TUT4_HUMAN - dbPTM
TUT4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TUT4_HUMAN
UniProt AC Q5TAX3
Protein Name Terminal uridylyltransferase 4
Gene Name ZCCHC11
Organism Homo sapiens (Human).
Sequence Length 1644
Subcellular Localization Nucleus . Cytoplasm . Mainly cytoplasmic (PubMed:19703396, PubMed:25480299). Translocates into the cytoplasm following treatment of the cell with LPS (PubMed:16643855).
Protein Description Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay. [PubMed: 25480299 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 (ES) cell pluripotency (By similarity 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 (By similarity May also suppress Toll-like receptor-induced NF-kappa-B activation via binding to T2BP. Does not play a role in replication-dependent histone mRNA degradation. Due to functional redundancy between ZCCHC6 and ZCCHC11, the identification of the specific role of each of these proteins is difficult.]
Protein Sequence MEESKTLKSENHEPKKNVICEESKAVQVIGNQTLKARNDKSVKEIENSSPNRNSSKKNKQNDICIEKTEVKSCKVNAANLPGPKDLGLVLRDQSHCKAKKFPNSPVKAEKATISQAKSEKATSLQAKAEKSPKSPNSVKAEKASSYQMKSEKVPSSPAEAEKGPSLLLKDMRQKTELQQIGKKIPSSFTSVDKVNIEAVGGEKCALQNSPRSQKQQTCTDNTGDSDDSASGIEDVSDDLSKMKNDESNKENSSEMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNILEKQEESELRSLPPPSPAHLAALSVAVIELAKEHGITDDDLRVRQEIVEEMSKVITTFLPECSLRLYGSSLTRFALKSSDVNIDIKFPPKMNHPDLLIKVLGILKKNVLYVDVESDFHAKVPVVVCRDRKSGLLCRVSAGNDMACLTTDLLTALGKIEPVFIPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLLPCLLGSWIEGFDPKRMDDFQLKGIVEEKFVKWECNSSSATEKNSIAEENKAKADQPKDDTKKTETDNQSNAMKEKHGKSPLALETPNRVSLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKRRIAIEDPFSVKRNVARSLNSQLVYEYVVERFRAAYRYFACPQTKGGNKSTVDFKKREKGKISNKKPVKSNNMATNGCILLGETTEKINAEREQPVQCDEMDCTSQRCIIDNNNLLVNELDFADHGQDSSSLSTSKSSEIEPKLDKKQDDLAPSETCLKKELSQCNCIDLSKSPDPDKSTGTDCRSNLETESSHQSVCTDTSATSCNCKATEDASDLNDDDNLPTQELYYVFDKFILTSGKPPTIVCSICKKDGHSKNDCPEDFRKIDLKPLPPMTNRFREILDLVCKRCFDELSPPCSEQHNREQILIGLEKFIQKEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEIIENLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPPVIPVLQEIFDGKQIPQRMVDGWNAFFFDKTEELKKRLPSLGKNTESLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWTSKCIAIEDPFDLNHNLGAGVSRKMTNFIMKAFINGRKLFGTPFYPLIGREAEYFFDSRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKSLLFRLKKKDSEEEKEGNEEEKDSRDVLDPRDLHDTRDFRDPRDLRCFICGDAGHVRRECPEVKLARQRNSSVAAAQLVRNLVNAQQVAGSAQQQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYNFPQSPPAQYSPMHNMGLLPMHPLQIPAPSWPIHGPVIHSAPGSAPSNIGLNDPSIIFAQPAARPVAIPNTSHDGHWPRTVAPNSLVNSGAVGNSEPGFRGLTPPIPWEHAPRPHFPLVPASWPYGLHQNFMHQGNARFQPNKPFYTQDRCATRRCRERCPHPPRGNVSE
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
33PhosphorylationVQVIGNQTLKARNDK
EEEECCHHHHHCCCC		33.94-
48PhosphorylationSVKEIENSSPNRNSS
CHHHHHCCCCCCCCC		34.0923663014
49PhosphorylationVKEIENSSPNRNSSK
HHHHHCCCCCCCCCC		37.4623401153
54PhosphorylationNSSPNRNSSKKNKQN
CCCCCCCCCCCCCCC		40.0529514088
55PhosphorylationSSPNRNSSKKNKQND
CCCCCCCCCCCCCCC		51.7229514088
97AcetylationLRDQSHCKAKKFPNS
EECCCHHCCCCCCCC		58.797965465
104PhosphorylationKAKKFPNSPVKAEKA
CCCCCCCCCHHHHHC		31.1630266825
107AcetylationKFPNSPVKAEKATIS
CCCCCCHHHHHCCHH		54.967965475
131PhosphorylationLQAKAEKSPKSPNSV
HHHHHHHCCCCCCCH		29.1223663014
134PhosphorylationKAEKSPKSPNSVKAE
HHHHCCCCCCCHHHH		32.4723663014
137PhosphorylationKSPKSPNSVKAEKAS
HCCCCCCCHHHHHHC		28.5120873877
150PhosphorylationASSYQMKSEKVPSSP
HCHHCCCCCCCCCCH		36.9923312004
155PhosphorylationMKSEKVPSSPAEAEK
CCCCCCCCCHHHHHH		52.5223401153
156PhosphorylationKSEKVPSSPAEAEKG
CCCCCCCCHHHHHHC		23.2730266825
165PhosphorylationAEAEKGPSLLLKDMR
HHHHHCCCHHHHHHH		40.0729978859
186PhosphorylationQIGKKIPSSFTSVDK
HHHHHCCCCCCCCCE		41.3723186163
187PhosphorylationIGKKIPSSFTSVDKV
HHHHCCCCCCCCCEE		27.4723186163
189PhosphorylationKKIPSSFTSVDKVNI
HHCCCCCCCCCEEEE		29.7723186163
190PhosphorylationKIPSSFTSVDKVNIE
HCCCCCCCCCEEEEE		26.7226657352
209PhosphorylationEKCALQNSPRSQKQQ
CCCCCCCCCCCCCCC		14.5530266825
212PhosphorylationALQNSPRSQKQQTCT
CCCCCCCCCCCCCCC		45.1528985074
217PhosphorylationPRSQKQQTCTDNTGD
CCCCCCCCCCCCCCC		18.1925954137
219PhosphorylationSQKQQTCTDNTGDSD
CCCCCCCCCCCCCCC		35.3528450419
222PhosphorylationQQTCTDNTGDSDDSA
CCCCCCCCCCCCCCC		45.2128450419
225PhosphorylationCTDNTGDSDDSASGI
CCCCCCCCCCCCCCC		44.6628102081
228PhosphorylationNTGDSDDSASGIEDV
CCCCCCCCCCCCHHH		29.3528102081
230PhosphorylationGDSDDSASGIEDVSD
CCCCCCCCCCHHHHH		44.2328450419
236PhosphorylationASGIEDVSDDLSKMK
CCCCHHHHHHHHHHC		37.4223090842
240PhosphorylationEDVSDDLSKMKNDES
HHHHHHHHHHCCCCC		37.3823090842
270PhosphorylationVIDESALTPEQRLGL
EECHHHCCHHHHHCH		25.2125159151
278UbiquitinationPEQRLGLKQAEERLE
HHHHHCHHHHHHHHH		45.74-
296PhosphorylationIFRLEKRSPEYTNCR
HEEHHHCCCCCCCHH		32.9025159151
343PhosphorylationQEESELRSLPPPSPA
HHHHHHHCCCCCCHH		58.83-
348PhosphorylationLRSLPPPSPAHLAAL
HHCCCCCCHHHHHHH		40.26-
356PhosphorylationPAHLAALSVAVIELA
HHHHHHHHHHHHHHH		11.87-
437AcetylationIKVLGILKKNVLYVD
HHHHHHHHCCEEEEE		40.1425953088
479PhosphorylationGNDMACLTTDLLTAL
CCCCHHHHHHHHHHH		20.3923401153
480PhosphorylationNDMACLTTDLLTALG
CCCHHHHHHHHHHHC		16.2323401153
484PhosphorylationCLTTDLLTALGKIEP
HHHHHHHHHHCCCCC		27.4223401153
566UbiquitinationLKGIVEEKFVKWECN
CEEHHEEEEEEEECC		41.79-
569UbiquitinationIVEEKFVKWECNSSS
HHEEEEEEEECCCCC		40.17-
574PhosphorylationFVKWECNSSSATEKN
EEEEECCCCCHHCCC		37.01-
588AcetylationNSIAEENKAKADQPK
CCHHHHHHHHCCCCC		55.3290517
590AcetylationIAEENKAKADQPKDD
HHHHHHHHCCCCCCC		54.8590521
595AcetylationKAKADQPKDDTKKTE
HHHCCCCCCCCCCCH		63.7090525
678PhosphorylationIAIEDPFSVKRNVAR
CCCCCCHHHCHHHHH		31.92-
680 (in isoform 1)Ubiquitination-36.7421890473
680 (in isoform 2)Ubiquitination-36.7421890473
680UbiquitinationIEDPFSVKRNVARSL
CCCCHHHCHHHHHHC		36.7421906983
686PhosphorylationVKRNVARSLNSQLVY
HCHHHHHHCCHHHHH		23.3624719451
689PhosphorylationNVARSLNSQLVYEYV
HHHHHCCHHHHHHHH		30.1324719451
717UbiquitinationPQTKGGNKSTVDFKK
CCCCCCCCCCCCCHH		51.26-
773PhosphorylationCDEMDCTSQRCIIDN
CCCCCCCCCEEEECC		23.2017525332
831PhosphorylationTCLKKELSQCNCIDL
HHHHHHHHHCCCEEC		33.5023927012
839PhosphorylationQCNCIDLSKSPDPDK
HCCCEECCCCCCCCC		27.6023663014
841PhosphorylationNCIDLSKSPDPDKST
CCEECCCCCCCCCCC		31.0323663014
847PhosphorylationKSPDPDKSTGTDCRS
CCCCCCCCCCCCHHH		39.1823927012
848PhosphorylationSPDPDKSTGTDCRSN
CCCCCCCCCCCHHHH		50.2523927012
850PhosphorylationDPDKSTGTDCRSNLE
CCCCCCCCCHHHHCC		31.8223927012
938UbiquitinationDFRKIDLKPLPPMTN
HHHHCCCCCCCCCCH		40.54-
981UbiquitinationQILIGLEKFIQKEYD
HHHHHHHHHHHHHCH		53.46-
985UbiquitinationGLEKFIQKEYDEKAR
HHHHHHHHHCHHHHC		54.12-
1000UbiquitinationLCLFGSSKNGFGFRD
EEHHCCCCCCCCCCC		63.89-
1036 (in isoform 2)Ubiquitination-52.3021890473
1036 (in isoform 1)Ubiquitination-52.3021890473
1036UbiquitinationEIIENLAKILKRHPG
HHHHHHHHHHHHCCC		52.3021890473
1054UbiquitinationILPITTAKVPIVKFE
CCCCCCCCCEEEECC		46.59-
1097PhosphorylationAIDPRVQYLGYTMKV
HCCCCHHHHHHHHHH		10.15-
1100PhosphorylationPRVQYLGYTMKVFAK
CCHHHHHHHHHHHHH		10.89-
1101PhosphorylationRVQYLGYTMKVFAKR
CHHHHHHHHHHHHHH		14.55-
1167UbiquitinationWNAFFFDKTEELKKR
CCEEECCCHHHHHHH		53.32-
1213UbiquitinationVISIRQKKLLTTFEK
HHHHHHHHHHHHHHH		40.15-
1217PhosphorylationRQKKLLTTFEKQWTS
HHHHHHHHHHHHHCC		29.7529496907
1223PhosphorylationTTFEKQWTSKCIAIE
HHHHHHHCCEEEEEC		18.8029496907
1225UbiquitinationFEKQWTSKCIAIEDP
HHHHHCCEEEEECCC		23.45-
1260UbiquitinationKAFINGRKLFGTPFY
HHHHCCHHCCCCCCH		49.9521890473
1260 (in isoform 1)Ubiquitination-49.9521890473
1260 (in isoform 2)Ubiquitination-49.9521890473
1284PhosphorylationFFDSRVLTDGELAPN
HCCCEECCCCCCCCC		38.8228188228
1323PhosphorylationFRLKKKDSEEEKEGN
HHHHHCCCHHHHCCC		56.6530576142
1383PhosphorylationKLARQRNSSVAAAQL
HHHHHCCCHHHHHHH		28.5128555341
1384PhosphorylationLARQRNSSVAAAQLV
HHHHCCCHHHHHHHH		21.2328857561
1403PhosphorylationNAQQVAGSAQQQGDQ
HHHHHHHHHHHHCCC		17.1128555341
1411PhosphorylationAQQQGDQSIRTRQSS
HHHHCCCCCHHHCCC		20.8328555341
1624MethylationKPFYTQDRCATRRCR
CCCCCCCCHHHHHHH		11.3630761595
1628MethylationTQDRCATRRCRERCP
CCCCHHHHHHHHHCC		19.71115920337
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TUT4_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIFA_HUMANTIFAphysical
16643855
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TUT4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773, AND MASSSPECTROMETRY.

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