O75530 · EED_HUMAN
- ProteinPolycomb protein EED
- GeneEED
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids441 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | cytosol | |
Cellular Component | ESC/E(Z) complex | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | enzyme activator activity | |
Molecular Function | histone methyltransferase activity | |
Molecular Function | identical protein binding | |
Molecular Function | transcription corepressor binding | |
Biological Process | heterochromatin formation | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | spinal cord development |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePolycomb protein EED
- Short nameshEED
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75530
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cohen-Gibson syndrome (COGIS)
- Note
- DescriptionAn autosomal dominant overgrowth disorder characterized by accelerated osseous maturation, advanced bone age, skeletal abnormalities including flaring of the metaphyses of the long bones, large hands with long fingers and camptodactyly, scoliosis, cervical spine anomalies, dysmorphic facial features, and variable intellectual disability.
- See alsoMIM:617561
Natural variants in COGIS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_079255 | 194 | N>S | in COGIS | |
VAR_079256 | 236 | R>G | in COGIS | |
VAR_078316 | 236 | R>T | in COGIS; decreased trimethylation of 'Lys-27' of histone H3; no effect on interaction with EZH2; dbSNP:rs1131692176 | |
VAR_079257 | 258 | H>Y | in COGIS; dbSNP:rs1131692174 | |
VAR_079258 | 302 | R>G | in COGIS; dbSNP:rs1131692175 | |
VAR_078317 | 302 | R>S | in COGIS; decreased trimethylation of 'Lys-27' of histone H3; dbSNP:rs1131692173 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 97 | Abolishes binding to H3K27me3. | ||||
Sequence: F → A | ||||||
Mutagenesis | 148 | Abolishes binding to H3K27me3. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 193 | Impairs interaction with EZH2. | ||||
Sequence: I → N | ||||||
Natural variant | VAR_079255 | 194 | in COGIS | |||
Sequence: N → S | ||||||
Mutagenesis | 196 | Impairs interaction with EZH2. | ||||
Sequence: L → P | ||||||
Natural variant | VAR_079256 | 236 | in COGIS | |||
Sequence: R → G | ||||||
Natural variant | VAR_078316 | 236 | in COGIS; decreased trimethylation of 'Lys-27' of histone H3; no effect on interaction with EZH2; dbSNP:rs1131692176 | |||
Sequence: R → T | ||||||
Natural variant | VAR_079257 | 258 | in COGIS; dbSNP:rs1131692174 | |||
Sequence: H → Y | ||||||
Mutagenesis | 300-301 | Impairs interaction with the matrix protein MA of HIV-1. | ||||
Sequence: ST → AA | ||||||
Natural variant | VAR_079258 | 302 | in COGIS; dbSNP:rs1131692175 | |||
Sequence: R → G | ||||||
Natural variant | VAR_078317 | 302 | in COGIS; decreased trimethylation of 'Lys-27' of histone H3; dbSNP:rs1131692173 | |||
Sequence: R → S | ||||||
Mutagenesis | 305-308 | Impairs interaction with the matrix protein MA of HIV-1. | ||||
Sequence: HRNY → AAAA | ||||||
Mutagenesis | 364 | Abolishes binding to H3K27me3. | ||||
Sequence: W → A | ||||||
Mutagenesis | 364 | Abolishes binding to H3K27me3. | ||||
Sequence: W → L | ||||||
Mutagenesis | 365 | Abolishes binding to H3K27me3. | ||||
Sequence: Y → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 443 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000343725 | 2-441 | UniProt | Polycomb protein EED | |||
Sequence: SEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR | |||||||
Modified residue | 34 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 55 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 66 | UniProt | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 66 | UniProt | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 66 | UniProt | N6-methyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 197 | UniProt | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 197 | UniProt | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 197 | UniProt | N6-methyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 268 | UniProt | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 268 | UniProt | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 268 | UniProt | N6-methyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 284 | UniProt | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 284 | UniProt | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 284 | UniProt | N6-methyllysine; alternate | ||||
