Q9UPP1 (PHF8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone lysine demethylase PHF8
EC=1.14.11.27

Alternative name(s):
PHD finger protein 8

Gene names

Name:	PHF8
Synonyms:	KIAA1111, ZNF422

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	1060 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ref.24
Catalytic activity	Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2. Ref.13 Ref.24 Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2. Ref.13 Ref.24
Cofactor	Binds 1 Fe2+ ion per subunit Probable. Ref.13 Ref.24
Subunit structure	Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and ZNF711. Ref.14 Ref.16 Ref.18
Subcellular location	Nucleus. Nucleus › nucleolus. Note: Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis. Ref.11 Ref.13 Ref.16 Ref.18
Domain	The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 promotes its access to H3K9me2. Ref.14 Ref.15 Ref.17 Ref.18 Ref.24 The linker region is a critical determinant of demethylase specificity. It enables the active site of JmjC to reach the target H3K9me2 when the PHD-type zinc finger binds to H3K4me3. Ref.14 Ref.15 Ref.17 Ref.18 Ref.24
Post-translational modification	Phosphorylation at Ser-69 and Ser-120 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase.
Involvement in disease	Mental retardation, X-linked, syndromic, Siderius type (MRXSSD) [MIM:300263]: A syndrome characterized by mild to borderline mental retardation with or without cleft lip/cleft palate. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ref.25
Sequence similarities	Belongs to the JHDM1 histone demethylase family. JHDM1D subfamily. Contains 1 JmjC domain. Contains 1 PHD-type zinc finger.
Biophysicochemical properties	Kinetic parameters: KM=134 µM for histone H3 H3K9Me2 Ref.24 KM=8 µM for histone H3 H3K4me3 and H3K9Me2
Sequence caution	The sequence BAA83063.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAB13877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAI41577.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI41581.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI41582.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI42861.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI45929.1 differs from that shown. Reason: Erroneous termination at position 419. Translated as Arg.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Mental retardation
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	G1/S transition of mitotic cell cycle Inferred from mutant phenotype Ref.18. Source: UniProtKB brain development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of chromatin silencing at rDNA Inferred from direct assay Ref.16. Source: UniProtKB positive regulation of transcription from RNA polymerase I promoter Inferred from direct assay Ref.16. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from direct assay Ref.16. Source: UniProtKB
Molecular_function	chromatin binding Inferred from direct assay Ref.18. Source: UniProtKB histone demethylase activity (H3-K27 specific) Inferred from direct assay Ref.17Ref.18. Source: UniProtKB histone demethylase activity (H3-K36 specific) Inferred from direct assay Ref.16Ref.17. Source: UniProtKB histone demethylase activity (H3-K9 specific) Inferred from direct assay Ref.24Ref.16Ref.14Ref.17Ref.18. Source: UniProtKB histone demethylase activity (H4-K20 specific) Inferred from direct assay Ref.17Ref.18. Source: UniProtKB iron ion binding Inferred from direct assay Ref.24. Source: UniProtKB methylated histone residue binding Inferred from direct assay Ref.24Ref.16Ref.14Ref.17Ref.18PubMed 21029866. 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.24. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UPP1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UPP1-2)

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

Isoform 3 (identifier: Q9UPP1-3)

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

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9UPP1-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1060

1060

Histone lysine demethylase PHF8

PRO_0000059295

Regions

Domain

231 – 387

157

JmjC

Zinc finger

41 – 92

52

PHD-type

Region

101 – 115

15

Linker

Compositional bias

769 – 807

39

Ser-rich

Sites

Metal binding

283

1

Iron; catalytic

Metal binding

285

1

Iron; catalytic

Metal binding

355

1

Iron; catalytic

Binding site

280

1

Substrate

Binding site

300

1

Substrate

Amino acid modifications

Modified residue

69

1

Phosphoserine; by CDK1 Ref.18

Modified residue

120

1

Phosphoserine; by CDK1 Ref.18

Modified residue

651

1

Phosphoserine Ref.10

Modified residue

705

1

Phosphothreonine Ref.9 Ref.10

Modified residue

706

1

Phosphothreonine Ref.9 Ref.10

Modified residue

804

1

Phosphoserine Ref.19

Modified residue

854

1

Phosphoserine Ref.9 Ref.10 Ref.21

Modified residue

857

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.19 Ref.21

Modified residue

880

1

Phosphoserine Ref.9 Ref.19 Ref.21

Natural variations

Alternative sequence

1 – 36

36

Missing in isoform 2 and isoform 4.

