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Q8IWS0 (PHF6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PHD finger protein 6
Alternative name(s):
PHD-like zinc finger protein
Gene names
Name:PHF6
Synonyms:KIAA1823
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription. Ref.17

Subunit structure

Interacts with UBTF. Interacts with the NuRD complex component RBBP4 (via the nucleolar localization motif), the interaction mediates transcriptional repression activity. Ref.17 Ref.18

Subcellular location

Nucleus. Nucleusnucleolus. Note: Nuclear, it particularly localizes to the nucleolus. Ref.1 Ref.17

Tissue specificity

Ubiquitously expressed. Ref.1

Domain

The PHD-type zinc finger 1 mediates both nucleolar localization and interaction with UBTF. Ref.18

The ePHD2 domain folds as an integrated structural module comprizing the C2HC-type zinc finger (pre-PHD) and the atypical PHD-type 2 zinc finger. It mediates non-specific binding to dsDNA, but doesn't bind histones in contrast to many PHD-type zinc fingers. Ref.18

Involvement in disease

Boerjeson-Forssman-Lehmann syndrome (BFLS) [MIM:301900]: A X-linked recessive disorder characterized by moderate to severe mental retardation, epilepsy, hypogonadism, hypometabolism, obesity with marked gynecomastia, swelling of subcutaneous tissue of the face, narrow palpebral fissure and large but not deformed ears.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.17

Sequence similarities

Contains 2 C2HC-type zinc fingers.

Contains 2 PHD-type zinc fingers.

Sequence caution

The sequence BAB47452.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Epilepsy
Mental retardation
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from direct assay PubMed 22720776. Source: UniProt

nucleoplasm

Inferred from direct assay PubMed 22720776. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

histone binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

histone deacetylase binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

phosphoprotein binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

ribonucleoprotein complex binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

scaffold protein binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

tubulin binding

Inferred from physical interaction PubMed 22720776. Source: UniProt

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IWS0-1)

Also known as: PHF6a; PHF6b;

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: Q8IWS0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     140-140: A → AA
     279-311: KCTLCSQPGATIGCEIKACVKTYHYHCGVQDKA → VCSFYICYATLHLICCFKFRVHPKFIQSSENLK
     312-365: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 146.
Isoform 3 (identifier: Q8IWS0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     140-140: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8IWS0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     140-140: Missing.
     279-311: KCTLCSQPGATIGCEIKACVKTYHYHCGVQDKA → VCSFYICYATLHLICCFKFRVHPKFIQSSENLK
     312-365: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8IWS0-5)

The sequence of this isoform differs from the canonical sequence as follows:
     47-80: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 365364PHD finger protein 6
PRO_0000059293

Regions

Zinc finger17 – 5034C2HC-type; pre-PHD
Zinc finger79 – 13153PHD-type 1; degenerate
Zinc finger212 – 24736C2HC-type; pre-PHD
Zinc finger277 – 32953PHD-type 2; degenerate
Region14 – 131118Extended PHD1 domain (ePHD1)
Region208 – 329122Extended PHD2 domain (ePHD2)
Motif13 – 164Nuclear localization signal Potential
Motif129 – 1335Nuclear localization signal Potential
Motif157 – 16913Nucleolar localization signal Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.16
Modified residue1381Phosphoserine Ref.10 Ref.12
Modified residue1451Phosphoserine Ref.10 Ref.13
Modified residue1551Phosphoserine Ref.15
Modified residue1991Phosphoserine Ref.15
Modified residue3581Phosphothreonine Ref.8

Natural variations

Alternative sequence47 – 8034Missing in isoform 5.
VSP_054937
Alternative sequence1401A → AA in isoform 2.
VSP_009372
Alternative sequence1401Missing in isoform 3 and isoform 4.
VSP_053441
Alternative sequence279 – 31133KCTLC…VQDKA → VCSFYICYATLHLICCFKFR VHPKFIQSSENLK in isoform 2 and isoform 4.
VSP_009373
Alternative sequence312 – 36554Missing in isoform 2 and isoform 4.
VSP_009374
Natural variant451C → Y in BFLS; Loss of interaction with UBTF. Ref.1 Ref.17
Corresponds to variant rs28935179 [ dbSNP | Ensembl ].
VAR_017633
Natural variant991C → F in BFLS; Loss of interaction with UBTF. Ref.1 Ref.17
VAR_017634
Natural variant2291H → R in BFLS. Ref.1
VAR_017635
Natural variant2341K → E in BFLS. Ref.1
VAR_017636
Natural variant2571R → G in BFLS. Ref.1
VAR_017637

Experimental info

Sequence conflict1261V → A in AAH05994. Ref.6

Secondary structure

........................... 365
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PHF6a) (PHF6b) [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E8E587909EF9701D

FASTA36541,290
        10         20         30         40         50         60 
MSSSVEQKKG PTRQRKCGFC KSNRDKECGQ LLISENQKVA AHHKCMLFSS ALVSSHSDNE 

        70         80         90        100        110        120 
SLGGFSIEDV QKEIKRGTKL MCSLCHCPGA TIGCDVKTCH RTYHYHCALH DKAQIREKPS 

       130        140        150        160        170        180 
QGIYMVYCRK HKKTAHNSEA DLEESFNEHE LEPSSPKSKK KSRKGRPRKT NFKGLSEDTR 

       190        200        210        220        230        240 
STSSHGTDEM ESSSYRDRSP HRSSPSDTRP KCGFCHVGEE ENEARGKLHI FNAKKAAAHY 

       250        260        270        280        290        300 
KCMLFSSGTV QLTTTSRAEF GDFDIKTVLQ EIKRGKRMKC TLCSQPGATI GCEIKACVKT 

       310        320        330        340        350        360 
YHYHCGVQDK AKYIENMSRG IYKLYCKNHS GNDERDEEDE ERESKSRGKV EIDQQQLTQQ 


QLNGN 

« Hide

Isoform 2 [UniParc].

Checksum: 107F45F45063D7A0
Show »

FASTA31235,329
Isoform 3 [UniParc].

Checksum: 2BEB117AF92F7ECC
Show »

FASTA36441,219
Isoform 4 [UniParc].

Checksum: B6091E6AC014F78A
Show »

FASTA31035,187
Isoform 5 [UniParc].

Checksum: CA296A2F39167444
Show »

FASTA33137,628

References

« Hide 'large scale' references
[1]"Mutations in PHF6 are associated with Boerjeson-Forssman-Lehmann syndrome."
Lower K.M., Turner G., Kerr B.A., Mathews K.D., Shaw M.A., Gedeon A.K., Schelley S., Hoyme H.E., White S.M., Delatycki M.B., Lampe A.K., Clayton-Smith J., Stewart H., van Ravenswaay C.M.A., de Vries B.B.A., Cox B., Grompe M., Ross S. expand/collapse author list , Thomas P., Mulley J.C., Gecz J.
Nat. Genet. 32:661-665(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, VARIANTS BFLS TYR-45; PHE-99; ARG-229; GLU-234 AND GLY-257.
[2]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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. expand/collapse author list , 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] (ISOFORMS 4 AND 5).
Tissue: Subthalamic nucleus and Thymus.
[4]"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. expand/collapse author list , 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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: Bone marrow.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-145, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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-155 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"PHF6 regulates cell cycle progression by suppressing ribosomal RNA synthesis."
Wang J., Leung J.W., Gong Z., Feng L., Shi X., Chen J.
J. Biol. Chem. 288:3174-3183(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBTF, CHARACTERIZATION OF VARIANTS BFLS TYR-45 AND PHE-99.
[18]"Structural and functional insights into the human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6."
Liu Z., Li F., Ruan K., Zhang J., Mei Y., Wu J., Shi Y.
J. Biol. Chem. 289:10069-10083(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 208-333, INTERACTION WITH RBBP4, ZINC-FINGERS, EXTENDED PHD DOMAIN, DNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY157622 mRNA. Translation: AAO13214.1.
AB058726 mRNA. Translation: BAB47452.1. Different initiation.
AK290095 mRNA. Translation: BAF82784.1.
AK303369 mRNA. Translation: BAG64426.1.
AL591668, AC004383 Genomic DNA. Translation: CAI41600.1.
AL591668 Genomic DNA. Translation: CAI41601.1.
CH471107 Genomic DNA. Translation: EAX11762.1.
CH471107 Genomic DNA. Translation: EAX11763.1.
CH471107 Genomic DNA. Translation: EAX11766.1.
BC005994 mRNA. Translation: AAH05994.1.
CCDSCCDS14639.1. [Q8IWS0-1]
CCDS14640.1. [Q8IWS0-2]
RefSeqNP_001015877.1. NM_001015877.1. [Q8IWS0-1]
NP_115711.2. NM_032335.3. [Q8IWS0-2]
NP_115834.1. NM_032458.2. [Q8IWS0-1]
UniGeneHs.356501.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4NN2X-ray1.47A/B208-333[»]
ProteinModelPortalQ8IWS0.
SMRQ8IWS0. Positions 16-131, 208-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124022. 7 interactions.
IntActQ8IWS0. 2 interactions.
MINTMINT-4534083.
STRING9606.ENSP00000329097.

PTM databases

PhosphoSiteQ8IWS0.

Polymorphism databases

DMDM42559482.

Proteomic databases

MaxQBQ8IWS0.
PaxDbQ8IWS0.
PeptideAtlasQ8IWS0.
PRIDEQ8IWS0.

Protocols and materials databases

DNASU84295.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332070; ENSP00000329097; ENSG00000156531. [Q8IWS0-1]
ENST00000370800; ENSP00000359836; ENSG00000156531. [Q8IWS0-2]
ENST00000370803; ENSP00000359839; ENSG00000156531. [Q8IWS0-1]
ENST00000416404; ENSP00000394480; ENSG00000156531.
GeneID84295.
KEGGhsa:84295.
UCSCuc004exh.3. human. [Q8IWS0-2]
uc004exj.3. human. [Q8IWS0-1]

Organism-specific databases

CTD84295.
GeneCardsGC0XP133507.
HGNCHGNC:18145. PHF6.
HPAHPA001023.
MIM300414. gene.
301900. phenotype.
neXtProtNX_Q8IWS0.
Orphanet127. Borjeson-Forssman-Lehmann syndrome.
PharmGKBPA33263.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282606.
HOGENOMHOG000026798.
HOVERGENHBG049389.
OMAISESPHI.
OrthoDBEOG708W01.
PhylomeDBQ8IWS0.
TreeFamTF325426.

Gene expression databases

ArrayExpressQ8IWS0.
BgeeQ8IWS0.
CleanExHS_PHF6.
GenevestigatorQ8IWS0.

Family and domain databases

InterProIPR001965. Znf_PHD.
[Graphical view]
SMARTSM00249. PHD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPHF6. human.
GeneWikiPHF6.
GenomeRNAi84295.
NextBio35476748.
PROQ8IWS0.
SOURCESearch...

Entry information

Entry namePHF6_HUMAN
AccessionPrimary (citable) accession number: Q8IWS0
Secondary accession number(s): A8K230 expand/collapse secondary AC list , B4E0G4, D3DTG3, E9PC97, Q5JRC7, Q5JRC8, Q96JK3, Q9BRU0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM