Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q80TJ7

- PHF8_MOUSE

UniProt

Q80TJ7 - PHF8_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone lysine demethylase PHF8

Gene

Phf8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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.

Cofactori

Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei244 – 2441SubstrateBy similarity
Metal bindingi247 – 2471Iron; catalyticPROSITE-ProRule annotation
Metal bindingi249 – 2491Iron; catalyticPROSITE-ProRule annotation
Binding sitei264 – 2641SubstrateBy similarity
Metal bindingi319 – 3191Iron; catalyticPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri5 – 5652PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. histone demethylase activity Source: UniProtKB
  3. histone demethylase activity (H3-K27 specific) Source: UniProtKB
  4. histone demethylase activity (H3-K36 specific) Source: UniProtKB
  5. histone demethylase activity (H3-K9 specific) Source: UniProtKB
  6. histone demethylase activity (H4-K20 specific) Source: UniProtKB
  7. iron ion binding Source: UniProtKB
  8. methylated histone binding Source: UniProtKB
  9. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: UniProtKB
  10. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. brain development Source: UniProtKB
  2. G1/S transition of mitotic cell cycle Source: UniProtKB
  3. histone H3-K27 demethylation Source: UniProtKB
  4. histone H3-K36 demethylation Source: UniProtKB
  5. histone H3-K9 demethylation Source: UniProtKB
  6. histone H4-K20 demethylation Source: UniProtKB
  7. negative regulation of chromatin silencing at rDNA Source: UniProtKB
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. positive regulation of transcription from RNA polymerase I promoter Source: UniProtKB
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196580. Condensation of Prophase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone lysine demethylase PHF8 (EC:1.14.11.27)
Alternative name(s):
PHD finger protein 8
Gene namesi
Name:Phf8
Synonyms:Kiaa1111
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:2444341. Phf8.

Subcellular locationi

Nucleus By similarity. Nucleusnucleolus By similarity
Note: Recruited to H3K4me3 sites on chromatin during interphase. Dissociates from chromatin when cells enter mitosis (By similarity).By similarity

GO - Cellular componenti

  1. nucleolus Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10231023Histone lysine demethylase PHF8PRO_0000059296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331Phosphoserine; by CDK1By similarity
Modified residuei84 – 841Phosphoserine; by CDK1By similarity
Modified residuei615 – 6151Phosphoserine1 Publication
Modified residuei669 – 6691PhosphothreonineBy similarity
Modified residuei670 – 6701PhosphothreonineBy similarity
Modified residuei768 – 7681PhosphoserineBy similarity
Modified residuei817 – 8171PhosphoserineBy similarity
Modified residuei820 – 8201Phosphoserine2 Publications
Modified residuei843 – 8431PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-33 and Ser-84 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ80TJ7.
PaxDbiQ80TJ7.
PRIDEiQ80TJ7.

PTM databases

PhosphoSiteiQ80TJ7.

Expressioni

Gene expression databases

BgeeiQ80TJ7.
CleanExiMM_PHF8.
ExpressionAtlasiQ80TJ7. baseline and differential.
GenevestigatoriQ80TJ7.

Interactioni

Subunit structurei

Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and ZNF711.By similarity

Structurei

Secondary structure

1
1023
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 183
Beta strandi20 – 234
Turni24 – 263
Beta strandi29 – 313
Helixi32 – 354
Helixi39 – 424
Beta strandi46 – 483
Turni51 – 566

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WEPNMR-A1-63[»]
ProteinModelPortaliQ80TJ7.
SMRiQ80TJ7. Positions 3-447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80TJ7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 351157JmjCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 7915LinkerBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi733 – 77139Ser-richAdd
BLAST

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 promotes its access to H3K9me2 (By similarity).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).By similarity

Sequence similaritiesi

Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri5 – 5652PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG290496.
GeneTreeiENSGT00550000074396.
HOVERGENiHBG045631.
InParanoidiQ80TJ7.
KOiK11445.
OMAiEIDLYHC.
OrthoDBiEOG73JKV9.
PhylomeDBiQ80TJ7.
TreeFamiTF106480.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q80TJ7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC
60 70 80 90 100
PNCEVLHGPS IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD
110 120 130 140 150
EVILKPTGSQ LTVEFLEENS FSVPILVLKK DGLGMTLPSP SFTVRDVEHY
160 170 180 190 200
VGSDKEIDVI DVARQADCKM KLGDFVKYYY SGKREKVLNV ISLEFSDTRL
210 220 230 240 250
SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR DSYTDFHIDF
260 270 280 290 300
GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC
310 320 330 340 350
YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE
360 370 380 390 400
KRLSTADLFK FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL
410 420 430 440 450
NLAFRAWTKK EALPDHEDEI PETVRTVQLI KDLAREIRLV EDIFQQNVGK
460 470 480 490 500
TSNIFGLQRI FPAGSIPLTK PAHSTSVSMS KLSLPSKNGS KKKGLKPKDI
510 520 530 540 550
FKKAERKGKQ SSALGPAGQL SYNLMDPYSH QALKTGPSQK AKFNMSGTSL
560 570 580 590 600
NDSDDDSADM DLDGSENPLA LLMANGSTKR MKSVSKSRRA KIAKKVDSAR
610 620 630 640 650
LVAEQVMGDE FDLDSDDELQ IDERLGKEKA NLLIRSKFPR KLPRAKPCSD
660 670 680 690 700
PNRIREPGEV EFDIEEDYTT DEDMVEGVES KLGNGSGAGG ILDLLKASRQ
710 720 730 740 750
VGGPDYAALT EAPASPSTQE AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG
760 770 780 790 800
QERSSGSSSS GLGTVSSSPA SQRTPGKRPI KRPAYWKNES EEEENASLDE
810 820 830 840 850
QDSLGACFKD AEYIYPSLES DDDDPALKSR PKKKKNSDDA PWSPKARVTP
860 870 880 890 900
TLPKQDRPVR EGTRVASIET GLAAAAAKLA QQELQKAQKK KYIKKKPLLK
910 920 930 940 950
EVEQPRPQDS NPIMTMPAPT VATTPQPDTS SSPQPPPEPK QEALSGSLAD
960 970 980 990 1000
HEYTARPNAF GMAQANRSTT PMAPGVFLTQ RRPSVGSQSS QAGQGKRPKK
1010 1020
GLATAKQRLG RILKIHRNGK LLL
Length:1,023
Mass (Da):113,553
Last modified:August 16, 2005 - v2
Checksum:i7B9351944C000487
GO
Isoform 2 (identifier: Q80TJ7-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:795
Mass (Da):88,919
Checksum:iE14CF1810F1D3492
GO
Isoform 3 (identifier: Q80TJ7-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:464
Mass (Da):53,421
Checksum:iA0A47C4A877F9291
GO

Sequence cautioni

The sequence CAM17163.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei442 – 542101Missing in isoform 2. 1 PublicationVSP_014966Add
BLAST
Alternative sequencei442 – 46423DIFQQ…IFPAG → VRSMGEGKAFGKGWRLKWQV RTL in isoform 3. 1 PublicationVSP_014967Add
BLAST
Alternative sequencei465 – 1023559Missing in isoform 3. 1 PublicationVSP_014968Add
BLAST
Alternative sequencei883 – 89614ELQKA…YIKKK → VRVDTQLVALLLMT in isoform 2. 1 PublicationVSP_014969Add
BLAST
Alternative sequencei897 – 1023127Missing in isoform 2. 1 PublicationVSP_014970Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30470.1. [Q80TJ7-2]
CCDS53223.1. [Q80TJ7-1]
RefSeqiNP_001009544.1. NM_001009544.2.
NP_001106825.1. NM_001113354.1. [Q80TJ7-1]
NP_796175.1. NM_177201.5. [Q80TJ7-2]
XP_006528938.1. XM_006528875.1. [Q80TJ7-1]
XP_006528939.1. XM_006528876.1. [Q80TJ7-1]
XP_006528940.1. XM_006528877.1. [Q80TJ7-1]
XP_006528943.1. XM_006528880.1. [Q80TJ7-1]
UniGeneiMm.17156.
Mm.84774.

Genome annotation databases

EnsembliENSMUST00000024121; ENSMUSP00000024121; ENSMUSG00000023350.
ENSMUST00000046950; ENSMUSP00000040765; ENSMUSG00000041229. [Q80TJ7-1]
ENSMUST00000046962; ENSMUSP00000041312; ENSMUSG00000041229. [Q80TJ7-2]
ENSMUST00000112662; ENSMUSP00000108281; ENSMUSG00000041229. [Q80TJ7-2]
ENSMUST00000112666; ENSMUSP00000108285; ENSMUSG00000041229. [Q80TJ7-3]
ENSMUST00000168501; ENSMUSP00000127653; ENSMUSG00000041229. [Q80TJ7-1]
GeneIDi320595.
74042.
KEGGimmu:320595.
mmu:74042.
UCSCiuc009upd.1. mouse. [Q80TJ7-3]
uc009upe.1. mouse. [Q80TJ7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS30470.1. [Q80TJ7-2 ]
CCDS53223.1. [Q80TJ7-1 ]
RefSeqi NP_001009544.1. NM_001009544.2.
NP_001106825.1. NM_001113354.1. [Q80TJ7-1 ]
NP_796175.1. NM_177201.5. [Q80TJ7-2 ]
XP_006528938.1. XM_006528875.1. [Q80TJ7-1 ]
XP_006528939.1. XM_006528876.1. [Q80TJ7-1 ]
XP_006528940.1. XM_006528877.1. [Q80TJ7-1 ]
XP_006528943.1. XM_006528880.1. [Q80TJ7-1 ]
UniGenei Mm.17156.
Mm.84774.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WEP NMR - A 1-63 [» ]
ProteinModelPortali Q80TJ7.
SMRi Q80TJ7. Positions 3-447.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL3038497.

PTM databases

PhosphoSitei Q80TJ7.

Proteomic databases

MaxQBi Q80TJ7.
PaxDbi Q80TJ7.
PRIDEi Q80TJ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000024121 ; ENSMUSP00000024121 ; ENSMUSG00000023350 .
ENSMUST00000046950 ; ENSMUSP00000040765 ; ENSMUSG00000041229 . [Q80TJ7-1 ]
ENSMUST00000046962 ; ENSMUSP00000041312 ; ENSMUSG00000041229 . [Q80TJ7-2 ]
ENSMUST00000112662 ; ENSMUSP00000108281 ; ENSMUSG00000041229 . [Q80TJ7-2 ]
ENSMUST00000112666 ; ENSMUSP00000108285 ; ENSMUSG00000041229 . [Q80TJ7-3 ]
ENSMUST00000168501 ; ENSMUSP00000127653 ; ENSMUSG00000041229 . [Q80TJ7-1 ]
GeneIDi 320595.
74042.
KEGGi mmu:320595.
mmu:74042.
UCSCi uc009upd.1. mouse. [Q80TJ7-3 ]
uc009upe.1. mouse. [Q80TJ7-1 ]

Organism-specific databases

CTDi 23133.
MGIi MGI:2444341. Phf8.
Rougei Search...

Phylogenomic databases

eggNOGi NOG290496.
GeneTreei ENSGT00550000074396.
HOVERGENi HBG045631.
InParanoidi Q80TJ7.
KOi K11445.
OMAi EIDLYHC.
OrthoDBi EOG73JKV9.
PhylomeDBi Q80TJ7.
TreeFami TF106480.

Enzyme and pathway databases

Reactomei REACT_196580. Condensation of Prophase Chromosomes.

Miscellaneous databases

EvolutionaryTracei Q80TJ7.
NextBioi 339610.
PROi Q80TJ7.
SOURCEi Search...

Gene expression databases

Bgeei Q80TJ7.
CleanExi MM_PHF8.
ExpressionAtlasi Q80TJ7. baseline and differential.
Genevestigatori Q80TJ7.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR003347. JmjC_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 AND SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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.

Entry informationi

Entry nameiPHF8_MOUSE
AccessioniPrimary (citable) accession number: Q80TJ7
Secondary accession number(s): A2ABU8
, A2ABV0, A2ABV2, Q8BLX8, Q8BLY0, Q8BZ61, Q8CG26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: August 16, 2005
Last modified: October 29, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3