dbPTM

TUT7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TUT7_HUMAN
UniProt AC	Q5VYS8
Protein Name	Terminal uridylyltransferase 7
Gene Name	ZCCHC6
Organism	Homo sapiens (Human).
Sequence Length	1495
Subcellular Localization	Cytoplasm .
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: 19703396]
Protein Sequence	MGDTAKPYFVKRTKDRGTMDDDDFRRGHPQQDYLIIDDHAKGHGSKMEKGLQKKKITPGNYGNTPRKGPCAVSSNPYAFKNPIYSQPAWMNDSHKDQSKRWLSDEHTGNSDNWREFKPGPRIPVINRQRKDSFQENEDGYRWQDTRGCRTVRRLFHKDLTSLETTSEMEAGSPENKKQRSRPRKPRKTRNEENEQDGDLEGPVIDESVLSTKELLGLQQAEERLKRDCIDRLKRRPRNYPTAKYTCRLCDVLIESIAFAHKHIKEKRHKKNIKEKQEEELLTTLPPPTPSQINAVGIAIDKVVQEFGLHNENLEQRLEIKRIMENVFQHKLPDCSLRLYGSSCSRLGFKNSDVNIDIQFPAIMSQPDVLLLVQECLKNSDSFIDVDADFHARVPVVVCREKQSGLLCKVSAGNENACLTTKHLTALGKLEPKLVPLVIAFRYWAKLCSIDRPEEGGLPPYVFALMAIFFLQQRKEPLLPVYLGSWIEGFSLSKLGNFNLQDIEKDVVIWEHTDSAAGDTGITKEEAPRETPIKRGQVSLILDVKHQPSVPVGQLWVELLRFYALEFNLADLVISIRVKELVSRELKDWPKKRIAIEDPYSVKRNVARTLNSQPVFEYILHCLRTTYKYFALPHKITKSSLLKPLNAITCISEHSKEVINHHPDVQTKDDKLKNSVLAQGPGATSSAANTCKVQPLTLKETAESFGSPPKEEMGNEHISVHPENSDCIQADVNSDDYKGDKVYHPETGRKNEKEKVGRKGKHLLTVDQKRGEHVVCGSTRNNESESTLDLEGFQNPTAKECEGLATLDNKADLDGESTEGTEELEDSLNHFTHSVQGQTSEMIPSDEEEEDDEEEEEEEEPRLTINQREDEDGMANEDELDNTYTGSGDEDALSEEDDELGEAAKYEDVKECGKHVERALLVELNKISLKEENVCEEKNSPVDQSDFFYEFSKLIFTKGKSPTVVCSLCKREGHLKKDCPEDFKRIQLEPLPPLTPKFLNILDQVCIQCYKDFSPTIIEDQAREHIRQNLESFIRQDFPGTKLSLFGSSKNGFGFKQSDLDVCMTINGLETAEGLDCVRTIEELARVLRKHSGLRNILPITTAKVPIVKFFHLRSGLEVDISLYNTLALHNTRLLSAYSAIDPRVKYLCYTMKVFTKMCDIGDASRGSLSSYAYTLMVLYFLQQRNPPVIPVLQEIYKGEKKPEIFVDGWNIYFFDQIDELPTYWSECGKNTESVGQLWLGLLRFYTEEFDFKEHVISIRRKSLLTTFKKQWTSKYIVIEDPFDLNHNLGAGLSRKMTNFIMKAFINGRRVFGIPVKGFPKDYPSKMEYFFDPDVLTEGELAPNDRCCRICGKIGHFMKDCPMRRKVRRRRDQEDALNQRYPENKEKRSKEDKEIHNKYTEREVSTKEDKPIQCTPQKAKPMRAAADLGREKILRPPVEKWKRQDDKDLREKRCFICGREGHIKKECPQFKGSSGSLSSKYMTQGKASAKRTQQES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Ubiquitination	TAKPYFVKRTKDRGT CCCCCEEEECCCCCC	44.44	-
33	Phosphorylation	RGHPQQDYLIIDDHA CCCCCCCEEEECCCC	8.75	28796482
57	Phosphorylation	GLQKKKITPGNYGNT CCCCCCCCCCCCCCC	33.74	25159151
61	Phosphorylation	KKITPGNYGNTPRKG CCCCCCCCCCCCCCC	20.05	29396449
64	Phosphorylation	TPGNYGNTPRKGPCA CCCCCCCCCCCCCCC	21.80	25159151
73	Phosphorylation	RKGPCAVSSNPYAFK CCCCCCCCCCCCCCC	13.08	29759185
74	Phosphorylation	KGPCAVSSNPYAFKN CCCCCCCCCCCCCCC	34.91	28152594
77	Phosphorylation	CAVSSNPYAFKNPIY CCCCCCCCCCCCCCC	28.99	28152594
84	Phosphorylation	YAFKNPIYSQPAWMN CCCCCCCCCCCCCCC	11.51	21945579
85	Phosphorylation	AFKNPIYSQPAWMND CCCCCCCCCCCCCCC	30.33	21945579
93	Phosphorylation	QPAWMNDSHKDQSKR CCCCCCCCCCCHHHH	27.68	21945579
110	Phosphorylation	SDEHTGNSDNWREFK CCCCCCCCCCHHHCC	33.40	21712546
132	Phosphorylation	INRQRKDSFQENEDG ECCCCCCCCCCCCCC	31.68	27273156
140	Phosphorylation	FQENEDGYRWQDTRG CCCCCCCCCCHHHCC	22.47	29978859
145	Phosphorylation	DGYRWQDTRGCRTVR CCCCCHHHCCHHHHH	17.54	27251275
160	Phosphorylation	RLFHKDLTSLETTSE HHHHCCCCCCCCCCC	41.20	29255136
161	Phosphorylation	LFHKDLTSLETTSEM HHHCCCCCCCCCCCC	31.35	29255136
164	Phosphorylation	KDLTSLETTSEMEAG CCCCCCCCCCCCCCC	40.70	23663014
165	Phosphorylation	DLTSLETTSEMEAGS CCCCCCCCCCCCCCC	17.20	23663014
166	Phosphorylation	LTSLETTSEMEAGSP CCCCCCCCCCCCCCC	42.22	23663014
172	Phosphorylation	TSEMEAGSPENKKQR CCCCCCCCCCCHHHC	35.77	29255136
180	Phosphorylation	PENKKQRSRPRKPRK CCCHHHCCCCCCCCC	44.11	-
212	Ubiquitination	DESVLSTKELLGLQQ CHHHHCHHHHHCHHH	42.88	-
330	Ubiquitination	MENVFQHKLPDCSLR HHHHHHHCCCCCCEE	51.43	-
401	Ubiquitination	PVVVCREKQSGLLCK CEEEEECCCCCCEEE	30.34	-
408	Ubiquitination	KQSGLLCKVSAGNEN CCCCCEEEEECCCCC	38.91	-
421	Ubiquitination	ENACLTTKHLTALGK CCEEEEHHHHHHHCC	31.23	-
428	Ubiquitination	KHLTALGKLEPKLVP HHHHHHCCCCCCHHH	50.99	-
504	Ubiquitination	FNLQDIEKDVVIWEH CCHHHHCCCEEEEEE	57.04	-
512	Phosphorylation	DVVIWEHTDSAAGDT CEEEEEECCCCCCCC	21.82	29396449
514	Phosphorylation	VIWEHTDSAAGDTGI EEEEECCCCCCCCCC	22.60	29396449
519	Phosphorylation	TDSAAGDTGITKEEA CCCCCCCCCCCCCCC	29.57	29396449
522	Phosphorylation	AAGDTGITKEEAPRE CCCCCCCCCCCCCCC	33.47	29396449
530	Phosphorylation	KEEAPRETPIKRGQV CCCCCCCCCCCCCEE	31.43	25159151
538	Phosphorylation	PIKRGQVSLILDVKH CCCCCEEEEEEEECC	11.21	-
582	Phosphorylation	IRVKELVSRELKDWP HHHHHHHHHHCCCCC	32.44	22673903
592 (in isoform 2)	Methylation	-	29.69	-
599	Phosphorylation	RIAIEDPYSVKRNVA CCCCCCCCHHHHHHH	38.12	18669648
599 (in isoform 2)	Phosphorylation	-	38.12	22985185
600	Phosphorylation	IAIEDPYSVKRNVAR CCCCCCCHHHHHHHH	26.93	25159151
602	Ubiquitination	IEDPYSVKRNVARTL CCCCCHHHHHHHHHH	32.11	-
608	Phosphorylation	VKRNVARTLNSQPVF HHHHHHHHHCCCHHH	22.13	26074081
611	Phosphorylation	NVARTLNSQPVFEYI HHHHHHCCCHHHHHH	38.69	26074081
617	Phosphorylation	NSQPVFEYILHCLRT CCCHHHHHHHHHHHH	9.41	26074081
624	Phosphorylation	YILHCLRTTYKYFAL HHHHHHHHHHHHHHC	22.87	26074081
625	Phosphorylation	ILHCLRTTYKYFALP HHHHHHHHHHHHHCC	16.16	26074081
626	Phosphorylation	LHCLRTTYKYFALPH HHHHHHHHHHHHCCC	11.77	26074081
637	Ubiquitination	ALPHKITKSSLLKPL HCCCCCCHHHHCHHH	41.33	-
639	Phosphorylation	PHKITKSSLLKPLNA CCCCCHHHHCHHHHH	39.00	24719451
642	Ubiquitination	ITKSSLLKPLNAITC CCHHHHCHHHHHHHH	53.40	-
700	Phosphorylation	QPLTLKETAESFGSP CCCCHHHHHHHHCCC	33.85	26471730
703	Phosphorylation	TLKETAESFGSPPKE CHHHHHHHHCCCCHH	32.23	27050516
706	Phosphorylation	ETAESFGSPPKEEMG HHHHHHCCCCHHHHC	35.70	21815630
718	Phosphorylation	EMGNEHISVHPENSD HHCCCCCEECCCCCC	19.11	23186163
724	Phosphorylation	ISVHPENSDCIQADV CEECCCCCCCEECCC	32.00	23186163
733	Phosphorylation	CIQADVNSDDYKGDK CEECCCCCCCCCCCE	31.54	23186163
736	Phosphorylation	ADVNSDDYKGDKVYH CCCCCCCCCCCEEEC	23.12	26471730
742	Phosphorylation	DYKGDKVYHPETGRK CCCCCEEECCCCCCC	19.87	-
752	Acetylation	ETGRKNEKEKVGRKG CCCCCCHHHHHCCCC	72.70	7692137
768	Ubiquitination	HLLTVDQKRGEHVVC EEEEECCCCCCEEEE	58.88	-
778	Phosphorylation	EHVVCGSTRNNESES CEEEECCCCCCCCCC	23.77	29116813
783	Phosphorylation	GSTRNNESESTLDLE CCCCCCCCCCEECCC	38.68	28555341
785	Phosphorylation	TRNNESESTLDLEGF CCCCCCCCEECCCCC	43.48	28555341
796	Phosphorylation	LEGFQNPTAKECEGL CCCCCCCCHHHCCCE	58.89	29116813
816	Phosphorylation	KADLDGESTEGTEEL CCCCCCCCCCCHHHH	36.97	26657352
817	Phosphorylation	ADLDGESTEGTEELE CCCCCCCCCCHHHHH	33.85	26657352
844	Phosphorylation	QTSEMIPSDEEEEDD CCCCCCCCCCCCCCC	46.89	18669648
882	Phosphorylation	NEDELDNTYTGSGDE CHHHCCCCCCCCCCH	23.33	28348404
883	Phosphorylation	EDELDNTYTGSGDED HHHCCCCCCCCCCHH	18.50	27422710
884	Phosphorylation	DELDNTYTGSGDEDA HHCCCCCCCCCCHHH	23.88	28348404
886	Phosphorylation	LDNTYTGSGDEDALS CCCCCCCCCCHHHCC	34.96	25850435
893	Phosphorylation	SGDEDALSEEDDELG CCCHHHCCCCCHHHH	40.43	27422710
905	Phosphorylation	ELGEAAKYEDVKECG HHHHHHCHHHHHHHH	16.79	28796482
939	Phosphorylation	NVCEEKNSPVDQSDF CCCCCCCCCCCHHHH	37.05	25159151
944	Phosphorylation	KNSPVDQSDFFYEFS CCCCCCHHHHHHHHH	31.74	24245541
948	Phosphorylation	VDQSDFFYEFSKLIF CCHHHHHHHHHHHHC	18.96	-
951	Phosphorylation	SDFFYEFSKLIFTKG HHHHHHHHHHHCCCC	18.02	-
960	Phosphorylation	LIFTKGKSPTVVCSL HHCCCCCCCEEEHHH	34.18	25159151
962	Phosphorylation	FTKGKSPTVVCSLCK CCCCCCCEEEHHHHC	32.44	29514088
966	Phosphorylation	KSPTVVCSLCKREGH CCCEEEHHHHCCCCC	25.78	29514088
994	Phosphorylation	LEPLPPLTPKFLNIL CCCCCCCCHHHHHHH	30.15	21406692
1009	Phosphorylation	DQVCIQCYKDFSPTI HHHHHHHHCCCCCCC	9.38	-
1043	Phosphorylation	DFPGTKLSLFGSSKN CCCCCEEEEECCCCC	24.17	29759185
1048	Phosphorylation	KLSLFGSSKNGFGFK EEEEECCCCCCCCCC	30.44	29759185
1103	Ubiquitination	ILPITTAKVPIVKFF CCCCCCCCCCEEEEE	46.59	-
1233	Phosphorylation	ECGKNTESVGQLWLG HCCCCCHHHHHHHHH	29.52	21964256
1262	Phosphorylation	VISIRRKSLLTTFKK HHHHCHHHHHHHHHH	27.14	23403867
1265	Phosphorylation	IRRKSLLTTFKKQWT HCHHHHHHHHHHHCC	35.16	24275569
1266	Phosphorylation	RRKSLLTTFKKQWTS CHHHHHHHHHHHCCC	33.17	23403867
1275	Phosphorylation	KKQWTSKYIVIEDPF HHHCCCCEEEEECCC	10.53	-
1293	Phosphorylation	HNLGAGLSRKMTNFI CCCCCCCCHHHHHHH	29.01	-
1297	Phosphorylation	AGLSRKMTNFIMKAF CCCCHHHHHHHHHHH	29.97	20068231
1316	Ubiquitination	RVFGIPVKGFPKDYP EECCCCCCCCCCCCC	49.86	-
1325	Ubiquitination	FPKDYPSKMEYFFDP CCCCCCCCCCEECCH	31.11	-
1352	Acetylation	RCCRICGKIGHFMKD HHHHHHHHHHHHHHH	40.89	19815555
1397	Ubiquitination	EDKEIHNKYTEREVS HHHHHHHHHCCCCCC	39.11	-
1399	Phosphorylation	KEIHNKYTEREVSTK HHHHHHHCCCCCCCC	30.12	28258704
1404	Phosphorylation	KYTEREVSTKEDKPI HHCCCCCCCCCCCCC	29.07	23312004
1405	Phosphorylation	YTEREVSTKEDKPIQ HCCCCCCCCCCCCCC	43.56	23312004
1409	Acetylation	EVSTKEDKPIQCTPQ CCCCCCCCCCCCCCC	45.15	27452117
1414	Phosphorylation	EDKPIQCTPQKAKPM CCCCCCCCCCCCCCC	16.63	25850435
1441	Acetylation	RPPVEKWKRQDDKDL CCCHHHHCCCCCHHH	51.77	30593485
1472	Phosphorylation	ECPQFKGSSGSLSSK CCCCCCCCCCCCCHH	31.92	27251275
1473	Phosphorylation	CPQFKGSSGSLSSKY CCCCCCCCCCCCHHH	40.86	27251275
1475	Phosphorylation	QFKGSSGSLSSKYMT CCCCCCCCCCHHHHH	27.33	27251275
1487	Phosphorylation	YMTQGKASAKRTQQE HHHCCCCCCHHHHCC	37.50	24719451

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 TUT7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TUT7_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 TUT7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049
XPC_HUMAN	XPC	physical	22939629

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 TUT7_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; THR-64; SER-172 ANDSER-844, AND MASS SPECTROMETRY.	18669648 [Abstract]