VSP_014964

Alternative sequence

478 – 578

101

Missing in isoform 3 and isoform 4.

VSP_014965

Alternative sequence

1060

1

L → LRQVIVQAECRQAIHEPKLK RRDAHP in isoform 4.

VSP_043640

Natural variant

315

1

F → S in MRXSSD; abolishes histone methyltransferase activity. Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ref.25

VAR_062250

Experimental info

Mutagenesis

43

1

Y → A: Abolishes binding to H3K4me3; when associated with A-50. Ref.16 Ref.17

Mutagenesis

50

1

Y → A: Abolishes binding to H3K4me3; when associated with A-43. Abolishes binding to H3K4me3; when associated with A-65. Ref.17

Mutagenesis

65

1

W → A: Abolishes binding to H3K4me3; when associated with A-50. Ref.17

Mutagenesis

69

1

S → A: Impairs phosphorylation by CDK1 and dissociation from chromatin when cells enter mitosis; when associated with A-120. Ref.18

Mutagenesis

120

1

S → A: Impairs phosphorylation by CDK1 and dissociation from chromatin when cells enter mitosis; when associated with A-69. Ref.18

Mutagenesis

283 – 285

3

HID → AAA: Abolishes histone methyltransferase activity. Ref.11 Ref.14 Ref.16 Ref.18

Mutagenesis

283

1

H → A: Abolishes histone methyltransferase activity. Ref.11 Ref.14 Ref.18

Sequence conflict

232

1

S → P in BAB13877. Ref.2

Secondary structure

1

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1060

Helix Strand Turn

Details...

