand

169 – 173

5

Helix

174 – 181

8

Beta strand

190 – 196

7

Helix

201 – 205

5

Helix

210 – 215

6

Helix

217 – 221

5

Beta strand

236 – 240

5

Beta strand

245 – 249

5

Helix

252 – 254

3

Beta strand

256 – 271

16

Helix

275 – 286

12

Helix

290 – 292

3

Helix

295 – 298

4

Beta strand

303 – 308

6

Beta strand

312 – 315

4

Beta strand

320 – 336

17

Helix

339 – 341

3

Helix

342 – 355

14

Beta strand

359 – 361

3

Helix

366 – 387

22

Helix

393 – 409

17

Turn

412 – 414

3

Helix

415 – 418

4

Helix

419 – 421

3

Helix

428 – 443

16

Sequences

	Sequence		Length	Mass (Da)
	O75151 [UniParc]. Last modified November 25, 2008. Version 4. Checksum: DD088363DB76674D	FASTA	1,096	120,775
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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, MASS SPECTROMETRY.
[13]	"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.
[14]	"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.

IPI

IPI00867617.

PIR

T00369.

RefSeq

NP_005383.3. NM_005392.3.

UniGene

Hs.211441.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O75151.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000352185.

PTM databases

PhosphoSite

O75151.

Proteomic databases

PaxDb

O75151.

PRIDE

O75151.

Protocols and materials databases

DNASU

5253.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359246; ENSP00000352185; ENSG00000197724.

GeneID

5253.

KEGG

hsa:5253.

UCSC

uc004aub.3. human.

Organism-specific databases

CTD

5253.

GeneCards

GC09P096338.

H-InvDB

HIX0008184.

HGNC

HGNC:8920. PHF2.

HPA

HPA010831.

MIM

604351. gene.

neXtProt

NX_O75151.

PharmGKB

PA33260.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG290496.

HOGENOM

HOG000231232.

HOVERGEN

HBG045631.

InParanoid

O75151.

KO

K11445.

OMA

SKSEAKW.

OrthoDB

EOG46HG91.

PhylomeDB

O75151.

Gene expression databases

ArrayExpress

O75151.

Bgee

O75151.

CleanEx

HS_PHF2.

Genevestigator

O75151.

GermOnline

ENSG00000197724. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

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]

Pfam

PF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]

SMART

SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O75151.

GenomeRNAi

5253.

NextBio

20296.

SOURCE

Search...

Entry information

Entry name

PHF2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 101 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.