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Protein

Zinc finger MYND domain-containing protein 11

Gene

Zmynd11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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). Colocalizes with highly expressed genes and functions as a transcription corepressor by modulating RNA polymerase II at the elongation stage (PubMed:24590075). Binds non-specifically to dsDNA (By similarity). Acts as a tumor-suppressor by repressing a transcriptional program essential for tumor cell growth (PubMed:24590075).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi258ZincCombined sources1 Publication1
Metal bindingi261ZincCombined sources1 Publication1
Metal bindingi277ZincCombined sources1 Publication1
Metal bindingi281Zinc; via tele nitrogenCombined sources1 Publication1

Regions

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

GO - Molecular functioni

  • chromatin binding Source: GO_Central
  • double-stranded DNA binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: GO_Central
  • transcription corepressor activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger MYND domain-containing protein 11
Gene namesi
Name:Zmynd11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1913755 Zmynd11

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi168R → A: Impaired H3.3K36me3 binding. 1 Publication1
Mutagenesisi234 – 236DSE → ASA: No effect on protein folding and histone binding. 1 Publication3
Mutagenesisi251E → A: Impaired H3.3K36me3 binding. 1 Publication1
Mutagenesisi266N → A: Impaired H3.3K36me3 binding. 1 Publication1
Mutagenesisi291F → A: Abolished H3.3K36me3 binding. 1 Publication1
Mutagenesisi294W → A: Abolished H3.3K36me3 binding. 1 Publication1
Mutagenesisi307D → A: Impaired H3.3K36me3 binding. 1 Publication1
Mutagenesisi310F → A: Abolished H3.3K36me3 binding. 1 Publication1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002112191 – 602Zinc finger MYND domain-containing protein 11Add BLAST602

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki407Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki408Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei421PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated, leading to proteasomal degradation.By similarity
Sumoylated following its interaction with PIAS1 and UBE2I.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8R5C8
MaxQBiQ8R5C8
PaxDbiQ8R5C8
PeptideAtlasiQ8R5C8
PRIDEiQ8R5C8

PTM databases

iPTMnetiQ8R5C8
PhosphoSitePlusiQ8R5C8

Expressioni

Gene expression databases

BgeeiENSMUSG00000021156
CleanExiMM_ZMYND11
ExpressionAtlasiQ8R5C8 baseline and differential
GenevisibleiQ8R5C8 MM

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 (By similarity).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi211523, 1 interactor
DIPiDIP-49596N
IntActiQ8R5C8, 4 interactors
MINTiQ8R5C8
STRINGi10090.ENSMUSP00000106264

Structurei

Secondary structure

1602
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi155 – 171Combined sources17
Helixi173 – 175Combined sources3
Helixi188 – 191Combined sources4
Helixi198 – 206Combined sources9
Helixi213 – 231Combined sources19
Helixi236 – 257Combined sources22
Helixi259 – 267Combined sources9
Helixi272 – 274Combined sources3
Beta strandi283 – 287Combined sources5
Turni289 – 291Combined sources3
Beta strandi293 – 302Combined sources10
Beta strandi305 – 312Combined sources8
Helixi313 – 315Combined sources3
Beta strandi317 – 321Combined sources5
Helixi322 – 324Combined sources3
Beta strandi325 – 327Combined sources3
Turni332 – 334Combined sources3
Helixi341 – 359Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4N4GX-ray1.95A154-371[»]
4N4HX-ray2.30A154-371[»]
4N4IX-ray2.00A154-371[»]
ProteinModelPortaliQ8R5C8
SMRiQ8R5C8
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
Regioni291 – 310Aromatic cage required for H3.3K36me3-specific bindingAdd BLAST20

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 (PubMed:24590075).1 Publication

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
GeneTreeiENSGT00910000144099
HOGENOMiHOG000038026
HOVERGENiHBG054949
InParanoidiQ8R5C8

Family and domain databases

CDDicd05841 BS69_related, 1 hit
Gene3Di1.20.920.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR000313 PWWP_dom
IPR019786 Zinc_finger_PHD-type_CS
IPR035505 ZMYND8/11_PWWP
IPR011011 Znf_FYVE_PHD
IPR002893 Znf_MYND
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF00439 Bromodomain, 1 hit
PF00855 PWWP, 1 hit
SMARTiView protein in SMART
SM00297 BROMO, 1 hit
SM00249 PHD, 1 hit
SM00293 PWWP, 1 hit
SUPFAMiSSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

Q8R5C8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK
60 70 80 90 100
ETTRQLSLAV KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETETHD
110 120 130 140 150
WYCFECHLPG EVLICDLCFR VYHSKCLSDE FRLRDSSSHW QCPVCRSIKK
160 170 180 190 200
KHSNKQEMGT YLRFIVSRMK ERAIDLNKKG KDSKHPMYRR 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 NVHRLHVKRS MGWKKACDEL
360 370 380 390 400
ELHQRFLREG RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR
410 420 430 440 450
NQSVEPKKEE PEPETEAVSS SQEIPTMPQP IERVSVSTQT KKLSASSPRM
460 470 480 490 500
LHRSTQTTSD GVCQSMCHDK YTKIFNDFKD RMKSDHKRET ERVVREALEK
510 520 530 540 550
LRSEMEEEKR QAVNKAVASL QGDMDRKGKQ LKEKCKEEFV EEIKKLAAQH
560 570 580 590 600
KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR

KR
Length:602
Mass (Da):70,838
Last modified:November 28, 2012 - v2
Checksum:i963A9EF2ABBCD3C2
GO

Sequence cautioni

The sequence AAH22945 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti371G → S in BAC26199 (PubMed:16141072).Curated1
Sequence conflicti519S → N in AAH22945 (PubMed:15489334).Curated1
Sequence conflicti523D → E in AAH22945 (PubMed:15489334).Curated1
Sequence conflicti528G → C in AAH22945 (PubMed:15489334).Curated1
Sequence conflicti531L → V in AAH22945 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC146596 Genomic DNA No translation available.
AC153144 Genomic DNA No translation available.
CH466588 Genomic DNA Translation: EDL32291.1
CH466588 Genomic DNA Translation: EDL32294.1
BC022945 mRNA Translation: AAH22945.1 Different initiation.
AK028931 mRNA Translation: BAC26199.1
CCDSiCCDS56870.1
RefSeqiNP_001186070.1, NM_001199141.2
NP_001334403.1, NM_001347474.1
NP_001334405.1, NM_001347476.1
XP_006516569.1, XM_006516506.3
UniGeneiMm.397307
Mm.488717

Genome annotation databases

EnsembliENSMUST00000110634; ENSMUSP00000106264; ENSMUSG00000021156
ENSMUST00000110636; ENSMUSP00000106266; ENSMUSG00000021156
GeneIDi66505
KEGGimmu:66505
UCSCiuc007pkx.1 mouse

Similar proteinsi

Entry informationi

Entry nameiZMY11_MOUSE
AccessioniPrimary (citable) accession number: Q8R5C8
Secondary accession number(s): G5E8Q2, Q8C155
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: November 28, 2012
Last modified: April 25, 2018
This is version 128 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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