CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012534
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger MYND domain-containing protein 11 
Protein Synonyms/Alias
 Adenovirus 5 E1A-binding protein; Protein BS69 
Gene Name
 ZMYND11 
Gene Synonyms/Alias
 BS69 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
77TVGCKGSKAGIEQEGubiquitination[1]
366EGRFWKSKNEDRGEEsumoylation[2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] 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. 2009 Dec 10;315(20):3543-53. [PMID: 19766626] 
Functional Description
 Corepressor of transcription (Probable). May be involved in chromatin remodeling through association with several remodeling factors. 
Sequence Annotation
 DOMAIN 168 238 Bromo.
 DOMAIN 280 331 PWWP.
 ZN_FING 100 148 PHD-type.
 ZN_FING 563 598 MYND-type.
 REGION 452 572 Interaction with human adenovirus E1A.
 MOTIF 394 400 Nuclear localization signal (Potential).
 MOD_RES 421 421 Phosphoserine.  
Keyword
 Alternative splicing; Bromodomain; Cell cycle; Chromatin regulator; Chromosome; Complete proteome; DNA-binding; Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 602 AA 
Protein Sequence
MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV 60
KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETENHD WYCFECHLPG EVLICDLCFR 120
VYHSKCLSDE FRLRDSSSPW QCPVCRSIKK KNTNKQEMGT YLRFIVSRMK ERAIDLNKKG 180
KDNKHPMYRR LVHSAVDVPT IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI 240
ARMLYKDTCH ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ 300
KEDNQVDVRF FGHHHQRAWI PSENIQDITV NIHRLHVKRS MGWKKACDEL ELHQRFLREG 360
RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR NQSVEPKKEE PEPETEAVSS 420
SQEIPTMPQP IEKVSVSTQT KKLSASSPRM LHRSTQTTND GVCQSMCHDK YTKIFNDFKD 480
RMKSDHKRET ERVVREALEK LRSEMEEEKR QAVNKAVANM QGEMDRKCKQ VKEKCKEEFV 540
EEIKKLATQH KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR 600
KR 602 
Gene Ontology
 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
 GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR001487; Bromodomain.
 IPR000313; PWWP.
 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. 
Pfam
 PF00439; Bromodomain
 PF00855; PWWP 
SMART
 SM00297; BROMO
 SM00249; PHD
 SM00293; PWWP
 SM00184; RING 
PROSITE
 PS50014; BROMODOMAIN_2
 PS50812; PWWP
 PS01360; ZF_MYND_1
 PS50865; ZF_MYND_2
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS