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Q92800

- EZH1_HUMAN

UniProt

Q92800 - EZH1_HUMAN

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Protein

Histone-lysine N-methyltransferase EZH1

Gene

EZH1

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

Functioni

Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

GO - Molecular functioni

  1. chromatin binding Source: ProtInc
  2. histone methyltransferase activity (H3-K27 specific) Source: Ensembl

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase EZH1 (EC:2.1.1.43)
Alternative name(s):
ENX-2
Enhancer of zeste homolog 1
Gene namesi
Name:EZH1
Synonyms:KIAA0388
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:3526. EZH1.

Subcellular locationi

Nucleus 1 Publication
Note: Colocalizes with trimethylated 'Lys-27' of histone H3.

GO - Cellular componenti

  1. ESC/E(Z) complex Source: UniProtKB
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi690 – 6901H → A: Loss of methyltransferase activity. 1 Publication

Organism-specific databases

PharmGKBiPA27938.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747Histone-lysine N-methyltransferase EZH1PRO_0000213990Add
BLAST

Proteomic databases

MaxQBiQ92800.
PaxDbiQ92800.
PRIDEiQ92800.

PTM databases

PhosphoSiteiQ92800.

Expressioni

Gene expression databases

BgeeiQ92800.
CleanExiHS_EZH1.
ExpressionAtlasiQ92800. baseline and differential.
GenevestigatoriQ92800.

Organism-specific databases

HPAiHPA005478.

Interactioni

Subunit structurei

Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2/EED-EZH1 is less abundant than the PRC2/EED-EZH2 complex, has weak methyltransferase activity and compacts chromatin in the absence of the methyltransferase cofactor S-adenosyl-L-methionine (SAM).1 Publication

Protein-protein interaction databases

BioGridi108445. 10 interactions.
DIPiDIP-58580N.

Structurei

3D structure databases

ProteinModelPortaliQ92800.
SMRiQ92800. Positions 521-730.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini504 – 606103CXCPROSITE-ProRule annotationAdd
BLAST
Domaini613 – 728116SETPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi491 – 4966Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi524 – 60683Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.PROSITE-ProRule annotation
Contains 1 CXC domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000118855.
HOVERGENiHBG002453.
InParanoidiQ92800.
KOiK17451.
OMAiSTQVYNY.
OrthoDBiEOG7VB2DR.
PhylomeDBiQ92800.
TreeFamiTF314509.

Family and domain databases

InterProiIPR026489. CXC_dom.
IPR021654. EZH2_WD-Binding.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view]
PfamiPF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92800-1) [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
MEIPNPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ
60 70 80 90 100
EKTQILNEEW KKLRVQPVQS MKPVSGHPFL KKCTIESIFP GFASQHMLMR
110 120 130 140 150
SLNTVALVPI MYSWSPLQQN FMVEDETVLC NIPYMGDEVK EEDETFIEEL
160 170 180 190 200
INNYDGKVHG EEEMIPGSVL ISDAVFLELV DALNQYSDEE EEGHNDTSDG
210 220 230 240 250
KQDDSKEDLP VTRKRKRHAI EGNKKSSKKQ FPNDMIFSAI ASMFPENGVP
260 270 280 290 300
DDMKERYREL TEMSDPNALP PQCTPNIDGP NAKSVQREQS LHSFHTLFCR
310 320 330 340 350
RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL LEGAKEYAML
360 370 380 390 400
HNPRSKCSGR RRRRHHIVSA SCSNASASAV AETKEGDSDR DTGNDWASSS
410 420 430 440 450
SEANSRCQTP TKQKASPAPP QLCVVEAPSE PVEWTGAEES LFRVFHGTYF
460 470 480 490 500
NNFCSIARLL GTKTCKQVFQ FAVKESLILK LPTDELMNPS QKKKRKHRLW
510 520 530 540 550
AAHCRKIQLK KDNSSTQVYN YQPCDHPDRP CDSTCPCIMT QNFCEKFCQC
560 570 580 590 600
NPDCQNRFPG CRCKTQCNTK QCPCYLAVRE CDPDLCLTCG ASEHWDCKVV
610 620 630 640 650
SCKNCSIQRG LKKHLLLAPS DVAGWGTFIK ESVQKNEFIS EYCGELISQD
660 670 680 690 700
EADRRGKVYD KYMSSFLFNL NNDFVVDATR KGNKIRFANH SVNPNCYAKV
710 720 730 740
VMVNGDHRIG IFAKRAIQAG EELFFDYRYS QADALKYVGI ERETDVL
Length:747
Mass (Da):85,271
Last modified:July 15, 1998 - v2
Checksum:i7CFC52269CDA011B
GO
Isoform 2 (identifier: Q92800-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEDYSKM

Note: No experimental confirmation available.

