CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-028430
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein Zmynd8 
Protein Synonyms/Alias
  
Gene Name
 Zmynd8 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
351YVENIRRKFGVFNYSubiquitination[1]
408SPKILLSKPLLSGGAacetylation[2, 3, 4, 5]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 492 AA 
Protein Sequence
SLAEEEIKTE QEVVEGMDIS TRSKEPKEDP VSTEKTAPKR RFPSPPHSSN GHSPQDSSTS 60
PIKKKKKPGL LNSSNKEQDG RNDFYCWVCH REGQVLCCEL CPRVYHAKCL RLTSEPEGDW 120
FCPECEKITV AECIETQSKA MTMLTIEQLS YLLKFAIQKM KQPGTDAFQK PVPLEQHPDY 180
AEYIFHPMDL CTLEKNAKKK MYGCTEAFLA DAKWILHNCI IYNGGNHKLT QIAKVVIKIC 240
EHEMNEIEVC PECYLAACQK RDNWFCEPCS NPHPLVWAKL KGFPFWPAKA LRDKDGQVDA 300
RFFGQHDRAW VPVNNCYLMS KEIPFSVKKT KSIFNSAMQE MEVYVENIRR KFGVFNYSPF 360
RTPYTPNNQY QMLLDPSNPS AGTAKTDKQE KVKLNFDMTA SPKILLSKPL LSGGAGRRIS 420
LSDMPRSPTS TNSSVHTGSD VEQDPEKKAP SSHFSASEES MDFLDKSTGQ PQLGELGRRP 480
LGAFWRPWMP PS 492 
Gene Ontology
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001487; Bromodomain.
 IPR021931; DUF3544.
 IPR000313; PWWP.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF12064; DUF3544
 PF00628; PHD
 PF00855; PWWP 
SMART
 SM00297; BROMO
 SM00249; PHD 
PROSITE
 PS50014; BROMODOMAIN_2
 PS50812; PWWP
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS
 PR00503; BROMODOMAIN.