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Protein

Polycomb group RING finger protein 6

Gene

PCGF6

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

Functioni

Transcriptional repressor. May modulate the levels of histone H3K4Me3 by activating KDM5D histone demethylase. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri134 – 17340RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Polycomb group RING finger protein 6
Alternative name(s):
Mel18 and Bmi1-like RING finger
RING finger protein 134
Gene namesi
Name:PCGF6
Synonyms:MBLR, RNF134
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:21156. PCGF6.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
  • PcG protein complex Source: UniProtKB
  • PRC1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301S → A: Abolishes phosphorylation. 1 Publication
Mutagenesisi57 – 571S → A: Does not abolish phosphorylation. 1 Publication
Mutagenesisi59 – 591S → A: Does not abolish phosphorylation. 1 Publication
Mutagenesisi69 – 691S → A: Does not abolish phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA134887110.

Polymorphism and mutation databases

BioMutaiPCGF6.
DMDMi116242703.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Polycomb group RING finger protein 6PRO_0000055989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Phosphoserine1 Publication
Modified residuei115 – 1151PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated during mitosis. Phosphorylated on Ser-30 by CDK7 in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BYE7.
MaxQBiQ9BYE7.
PaxDbiQ9BYE7.
PRIDEiQ9BYE7.

PTM databases

iPTMnetiQ9BYE7.
PhosphoSiteiQ9BYE7.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9BYE7.
CleanExiHS_PCGF6.
GenevisibleiQ9BYE7. HS.

Organism-specific databases

HPAiHPA054086.

Interactioni

Subunit structurei

Component of a PRC1-like complex. Interacts with BMI1/PCGF4, RING1 and RNF2. Interacts with KDM5D. Interacts with CBX4, CBX6, CBX7 and CBX8.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX4O00257-32EBI-1048026,EBI-4392727
CBX7O959312EBI-1048026,EBI-3923843
CBX8Q9HC522EBI-1048026,EBI-712912

Protein-protein interaction databases

BioGridi123896. 65 interactions.
DIPiDIP-50946N.
IntActiQ9BYE7. 19 interactions.
STRINGi9606.ENSP00000358862.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi130 – 1323Combined sources
Turni135 – 1373Combined sources
Beta strandi148 – 1503Combined sources
Helixi156 – 16510Combined sources
Turni170 – 1723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJBNMR-A124-182[»]
ProteinModelPortaliQ9BYE7.
SMRiQ9BYE7. Positions 65-214.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BYE7.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili72 – 11039Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 6645Pro-richAdd
BLAST
Compositional biasi63 – 12058Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri134 – 17340RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2660. Eukaryota.
ENOG410XPCN. LUCA.
GeneTreeiENSGT00550000074463.
HOGENOMiHOG000231946.
HOVERGENiHBG052826.
InParanoidiQ9BYE7.
KOiK11470.
OMAiIGANEDT.
OrthoDBiEOG754HQ5.
PhylomeDBiQ9BYE7.
TreeFamiTF324206.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR029071. Ubiquitin-rel_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BYE7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEGVAVVTAG SVGAAKTEGA AALPPPPPVS PPALTPAPAA GEEGPAPLSE
60 70 80 90 100
TGAPGCSGSR PPELEPERSL GRFRGRFEDE DEELEEEEEL EEEEEEEEED
110 120 130 140 150
MSHFSLRLEG GRQDSEDEEE RLINLSELTP YILCSICKGY LIDATTITEC
160 170 180 190 200
LHTFCKSCIV RHFYYSNRCP KCNIVVHQTQ PLYNIRLDRQ LQDIVYKLVI
210 220 230 240 250
NLEEREKKQM HDFYKERGLE VPKPAVPQPV PSSKGRSKKV LESVFRIPPE
260 270 280 290 300
LDMSLLLEFI GANEGTGHFK PLEKKFVRVS GEATIGHVEK FLRRKMGLDP
310 320 330 340 350
ACQVDIICGD HLLEQYQTLR EIRRAIGDAA MQDGLLVLHY GLVVSPLKIT
Length:350
Mass (Da):39,047
Last modified:October 17, 2006 - v2
Checksum:i05977FE6F14972DE
GO
Isoform 3 (identifier: Q9BYE7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     186-186: R → S
     187-261: Missing.

Show »
Length:275
Mass (Da):30,249
Checksum:iFA50B97D5A39281B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571L → P in BAF83368 (PubMed:14702039).Curated
Sequence conflicti261 – 2611G → S in AAH07602 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231L → LPP.2 Publications
VAR_054312

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei186 – 1861R → S in isoform 3. 1 PublicationVSP_042007
Alternative sequencei187 – 26175Missing in isoform 3. 1 PublicationVSP_042008Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047006 mRNA. Translation: BAB40779.1.
AK027885 mRNA. No translation available.
AK290679 mRNA. Translation: BAF83368.1.
AL591408 Genomic DNA. Translation: CAI16745.1.
AL591408 Genomic DNA. Translation: CAI16746.1.
BC007602 mRNA. Translation: AAH07602.1.
BC010235 mRNA. Translation: AAH10235.1.
CCDSiCCDS31275.1. [Q9BYE7-1]
CCDS7546.1. [Q9BYE7-3]
RefSeqiNP_001011663.1. NM_001011663.1. [Q9BYE7-1]
NP_115530.2. NM_032154.3. [Q9BYE7-3]
UniGeneiHs.335808.

Genome annotation databases

EnsembliENST00000337211; ENSP00000338845; ENSG00000156374. [Q9BYE7-3]
ENST00000369847; ENSP00000358862; ENSG00000156374. [Q9BYE7-1]
GeneIDi84108.
KEGGihsa:84108.
UCSCiuc001kwt.3. human. [Q9BYE7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047006 mRNA. Translation: BAB40779.1.
AK027885 mRNA. No translation available.
AK290679 mRNA. Translation: BAF83368.1.
AL591408 Genomic DNA. Translation: CAI16745.1.
AL591408 Genomic DNA. Translation: CAI16746.1.
BC007602 mRNA. Translation: AAH07602.1.
BC010235 mRNA. Translation: AAH10235.1.
CCDSiCCDS31275.1. [Q9BYE7-1]
CCDS7546.1. [Q9BYE7-3]
RefSeqiNP_001011663.1. NM_001011663.1. [Q9BYE7-1]
NP_115530.2. NM_032154.3. [Q9BYE7-3]
UniGeneiHs.335808.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DJBNMR-A124-182[»]
ProteinModelPortaliQ9BYE7.
SMRiQ9BYE7. Positions 65-214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123896. 65 interactions.
DIPiDIP-50946N.
IntActiQ9BYE7. 19 interactions.
STRINGi9606.ENSP00000358862.

PTM databases

iPTMnetiQ9BYE7.
PhosphoSiteiQ9BYE7.

Polymorphism and mutation databases

BioMutaiPCGF6.
DMDMi116242703.

Proteomic databases

EPDiQ9BYE7.
MaxQBiQ9BYE7.
PaxDbiQ9BYE7.
PRIDEiQ9BYE7.

Protocols and materials databases

DNASUi84108.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337211; ENSP00000338845; ENSG00000156374. [Q9BYE7-3]
ENST00000369847; ENSP00000358862; ENSG00000156374. [Q9BYE7-1]
GeneIDi84108.
KEGGihsa:84108.
UCSCiuc001kwt.3. human. [Q9BYE7-1]

Organism-specific databases

CTDi84108.
GeneCardsiPCGF6.
H-InvDBHIX0014963.
HGNCiHGNC:21156. PCGF6.
HPAiHPA054086.
MIMi607816. gene.
neXtProtiNX_Q9BYE7.
PharmGKBiPA134887110.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2660. Eukaryota.
ENOG410XPCN. LUCA.
GeneTreeiENSGT00550000074463.
HOGENOMiHOG000231946.
HOVERGENiHBG052826.
InParanoidiQ9BYE7.
KOiK11470.
OMAiIGANEDT.
OrthoDBiEOG754HQ5.
PhylomeDBiQ9BYE7.
TreeFamiTF324206.

Miscellaneous databases

ChiTaRSiPCGF6. human.
EvolutionaryTraceiQ9BYE7.
GeneWikiiPCGF6.
GenomeRNAii84108.
NextBioi73375.
PROiQ9BYE7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BYE7.
CleanExiHS_PCGF6.
GenevisibleiQ9BYE7. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR029071. Ubiquitin-rel_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation."
    Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.
    Genes Cells 7:835-850(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSCRIPTIONAL REPRESSION, INTERACTION WITH BMI1; RING1 AND RNF2, PHOSPHORYLATION AT SER-30, MUTAGENESIS OF SER-30; SER-57; SER-59 AND SER-69, VARIANT PRO-PRO-23 INS, SUBCELLULAR LOCATION.
    Tissue: Testis.
  2. "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] (ISOFORM 1).
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 3), VARIANT PRO-PRO-23 INS.
    Tissue: Cervix and Eye.
  5. "Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein."
    Lee M.G., Norman J., Shilatifard A., Shiekhattar R.
    Cell 128:877-887(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KDM5D, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus."
    Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.
    PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX.
  7. "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-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells."
    Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX4; CBX6; CBX7 AND CBX8, SUBCELLULAR LOCATION.
  9. "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-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Solution structure of the RING domain of the human polycomb group RING finger protein 6."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 124-182.

Entry informationi

Entry nameiPCGF6_HUMAN
AccessioniPrimary (citable) accession number: Q9BYE7
Secondary accession number(s): A8K3R4
, Q5SYD1, Q5SYD6, Q96ID9, Q96SJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 17, 2006
Last modified: May 11, 2016
This is version 137 of the entry and version 2 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 10
    Human chromosome 10: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.