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Q80TJ7

- PHF8_MOUSE

UniProt

Q80TJ7 - PHF8_MOUSE

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Protein
Histone lysine demethylase PHF8
Gene
Phf8, Kiaa1111
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.

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 – 2441Substrate By similarity
Metal bindingi247 – 2471Iron; catalytic By similarity
Metal bindingi249 – 2491Iron; catalytic By similarity
Binding sitei264 – 2641Substrate By similarity
Metal bindingi319 – 3191Iron; catalytic By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri5 – 5652PHD-type
Add
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. G1/S transition of mitotic cell cycle Source: UniProtKB
  2. brain development 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 from RNA polymerase I promoter Source: UniProtKB
  9. positive regulation of transcription, DNA-templated 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.

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 PHF8
PRO_0000059296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331Phosphoserine; by CDK1 By similarity
Modified residuei84 – 841Phosphoserine; by CDK1 By similarity
Modified residuei615 – 6151Phosphoserine1 Publication
Modified residuei669 – 6691Phosphothreonine By similarity
Modified residuei670 – 6701Phosphothreonine By similarity
Modified residuei768 – 7681Phosphoserine By similarity
Modified residuei817 – 8171Phosphoserine By similarity
Modified residuei820 – 8201Phosphoserine2 Publications
Modified residuei843 – 8431Phosphoserine By 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

PaxDbiQ80TJ7.
PRIDEiQ80TJ7.

PTM databases

PhosphoSiteiQ80TJ7.

Expressioni

Gene expression databases

ArrayExpressiQ80TJ7.
BgeeiQ80TJ7.
CleanExiMM_PHF8.
GenevestigatoriQ80TJ7.

Interactioni

Subunit structurei

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ80TJ7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 351157JmjC
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 7915Linker By similarity
Add
BLAST

Compositional bias

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

Domaini

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.

Sequence similaritiesi

Contains 1 JmjC domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG290496.
GeneTreeiENSGT00550000074396.
HOVERGENiHBG045631.
InParanoidiA2ABU8.
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

MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC     50
PNCEVLHGPS IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD 100
EVILKPTGSQ LTVEFLEENS FSVPILVLKK DGLGMTLPSP SFTVRDVEHY 150
VGSDKEIDVI DVARQADCKM KLGDFVKYYY SGKREKVLNV ISLEFSDTRL 200
SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR DSYTDFHIDF 250
GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC 300
YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE 350
KRLSTADLFK FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL 400
NLAFRAWTKK EALPDHEDEI PETVRTVQLI KDLAREIRLV EDIFQQNVGK 450
TSNIFGLQRI FPAGSIPLTK PAHSTSVSMS KLSLPSKNGS KKKGLKPKDI 500
FKKAERKGKQ SSALGPAGQL SYNLMDPYSH QALKTGPSQK AKFNMSGTSL 550
NDSDDDSADM DLDGSENPLA LLMANGSTKR MKSVSKSRRA KIAKKVDSAR 600
LVAEQVMGDE FDLDSDDELQ IDERLGKEKA NLLIRSKFPR KLPRAKPCSD 650
PNRIREPGEV EFDIEEDYTT DEDMVEGVES KLGNGSGAGG ILDLLKASRQ 700
VGGPDYAALT EAPASPSTQE AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG 750
QERSSGSSSS GLGTVSSSPA SQRTPGKRPI KRPAYWKNES EEEENASLDE 800
QDSLGACFKD AEYIYPSLES DDDDPALKSR PKKKKNSDDA PWSPKARVTP 850
TLPKQDRPVR EGTRVASIET GLAAAAAKLA QQELQKAQKK KYIKKKPLLK 900
EVEQPRPQDS NPIMTMPAPT VATTPQPDTS SSPQPPPEPK QEALSGSLAD 950
HEYTARPNAF GMAQANRSTT PMAPGVFLTQ RRPSVGSQSS QAGQGKRPKK 1000
GLATAKQRLG RILKIHRNGK LLL 1023
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.
VSP_014966Add
BLAST
Alternative sequencei442 – 46423DIFQQ…IFPAG → VRSMGEGKAFGKGWRLKWQV RTL in isoform 3.
VSP_014967Add
BLAST
Alternative sequencei465 – 1023559Missing in isoform 3.
VSP_014968Add
BLAST
Alternative sequencei883 – 89614ELQKA…YIKKK → VRVDTQLVALLLMT in isoform 2.
VSP_014969Add
BLAST
Alternative sequencei897 – 1023127Missing in isoform 2.
VSP_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

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 A2ABU8.
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

ArrayExpressi Q80TJ7.
Bgeei Q80TJ7.
CleanExi MM_PHF8.
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: September 3, 2014
This is version 96 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

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