CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014019
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Terminal uridylyltransferase 4 
Protein Synonyms/Alias
 TUTase 4; Zinc finger CCHC domain-containing protein 11 
Gene Name
 ZCCHC11 
Gene Synonyms/Alias
 KIAA0191; TUT4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
569IVEEKFVKWECNSSSubiquitination[1]
680IEDPFSVKRNVARSLubiquitination[1, 2]
717PQTKGGNKSTVDFKKubiquitination[1]
938DFRKIDLKPLPPMTNubiquitination[1]
981QILIGLEKFIQKEYDubiquitination[1]
1000LCLFGSSKNGFGFRDubiquitination[1]
1036EIIENLAKILKRHPGubiquitination[3]
1054ILPITTAKVPIVKFEubiquitination[1]
1167WNAFFFDKTEELKKRubiquitination[1]
1260KAFINGRKLFGTPFYubiquitination[1, 3]
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] 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
 Uridylyltransferase that acts as a suppressor of microRNA (miRNA) biogenesis by specifically mediating the terminal uridylation of some miRNAs. Catalyzes the 3' uridylation of precursor let-7 (pre-let-7), a miRNA precursor. Uridylated pre- let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cells and is required for ES cells to maintain pluripotency. Does not bind RNA by itself, recruited to pre-let-7 miRNAs via its interaction with LIN28A and LIN28B. Also catalyzes the 3' uridylation of miR-26A, a miRNA that represses IL6 transcript, leading to abrogate IL6 transcript repression and promote cytokine expression. May also suppress Toll-like receptor-induced NF-kappa-B activity via binding to T2BP. Does not play a role in replication-dependent histone mRNA degradation. 
Sequence Annotation
 DOMAIN 628 678 PAP-associated 1.
 DOMAIN 1184 1237 PAP-associated 2.
 ZN_FING 913 930 CCHC-type 1.
 ZN_FING 1293 1310 CCHC-type 2.
 ZN_FING 1357 1374 CCHC-type 3.
 METAL 1009 1009 Magnesium or manganese; catalytic (By
 METAL 1011 1011 Magnesium or manganese; catalytic (By  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Magnesium; Manganese; Metal-binding; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Repeat; RNA-mediated gene silencing; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1644 AA 
Protein Sequence
MEESKTLKSE NHEPKKNVIC EESKAVQVIG NQTLKARNDK SVKEIENSSP NRNSSKKNKQ 60
NDICIEKTEV KSCKVNAANL PGPKDLGLVL RDQSHCKAKK FPNSPVKAEK ATISQAKSEK 120
ATSLQAKAEK SPKSPNSVKA EKASSYQMKS EKVPSSPAEA EKGPSLLLKD MRQKTELQQI 180
GKKIPSSFTS VDKVNIEAVG GEKCALQNSP RSQKQQTCTD NTGDSDDSAS GIEDVSDDLS 240
KMKNDESNKE NSSEMDYLEN ATVIDESALT PEQRLGLKQA EERLERDHIF RLEKRSPEYT 300
NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE LRSLPPPSPA HLAALSVAVI 360
ELAKEHGITD DDLRVRQEIV EEMSKVITTF LPECSLRLYG SSLTRFALKS SDVNIDIKFP 420
PKMNHPDLLI KVLGILKKNV LYVDVESDFH AKVPVVVCRD RKSGLLCRVS AGNDMACLTT 480
DLLTALGKIE PVFIPLVLAF RYWAKLCYID SQTDGGIPSY CFALMVMFFL QQRKPPLLPC 540
LLGSWIEGFD PKRMDDFQLK GIVEEKFVKW ECNSSSATEK NSIAEENKAK ADQPKDDTKK 600
TETDNQSNAM KEKHGKSPLA LETPNRVSLG QLWLELLKFY TLDFALEEYV ICVRIQDILT 660
RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF RAAYRYFACP QTKGGNKSTV 720
DFKKREKGKI SNKKPVKSNN MATNGCILLG ETTEKINAER EQPVQCDEMD CTSQRCIIDN 780
NNLLVNELDF ADHGQDSSSL STSKSSEIEP KLDKKQDDLA PSETCLKKEL SQCNCIDLSK 840
SPDPDKSTGT DCRSNLETES SHQSVCTDTS ATSCNCKATE DASDLNDDDN LPTQELYYVF 900
DKFILTSGKP PTIVCSICKK DGHSKNDCPE DFRKIDLKPL PPMTNRFREI LDLVCKRCFD 960
ELSPPCSEQH NREQILIGLE KFIQKEYDEK ARLCLFGSSK NGFGFRDSDL DICMTLEGHE 1020
NAEKLNCKEI IENLAKILKR HPGLRNILPI TTAKVPIVKF EHRRSGLEGD ISLYNTLAQH 1080
NTRMLATYAA IDPRVQYLGY TMKVFAKRCD IGDASRGSLS SYAYILMVLY FLQQRKPPVI 1140
PVLQEIFDGK QIPQRMVDGW NAFFFDKTEE LKKRLPSLGK NTESLGELWL GLLRFYTEEF 1200
DFKEYVISIR QKKLLTTFEK QWTSKCIAIE DPFDLNHNLG AGVSRKMTNF IMKAFINGRK 1260
LFGTPFYPLI GREAEYFFDS RVLTDGELAP NDRCCRVCGK IGHYMKDCPK RKSLLFRLKK 1320
KDSEEEKEGN EEEKDSRDVL DPRDLHDTRD FRDPRDLRCF ICGDAGHVRR ECPEVKLARQ 1380
RNSSVAAAQL VRNLVNAQQV AGSAQQQGDQ SIRTRQSSEC SESPSYSPQP QPFPQNSSQS 1440
AAITQPSSQP GSQPKLGPPQ QGAQPPHQVQ MPLYNFPQSP PAQYSPMHNM GLLPMHPLQI 1500
PAPSWPIHGP VIHSAPGSAP SNIGLNDPSI IFAQPAARPV AIPNTSHDGH WPRTVAPNSL 1560
VNSGAVGNSE PGFRGLTPPI PWEHAPRPHF PLVPASWPYG LHQNFMHQGN ARFQPNKPFY 1620
TQDRCATRRC RERCPHPPRG NVSE 1644 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0001816; P:cytokine production; IEA:Compara.
 GO:0070102; P:interleukin-6-mediated signaling pathway; IEA:Compara.
 GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
 GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Compara.
 GO:0032755; P:positive regulation of interleukin-6 production; IEA:Compara.
 GO:0031054; P:pre-miRNA processing; IMP:UniProtKB.
 GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; IEA:Compara.
 GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
 GO:0019827; P:stem cell maintenance; IMP:UniProtKB. 
Interpro
 IPR002934; Nucleotidyltransferase.
 IPR002058; PAP_assoc.
 IPR001878; Znf_CCHC. 
Pfam
 PF01909; NTP_transf_2
 PF03828; PAP_assoc
 PF00098; zf-CCHC 
SMART
 SM00343; ZnF_C2HC 
PROSITE
 PS50158; ZF_CCHC
 PS00028; ZINC_FINGER_C2H2_1 
PRINTS