Turn

44 – 47

4

Beta strand

56 – 58

3

Turn

60 – 62

3

Beta strand

65 – 67

3

Helix

68 – 71

4

Helix

75 – 78

4

Beta strand

81 – 83

3

Helix

87 – 93

7

Helix

121 – 129

9

Turn

136 – 138

3

Turn

144 – 146

3

Helix

149 – 155

7

Beta strand

161 – 165

5

Turn

167 – 170

4

Helix

180 – 187

8

Beta strand

192 – 197

6

Turn

198 – 201

4

Beta strand

202 – 207

6

Helix

208 – 215

8

Beta strand

224 – 230

7

Helix

235 – 238

4

Helix

244 – 249

6

Helix

251 – 255

5

Beta strand

270 – 274

5

Beta strand

278 – 283

6

Helix

286 – 288

3

Beta strand

290 – 305

16

Helix

309 – 319

11

Helix

324 – 326

3

Helix

329 – 331

3

Beta strand

332 – 334

3

Beta strand

337 – 342

6

Beta strand

346 – 349

4

Beta strand

354 – 370

17

Beta strand

373 – 375

3

Helix

376 – 389

14

Helix

393 – 395

3

Helix

400 – 420

21

Helix

427 – 444

18

Turn

446 – 448

3

Helix

449 – 451

3

Helix

453 – 455

3

Helix

462 – 477

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2005. Version 3. Checksum: 04C83D7C5E9E56B8	FASTA	1,060	117,864
	10 20 30 40 50 60 MNRSRAIVQR GRVLPPPAPL DTTNLAGRRT LQGRAKMASV PVYCLCRLPY DVTRFMIECD 70 80 90 100 110 120 MCQDWFHGSC VGVEEEKAAD IDLYHCPNCE VLHGPSIMKK RRGSSKGHDT HKGKPVKTGS 130 140 150 160 170 180 PTFVRELRSR TFDSSDEVIL KPTGNQLTVE FLEENSFSVP ILVLKKDGLG MTLPSPSFTV 190 200 210 220 230 240 RDVEHYVGSD KEIDVIDVTR QADCKMKLGD FVKYYYSGKR EKVLNVISLE FSDTRLSNLV 250 260 270 280 290 300 ETPKIVRKLS WVENLWPEEC VFERPNVQKY CLMSVRDSYT DFHIDFGGTS VWYHVLKGEK 310 320 330 340 350 360 IFYLIRPTNA NLTLFECWSS SSNQNEMFFG DQVDKCYKCS VKQGQTLFIP TGWIHAVLTP 370 380 390 400 410 420 VDCLAFGGNF LHSLNIEMQL KAYEIEKRLS TADLFRFPNF ETICWYVGKH ILDIFRGLRE 430 440 450 460 470 480 NRRHPASYLV HGGKALNLAF RAWTRKEALP DHEDEIPETV RTVQLIKDLA REIRLVEDIF 490 500 510 520 530 540 QQNVGKTSNI FGLQRIFPAG SIPLTRPAHS TSVSMSRLSL PSKNGSKKKG LKPKELFKKA 550 560 570 580 590 600 ERKGKESSAL GPAGQLSYNL MDTYSHQALK TGSFQKAKFN ITGACLNDSD DDSPDLDLDG 610 620 630 640 650 660 NESPLALLMS NGSTKRVKSL SKSRRTKIAK KVDKARLMAE QVMEDEFDLD SDDELQIDER 670 680 690 700 710 720 LGKEKATLII RPKFPRKLPR AKPCSDPNRV REPGEVEFDI EEDYTTDEDM VEGVEGKLGN 730 740 750 760 770 780 GSGAGGILDL LKASRQVGGP DYAALTEAPA SPSTQEAIQG MLCMANLQSS SSSPATSSLQ 790 800 810 820 830 840 AWWTGGQDRS SGSSSSGLGT VSNSPASQRT PGKRPIKRPA YWRTESEEEE ENASLDEQDS 850 860 870 880 890 900 LGACFKDAEY IYPSLESDDD DPALKSRPKK KKNSDDAPWS PKARVTPTLP KQDRPVREGT 910 920 930 940 950 960 RVASIETGLA AAAAKLAQQE LQKAQKKKYI KKKPLLKEVE QPRPQDSNLS LTVPAPTVAA 970 980 990 1000 1010 1020 TPQLVTSSSP LPPPEPKQEA LSGSLADHEY TARPNAFGMA QANRSTTPMA PGVFLTQRRP 1030 1040 1050 1060 SVGSQSNQAG QGKRPKKGLA TAKQRLGRIL KIHRNGKLLL
	Isoform 2 [UniParc]. Checksum: 75773C0918578FB0	FASTA	1,024	113,913
	10 20 30 40 50 60 MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS 70 80 90 100 110 120 IMKKRRGSSK GHDTHKGKPV KTGSPTFVRE LRSRTFDSSD EVILKPTGNQ LTVEFLEENS 130 140 150 160 170 180 FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVTRQADCKM KLGDFVKYYY 190 200 210 220 230 240 SGKREKVLNV ISLEFSDTRL SNLVETPKIV RKLSWVENLW PEECVFERPN VQKYCLMSVR 250 260 270 280 290 300 DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVDKC 310 320 330 340 350 360 YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFR 370 380 390 400 410 420 FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTRK EALPDHEDEI 430 440 450 460 470 480 PETVRTVQLI KDLAREIRLV EDIFQQNVGK TSNIFGLQRI FPAGSIPLTR PAHSTSVSMS 490 500 510 520 530 540 RLSLPSKNGS KKKGLKPKEL FKKAERKGKE SSALGPAGQL SYNLMDTYSH QALKTGSFQK 550 560 570 580 590 600 AKFNITGACL NDSDDDSPDL DLDGNESPLA LLMSNGSTKR VKSLSKSRRT KIAKKVDKAR 610 620 630 640 650 660 LMAEQVMEDE FDLDSDDELQ IDERLGKEKA TLIIRPKFPR KLPRAKPCSD PNRVREPGEV 670 680 690 700 710 720 EFDIEEDYTT DEDMVEGVEG KLGNGSGAGG ILDLLKASRQ VGGPDYAALT EAPASPSTQE 730 740 750 760 770 780 AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG QDRSSGSSSS GLGTVSNSPA SQRTPGKRPI 790 800 810 820 830 840 KRPAYWRTES EEEEENASLD EQDSLGACFK DAEYIYPSLE SDDDDPALKS RPKKKKNSDD 850 860 870 880 890 900 APWSPKARVT PTLPKQDRPV REGTRVASIE TGLAAAAAKL AQQELQKAQK KKYIKKKPLL 910 920 930 940 950 960 KEVEQPRPQD SNLSLTVPAP TVAATPQLVT SSSPLPPPEP KQEALSGSLA DHEYTARPNA 970 980 990 1000 1010 1020 FGMAQANRST TPMAPGVFLT QRRPSVGSQS NQAGQGKRPK KGLATAKQRL GRILKIHRNG KLLL
	Isoform 3 [UniParc]. Checksum: F54BE8A814BF1701	FASTA	959	106,902
	10 20 30 40 50 60 MNRSRAIVQR GRVLPPPAPL DTTNLAGRRT LQGRAKMASV PVYCLCRLPY DVTRFMIECD 70 80 90 100 110 120 MCQDWFHGSC VGVEEEKAAD IDLYHCPNCE VLHGPSIMKK RRGSSKGHDT HKGKPVKTGS 130 140 150 160 170 180 PTFVRELRSR TFDSSDEVIL KPTGNQLTVE FLEENSFSVP ILVLKKDGLG MTLPSPSFTV 190 200 210 220 230 240 RDVEHYVGSD KEIDVIDVTR QADCKMKLGD FVKYYYSGKR EKVLNVISLE FSDTRLSNLV 250 260 270 280 290 300 ETPKIVRKLS WVENLWPEEC VFERPNVQKY CLMSVRDSYT DFHIDFGGTS VWYHVLKGEK 310 320 330 340 350 360 IFYLIRPTNA NLTLFECWSS SSNQNEMFFG DQVDKCYKCS VKQGQTLFIP TGWIHAVLTP 370 380 390 400 410 420 VDCLAFGGNF LHSLNIEMQL KAYEIEKRLS TADLFRFPNF ETICWYVGKH ILDIFRGLRE 430 440 450 460 470 480 NRRHPASYLV HGGKALNLAF RAWTRKEALP DHEDEIPETV RTVQLIKDLA REIRLVEFNI 490 500 510 520 530 540 TGACLNDSDD DSPDLDLDGN ESPLALLMSN GSTKRVKSLS KSRRTKIAKK VDKARLMAEQ 550 560 570 580 590 600 VMEDEFDLDS DDELQIDERL GKEKATLIIR PKFPRKLPRA KPCSDPNRVR EPGEVEFDIE 610 620 630 640 650 660 EDYTTDEDMV EGVEGKLGNG SGAGGILDLL KASRQVGGPD YAALTEAPAS PSTQEAIQGM 670 680 690 700 710 720 LCMANLQSSS SSPATSSLQA WWTGGQDRSS GSSSSGLGTV SNSPASQRTP GKRPIKRPAY 730 740 750 760 770 780 WRTESEEEEE NASLDEQDSL GACFKDAEYI YPSLESDDDD PALKSRPKKK KNSDDAPWSP 790 800 810 820 830 840 KARVTPTLPK QDRPVREGTR VASIETGLAA AAAKLAQQEL QKAQKKKYIK KKPLLKEVEQ 850 860 870 880 890 900 PRPQDSNLSL TVPAPTVAAT PQLVTSSSPL PPPEPKQEAL SGSLADHEYT ARPNAFGMAQ 910 920 930 940 950 ANRSTTPMAP GVFLTQRRPS VGSQSNQAGQ GKRPKKGLAT AKQRLGRILK IHRNGKLLL
	Isoform 4 [UniParc]. Checksum: F32740CB7A2CE3F6	FASTA	948	105,913
	10 20 30 40 50 60 MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS 70 80 90 100 110 120 IMKKRRGSSK GHDTHKGKPV KTGSPTFVRE LRSRTFDSSD EVILKPTGNQ LTVEFLEENS 130 140 150 160 170 180 FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVTRQADCKM KLGDFVKYYY 190 200 210 220 230 240 SGKREKVLNV ISLEFSDTRL SNLVETPKIV RKLSWVENLW PEECVFERPN VQKYCLMSVR 250 260 270 280 290 300 DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVDKC 310 320 330 340 350 360 YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFR 370 380 390 400 410 420 FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTRK EALPDHEDEI 430 440 450 460 470 480 PETVRTVQLI KDLAREIRLV EFNITGACLN DSDDDSPDLD LDGNESPLAL LMSNGSTKRV 490 500 510 520 530 540 KSLSKSRRTK IAKKVDKARL MAEQVMEDEF DLDSDDELQI DERLGKEKAT LIIRPKFPRK 550 560 570 580 590 600 LPRAKPCSDP NRVREPGEVE FDIEEDYTTD EDMVEGVEGK LGNGSGAGGI LDLLKASRQV 610 620 630 640 650 660 GGPDYAALTE APASPSTQEA IQGMLCMANL QSSSSSPATS SLQAWWTGGQ DRSSGSSSSG 670 680 690 700 710 720 LGTVSNSPAS QRTPGKRPIK RPAYWRTESE EEEENASLDE QDSLGACFKD AEYIYPSLES 730 740 750 760 770 780 DDDDPALKSR PKKKKNSDDA PWSPKARVTP TLPKQDRPVR EGTRVASIET GLAAAAAKLA 790 800 810 820 830 840 QQELQKAQKK KYIKKKPLLK EVEQPRPQDS NLSLTVPAPT VAATPQLVTS SSPLPPPEPK 850 860 870 880 890 900 QEALSGSLAD HEYTARPNAF GMAQANRSTT PMAPGVFLTQ RRPSVGSQSN QAGQGKRPKK 910 920 930 940 GLATAKQRLG RILKIHRNGK LLLRQVIVQA ECRQAIHEPK LKRRDAHP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-927 (ISOFORM 3). Tissue: Embryo and Trachea.
[4]	"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] (ISOFORM 2). Tissue: Endometrial tumor.
[5]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Cervix.
[7]	"Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate." Laumonnier F., Holbert S., Ronce N., Faravelli F., Lenzner S., Schwartz C.E., Lespinasse J., Van Esch H., Lacombe D., Goizet C., Phan-Dinh Tuy F., van Bokhoven H., Fryns J.-P., Chelly J., Ropers H.-H., Moraine C., Hamel B.C.J., Briault S. J. Med. Genet. 42:780-786(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MRXSSD.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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 THR-705; THR-706; SER-854; SER-857 AND SER-880, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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-651; THR-705; THR-706; SER-854 AND SER-857, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis." Zhu Z., Wang Y., Li X., Wang Y., Xu L., Wang X., Sun T., Dong X., Chen L., Mao H., Yu Y., Li J., Chen P.A., Chen C.D. Cell Res. 20:794-801(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-283.
[12]	"The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation." Qiu J., Shi G., Jia Y., Li J., Wu M., Li J., Dong S., Wong J. Cell Res. 20:908-918(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CHARACTERIZATION OF VARIANT MRXSSD SER-315.
[13]	"PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase." Loenarz C., Ge W., Coleman M.L., Rose N.R., Cooper C.D.O., Klose R.J., Ratcliffe P.J., Schofield C.J. Hum. Mol. Genet. 19:217-222(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
[14]	"A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation." Kleine-Kohlbrecher D., Christensen J., Vandamme J., Abarrategui I., Bak M., Tommerup N., Shi X., Gozani O., Rappsilber J., Salcini A.E., Helin K. Mol. Cell 38:165-178(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN PHD-FINGER, INTERACTION WITH ZNF711, CHARACTERIZATION OF VARIANT MRXSSD SER-315, MUTAGENESIS OF HIS-283.
[15]	"PHF8 targets histone methylation and RNA polymerase II to activate transcription." Fortschegger K., de Graaf P., Outchkourov N.S., van Schaik F.M., Timmers H.T., Shiekhattar R. Mol. Cell. Biol. 30:3286-3298(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN PHD-FINGER, CHARACTERIZATION OF VARIANT MRXSSD SER-315.
[16]	"PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation." Feng W., Yonezawa M., Ye J., Jenuwein T., Grummt I. Nat. Struct. Mol. Biol. 17:445-450(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POLR1B AND UBTF, CHARACTERIZATION OF VARIANT MRXSSD SER-315, MUTAGENESIS OF TYR-43 AND 283-HIS--ASP-285.
