TUT4_MOUSE - dbPTM
TUT4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TUT4_MOUSE
UniProt AC B2RX14
Protein Name Terminal uridylyltransferase 4
Gene Name Zcchc11
Organism Mus musculus (Mouse).
Sequence Length 1644
Subcellular Localization Nucleus . Cytoplasm . Mainly cytoplasmic (PubMed:19703396). Translocates into the cytoplasm following treatment of the cell with LPS (By similarity).
Protein Description Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay. Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem cell pluripotency. [PubMed: 19703396 Does not bind RNA directly, but recruited to RNA targets by RNA-binding protein LIN28A. Also catalyzes the 3' uridylation of miR-26A, a miRNA that targets IL6 transcript. This abrogates the silencing of IL6 transcript, hence promoting cytokine expression]
Protein Sequence MEEPKTSKNENHEPKKNIICEESKAVKIISNQTLKPRNDKSEIGTSSLNRNSSKKTKQNDICIEKTEAKSCKVNAASVPGPKDLGLVHRDQSHCKMKKLPNSPMKAQKGSSQTKLEKTPSLQTKAEKVPKSPNLPVKAEKAPCTTAEATTEKALNSQRKEENTPTSQMKLQKTPRSPLEPENVPSLLLKENVKQTESQQTGKKLTSSFVSMDKRKSEALQGEKSALENSSLSQKQQTQTDNIADSDDSASGIEDTADDLSKMKSEESNKENSSEMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNILEKQEESELRSLPSPSSAHLAALSVAVVELAKEQGITDDDLRIRQDIVEEMSKVIMTFLPECSLRLYGSSLTKFALKSSDVNIDIKFPPKMNHPDLLIQVLGILKKSALYIDVESDFHAKVPVVVCKDRKSALLCRVSAGNDMACLTTDLLAALGKVEPVFTPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLLPCLLGSWIEGFDPKRMDDFQLKGIVEEKFVKWEYNSSSATEKNLIADENKAKADEPKDDTKKTETDNQSNAAKAKHGKSPLTLEAPNQVPLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKRRIAIEDPFSVKRNVARSLNSQLVYEYVVERFRAAYRYFACPQKKGGNKSTMDPKKKEKGKLSSKKPVKSDCSATNCCILGESAEKIHMERGQPAKHDETEFTSQRCIVDNDSLLVNELGLANHGQDSSSLSTASGGSDLKQKSAEKQGDLTPSETSLKKELSQCICIGTPDGAESAGTDCRSNLEMDSSHQIVCNNVSATSCNCKATEVTSDLVDEDNLPSQELYYVFDKFILTSGKPPTIVCSICKKDGHSKNDCPEDFRKIDLKPLPPMTNRFREILDLVCKRCFDELSPPCSEQHNREQILIGLEKFIQKEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEIIENLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPPVIPVLQEIFDGKQIPQRMVDGWNAFFFDKTEELKKRLPSLGKNTESLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWTSKCIAIEDPFDLNHNLGAGVSRKMTNFIMKAFINGRKLFGTPFYPLIGREAEYFFDSRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKRLKKKDSEEEKEGNEEEKDSRDLLDSRDLRCFICGDAGHVRRECPEVKMARQRNSSVAAAQLVRNLVNAQQVAGSAQQQSDQSIRTRQSSECSDSPSYSPQPQPFPQNSPQPSALPPPPSQPGSQPKLGPPQQGGQPPHQVQMPLYNFPQSPPAHYSPMHSMGLLPMHPLQIPAPSWPIHGPMLHSAPGSTPSNIGLNDPSIIFAQPAARPMAIPSPSHDGHWPRTVAPNSLVNNGAVGNSEPRFRGLNPPIPWEHAPRHFPLVPASWPYGLHQNFMHQGNPRFQPKPFYAQADRCATRRCRERCPHPPRGNVSE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
23PhosphorylationKNIICEESKAVKIIS
CCEECCCHHHEEEEC		12.01-
47PhosphorylationKSEIGTSSLNRNSSK
CCCCCCCHHCCCCCC		29.5125338131
52PhosphorylationTSSLNRNSSKKTKQN
CCHHCCCCCCCCCCC		40.0525338131
53PhosphorylationSSLNRNSSKKTKQND
CHHCCCCCCCCCCCC		41.5429514104
102PhosphorylationKMKKLPNSPMKAQKG
CCCCCCCCCCCCCCC		25.1624453211
120PhosphorylationTKLEKTPSLQTKAEK
CCCCCCCCHHHHHHH		38.0427149854
123PhosphorylationEKTPSLQTKAEKVPK
CCCCCHHHHHHHCCC		37.20-
131PhosphorylationKAEKVPKSPNLPVKA
HHHHCCCCCCCCCCC		16.9827087446
149PhosphorylationPCTTAEATTEKALNS
CCCCHHHHHHHHHHH		27.3026026062
163PhosphorylationSQRKEENTPTSQMKL
HHHHHCCCCCHHHHC		31.0925338131
173PhosphorylationSQMKLQKTPRSPLEP
HHHHCCCCCCCCCCC		15.8021082442
176PhosphorylationKLQKTPRSPLEPENV
HCCCCCCCCCCCCCC		34.7326824392
185PhosphorylationLEPENVPSLLLKENV
CCCCCCCHHHHHHCH		27.6328833060
207PhosphorylationTGKKLTSSFVSMDKR
HCHHHHHHHHCCCHH		25.1629514104
210PhosphorylationKLTSSFVSMDKRKSE
HHHHHHHCCCHHHHH		21.1829899451
216PhosphorylationVSMDKRKSEALQGEK
HCCCHHHHHHHHHHH		31.9425266776
237PhosphorylationSLSQKQQTQTDNIAD
CCCHHHHHCCCCCCC		30.8323984901
239PhosphorylationSQKQQTQTDNIADSD
CHHHHHCCCCCCCCC		34.1123984901
245PhosphorylationQTDNIADSDDSASGI
CCCCCCCCCCCCCCC		34.0021082442
248PhosphorylationNIADSDDSASGIEDT
CCCCCCCCCCCCCCC		29.3521082442
250PhosphorylationADSDDSASGIEDTAD
CCCCCCCCCCCCCHH		44.2322324799
255PhosphorylationSASGIEDTADDLSKM
CCCCCCCCHHHHHHH		21.1322324799
264PhosphorylationDDLSKMKSEESNKEN
HHHHHHCCHHHHCCC		43.00-
267PhosphorylationSKMKSEESNKENSSE
HHHCCHHHHCCCCHH		49.50-
272PhosphorylationEESNKENSSEMDYLE
HHHHCCCCHHHHHHH		28.85-
277PhosphorylationENSSEMDYLENATVI
CCCHHHHHHHHCEEE		18.01-
528PhosphorylationRYWAKLCYIDSQTDG
HHHHHHCCCCCCCCC		20.42-
531PhosphorylationAKLCYIDSQTDGGIP
HHHCCCCCCCCCCHH		25.97-
533PhosphorylationLCYIDSQTDGGIPSY
HCCCCCCCCCCHHHH		40.33-
715PhosphorylationNSQLVYEYVVERFRA
CHHHHHHHHHHHHHH		7.66-
840PhosphorylationAEKQGDLTPSETSLK
HHHCCCCCCCHHHHH		29.5229514104
910PhosphorylationVDEDNLPSQELYYVF
CCCCCCCHHHHHEEE		39.1825338131
1197UbiquitinationKRLPSLGKNTESLGE
HHCHHCCCCHHHHHH		67.02-
1265PhosphorylationAGVSRKMTNFIMKAF
CCCCHHHHHHHHHHH		29.9721183079
1333AcetylationPKRKRLKKKDSEEEK
HHHHHHCCCCCHHHH		67.427609297
1336PhosphorylationKRLKKKDSEEEKEGN
HHHCCCCCHHHHCCC		56.6529895711
1340AcetylationKKDSEEEKEGNEEEK
CCCCHHHHCCCHHHH		74.367609307
1384PhosphorylationKMARQRNSSVAAAQL
HHHHHCCCHHHHHHH		28.5128066266
1385PhosphorylationMARQRNSSVAAAQLV
HHHHCCCHHHHHHHH		21.2328066266
1418PhosphorylationQSIRTRQSSECSDSP
HCHHHHCCCCCCCCC		25.47-
1624MethylationPFYAQADRCATRRCR
CCCHHCHHHHHHHHH		18.2624129315
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TUT4_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TUT4_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TUT4_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TUT4_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TUT4_MOUSE

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Related Literatures of Post-Translational Modification

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