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Q15326

- ZMY11_HUMAN

UniProt

Q15326 - ZMY11_HUMAN

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Protein

Zinc finger MYND domain-containing protein 11

Gene

ZMYND11

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

Functioni

Chromatin reader that specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA polymerase II elongation. Does not bind other histone H3 subtypes (H3.1 or H3.2) (By similarity). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage. Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi258 – 2581ZincBy similarity
Metal bindingi261 – 2611ZincBy similarity
Metal bindingi277 – 2771ZincBy similarity
Metal bindingi281 – 2811Zinc; via tele nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri100 – 14849PHD-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri563 – 59836MYND-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. methylated histone binding Source: UniProtKB
  3. transcription corepressor activity Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell proliferation Source: ProtInc
  3. chromatin modification Source: UniProtKB-KW
  4. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  5. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  6. negative regulation of JNK cascade Source: UniProtKB
  7. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  8. regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
  10. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger MYND domain-containing protein 11
Alternative name(s):
Adenovirus 5 E1A-binding protein
Bone morphogenetic protein receptor-associated molecule 1
Protein BS69
Gene namesi
Name:ZMYND11
Synonyms:BRAM1, BS69
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:16966. ZMYND11.

Subcellular locationi

Nucleus. Chromosome
Note: Associates with chromatin and mitotic chromosomes.

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving ZMYND11 is a cause of acute poorly differentiated myeloid leukemia. Translocation (10;17)(p15;q21) with MBTD1.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi562 – 5621W → Y: Reduced interaction with PXLXP ligand MGA without affecting interaction with viral human adenovirus early E1A protein. 1 Publication
Mutagenesisi563 – 5631C → S: Abrogates binding to EZH2. 1 Publication
Mutagenesisi567 – 5682EE → KK: Reduced interaction with PXLXP ligand proteins. 1 Publication
Mutagenesisi599 – 6024RRKR → GGGG: Abolished interaction with PXLXP ligand proteins. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA128394578.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 602602Zinc finger MYND domain-containing protein 11PRO_0000211218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei421 – 4211Phosphoserine1 Publication

Post-translational modificationi

Sumoylated following its interaction with PIAS1 and UBE2I.1 Publication
Ubiquitinated, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15326.
PaxDbiQ15326.
PRIDEiQ15326.

PTM databases

PhosphoSiteiQ15326.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Down-regulated in breast cancer patients with poor prognosis.1 Publication

Gene expression databases

BgeeiQ15326.
CleanExiHS_ZMYND11.
ExpressionAtlasiQ15326. baseline and differential.
GenevestigatoriQ15326.

Organism-specific databases

HPAiHPA015816.
HPA030553.

Interactioni

Subunit structurei

Homooligomer; forms homooligomers via its C-terminus. Interacts with histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3). Interacts (via MYND-type zinc finger) with NCOR1. Interacts (via MYND-type zinc finger) with MGA protein (via PXLXP motif). Interacts (via MYND-type zinc finger) with EZH2. Interacts with C11orf30/EMSY and E2F6. Interacts with PIAS1 and UBE2I. Interacts (via MYND-type zinc finger) with human adenovirus early E1A protein (via PXLXP motif); this interaction inhibits E1A mediated transactivation. Interacts (via MYND-type zinc finger) with Epstein-Barr virus EBNA2 protein (via PXLXP motif). Interacts with Epstein-Barr virus-derived protein LMP1; leading to negatively regulate NF-kappa-B activation by Epstein-Barr virus-derived protein LMP1.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032553EBI-2623509,EBI-2603114From a different organism.
EBNA2P129782EBI-2623509,EBI-8052923From a different organism.
LMP1P032303EBI-2623509,EBI-6973030From a different organism.
LTBRP369415EBI-2623509,EBI-3509981
TRAF3Q131142EBI-2623509,EBI-357631

Protein-protein interaction databases

BioGridi115989. 36 interactions.
IntActiQ15326. 19 interactions.
MINTiMINT-156360.
STRINGi9606.ENSP00000309992.

Structurei

Secondary structure

1
602
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi157 – 16913Combined sources
Helixi198 – 2069Combined sources
Helixi213 – 23119Combined sources
Helixi236 – 25722Combined sources
Helixi259 – 2679Combined sources
Helixi272 – 2743Combined sources
Beta strandi283 – 2875Combined sources
Beta strandi293 – 30210Combined sources
Beta strandi305 – 3106Combined sources
Beta strandi317 – 3215Combined sources
Helixi322 – 3243Combined sources
Beta strandi325 – 3273Combined sources
Helixi332 – 3343Combined sources
Helixi341 – 35919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NS5X-ray1.90A154-371[»]
ProteinModelPortaliQ15326.
SMRiQ15326. Positions 99-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 23871BromoPROSITE-ProRule annotationAdd
BLAST
Domaini280 – 33152PWWPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni452 – 572121Interaction with human adenovirus E1AAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi394 – 4007Nuclear localization signalSequence Analysis

Domaini

The PWWP domain specifically recognizes and binds histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and adopts a five-bladed beta-barrel fold with an extended C-terminal alpha-helix, with a conserved H3.3K36me3-binding aromatic cage formed by Phe-291 and Trp-294 of the beta1-beta2 loop and Phe-310 of the beta3-beta4 loop. Specific recognition of H3.3 histone is mediated by the encapsulation of the H3.3-specific 'Ser 31' residue in a composite pocket formed by the tandem bromo-PWWP domains (By similarity).By similarity

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 PWWP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri100 – 14849PHD-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri563 – 59836MYND-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Zinc-finger

Phylogenomic databases

eggNOGiNOG265768.
GeneTreeiENSGT00530000063428.
HOGENOMiHOG000038026.
HOVERGENiHBG054949.
InParanoidiQ15326.
OMAiTSDGVCQ.
OrthoDBiEOG700875.
PhylomeDBiQ15326.
TreeFamiTF106407.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR001487. Bromodomain.
IPR000313. PWWP_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR002893. Znf_MYND.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTiSM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00293. PWWP. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50014. BROMODOMAIN_2. 1 hit.
PS50812. PWWP. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15326-1) [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
MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK
60 70 80 90 100
ETTRQLSLAV KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD
110 120 130 140 150
WYCFECHLPG EVLICDLCFR VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK
160 170 180 190 200
KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG KDNKHPMYRR LVHSAVDVPT
210 220 230 240 250
IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI ARMLYKDTCH
260 270 280 290 300
ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ
310 320 330 340 350
KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL
360 370 380 390 400
ELHQRFLREG RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR
410 420 430 440 450
NQSVEPKKEE PEPETEAVSS SQEIPTMPQP IEKVSVSTQT KKLSASSPRM
460 470 480 490 500
LHRSTQTTND GVCQSMCHDK YTKIFNDFKD RMKSDHKRET ERVVREALEK
510 520 530 540 550
LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV EEIKKLATQH
560 570 580 590 600
KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR

KR
Length:602
Mass (Da):70,963
Last modified:November 28, 2012 - v2
Checksum:i3AD525B90574BDE8
GO
Isoform 2 (identifier: Q15326-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.

Show »
Length:548
Mass (Da):64,426
Checksum:i5EDF3D170E2EDD11
GO
Isoform 3 (identifier: Q15326-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

Show »
Length:568
Mass (Da):66,590
Checksum:i597E186F867E225B
GO
Isoform 4 (identifier: Q15326-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

Show »
Length:514
Mass (Da):60,053
Checksum:iC20F5B606BAB0E2E
GO
Isoform 5 (identifier: Q15326-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-146: Missing.
     173-203: Missing.

Note: No experimental confirmation available.

Show »
Length:517
Mass (Da):60,869
Checksum:iE8EA00DD12FA4FF8
GO
Isoform 6 (identifier: Q15326-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     233-233: Missing.
     563-602: CYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR → VNTSLF

Note: No experimental confirmation available.

Show »
Length:567
Mass (Da):66,519
Checksum:i86FC85955F1022E5
GO

Sequence cautioni

The sequence AAH34784.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG35465.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA60052.1 differs from that shown. Reason: Frameshift at positions 11 and 39. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 14654Missing in isoform 2, isoform 4 and isoform 5. 2 PublicationsVSP_044482Add
BLAST
Alternative sequencei173 – 20331Missing in isoform 5. 1 PublicationVSP_046246Add
BLAST
Alternative sequencei233 – 2331Missing in isoform 6. 1 PublicationVSP_047209
Alternative sequencei563 – 60240CYNCE…CRRKR → VNTSLF in isoform 3, isoform 4 and isoform 6. 2 PublicationsVSP_044483Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86098 mRNA. Translation: CAA60052.1. Frameshift.
DQ335452 mRNA. Translation: ABC72408.1.
DQ335453 mRNA. Translation: ABC72409.1.
DQ335454 mRNA. Translation: ABC72410.1.
DQ335455 mRNA. Translation: ABC72411.1.
AK294469 mRNA. Translation: BAH11779.1.
AK312570 mRNA. Translation: BAG35465.1. Different initiation.
AL589988, AL603831 Genomic DNA. Translation: CAH69845.1.
AL603831, AL589988 Genomic DNA. Translation: CAI40899.1.
AL713922 Genomic DNA. No translation available.
AL731539 Genomic DNA. No translation available.
CH471072 Genomic DNA. Translation: EAW86539.1.
CH471072 Genomic DNA. Translation: EAW86540.1.
CH471072 Genomic DNA. Translation: EAW86541.1.
BC034784 mRNA. Translation: AAH34784.1. Different initiation.
CCDSiCCDS55696.1. [Q15326-3]
CCDS55697.1. [Q15326-5]
CCDS7052.2. [Q15326-1]
CCDS7053.2. [Q15326-6]
CCDS73060.1. [Q15326-2]
PIRiS56145.
RefSeqiNP_001189393.1. NM_001202464.1. [Q15326-2]
NP_001189394.1. NM_001202465.1. [Q15326-5]
NP_001189396.1. NM_001202467.1. [Q15326-4]
NP_001189397.1. NM_001202468.1. [Q15326-3]
NP_006615.2. NM_006624.5. [Q15326-1]
NP_997644.2. NM_212479.3. [Q15326-6]
XP_005252416.1. XM_005252359.2. [Q15326-1]
XP_005252418.1. XM_005252361.1. [Q15326-2]
XP_005252419.1. XM_005252362.1. [Q15326-2]
XP_006717439.1. XM_006717376.1. [Q15326-2]
UniGeneiHs.292265.
Hs.740145.

Genome annotation databases

EnsembliENST00000381591; ENSP00000371003; ENSG00000015171. [Q15326-1]
ENST00000381607; ENSP00000371020; ENSG00000015171. [Q15326-2]
ENST00000397959; ENSP00000381050; ENSG00000015171. [Q15326-5]
ENST00000397962; ENSP00000381053; ENSG00000015171. [Q15326-1]
ENST00000509513; ENSP00000424205; ENSG00000015171. [Q15326-6]
ENST00000558098; ENSP00000452959; ENSG00000015171. [Q15326-3]
ENST00000602682; ENSP00000473321; ENSG00000015171. [Q15326-5]
GeneIDi10771.
KEGGihsa:10771.
UCSCiuc001ifk.3. human.
uc001ifm.3. human. [Q15326-2]
uc001ifn.3. human. [Q15326-4]
uc010pzu.2. human. [Q15326-1]
uc010pzw.2. human.
uc010pzx.2. human. [Q15326-3]

Polymorphism databases

DMDMi425906058.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86098 mRNA. Translation: CAA60052.1 . Frameshift.
DQ335452 mRNA. Translation: ABC72408.1 .
DQ335453 mRNA. Translation: ABC72409.1 .
DQ335454 mRNA. Translation: ABC72410.1 .
DQ335455 mRNA. Translation: ABC72411.1 .
AK294469 mRNA. Translation: BAH11779.1 .
AK312570 mRNA. Translation: BAG35465.1 . Different initiation.
AL589988 , AL603831 Genomic DNA. Translation: CAH69845.1 .
AL603831 , AL589988 Genomic DNA. Translation: CAI40899.1 .
AL713922 Genomic DNA. No translation available.
AL731539 Genomic DNA. No translation available.
CH471072 Genomic DNA. Translation: EAW86539.1 .
CH471072 Genomic DNA. Translation: EAW86540.1 .
CH471072 Genomic DNA. Translation: EAW86541.1 .
BC034784 mRNA. Translation: AAH34784.1 . Different initiation.
CCDSi CCDS55696.1. [Q15326-3 ]
CCDS55697.1. [Q15326-5 ]
CCDS7052.2. [Q15326-1 ]
CCDS7053.2. [Q15326-6 ]
CCDS73060.1. [Q15326-2 ]
PIRi S56145.
RefSeqi NP_001189393.1. NM_001202464.1. [Q15326-2 ]
NP_001189394.1. NM_001202465.1. [Q15326-5 ]
NP_001189396.1. NM_001202467.1. [Q15326-4 ]
NP_001189397.1. NM_001202468.1. [Q15326-3 ]
NP_006615.2. NM_006624.5. [Q15326-1 ]
NP_997644.2. NM_212479.3. [Q15326-6 ]
XP_005252416.1. XM_005252359.2. [Q15326-1 ]
XP_005252418.1. XM_005252361.1. [Q15326-2 ]
XP_005252419.1. XM_005252362.1. [Q15326-2 ]
XP_006717439.1. XM_006717376.1. [Q15326-2 ]
UniGenei Hs.292265.
Hs.740145.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4NS5 X-ray 1.90 A 154-371 [» ]
ProteinModelPortali Q15326.
SMRi Q15326. Positions 99-366.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115989. 36 interactions.
IntActi Q15326. 19 interactions.
MINTi MINT-156360.
STRINGi 9606.ENSP00000309992.

PTM databases

PhosphoSitei Q15326.

Polymorphism databases

DMDMi 425906058.

Proteomic databases

MaxQBi Q15326.
PaxDbi Q15326.
PRIDEi Q15326.

Protocols and materials databases

DNASUi 10771.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381591 ; ENSP00000371003 ; ENSG00000015171 . [Q15326-1 ]
ENST00000381607 ; ENSP00000371020 ; ENSG00000015171 . [Q15326-2 ]
ENST00000397959 ; ENSP00000381050 ; ENSG00000015171 . [Q15326-5 ]
ENST00000397962 ; ENSP00000381053 ; ENSG00000015171 . [Q15326-1 ]
ENST00000509513 ; ENSP00000424205 ; ENSG00000015171 . [Q15326-6 ]
ENST00000558098 ; ENSP00000452959 ; ENSG00000015171 . [Q15326-3 ]
ENST00000602682 ; ENSP00000473321 ; ENSG00000015171 . [Q15326-5 ]
GeneIDi 10771.
KEGGi hsa:10771.
UCSCi uc001ifk.3. human.
uc001ifm.3. human. [Q15326-2 ]
uc001ifn.3. human. [Q15326-4 ]
uc010pzu.2. human. [Q15326-1 ]
uc010pzw.2. human.
uc010pzx.2. human. [Q15326-3 ]

Organism-specific databases

CTDi 10771.
GeneCardsi GC10P000170.
H-InvDB HIX0025946.
HGNCi HGNC:16966. ZMYND11.
HPAi HPA015816.
HPA030553.
MIMi 608668. gene.
neXtProti NX_Q15326.
PharmGKBi PA128394578.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG265768.
GeneTreei ENSGT00530000063428.
HOGENOMi HOG000038026.
HOVERGENi HBG054949.
InParanoidi Q15326.
OMAi TSDGVCQ.
OrthoDBi EOG700875.
PhylomeDBi Q15326.
TreeFami TF106407.

Miscellaneous databases

ChiTaRSi ZMYND11. human.
GeneWikii ZMYND11.
GenomeRNAii 10771.
NextBioi 40897.
PROi Q15326.
SOURCEi Search...

Gene expression databases

Bgeei Q15326.
CleanExi HS_ZMYND11.
ExpressionAtlasi Q15326. baseline and differential.
Genevestigatori Q15326.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR001487. Bromodomain.
IPR000313. PWWP_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR002893. Znf_MYND.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF00439. Bromodomain. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view ]
SMARTi SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00293. PWWP. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEi PS50014. BROMODOMAIN_2. 1 hit.
PS50812. PWWP. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "BS69, a novel adenovirus E1A-associated protein that inhibits E1A transactivation."
    Hateboer G., Gennissen A., Ramos Y.F.M., Kerkhoven R.M., Sonntag-Buck V., Stunnenberg H.G., Bernards R.
    EMBO J. 14:3159-3169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon carcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, UBIQUITINATION, INTERACTION WITH E2F6 AND EZH2, MUTAGENESIS OF CYS-563.
  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 1 AND 5).
    Tissue: Amygdala and Brain.
  4. "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].
  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 6).
    Tissue: Brain.
  7. "The adenovirus E1A binding protein BS69 is a corepressor of transcription through recruitment of N-CoR."
    Masselink H., Bernards R.
    Oncogene 19:1538-1546(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCOR1.
  8. "The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif."
    Ansieau S., Leutz A.
    J. Biol. Chem. 277:4906-4910(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2 PROTEIN.
  9. "Negative regulation of Epstein-Barr virus latent membrane protein 1-mediated functions by the bone morphogenetic protein receptor IA-binding protein, BRAM1."
    Chung P.J., Chang Y.S., Liang C.L., Meng C.L.
    J. Biol. Chem. 277:39850-39857(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
  10. Cited for: INTERACTION WITH C11ORF30.
  11. "BS69, a specific adaptor in the latent membrane protein 1-mediated c-Jun N-terminal kinase pathway."
    Wan J., Zhang W., Wu L., Bai T., Zhang M., Lo K.W., Chui Y.L., Cui Y., Tao Q., Yamamoto M., Akira S., Wu Z.
    Mol. Cell. Biol. 26:448-456(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "BS69 negatively regulates the canonical NF-kappaB activation induced by Epstein-Barr virus-derived LMP1."
    Ikeda O., Sekine Y., Mizushima A., Oritani K., Yasui T., Fujimuro M., Muromoto R., Nanbo A., Matsuda T.
    FEBS Lett. 583:1567-1574(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
  15. "BS69 undergoes SUMO modification and plays an inhibitory role in muscle and neuronal differentiation."
    Yu B., Shao Y., Zhang C., Chen Y., Zhong Q., Zhang J., Yang H., Zhang W., Wan J.
    Exp. Cell Res. 315:3543-3553(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUMOYLATION, INTERACTION WITH PIAS1 AND UBE2I.
  16. "BS69 cooperates with TRAF3 in the regulation of Epstein-Barr virus-derived LMP1/CTAR1-induced NF-kappaB activation."
    Ikeda O., Miyasaka Y., Yoshida R., Mizushima A., Oritani K., Sekine Y., Kuroda M., Yasui T., Fujimuro M., Muromoto R., Nanbo A., Matsuda T.
    FEBS Lett. 584:865-872(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN EPSTEIN-BARR VIRUS PROTEIN LMP1.
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Recurrent translocation (10;17)(p15;q21) in acute poorly differentiated myeloid leukemia likely results in ZMYND11-MBTD1 fusion."
    De Braekeleer E., Auffret R., Douet-Guilbert N., Basinko A., Le Bris M.J., Morel F., De Braekeleer M.
    Leuk. Lymphoma 55:1189-1190(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH MBTD1.
  19. Cited for: INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN, INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2 PROTEIN, INTERACTION WITH MGA, MUTAGENESIS OF TRP-562; 567-GLU-GLU-568 AND 599-ARG--ARG-602.
  20. "ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression."
    Wen H., Li Y., Xi Y., Jiang S., Stratton S., Peng D., Tanaka K., Ren Y., Xia Z., Wu J., Li B., Barton M.C., Li W., Li H., Shi X.
    Nature 508:263-268(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiZMY11_HUMAN
AccessioniPrimary (citable) accession number: Q15326
Secondary accession number(s): B2R6G8
, B7Z293, F6UH50, Q2LD45, Q2LD46, Q2LD47, Q2LD48, Q5VUI1, Q8N4B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 28, 2012
Last modified: November 26, 2014
This is version 136 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3