[17]	"Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development." Qi H.H., Sarkissian M., Hu G.Q., Wang Z., Bhattacharjee A., Gordon D.B., Gonzales M., Lan F., Ongusaha P.P., Huarte M., Yaghi N.K., Lim H., Garcia B.A., Brizuela L., Zhao K., Roberts T.M., Shi Y. Nature 466:503-507(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN PHD-FINGER, CHARACTERIZATION OF VARIANT MRXSSD SER-315, MUTAGENESIS OF TYR-43; TYR-50 AND TRP-65.
[18]	"PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression." Liu W., Tanasa B., Tyurina O.V., Zhou T.Y., Gassmann R., Liu W.T., Ohgi K.A., Benner C., Garcia-Bassets I., Aggarwal A.K., Desai A., Dorrestein P.C., Glass C.K., Rosenfeld M.G. Nature 466:508-512(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN PHD-FINGER, INTERACTION WITH SETD1A; HCFC1 AND E2F1, CHARACTERIZATION OF VARIANT MRXSSD SER-315, PHOSPHORYLATION AT SER-69 AND SER-120, MUTAGENESIS OF SER-69; SER-120 AND HIS-283.
[19]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-804; SER-857 AND SER-880, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854; SER-857 AND SER-880, MASS SPECTROMETRY.
[22]	"Structural insights into a novel histone demethylase PHF8." Yu L., Wang Y., Huang S., Wang J., Deng Z., Zhang Q., Wu W., Zhang X., Liu Z., Gong W., Chen Z. Cell Res. 20:166-173(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 122-483 IN COMPLEX WITH IRON AND ALPHA-KETOGLUTARATE, FUNCTION, CHARACTERIZATION OF VARIANT MRXSSD SER-315.
[23]	"Crystal structure of the PHF8 Jumonji domain, an N(epsilon)-methyl lysine demethylase." Yue W.W., Hozjan V., Ge W., Loenarz C., Cooper C.D., Schofield C.J., Kavanagh K.L., Oppermann U., McDonough M.A. FEBS Lett. 584:825-830(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 115-483.
[24]	"Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases." Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X. Nat. Struct. Mol. Biol. 17:38-43(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-447 IN COMPLEX WITH IRON AND N-OXALYLGLYCINE, ZINC-BINDING, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DOMAIN LINKER AND PHD-FINGER.
[25]	"Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate." Koivisto A.M., Ala-Mello S., Lemmelae S., Komu H.A., Rautio J., Jaervelae I. Clin. Genet. 72:145-149(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MRXSSD SER-315.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB029034 mRNA. Translation: BAA83063.1. Different initiation.
CR933612 mRNA. Translation: CAI45929.1. Sequence problems.
AK021696 mRNA. Translation: BAB13877.1. Different initiation.
AK304272 mRNA. Translation: BAH14147.1.
AL589872, AL732374, Z98051 Genomic DNA. Translation: CAH70724.1.
Z98051, AL732374 Genomic DNA. Translation: CAQ08299.1.
AL732374, Z98051 Genomic DNA. Translation: CAI41578.2.
AL732374, AL589872, Z98051 Genomic DNA. Translation: CAI41576.1.
AL732374, Z98051 Genomic DNA. Translation: CAI41577.1. Sequence problems.
Z98051, AL732374 Genomic DNA. Translation: CAI42861.1. Sequence problems.
Z98051, AL589872, AL732374 Genomic DNA. Translation: CAI42860.1.
AL732374 Genomic DNA. Translation: CAI41582.1. Sequence problems.
AL732374 Genomic DNA. Translation: CAI41581.1. Sequence problems.
BC053861 mRNA. Translation: AAH53861.1.

IPI

IPI00183302.
IPI00430079.
IPI00480187.
IPI00922520.

RefSeq

NP_001171825.1. NM_001184896.1.
NP_001171826.1. NM_001184897.1.
NP_055922.1. NM_015107.2.

UniGene

Hs.731707.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WWU	X-ray	2.15	A	115-483	[»]
3K3N	X-ray	2.40	A	122-483	[»]
3K3O	X-ray	2.10	A	122-483	[»]
3KV4	X-ray	2.19	A	37-483	[»]
4DO0	X-ray	2.55	A	115-483	[»]

ProteinModelPortal

Q9UPP1.

SMR

Q9UPP1. Positions 39-483.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-4651164.

STRING

9606.ENSP00000338868.

PTM databases

PhosphoSite

Q9UPP1.

Polymorphism databases

DMDM

73620986.

Proteomic databases

PaxDb

Q9UPP1.

PRIDE

Q9UPP1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322659; ENSP00000319473; ENSG00000172943.
ENST00000338154; ENSP00000338868; ENSG00000172943.
ENST00000338946; ENSP00000340051; ENSG00000172943.
ENST00000357988; ENSP00000350676; ENSG00000172943.
ENST00000595978; ENSP00000469335; ENSG00000268312.
ENST00000596621; ENSP00000473074; ENSG00000268312.
ENST00000597844; ENSP00000472550; ENSG00000268312.
ENST00000601647; ENSP00000472063; ENSG00000268312.

GeneID

23133.

KEGG

hsa:23133.

UCSC

uc004dst.3. human.
uc004dsw.3. human.

Organism-specific databases

CTD

23133.

GeneCards

GC0XM053979.

HGNC

HGNC:20672. PHF8.

HPA

HPA038779.

MIM

300263. phenotype.
300560. gene.

neXtProt

NX_Q9UPP1.

Orphanet

85287. Intellectual deficit, X-linked, Siderius type.

PharmGKB

PA134889361.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG290496.

HOGENOM

HOG000231232.

HOVERGEN

HBG045631.

InParanoid

Q9UPP1.

KO

K11445.

OMA

MSNGSTK.

OrthoDB

EOG4G4GPT.

Gene expression databases

ArrayExpress

Q9UPP1.

Bgee

Q9UPP1.

CleanEx

HS_PHF8.

Genevestigator

Q9UPP1.

GermOnline

ENSG00000172943. 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

BindingDB

Q9UPP1.

ChEMBL

CHEMBL1938212.

ChiTaRS

PHF8. human.

EvolutionaryTrace

Q9UPP1.

GenomeRNAi

23133.

NextBio

44387.

SOURCE

Search...

Entry information

Entry name

PHF8_HUMAN

Accession

Primary (citable) accession number: Q9UPP1
Secondary accession number(s): B7Z911 , Q5H9U5, Q5JPR9, Q5JPS0, Q5JPS2, Q5JPS3, Q5VUJ4, Q7Z6D4, Q9HAH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	August 16, 2005
Last modified:	May 29, 2013
This is version 105 of the entry and version 3 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.