CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029108
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Zinc finger MYM-type protein 3 
Protein Synonyms/Alias
  
Gene Name
 ZMYM3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
441CSDSCFSKFRANKGLubiquitination[1]
508VWCKTLCKNFEMLSHubiquitination[2]
563SDPCYYNKVDRTVYQubiquitination[1]
626RDCCEDFKRLRGVVSubiquitination[1]
647QEKLLHEKLRFSGVEubiquitination[1]
838KNKAAMCKPLMQNRGubiquitination[1]
922VETIEELKVKIPSNPubiquitination[1, 2, 3, 4, 5, 6]
924TIEELKVKIPSNPLEubiquitination[2]
1074SYGVNAWKCWVQSKYubiquitination[1, 7]
1080WKCWVQSKYANGETSubiquitination[1, 7]
1088YANGETSKGDELRFGacetylation[2]
1088YANGETSKGDELRFGubiquitination[1, 2, 4, 7, 8]
1097DELRFGPKPMRIKEDubiquitination[1]
1102GPKPMRIKEDILACSubiquitination[1]
1253TTPRGTTKVVSIRYYubiquitination[1, 2, 4]
1300NPLRCPVKFYEFYLSubiquitination[1, 7, 8]
1308FYEFYLSKCPESLRTubiquitination[1, 2, 7, 8]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1372 AA 
Protein Sequence
MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PTRGWAPPGP SPSSGALDLL 60
DTPAGLEKDP GVLDGATELL GLGGLLYKAP SPPEVDHGPE GTLAWDAGDQ TLEPGPGGQT 120
PEVVPPDPGA GANSCSPEGL LEPLAPDSPI TLQSPHIEEE ETTSIATARR GSPGQEEELP 180
QGQPQSPNAP PSPSVGETLG DGINSSQTKP GGSSPPAHPS LPGDGLTAKA SEKPPERVQK 240
RSERVRRAEP PKPEVVDSTE SIPVSDEDSD AMVDDPNDED FVPFRPRRSP RMSLRSSVSQ 300
RAGRSAVGTK MTCAHCRTPL QKGQTAYQRK GLPQLFCSSS CLTTFSKKPS GKKTCTFCKK 360
EIWNTKDSVV AQTGSGGSFH EFCTSVCLSL YEAQQQRPIP QSGDPADATR CSICQKTGEV 420
LHEVSNGSVV HRLCSDSCFS KFRANKGLKT NCCDQCGAYI YTKTGSPGPE LLFHEGQQKR 480
FCNTTCLGAY KKKNTRVYPC VWCKTLCKNF EMLSHVDRNG KTSLFCSLCC TTSYKVKQAG 540
LTGPPRPCSF CRRSLSDPCY YNKVDRTVYQ FCSPSCWTKF QRTSPEGGIH LSCHYCHSLF 600
SGKPEVLDWQ DQVFQFCCRD CCEDFKRLRG VVSQCEHCRQ EKLLHEKLRF SGVEKSFCSE 660
GCVLLYKQDF TKKLGLCCIT CTYCSQTCQR GVTEQLDGST WDFCSEDCKS KYLLWYCKAA 720
RCHACKRQGK LLETIHWRGQ IRHFCNQQCL LRFYSQQNQP NLDTQSGPES LLNSQSPESK 780
PQTPSQTKVE NSNTVRTPEE NGNLGKIPVK TRSAPTAPTP PPPPPPATPR KNKAAMCKPL 840
MQNRGVSCKV EMKSKGSQTE EWKPQVIVLP IPVPIFVPVP MHLYCQKVPV PFSMPIPVPV 900
PMFLPTTLES TDKIVETIEE LKVKIPSNPL EADILAMAEM IAEAEELDKA SSDLCDLVSN 960
QSAEGLLEDC DLFGPARDDV LAMAVKMANV LDEPGQDLEA DFPKNPLDIN PSVDFLFDCG 1020
LVGPEDVSTE QDLPRTMRKG QKRLVLSESC SRDSMSSQPS CTGLNYSYGV NAWKCWVQSK 1080
YANGETSKGD ELRFGPKPMR IKEDILACSA AELNYGLAQF VREITRPNGE RYEPDSIYYL 1140
CLGIQQYLLE NNRMVNIFTD LYYLTFVQEL NKSLSTWQPT LLPNNTVFSR VEEEHLWECK 1200
QLGVYSPFVL LNTLMFFNTK FFGLQTAEEH MQLSFTNVVR QSRKCTTPRG TTKVVSIRYY 1260
APVRQRKGRD TGPGKRKRED EAPILEQREN RMNPLRCPVK FYEFYLSKCP ESLRTRNDVF 1320
YLQPERSCIA ESPLWYSVIP MDRSMLESML NRILAVREIY EELGRPGEED LD 1372 
Gene Ontology
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR021893; DUF3504.
 IPR011017; TRASH_dom.
 IPR010507; Znf_MYM. 
Pfam
 PF12012; DUF3504
 PF06467; zf-FCS 
SMART
 SM00746; TRASH 
PROSITE
  
PRINTS