CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014808
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase listerin 
Protein Synonyms/Alias
 RING finger protein 160; Zinc finger protein 294; Zfp-294 
Gene Name
 Ltn1 
Gene Synonyms/Alias
 Kiaa0714; Lister; Rnf160; Zfp294; Znf294 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
707EVLDDLTKEDLKWSSubiquitination[1]
1363KDQLLSHKLPARLVAubiquitination[1]
1537TAIEVSSKDPKTFFTubiquitination[1]
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] 
Functional Description
 E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. 
Sequence Annotation
 ZN_FING 1716 1763 RING-type.
 MOD_RES 785 785 Phosphotyrosine.  
Keyword
 Complete proteome; Ligase; Metal-binding; Neurodegeneration; Phosphoprotein; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1767 AA 
Protein Sequence
MGGKNKQRTK GNLRPSNSGR AAELLAKEQG TVPGFIGFGT SHSDLGYVPA VQGAEDIDSL 60
VDSDFRMVLR KLSKKDVTTK LKAMQEFGIM CTERDTEAVK GVLPYWPRIF CKISLDHDRR 120
VREATQQAFE KLILKVKKHL APYLKSVMGY WLMAQCDTYP PAALAAKDAF EAAFPPSKQP 180
EAIAFCKEEI TTVLQDHLLK ETPDTLSDPQ TVPEEEREAK FHRVVTCSLL ALKRLLCFLP 240
NNELDSLEEK FKSLLSQNKF WKYGKHSVPQ VRSAYFELVS ALCQHVPQVM KEEAAKVSPS 300
VLLSIDDSDP VVCPALWEAV LYTLTTIEDC WFHVNAKKSV FPKLMAMIRE GGRGLAAVMY 360
PYLLPFISKL PQSITEPKLD FFKNFLTSLV TGLSTERTKS SSSECSAVIS AFFECLRFIM 420
QQNLGEEEMV QMLINEQLIP FIDTVLKDSG LHHGPMFDHL ADTLSSWEAK ADAERDPGAV 480
YNLENVLLSF WGRLSEICTE KIRQPEADVK SVLCVSSLVG VLQRPRSSLK LHRKKTAQVR 540
FAINIPEAHK GDEKSMSSEG ENSEGSDGGA QSPLSNTSSD LVSPLRKKPL EDLVCKLAEV 600
SISFVNERKS EQHLQFLSTL LDSFSSVQVF NILLSDKQKN VVKAKPLEIT KLAEKNPAVK 660
FLYHKLIGWL NDSQKEDGGF LVDILYSALR CCDSGVERKE VLDDLTKEDL KWSSLLQVIE 720
KACSSSDKHA LVTPWLKGSI LGEKLVALAD CLCDKDLEAT TSESHSSEQW SLLRLALSQH 780
VKNDYLIGEV YVGRIIVKLH ETLSKTKDLS EAANSDSSVS FVCDVVHSFF SSAGGGLLMP 840
PSEDLLLTLF QLCAQSKERT HLPDFLICKL KNTLLSGVNL LVHQTASTYE QSTFLRLSVL 900
WLKDQVQSSA LDNTSLQVLL SAAGDLLGTL VESEDTSLLG VYIGSVMPSD SEWEKMRQAL 960
PVQWLHRPLL EGRLSLNYEC FKTDFKEQDT KTLPNHLCTS SLLSKMILVA QKKKLVLEDN 1020
VLEKIIAELL YSLQWCEELD NAPSFLSGFC GILQKMNITY SNLSVLSETS SLLQLLFDRS 1080
RKNGTLWSLI IAKLILSRSI SSDEVKPYYK RKESFFPLTE GSLHTIQSLC PFLSKEEKKE 1140
FSAQCIPAFL GWTKEDLCSI NGAFGHLAIF NSCLQTRSID DKQLLHGILK IITSWRKQHE 1200
DIFLFSCNLS EASPEVLGLN IEIMRFLSLF LKHCAYPLPL ADSEWDFIMC SMLAWLETTS 1260
ENQALYSVPL VQLFACVSFD LACDLCAFFD SITPDIVDNL PVNLISEWKE FFSKGIHSLL 1320
LPLLVNAIGE NKDLSETSFQ NAMLKPMCET LTYISKDQLL SHKLPARLVA SQKTNLPEHL 1380
QTLLNTLTPL LLFRARPVQI AAYHMLCKLM PELPQHDQDN LRSYGDEEEE PALSPPAALM 1440
SLLSSQEELL ENVLGCVPVG QIVTVKPLSE DFCYVLGYLL TWKLILTFFK AASSQLRALY 1500
SMYLRKTKSL NKLLYHLFRL MPENPTYGET AIEVSSKDPK TFFTEEVQLS IRETATLPYH 1560
IPHLACSVYH MTLKDLPAMV RLWWNSSEKR VFNIVDRFTS KYVSNVLSFQ EISSVQTSTQ 1620
LFNGMTVKAR ATTREVMATY TIEDIVIELI IQLPSNYPLG SITVESGKRI GVAVQQWRNW 1680
MLQLSTYLTH QNGSIMEGLA LWKNNVDKRF EGVEDCMICF SVIHGFNYSL PKKACRTCKK 1740
KFHSACLYKW FTSSNKSTCP LCRETFF 1767 
Gene Ontology
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
  
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS