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Q8IWS0

- PHF6_HUMAN

UniProt

Q8IWS0 - PHF6_HUMAN

Protein

PHD finger protein 6

Gene

PHF6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri17 – 5034C2HC-type; pre-PHDAdd
    BLAST
    Zinc fingeri79 – 13153PHD-type 1; degenerateAdd
    BLAST
    Zinc fingeri212 – 24736C2HC-type; pre-PHDAdd
    BLAST
    Zinc fingeri277 – 32953PHD-type 2; degenerateAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. enzyme binding Source: UniProt
    3. histone binding Source: UniProt
    4. histone deacetylase binding Source: UniProt
    5. phosphoprotein binding Source: UniProt
    6. poly(A) RNA binding Source: UniProtKB
    7. protein binding Source: UniProt
    8. ribonucleoprotein complex binding Source: UniProt
    9. scaffold protein binding Source: UniProt
    10. tubulin binding Source: UniProt
    11. zinc ion binding Source: InterPro

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PHD finger protein 6
    Alternative name(s):
    PHD-like zinc finger protein
    Gene namesi
    Name:PHF6
    Synonyms:KIAA1823
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:18145. PHF6.

    Subcellular locationi

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

    GO - Cellular componenti

    1. nucleolus Source: UniProt
    2. nucleoplasm Source: UniProt
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451C → Y in BFLS; Loss of interaction with UBTF. 1 Publication
    Corresponds to variant rs28935179 [ dbSNP | Ensembl ].
    VAR_017633
    Natural varianti99 – 991C → F in BFLS; Loss of interaction with UBTF. 1 Publication
    VAR_017634
    Natural varianti229 – 2291H → R in BFLS. 1 Publication
    VAR_017635
    Natural varianti234 – 2341K → E in BFLS. 1 Publication
    VAR_017636
    Natural varianti257 – 2571R → G in BFLS. 1 Publication
    VAR_017637

    Keywords - Diseasei

    Disease mutation, Epilepsy, Mental retardation

    Organism-specific databases

    MIMi301900. phenotype.
    Orphaneti127. Borjeson-Forssman-Lehmann syndrome.
    PharmGKBiPA33263.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 365364PHD finger protein 6PRO_0000059293Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei138 – 1381Phosphoserine2 Publications
    Modified residuei145 – 1451Phosphoserine2 Publications
    Modified residuei155 – 1551Phosphoserine1 Publication
    Modified residuei199 – 1991Phosphoserine1 Publication
    Modified residuei358 – 3581Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8IWS0.
    PaxDbiQ8IWS0.
    PeptideAtlasiQ8IWS0.
    PRIDEiQ8IWS0.

    PTM databases

    PhosphoSiteiQ8IWS0.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ8IWS0.
    BgeeiQ8IWS0.
    CleanExiHS_PHF6.
    GenevestigatoriQ8IWS0.

    Organism-specific databases

    HPAiHPA001023.

    Interactioni

    Subunit structurei

    Interacts with UBTF. Interacts with the NuRD complex component RBBP4 (via the nucleolar localization motif), the interaction mediates transcriptional repression activity.2 Publications

    Protein-protein interaction databases

    BioGridi124022. 9 interactions.
    IntActiQ8IWS0. 2 interactions.
    MINTiMINT-4534083.
    STRINGi9606.ENSP00000329097.

    Structurei

    Secondary structure

    1
    365
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni213 – 2153
    Helixi219 – 2213
    Helixi222 – 2254
    Beta strandi228 – 2303
    Beta strandi237 – 2393
    Helixi240 – 2445
    Beta strandi257 – 2593
    Helixi265 – 27511
    Turni281 – 2833
    Beta strandi290 – 2945
    Helixi303 – 3086
    Beta strandi312 – 3165
    Turni317 – 3204
    Beta strandi321 – 3255
    Helixi327 – 3293

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NN2X-ray1.47A/B208-333[»]
    ProteinModelPortaliQ8IWS0.
    SMRiQ8IWS0. Positions 16-131, 208-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 131118Extended PHD1 domain (ePHD1)Add
    BLAST
    Regioni208 – 329122Extended PHD2 domain (ePHD2)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi13 – 164Nuclear localization signalSequence Analysis
    Motifi129 – 1335Nuclear localization signalSequence Analysis
    Motifi157 – 16913Nucleolar localization signalSequence AnalysisAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 2 C2HC-type zinc fingers.Curated
    Contains 2 PHD-type zinc fingers.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri17 – 5034C2HC-type; pre-PHDAdd
    BLAST
    Zinc fingeri79 – 13153PHD-type 1; degenerateAdd
    BLAST
    Zinc fingeri212 – 24736C2HC-type; pre-PHDAdd
    BLAST
    Zinc fingeri277 – 32953PHD-type 2; degenerateAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG282606.
    HOGENOMiHOG000026798.
    HOVERGENiHBG049389.
    OMAiISESPHI.
    OrthoDBiEOG708W01.
    PhylomeDBiQ8IWS0.
    TreeFamiTF325426.

    Family and domain databases

    InterProiIPR001965. Znf_PHD.
    [Graphical view]
    SMARTiSM00249. PHD. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IWS0-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSSSVEQKKG PTRQRKCGFC KSNRDKECGQ LLISENQKVA AHHKCMLFSS    50
    ALVSSHSDNE SLGGFSIEDV QKEIKRGTKL MCSLCHCPGA TIGCDVKTCH 100
    RTYHYHCALH DKAQIREKPS QGIYMVYCRK HKKTAHNSEA DLEESFNEHE 150
    LEPSSPKSKK KSRKGRPRKT NFKGLSEDTR STSSHGTDEM ESSSYRDRSP 200
    HRSSPSDTRP KCGFCHVGEE ENEARGKLHI FNAKKAAAHY KCMLFSSGTV 250
    QLTTTSRAEF GDFDIKTVLQ EIKRGKRMKC TLCSQPGATI GCEIKACVKT 300
    YHYHCGVQDK AKYIENMSRG IYKLYCKNHS GNDERDEEDE ERESKSRGKV 350
    EIDQQQLTQQ QLNGN 365
    Length:365
    Mass (Da):41,290
    Last modified:March 1, 2003 - v1
    Checksum:iE8E587909EF9701D
    GO
    Isoform 2 (identifier: Q8IWS0-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:312
    Mass (Da):35,329
    Checksum:i107F45F45063D7A0
    GO
    Isoform 3 (identifier: Q8IWS0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         140-140: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:364
    Mass (Da):41,219
    Checksum:i2BEB117AF92F7ECC
    GO
    Isoform 4 (identifier: Q8IWS0-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:310
    Mass (Da):35,187
    Checksum:iB6091E6AC014F78A
    GO
    Isoform 5 (identifier: Q8IWS0-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         47-80: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:331
    Mass (Da):37,628
    Checksum:iCA296A2F39167444
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti126 – 1261V → A in AAH05994. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451C → Y in BFLS; Loss of interaction with UBTF. 1 Publication
    Corresponds to variant rs28935179 [ dbSNP | Ensembl ].
    VAR_017633
    Natural varianti99 – 991C → F in BFLS; Loss of interaction with UBTF. 1 Publication
    VAR_017634
    Natural varianti229 – 2291H → R in BFLS. 1 Publication
    VAR_017635
    Natural varianti234 – 2341K → E in BFLS. 1 Publication
    VAR_017636
    Natural varianti257 – 2571R → G in BFLS. 1 Publication
    VAR_017637

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei47 – 8034Missing in isoform 5. 1 PublicationVSP_054937Add
    BLAST
    Alternative sequencei140 – 1401A → AA in isoform 2. 1 PublicationVSP_009372
    Alternative sequencei140 – 1401Missing in isoform 3 and isoform 4. 1 PublicationVSP_053441
    Alternative sequencei279 – 31133KCTLC…VQDKA → VCSFYICYATLHLICCFKFR VHPKFIQSSENLK in isoform 2 and isoform 4. 2 PublicationsVSP_009373Add
    BLAST
    Alternative sequencei312 – 36554Missing in isoform 2 and isoform 4. 2 PublicationsVSP_009374Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14639.1. [Q8IWS0-1]
    CCDS14640.1. [Q8IWS0-2]
    RefSeqiNP_001015877.1. NM_001015877.1. [Q8IWS0-1]
    NP_115711.2. NM_032335.3. [Q8IWS0-2]
    NP_115834.1. NM_032458.2. [Q8IWS0-1]
    UniGeneiHs.356501.

