CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037708
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Terminal uridylyltransferase 4 
Protein Synonyms/Alias
  
Gene Name
 ZCCHC11 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
328IVEEKFVKWECNSSSubiquitination[1]
439IEDPFSVKRNVARSLubiquitination[1, 2, 3]
476PQTKGGNKSTVDFKKubiquitination[1]
697DFRKIDLKPLPPMTNubiquitination[1]
740QILIGLEKFIQKEYDubiquitination[1]
759LCLFGSSKNGFGFRDubiquitination[1]
795EIIENLAKILKRHPGubiquitination[4]
813ILPITTAKVPIVKFEubiquitination[1]
888WNAFFFDKTEELKKRubiquitination[1]
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] 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]
 [3] 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]
 [4] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 906 AA 
Protein Sequence
MKNDESNKEN SSEMDYLENA TVIDESALTP EQRLGLKQAE ERLERDHIFR LEKRSPEYTN 60
CRYLCKLCLI HIENIQGAHK HIKEKRHKKN ILEKQEESEL RSLPPPSPAH LAALSVAVIE 120
LAKEHGITDD DLRVRQEIVE EMSKVITTFL PECSLRLYGS SLTRFALKSS DVNIDIKFPP 180
KMNHPDLLIK VLGILKKNVL YVDVESDFHA KVPVVVCRDR KSGLLCRVSA GNDMACLTTD 240
LLTALGKIEP VFIPLVLAFR YWAKLCYIDS QTDGGIPSYC FALMVMFFLQ QRKPPLLPCL 300
LGSWIEGFDP KRMDDFQLKG IVEEKFVKWE CNSSSATEKN SIAEENKAKA DQPKDDTKKT 360
ETDNQSNAMK EKHGKSPLAL ETPNRVSLGQ LWLELLKFYT LDFALEEYVI CVRIQDILTR 420
ENKNWPKRRI AIEDPFSVKR NVARSLNSQL VYEYVVERFR AAYRYFACPQ TKGGNKSTVD 480
FKKREKGKIS NKKPVKSNNM ATNGCILLGE TTEKINAERE QPVQCDEMDC TSQRCIIDNN 540
NLLVNELDFA DHGQDSSSLS TSKSSEIEPK LDKKQDDLAP SETCLKKELS QCNCIDLSKS 600
PDPDKSTGTD CRSNLETESS HQSVCTDTSA TSCNCKATED ASDLNDDDNL PTQELYYVFD 660
KFILTSGKPP TIVCSICKKD GHSKNDCPED FRKIDLKPLP PMTNRFREIL DLVCKRCFDE 720
LSPPCSEQHN REQILIGLEK FIQKEYDEKA RLCLFGSSKN GFGFRDSDLD ICMTLEGHEN 780
AEKLNCKEII ENLAKILKRH PGLRNILPIT TAKVPIVKFE HRRSGLEGDI SLYNTLAQHN 840
TRMLATYAAI DPRVQYLGYT MKVFAKIFDG KQIPQRMVDG WNAFFFDKTE ELKKRLPSLG 900
KNTESL 906 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR002934; Nucleotidyltransferase.
 IPR002058; PAP_assoc.
 IPR001878; Znf_CCHC. 
Pfam
 PF01909; NTP_transf_2
 PF03828; PAP_assoc 
SMART
 SM00343; ZnF_C2HC 
PROSITE
 PS50158; ZF_CCHC 
PRINTS