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Q8IWS0

- PHF6_HUMAN

UniProt

Q8IWS0 - PHF6_HUMAN

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Protein

PHD finger protein 6

Gene

PHF6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. ribonucleoprotein complex binding Source: UniProt
  8. scaffold protein binding Source: UniProt
  9. tubulin binding Source: UniProt
  10. zinc ion binding Source: InterPro

GO - Biological processi

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

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
Complete GO annotation...

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

BgeeiQ8IWS0.
CleanExiHS_PHF6.
ExpressionAtlasiQ8IWS0. baseline and differential.
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 – 2153Combined sources
Helixi219 – 2213Combined sources
Helixi222 – 2254Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi237 – 2393Combined sources
Helixi240 – 2445Combined sources
Beta strandi257 – 2593Combined sources
Helixi265 – 27511Combined sources
Turni281 – 2833Combined sources
Beta strandi290 – 2945Combined sources
Helixi303 – 3086Combined sources
Beta strandi312 – 3165Combined sources
Turni317 – 3204Combined sources
Beta strandi321 – 3255Combined sources
Helixi327 – 3293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063780.
HOGENOMiHOG000026798.
HOVERGENiHBG049389.
InParanoidiQ8IWS0.
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

        10         20         30         40         50
MSSSVEQKKG PTRQRKCGFC KSNRDKECGQ LLISENQKVA AHHKCMLFSS
60 70 80 90 100
ALVSSHSDNE SLGGFSIEDV QKEIKRGTKL MCSLCHCPGA TIGCDVKTCH
110 120 130 140 150
RTYHYHCALH DKAQIREKPS QGIYMVYCRK HKKTAHNSEA DLEESFNEHE
160 170 180 190 200
LEPSSPKSKK KSRKGRPRKT NFKGLSEDTR STSSHGTDEM ESSSYRDRSP
210 220 230 240 250
HRSSPSDTRP KCGFCHVGEE ENEARGKLHI FNAKKAAAHY KCMLFSSGTV
260 270 280 290 300
QLTTTSRAEF GDFDIKTVLQ EIKRGKRMKC TLCSQPGATI GCEIKACVKT
310 320 330 340 350
YHYHCGVQDK AKYIENMSRG IYKLYCKNHS GNDERDEEDE ERESKSRGKV
360
EIDQQQLTQQ QLNGN
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. Curated

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:
EMBLi
GenBanki
DDBJi
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]
uc011mvk.2. human.

Polymorphism databases

DMDMi42559482.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ]
uc011mvk.2. human.

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.
GeneTreei ENSGT00530000063780.
HOGENOMi HOG000026798.
HOVERGENi HBG049389.
InParanoidi Q8IWS0.
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

Bgeei Q8IWS0.
CleanExi HS_PHF6.
ExpressionAtlasi Q8IWS0. baseline and differential.
Genevestigatori Q8IWS0.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: November 26, 2014
This is version 113 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

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