Q80TJ7 (PHF8_MOUSE) 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1023 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. Has activity toward H4K20Me1 only 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 By similarity.
Catalytic activity	Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2. Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.
Cofactor	Binds 1 Fe2+ ion per subunit By similarity.
Subunit structure	Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and ZNF711 By similarity.
Subcellular location	Nucleus By similarity. Nucleus › nucleolus By similarity. Note: Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis By similarity.
Domain	The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 promotes its access to H3K9me2 By similarity. 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 By similarity.
Post-translational modification	Phosphorylation at Ser-33 and Ser-84 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase By similarity.
Sequence similarities	Belongs to the JHDM1 histone demethylase family. JHDM1D subfamily. Contains 1 JmjC domain. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence CAM17163.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
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 sequence or structural similarity. Source: UniProtKB brain development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of chromatin silencing at rDNA Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase I promoter Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	chromatin binding Inferred from sequence or structural similarity. Source: UniProtKB histone demethylase activity (H3-K27 specific) Inferred from sequence or structural similarity. Source: UniProtKB histone demethylase activity (H3-K36 specific) Inferred from sequence or structural similarity. Source: UniProtKB histone demethylase activity (H3-K9 specific) Inferred from sequence or structural similarity. Source: UniProtKB histone demethylase activity (H4-K20 specific) Inferred from sequence or structural similarity. Source: UniProtKB iron ion binding Inferred from sequence or structural similarity. Source: UniProtKB methylated histone residue binding Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q80TJ7-1)

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: Q80TJ7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     442-542: Missing.
     883-896: ELQKAQKKKYIKKK → VRVDTQLVALLLMT
     897-1023: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q80TJ7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     442-464: DIFQQNVGKTSNIFGLQRIFPAG → VRSMGEGKAFGKGWRLKWQVRTL
     465-1023: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1023

1023

Histone lysine demethylase PHF8

PRO_0000059296

Regions

Domain

195 – 351

157

JmjC

Zinc finger

5 – 56

52

PHD-type

Region

65 – 79

15

Linker By similarity

Compositional bias

733 – 771

39

Ser-rich

Sites

Metal binding

247

1

Iron; catalytic By similarity

Metal binding

249

1

Iron; catalytic By similarity

Metal binding

319

1

Iron; catalytic By similarity

Binding site

244

1

Substrate By similarity

Binding site

264

1

Substrate By similarity

Amino acid modifications

Modified residue

33

1

Phosphoserine; by CDK1 By similarity

Modified residue

84

1

Phosphoserine; by CDK1 By similarity

Modified residue

615

1

Phosphoserine Ref.6

Modified residue

669

1

Phosphothreonine By similarity

Modified residue

670

1

Phosphothreonine By similarity

Modified residue

768

1

Phosphoserine By similarity

Modified residue

817

1

Phosphoserine By similarity

Modified residue

820

1

Phosphoserine Ref.5

Modified residue

843

1

Phosphoserine By similarity

Natural variations

Alternative sequence

442 – 542

101

Missing in isoform 2.

VSP_014966

Alternative sequence

442 – 464

23

DIFQQ…IFPAG → VRSMGEGKAFGKGWRLKWQV RTL in isoform 3.

VSP_014967

Alternative sequence

465 – 1023

559

Missing in isoform 3.

VSP_014968

Alternative sequence

883 – 896

14

ELQKA…YIKKK → VRVDTQLVALLLMT in isoform 2.

VSP_014969

Alternative sequence

897 – 1023

127

Missing in isoform 2.

VSP_014970

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1023

Helix Strand Turn

Details...

Beta strand

16 – 18

3

Beta strand

20 – 23

4

Turn

24 – 26

3

Beta strand

29 – 31

3

Helix

32 – 35

4

Helix

39 – 42

4

Beta strand

46 – 48

3

Turn

51 – 56

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: 7B9351944C000487	FASTA	1,023	113,553
	10 20 30 40 50 60 MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS 70 80 90 100 110 120 IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD EVILKPTGSQ LTVEFLEENS 130 140 150 160 170 180 FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVARQADCKM KLGDFVKYYY 190 200 210 220 230 240 SGKREKVLNV ISLEFSDTRL SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR 250 260 270 280 290 300 DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC 310 320 330 340 350 360 YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK 370 380 390 400 410 420 FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTKK EALPDHEDEI 430 440 450 460 470 480 PETVRTVQLI KDLAREIRLV EDIFQQNVGK TSNIFGLQRI FPAGSIPLTK PAHSTSVSMS 490 500 510 520 530 540 KLSLPSKNGS KKKGLKPKDI FKKAERKGKQ SSALGPAGQL SYNLMDPYSH QALKTGPSQK 550 560 570 580 590 600 AKFNMSGTSL NDSDDDSADM DLDGSENPLA LLMANGSTKR MKSVSKSRRA KIAKKVDSAR 610 620 630 640 650 660 LVAEQVMGDE FDLDSDDELQ IDERLGKEKA NLLIRSKFPR KLPRAKPCSD PNRIREPGEV 670 680 690 700 710 720 EFDIEEDYTT DEDMVEGVES KLGNGSGAGG ILDLLKASRQ VGGPDYAALT EAPASPSTQE 730 740 750 760 770 780 AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG QERSSGSSSS GLGTVSSSPA SQRTPGKRPI 790 800 810 820 830 840 KRPAYWKNES EEEENASLDE QDSLGACFKD AEYIYPSLES DDDDPALKSR PKKKKNSDDA 850 860 870 880 890 900 PWSPKARVTP TLPKQDRPVR EGTRVASIET GLAAAAAKLA QQELQKAQKK KYIKKKPLLK 910 920 930 940 950 960 EVEQPRPQDS NPIMTMPAPT VATTPQPDTS SSPQPPPEPK QEALSGSLAD HEYTARPNAF 970 980 990 1000 1010 1020 GMAQANRSTT PMAPGVFLTQ RRPSVGSQSS QAGQGKRPKK GLATAKQRLG RILKIHRNGK LLL
	Isoform 2 [UniParc]. Checksum: E14CF1810F1D3492	FASTA	795	88,919
	10 20 30 40 50 60 MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS 70 80 90 100 110 120 IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD EVILKPTGSQ LTVEFLEENS 130 140 150 160 170 180 FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVARQADCKM KLGDFVKYYY 190 200 210 220 230 240 SGKREKVLNV ISLEFSDTRL SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR 250 260 270 280 290 300 DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC 310 320 330 340 350 360 YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK 370 380 390 400 410 420 FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTKK EALPDHEDEI 430 440 450 460 470 480 PETVRTVQLI KDLAREIRLV EFNMSGTSLN DSDDDSADMD LDGSENPLAL LMANGSTKRM 490 500 510 520 530 540 KSVSKSRRAK IAKKVDSARL VAEQVMGDEF DLDSDDELQI DERLGKEKAN LLIRSKFPRK 550 560 570 580 590 600 LPRAKPCSDP NRIREPGEVE FDIEEDYTTD EDMVEGVESK LGNGSGAGGI LDLLKASRQV 610 620 630 640 650 660 GGPDYAALTE APASPSTQEA IQGMLCMANL QSSSSSPATS SLQAWWTGGQ ERSSGSSSSG 670 680 690 700 710 720 LGTVSSSPAS QRTPGKRPIK RPAYWKNESE EEENASLDEQ DSLGACFKDA EYIYPSLESD 730 740 750 760 770 780 DDDPALKSRP KKKKNSDDAP WSPKARVTPT LPKQDRPVRE GTRVASIETG LAAAAAKLAQ 790 QVRVDTQLVA LLLMT
	Isoform 3 [UniParc]. Checksum: A0A47C4A877F9291	FASTA	464	53,421
	10 20 30 40 50 60 MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS 70 80 90 100 110 120 IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD EVILKPTGSQ LTVEFLEENS 130 140 150 160 170 180 FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVARQADCKM KLGDFVKYYY 190 200 210 220 230 240 SGKREKVLNV ISLEFSDTRL SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR 250 260 270 280 290 300 DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC 310 320 330 340 350 360 YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK 370 380 390 400 410 420 FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTKK EALPDHEDEI 430 440 450 460 PETVRTVQLI KDLAREIRLV EVRSMGEGKA FGKGWRLKWQ VRTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-490 (ISOFORM 1). Strain: C57BL/6J. Tissue: Bone.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H. DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-1023 (ISOFORM 1). Tissue: Brain.
[4]	"Gene content of the 750-kb critical region for mouse embryonic ectoderm lethal tcl-w5." Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P., Nagaraja R. Mamm. Genome 15:265-276(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-899. Strain: 129/Sv.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820, MASS SPECTROMETRY. Tissue: Liver.
[6]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, MASS SPECTROMETRY. Tissue: Macrophage.
[7]	"Solution structure of PHD domain in protein AA017385." RIKEN structural genomics initiative (RSGI) Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: STRUCTURE BY NMR OF 1-66.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK036609 mRNA. Translation: BAC29505.1.
AK040943 mRNA. Translation: BAC30755.2.
AK040969 mRNA. Translation: BAC30763.1.
AL662922 Genomic DNA. Translation: CAM17161.1.
AL840642, AL662922 Genomic DNA. Translation: CAM15464.1.
AL662922, AL840642 Genomic DNA. Translation: CAM17159.1.
AL662922 Genomic DNA. Translation: CAM17163.1. Sequence problems.
AK122447 mRNA. Translation: BAC65729.1.
AF528164 Genomic DNA. Translation: AAO17385.1. Sequence problems.

IPI

IPI00109676.
IPI00227351.
IPI00649181.

RefSeq

NP_001009544.1. NM_001009544.2.
NP_001106825.1. NM_001113354.1.
NP_796175.1. NM_177201.5.

UniGene

Mm.17156.
Mm.84774.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WEP	NMR	-	A	1-63	[»]

ProteinModelPortal

Q80TJ7.

SMR

Q80TJ7. Positions 3-447.

ModBase

Search...

PTM databases

PhosphoSite

Q80TJ7.

Proteomic databases

PaxDb

Q80TJ7.

PRIDE

Q80TJ7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000024121; ENSMUSP00000024121; ENSMUSG00000023350.
ENSMUST00000046950; ENSMUSP00000040765; ENSMUSG00000041229.
ENSMUST00000046962; ENSMUSP00000041312; ENSMUSG00000041229.
ENSMUST00000112662; ENSMUSP00000108281; ENSMUSG00000041229.
ENSMUST00000112666; ENSMUSP00000108285; ENSMUSG00000041229.
ENSMUST00000112670; ENSMUSP00000108289; ENSMUSG00000041229.
ENSMUST00000168501; ENSMUSP00000127653; ENSMUSG00000041229.

GeneID

320595.
74042.

KEGG

mmu:320595.
mmu:74042.

UCSC

uc009upd.1. mouse.
uc009upe.1. mouse.

Organism-specific databases

CTD

23133.

MGI

MGI:2444341. Phf8.

Rouge

Search...

Phylogenomic databases

eggNOG

NOG290496.

GeneTree

ENSGT00550000074396.

HOVERGEN

HBG045631.

InParanoid

A2ABU8.

KO

K11445.

OrthoDB

EOG4G4GPT.

Gene expression databases

ArrayExpress

Q80TJ7.

Bgee

Q80TJ7.

CleanEx

MM_PHF8.

Genevestigator

Q80TJ7.

GermOnline

ENSMUSG00000041229. Mus musculus.

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

Q80TJ7.

NextBio

339610.

SOURCE

Search...

Entry information

Entry name

PHF8_MOUSE

Accession

Primary (citable) accession number: Q80TJ7
Secondary accession number(s): A2ABU8 , A2ABV0, A2ABV2, Q8BLX8, Q8BLY0, Q8BZ61, Q8CG26

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	August 16, 2005
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program