Show »
Length:753
Mass (Da):86,025
Checksum:iDC9F0DF9E60EFA55
GO
Isoform 3 (identifier: Q92800-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     83-122: Missing.

Note: No experimental confirmation available.

Show »
Length:707
Mass (Da):80,699
Checksum:i23A8A70A4B0A426F
GO
Isoform 4 (identifier: Q92800-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.

Note: No experimental confirmation available.

Show »
Length:677
Mass (Da):76,952
Checksum:i319C9A015FC818F1
GO
Isoform 5 (identifier: Q92800-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-162: MEIPNPPTSK...NYDGKVHGEE → MEEASCPTCSVNEACEWTPFSQK

Note: No experimental confirmation available.

Show »
Length:608
Mass (Da):68,961
Checksum:iE9C73223693D99DC
GO

Sequence cautioni

The sequence BAA20842.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241M → I in BAG58503. (PubMed:14702039)Curated
Sequence conflicti353 – 3531P → S in BAA25019. (PubMed:9473645)Curated
Sequence conflicti389 – 3891D → Y in BAG65579. (PubMed:14702039)Curated
Sequence conflicti488 – 4881N → Y in AAC50778. (PubMed:8921387)Curated
Sequence conflicti532 – 5354DSTC → EAL in BAA25019. (PubMed:9473645)Curated
Sequence conflicti591 – 60212ASEHW…KVVSC → PQSTGTARWFPV in BAA25019. (PubMed:9473645)CuratedAdd
BLAST
Sequence conflicti631 – 6311E → K in BAG61734. (PubMed:14702039)Curated
Sequence conflicti697 – 6971Y → C in BAG58659. (PubMed:14702039)Curated
Sequence conflicti700 – 74748VVMVN…ETDVL → GESQ in BAA25019. (PubMed:9473645)CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 162162MEIPN…VHGEE → MEEASCPTCSVNEACEWTPF SQK in isoform 5. 1 PublicationVSP_036384Add
BLAST
Alternative sequencei1 – 7070Missing in isoform 4. 1 PublicationVSP_036385Add
BLAST
Alternative sequencei1 – 11M → MEDYSKM in isoform 2. 1 PublicationVSP_036386
Alternative sequencei83 – 12240Missing in isoform 3. 1 PublicationVSP_036387Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50315 mRNA. Translation: AAC50778.1.
AB004818 mRNA. Translation: BAA25019.1.
AB002386 mRNA. Translation: BAA20842.2. Different initiation.
BT009782 mRNA. Translation: AAP88784.1.
AK304835 mRNA. Translation: BAG65579.1.
AK295626 mRNA. Translation: BAG58503.1.
AK295853 mRNA. Translation: BAG58659.1.
AK299887 mRNA. Translation: BAG61734.1.
AC100793 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60870.1.
BC015882 mRNA. Translation: AAH15882.1.
L38934 mRNA. Translation: AAB59574.1.
CCDSiCCDS32659.1. [Q92800-1]
RefSeqiNP_001982.2. NM_001991.3. [Q92800-1]
XP_005257201.1. XM_005257144.1. [Q92800-2]
XP_005257203.1. XM_005257146.1. [Q92800-3]
UniGeneiHs.194669.

Genome annotation databases

EnsembliENST00000428826; ENSP00000404658; ENSG00000108799. [Q92800-1]
ENST00000585893; ENSP00000467871; ENSG00000108799. [Q92800-3]
ENST00000590078; ENSP00000465220; ENSG00000108799. [Q92800-4]
ENST00000592743; ENSP00000466924; ENSG00000108799. [Q92800-1]
GeneIDi2145.
KEGGihsa:2145.
UCSCiuc002iaz.3. human. [Q92800-1]
uc010cyo.1. human. [Q92800-5]
uc010wgu.2. human. [Q92800-2]
uc010wgv.2. human. [Q92800-3]

Polymorphism databases

DMDMi3334182.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50315 mRNA. Translation: AAC50778.1 .
AB004818 mRNA. Translation: BAA25019.1 .
AB002386 mRNA. Translation: BAA20842.2 . Different initiation.
BT009782 mRNA. Translation: AAP88784.1 .
AK304835 mRNA. Translation: BAG65579.1 .
AK295626 mRNA. Translation: BAG58503.1 .
AK295853 mRNA. Translation: BAG58659.1 .
AK299887 mRNA. Translation: BAG61734.1 .
AC100793 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60870.1 .
BC015882 mRNA. Translation: AAH15882.1 .
L38934 mRNA. Translation: AAB59574.1 .
CCDSi CCDS32659.1. [Q92800-1 ]
RefSeqi NP_001982.2. NM_001991.3. [Q92800-1 ]
XP_005257201.1. XM_005257144.1. [Q92800-2 ]
XP_005257203.1. XM_005257146.1. [Q92800-3 ]
UniGenei Hs.194669.

3D structure databases

ProteinModelPortali Q92800.
SMRi Q92800. Positions 521-730.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108445. 10 interactions.
DIPi DIP-58580N.

Chemistry

ChEMBLi CHEMBL3137287.

PTM databases

PhosphoSitei Q92800.

Polymorphism databases

DMDMi 3334182.

Proteomic databases

MaxQBi Q92800.
PaxDbi Q92800.
PRIDEi Q92800.

Protocols and materials databases

DNASUi 2145.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000428826 ; ENSP00000404658 ; ENSG00000108799 . [Q92800-1 ]
ENST00000585893 ; ENSP00000467871 ; ENSG00000108799 . [Q92800-3 ]
ENST00000590078 ; ENSP00000465220 ; ENSG00000108799 . [Q92800-4 ]
ENST00000592743 ; ENSP00000466924 ; ENSG00000108799 . [Q92800-1 ]
GeneIDi 2145.
KEGGi hsa:2145.
UCSCi uc002iaz.3. human. [Q92800-1 ]
uc010cyo.1. human. [Q92800-5 ]
uc010wgu.2. human. [Q92800-2 ]
uc010wgv.2. human. [Q92800-3 ]

Organism-specific databases

CTDi 2145.
GeneCardsi GC17M040852.
HGNCi HGNC:3526. EZH1.
HPAi HPA005478.
MIMi 601674. gene.
neXtProti NX_Q92800.
PharmGKBi PA27938.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000118855.
HOVERGENi HBG002453.
InParanoidi Q92800.
KOi K17451.
OMAi STQVYNY.
OrthoDBi EOG7VB2DR.
PhylomeDBi Q92800.
TreeFami TF314509.

Miscellaneous databases

ChiTaRSi EZH1. human.
GeneWikii EZH1.
GenomeRNAii 2145.
NextBioi 8671.
PROi Q92800.
SOURCEi Search...

Gene expression databases

Bgeei Q92800.
CleanExi HS_EZH1.
ExpressionAtlasi Q92800. baseline and differential.
Genevestigatori Q92800.

Family and domain databases

InterProi IPR026489. CXC_dom.
IPR021654. EZH2_WD-Binding.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view ]
PROSITEi PS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning and expression of a human/mouse Polycomb group gene, ENX-2/Enx-2."
    Ogawa M., Hiraoka Y., Taniguchi K., Aiso S.
    Biochim. Biophys. Acta 1395:151-158(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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 2; 3; 4 AND 5).
    Tissue: Brain, Hippocampus and Uterus.
  6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1).
    Tissue: Uterus.
  9. "Generation of a transcription map at the HSD17B locus centromeric to BRCA1 at 17q21."
    Rommens J.M., Durocher F., McArthur J., Tonin P., Leblanc J.-F., Allen T., Samson C., Ferri L., Narod S., Morgan K., Simard J.
    Genomics 28:530-542(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 434-538.
  10. "Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms."
    Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L., Dynlacht B.D., Reinberg D.
    Mol. Cell 32:503-518(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX, MUTAGENESIS OF HIS-690.

Entry informationi

Entry nameiEZH1_HUMAN
AccessioniPrimary (citable) accession number: Q92800
Secondary accession number(s): A6NCH6
, B4DIJ1, B4DIZ7, B4DSS2, B4E3R7, O43287, Q14459, Q53XP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: October 29, 2014
This is version 135 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3