Sequence: K |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Developmental stage
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-72 | Disordered | ||||
Sequence: MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGK | ||||||
Compositional bias | 41-64 | Polar residues | ||||
Sequence: AVSIESGTNTERPDTPTNTPNAPG | ||||||
Region | 81-441 | Interaction with EZH2 | ||||
Sequence: SFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR | ||||||
Repeat | 91-134 | WD 1 | ||||
Sequence: DHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRL | ||||||
Repeat | 142-185 | WD 2 | ||||
Sequence: DADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKH | ||||||
Region | 149-303 | Required for interaction with the matrix protein MA of HIV-1 | ||||
Sequence: TCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRD | ||||||
Repeat | 188-228 | WD 3 | ||||
Sequence: GHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAI | ||||||
Repeat | 234-275 | WD 4 | ||||
Sequence: GHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIK | ||||||
Region | 301-441 | Required for interaction with the matrix protein MA of HIV-1 | ||||
Sequence: TRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR | ||||||
Repeat | 304-341 | WD 5 | ||||
Sequence: IHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDID | ||||||
Repeat | 359-399 | WD 6 | ||||
Sequence: SQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKA | ||||||
Repeat | 408-441 | WD 7 | ||||
Sequence: KCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing & Alternative initiation. Additional isoforms may be produced by alternative initiation, both from non-canonical start codons upstream of the initiator methionine displayed and from other canonical start codons downstream of that displayed (PubMed:15099518, PubMed:15684044). The precise sites of translation initiation have not been unambiguously identified.
O75530-1
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.
- Name1
- Length441
- Mass (Da)50,198
- Last updated2008-07-22 v2
- ChecksumD2E0A5BA27C0499A
O75530-2
- Name2
- Differences from canonical
- 322-322: K → KSGRAILHSHQQCMRDPVSPNLRQHL
O75530-3
- Name3
- Differences from canonical
- 401-441: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YEL4 | H0YEL4_HUMAN | EED | 115 | ||
A0A5F9ZI63 | A0A5F9ZI63_HUMAN | EED | 501 | ||
A0A9L9PY60 | A0A9L9PY60_HUMAN | EED | 406 | ||
E9PMU3 | E9PMU3_HUMAN | EED | 106 | ||
E9PJK2 | E9PJK2_HUMAN | EED | 361 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 32 | in Ref. 8; AAC68675 | ||||
Sequence: D → E | ||||||
Compositional bias | 41-64 | Polar residues | ||||
Sequence: AVSIESGTNTERPDTPTNTPNAPG | ||||||
Sequence conflict | 74 | in Ref. 3; AAD08714/AAD08815 | ||||
Sequence: K → S | ||||||
Alternative sequence | VSP_034691 | 322 | in isoform 2 | |||
Sequence: K → KSGRAILHSHQQCMRDPVSPNLRQHL | ||||||
Sequence conflict | 337 | in Ref. 3; AAD08714/AAD08815 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_034692 | 401-441 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 417 | in Ref. 4; BAF84809 | ||||
Sequence: S → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF080227 EMBL· GenBank· DDBJ | AAC95144.1 EMBL· GenBank· DDBJ | mRNA | ||
AF070418 EMBL· GenBank· DDBJ | AAC23685.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U90651 EMBL· GenBank· DDBJ | AAD08714.1 EMBL· GenBank· DDBJ | mRNA | ||
AF099032 EMBL· GenBank· DDBJ | AAD08815.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292120 EMBL· GenBank· DDBJ | BAF84809.1 EMBL· GenBank· DDBJ | mRNA | ||
AP003084 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471076 EMBL· GenBank· DDBJ | EAW75129.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471076 EMBL· GenBank· DDBJ | EAW75130.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC047672 EMBL· GenBank· DDBJ | AAH47672.1 EMBL· GenBank· DDBJ | mRNA | ||
BC068995 EMBL· GenBank· DDBJ | AAH68995.1 EMBL· GenBank· DDBJ | mRNA | ||
AF078933 EMBL· GenBank· DDBJ | AAC68675.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |