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Protein

Zinc finger MYND domain-containing protein 11

Gene

ZMYND11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi258ZincBy similarity1
Metal bindingi261ZincBy similarity1
Metal bindingi277ZincBy similarity1
Metal bindingi281Zinc; via tele nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri100 – 148PHD-typePROSITE-ProRule annotationAdd BLAST49
Zinc fingeri563 – 598MYND-typePROSITE-ProRule annotationAdd BLAST36

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell proliferation Source: ProtInc
  • chromatin modification Source: UniProtKB-KW
  • negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of JNK cascade Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • 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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000015171-MONOMER.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:16966. ZMYND11.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
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.

Mental retardation, autosomal dominant 30 (MRD30)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD30 patients manifest mild intellectual disability and subtle facial dysmorphisms, including hypertelorism, ptosis, and a wide mouth.
See also OMIM:616083

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi562W → Y: Reduced interaction with PXLXP ligand MGA without affecting interaction with viral human adenovirus early E1A protein. 1 Publication1
Mutagenesisi563C → S: Abrogates binding to EZH2. 1 Publication1
Mutagenesisi567 – 568EE → KK: Reduced interaction with PXLXP ligand proteins. 1 Publication2
Mutagenesisi599 – 602RRKR → GGGG: Abolished interaction with PXLXP ligand proteins. 1 Publication4

Keywords - Diseasei

Mental retardation, Tumor suppressor

Organism-specific databases

DisGeNETi10771.
MalaCardsiZMYND11.
MIMi616083. phenotype.
OpenTargetsiENSG00000015171.
PharmGKBiPA128394578.

Polymorphism and mutation databases

BioMutaiZMYND11.
DMDMi425906058.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002112181 – 602Zinc finger MYND domain-containing protein 11Add BLAST602

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki407Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei421PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15326.
PaxDbiQ15326.
PeptideAtlasiQ15326.
PRIDEiQ15326.

PTM databases

iPTMnetiQ15326.
PhosphoSitePlusiQ15326.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

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

Gene expression databases

BgeeiENSG00000015171.
CleanExiHS_ZMYND11.
ExpressionAtlasiQ15326. baseline and differential.
GenevisibleiQ15326. HS.

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 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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi115989. 57 interactors.
IntActiQ15326. 24 interactors.
MINTiMINT-156360.
STRINGi9606.ENSP00000371003.

Structurei

Secondary structure

1602
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi157 – 169Combined sources13
Helixi198 – 206Combined sources9
Helixi213 – 231Combined sources19
Helixi236 – 257Combined sources22
Helixi259 – 267Combined sources9
Helixi272 – 274Combined sources3
Beta strandi283 – 287Combined sources5
Beta strandi293 – 302Combined sources10
Beta strandi305 – 310Combined sources6
Beta strandi317 – 321Combined sources5
Helixi322 – 324Combined sources3
Beta strandi325 – 327Combined sources3
Helixi332 – 334Combined sources3
Helixi341 – 359Combined sources19
Helixi482 – 558Combined sources77
Beta strandi562 – 566Combined sources5
Beta strandi572 – 575Combined sources4
Beta strandi578 – 582Combined sources5
Helixi583 – 592Combined sources10
Helixi594 – 596Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NS5X-ray1.90A154-371[»]
5HDAX-ray2.39A/C480-602[»]
ProteinModelPortaliQ15326.
SMRiQ15326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini168 – 238BromoPROSITE-ProRule annotationAdd BLAST71
Domaini280 – 331PWWPPROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni452 – 572Interaction with human adenovirus E1AAdd BLAST121

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi394 – 400Nuclear localization signalSequence analysis7

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)DescriptionActionsGraphical viewLength
Zinc fingeri100 – 148PHD-typePROSITE-ProRule annotationAdd BLAST49
Zinc fingeri563 – 598MYND-typePROSITE-ProRule annotationAdd BLAST36

Keywords - Domaini

Bromodomain, Zinc-finger

Phylogenomic databases

eggNOGiKOG3612. Eukaryota.
ENOG410XTCC. LUCA.
GeneTreeiENSGT00530000063428.
HOGENOMiHOG000038026.
HOVERGENiHBG054949.
InParanoidiQ15326.
OMAiTSDGVCQ.
OrthoDBiEOG091G0B2W.
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.
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.
[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. AlignAdd to basket