    Genome annotation databases

    EnsembliENST00000332070; ENSP00000329097; ENSG00000156531. [Q8IWS0-1]
    ENST00000370800; ENSP00000359836; ENSG00000156531. [Q8IWS0-2]
    ENST00000370803; ENSP00000359839; ENSG00000156531. [Q8IWS0-1]
    GeneIDi84295.
    KEGGihsa:84295.
    UCSCiuc004exh.3. human. [Q8IWS0-2]
    uc004exj.3. human. [Q8IWS0-1]

    Polymorphism databases

    DMDMi42559482.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14639.1. [Q8IWS0-1 ]
    CCDS14640.1. [Q8IWS0-2 ]
    RefSeqi NP_001015877.1. NM_001015877.1. [Q8IWS0-1 ]
    NP_115711.2. NM_032335.3. [Q8IWS0-2 ]
    NP_115834.1. NM_032458.2. [Q8IWS0-1 ]
    UniGenei Hs.356501.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NN2 X-ray 1.47 A/B 208-333 [» ]
    ProteinModelPortali Q8IWS0.
    SMRi Q8IWS0. Positions 16-131, 208-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124022. 9 interactions.
    IntActi Q8IWS0. 2 interactions.
    MINTi MINT-4534083.
    STRINGi 9606.ENSP00000329097.

    PTM databases

    PhosphoSitei Q8IWS0.

    Polymorphism databases

    DMDMi 42559482.

    Proteomic databases

    MaxQBi Q8IWS0.
    PaxDbi Q8IWS0.
    PeptideAtlasi Q8IWS0.
    PRIDEi Q8IWS0.

    Protocols and materials databases

    DNASUi 84295.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332070 ; ENSP00000329097 ; ENSG00000156531 . [Q8IWS0-1 ]
    ENST00000370800 ; ENSP00000359836 ; ENSG00000156531 . [Q8IWS0-2 ]
    ENST00000370803 ; ENSP00000359839 ; ENSG00000156531 . [Q8IWS0-1 ]
    GeneIDi 84295.
    KEGGi hsa:84295.
    UCSCi uc004exh.3. human. [Q8IWS0-2 ]
    uc004exj.3. human. [Q8IWS0-1 ]

    Organism-specific databases

    CTDi 84295.
    GeneCardsi GC0XP133507.
    HGNCi HGNC:18145. PHF6.
    HPAi HPA001023.
    MIMi 300414. gene.
    301900. phenotype.
    neXtProti NX_Q8IWS0.
    Orphaneti 127. Borjeson-Forssman-Lehmann syndrome.
    PharmGKBi PA33263.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282606.
    HOGENOMi HOG000026798.
    HOVERGENi HBG049389.
    OMAi ISESPHI.
    OrthoDBi EOG708W01.
    PhylomeDBi Q8IWS0.
    TreeFami TF325426.

    Miscellaneous databases

    ChiTaRSi PHF6. human.
    GeneWikii PHF6.
    GenomeRNAii 84295.
    NextBioi 35476748.
    PROi Q8IWS0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IWS0.
    Bgeei Q8IWS0.
    CleanExi HS_PHF6.
    Genevestigatori Q8IWS0.

    Family and domain databases

    InterProi IPR001965. Znf_PHD.
    [Graphical view ]
    SMARTi SM00249. PHD. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.
      , 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. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiPHF6_HUMAN
    AccessioniPrimary (citable) accession number: Q8IWS0
    Secondary accession number(s): A8K230
    , B4E0G4, D3DTG3, E9PC97, Q5JRC7, Q5JRC8, Q96JK3, Q9BRU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3