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

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04448293 – 146Missing in isoform 2, isoform 4 and isoform 5. 2 PublicationsAdd BLAST54
Alternative sequenceiVSP_046246173 – 203Missing in isoform 5. 1 PublicationAdd BLAST31
Alternative sequenceiVSP_047209233Missing in isoform 6. 1 Publication1
Alternative sequenceiVSP_044483563 – 602CYNCE…CRRKR → VNTSLF in isoform 3, isoform 4 and isoform 6. 2 PublicationsAdd BLAST40

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_005252359.4. [Q15326-1]
XP_005252418.1. XM_005252361.3. [Q15326-2]
XP_005252419.1. XM_005252362.2. [Q15326-2]
XP_006717439.1. XM_006717376.2. [Q15326-2]
XP_016871076.1. XM_017015587.1. [Q15326-1]
XP_016871077.1. XM_017015588.1. [Q15326-1]
XP_016871078.1. XM_017015589.1. [Q15326-1]
XP_016871079.1. XM_017015590.1. [Q15326-1]
XP_016871081.1. XM_017015592.1. [Q15326-2]
XP_016871082.1. XM_017015593.1. [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.4. human. [Q15326-1]

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.
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_005252359.4. [Q15326-1]
XP_005252418.1. XM_005252361.3. [Q15326-2]
XP_005252419.1. XM_005252362.2. [Q15326-2]
XP_006717439.1. XM_006717376.2. [Q15326-2]
XP_016871076.1. XM_017015587.1. [Q15326-1]
XP_016871077.1. XM_017015588.1. [Q15326-1]
XP_016871078.1. XM_017015589.1. [Q15326-1]
XP_016871079.1. XM_017015590.1. [Q15326-1]
XP_016871081.1. XM_017015592.1. [Q15326-2]
XP_016871082.1. XM_017015593.1. [Q15326-2]
UniGeneiHs.292265.
Hs.740145.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NS5X-ray1.90A154-371[»]
5HDAX-ray2.39A/C480-602[»]
ProteinModelPortaliQ15326.
SMRiQ15326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115989. 57 interactors.
IntActiQ15326. 24 interactors.
MINTiMINT-156360.
STRINGi9606.ENSP00000371003.

PTM databases

iPTMnetiQ15326.
PhosphoSitePlusiQ15326.

Polymorphism and mutation databases

BioMutaiZMYND11.
DMDMi425906058.

Proteomic databases

EPDiQ15326.
PaxDbiQ15326.
PeptideAtlasiQ15326.
PRIDEiQ15326.

Protocols and materials databases

DNASUi10771.
Structural Biology KnowledgebaseSearch...

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.4. human. [Q15326-1]

Organism-specific databases

CTDi10771.
DisGeNETi10771.
GeneCardsiZMYND11.
H-InvDBHIX0025946.
HGNCiHGNC:16966. ZMYND11.
HPAiHPA015816.
HPA030553.
MalaCardsiZMYND11.
MIMi608668. gene.
616083. phenotype.
neXtProtiNX_Q15326.
OpenTargetsiENSG00000015171.
PharmGKBiPA128394578.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3612. Eukaryota.
ENOG410XTCC. LUCA.
GeneTreeiENSGT00530000063428.
HOGENOMiHOG000038026.
HOVERGENiHBG054949.
InParanoidiQ15326.
OMAiTSDGVCQ.
OrthoDBiEOG091G0B2W.
PhylomeDBiQ15326.
TreeFamiTF106407.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000015171-MONOMER.

Miscellaneous databases

ChiTaRSiZMYND11. human.
GeneWikiiZMYND11.
GenomeRNAii10771.
PROiQ15326.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000015171.
CleanExiHS_ZMYND11.
ExpressionAtlasiQ15326. baseline and differential.
GenevisibleiQ15326. HS.

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.
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.
[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]
ProtoNetiSearch...

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 2, 2016
This is version 156 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

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.