dbPTM

TTP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTP_HUMAN
UniProt AC	P26651
Protein Name	mRNA decay activator protein ZFP36 {ECO:0000305}
Gene Name	ZFP36 {ECO:0000312\|HGNC:HGNC:12862}
Organism	Homo sapiens (Human).
Sequence Length	326
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasmic granule . Cytoplasm, P-body . Shuttles between nucleus and cytoplasm in a CRM1-dependent manner (By similarity). Localized predominantly in the cytoplasm in a p38 MAPK- and YWHAB-dependent manner (By similarity). Col
Protein Description	Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. [PubMed: 9703499]
Protein Sequence	MDLTAIYESLLSLSPDVPVPSDHGGTESSPGWGSSGPWSLSPSDSSPSGVTSRLPGRSTSLVEGRSCGWVPPPPGFAPLAPRLGPELSPSPTSPTATSTTPSRYKTELCRTFSESGRCRYGAKCQFAHGLGELRQANRHPKYKTELCHKFYLQGRCPYGSRCHFIHNPSEDLAAPGHPPVLRQSISFSGLPSGRRTSPPPPGLAGPSLSSSSFSPSSSPPPPGDLPLSPSAFSAAPGTPLARRDPTPVCCPSCRRATPISVWGPLGGLVRTPSVQSLGSDPDEYASSGSSLGGSDSPVFEAGVFAPPQPVAAPRRLPIFNRISVSE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	AIYESLLSLSPDVPV HHHHHHHCCCCCCCC	31.90	16262601
18	Phosphorylation	LSLSPDVPVPSDHGG HCCCCCCCCCCCCCC	39.42	-
21	Phosphorylation	SPDVPVPSDHGGTES CCCCCCCCCCCCCCC	42.34	16262601
27	Phosphorylation	PSDHGGTESSPGWGS CCCCCCCCCCCCCCC	53.12	-
41	Phosphorylation	SSGPWSLSPSDSSPS CCCCCCCCCCCCCCC	19.49	16262601
43	Phosphorylation	GPWSLSPSDSSPSGV CCCCCCCCCCCCCCC	46.91	16262601
46	Phosphorylation	SLSPSDSSPSGVTSR CCCCCCCCCCCCCCC	28.24	16262601
47	Phosphorylation	LSPSDSSPSGVTSRL CCCCCCCCCCCCCCC	38.77	-
48	Phosphorylation	SPSDSSPSGVTSRLP CCCCCCCCCCCCCCC	48.09	16262601
49	Phosphorylation	PSDSSPSGVTSRLPG CCCCCCCCCCCCCCC	30.06	-
52	Phosphorylation	SSPSGVTSRLPGRST CCCCCCCCCCCCCCC	29.43	14688255
54	Phosphorylation	PSGVTSRLPGRSTSL CCCCCCCCCCCCCCE	5.44	-
58	Phosphorylation	TSRLPGRSTSLVEGR CCCCCCCCCCEECCC	28.41	26657352
59	Phosphorylation	SRLPGRSTSLVEGRS CCCCCCCCCEECCCC	25.39	26699800
60	Phosphorylation	RLPGRSTSLVEGRSC CCCCCCCCEECCCCC	31.50	23911959
66	Phosphorylation	TSLVEGRSCGWVPPP CCEECCCCCCCCCCC	28.04	16262601
72	Phosphorylation	RSCGWVPPPPGFAPL CCCCCCCCCCCCCCC	37.79	16262601
82	Methylation	GFAPLAPRLGPELSP CCCCCCCCCCCCCCC	46.82	115384921
88	Methylation	PRLGPELSPSPTSPT CCCCCCCCCCCCCCC	22.97	-
88	Phosphorylation	PRLGPELSPSPTSPT CCCCCCCCCCCCCCC	22.97	28355574
90	Phosphorylation	LGPELSPSPTSPTAT CCCCCCCCCCCCCCC	37.12	29255136
92	Phosphorylation	PELSPSPTSPTATST CCCCCCCCCCCCCCC	52.23	29255136
93	Phosphorylation	ELSPSPTSPTATSTT CCCCCCCCCCCCCCC	24.52	29255136
94	Phosphorylation	LSPSPTSPTATSTTP CCCCCCCCCCCCCCC	28.64	16262601
95	Phosphorylation	SPSPTSPTATSTTPS CCCCCCCCCCCCCCH	42.19	29255136
96	Phosphorylation	PSPTSPTATSTTPSR CCCCCCCCCCCCCHH	11.70	-
97	Phosphorylation	SPTSPTATSTTPSRY CCCCCCCCCCCCHHH	29.14	29255136
98	Phosphorylation	PTSPTATSTTPSRYK CCCCCCCCCCCHHHH	28.02	30108239
99	Phosphorylation	TSPTATSTTPSRYKT CCCCCCCCCCHHHHH	38.07	30576142
100	Phosphorylation	SPTATSTTPSRYKTE CCCCCCCCCHHHHHH	21.02	30108239
101	Phosphorylation	PTATSTTPSRYKTEL CCCCCCCCHHHHHHH	19.52	-
102	Phosphorylation	TATSTTPSRYKTELC CCCCCCCHHHHHHHE	46.26	30108239
105	Acetylation	STTPSRYKTELCRTF CCCCHHHHHHHEECC	34.12	27452117
105	Phosphorylation	STTPSRYKTELCRTF CCCCHHHHHHHEECC	34.12	-
105	Ubiquitination	STTPSRYKTELCRTF CCCCHHHHHHHEECC	34.12	-
106	Phosphorylation	TTPSRYKTELCRTFS CCCHHHHHHHEECCC	25.84	16262601
111	Phosphorylation	YKTELCRTFSESGRC HHHHHEECCCCCCCC	30.43	16262601
111	Ubiquitination	YKTELCRTFSESGRC HHHHHEECCCCCCCC	30.43	-
112	Phosphorylation	KTELCRTFSESGRCR HHHHEECCCCCCCCC	3.84	-
113	Phosphorylation	TELCRTFSESGRCRY HHHEECCCCCCCCCH	30.18	24670416
115	Phosphorylation	LCRTFSESGRCRYGA HEECCCCCCCCCHHC	30.27	26699800
117	Phosphorylation	RTFSESGRCRYGAKC ECCCCCCCCCHHCCC	15.83	-
119	Phosphorylation	FSESGRCRYGAKCQF CCCCCCCCHHCCCHH	31.40	-
120	Phosphorylation	SESGRCRYGAKCQFA CCCCCCCHHCCCHHH	25.68	-
123	Ubiquitination	GRCRYGAKCQFAHGL CCCCHHCCCHHHCHH	24.98	-
129	Ubiquitination	AKCQFAHGLGELRQA CCCHHHCHHHHHHHH	31.76	-
149	Ubiquitination	YKTELCHKFYLQGRC CCHHHCHHHHCCCCC	34.41	-
158	Phosphorylation	YLQGRCPYGSRCHFI HCCCCCCCCCCCEEE	31.21	16262601
160	Phosphorylation	QGRCPYGSRCHFIHN CCCCCCCCCCEEECC	26.37	16262601
164	Phosphorylation	PYGSRCHFIHNPSED CCCCCCEEECCCCHH	7.51	-
166	Phosphorylation	GSRCHFIHNPSEDLA CCCCEEECCCCHHCC	38.92	-
169	Phosphorylation	CHFIHNPSEDLAAPG CEEECCCCHHCCCCC	49.40	16262601
175	Phosphorylation	PSEDLAAPGHPPVLR CCHHCCCCCCCCCCC	35.70	16262601
184	Phosphorylation	HPPVLRQSISFSGLP CCCCCCEEECCCCCC	17.48	30266825
186	Phosphorylation	PVLRQSISFSGLPSG CCCCEEECCCCCCCC	20.71	23401153
188	Phosphorylation	LRQSISFSGLPSGRR CCEEECCCCCCCCCC	32.41	30266825
190	Phosphorylation	QSISFSGLPSGRRTS EEECCCCCCCCCCCC	2.71	-
192	Phosphorylation	ISFSGLPSGRRTSPP ECCCCCCCCCCCCCC	50.39	23927012
194	Phosphorylation	FSGLPSGRRTSPPPP CCCCCCCCCCCCCCC	42.94	-
196	Phosphorylation	GLPSGRRTSPPPPGL CCCCCCCCCCCCCCC	44.20	16262601
197	Phosphorylation	LPSGRRTSPPPPGLA CCCCCCCCCCCCCCC	33.33	16262601
202	Phosphorylation	RTSPPPPGLAGPSLS CCCCCCCCCCCCCCC	33.65	-
203	Phosphorylation	TSPPPPGLAGPSLSS CCCCCCCCCCCCCCC	6.50	16262601
207	Phosphorylation	PPGLAGPSLSSSSFS CCCCCCCCCCCCCCC	39.71	16262601
209	Phosphorylation	GLAGPSLSSSSFSPS CCCCCCCCCCCCCCC	32.29	27251275
210	Phosphorylation	LAGPSLSSSSFSPSS CCCCCCCCCCCCCCC	34.98	16262601
211	Phosphorylation	AGPSLSSSSFSPSSS CCCCCCCCCCCCCCC	31.84	27251275
212	Phosphorylation	GPSLSSSSFSPSSSP CCCCCCCCCCCCCCC	31.52	27251275
213	Phosphorylation	PSLSSSSFSPSSSPP CCCCCCCCCCCCCCC	15.64	-
214	Phosphorylation	SLSSSSFSPSSSPPP CCCCCCCCCCCCCCC	26.31	23909892
216	Phosphorylation	SSSSFSPSSSPPPPG CCCCCCCCCCCCCCC	42.10	27251275
217	Phosphorylation	SSSFSPSSSPPPPGD CCCCCCCCCCCCCCC	50.69	16262601
218	Phosphorylation	SSFSPSSSPPPPGDL CCCCCCCCCCCCCCC	45.85	16262601
220	Phosphorylation	FSPSSSPPPPGDLPL CCCCCCCCCCCCCCC	50.06	-
223	Phosphorylation	SSSPPPPGDLPLSPS CCCCCCCCCCCCCHH	55.66	-
224	Phosphorylation	SSPPPPGDLPLSPSA CCCCCCCCCCCCHHH	51.38	16262601
228	Phosphorylation	PPGDLPLSPSAFSAA CCCCCCCCHHHHCCC	18.18	7768935
230	Phosphorylation	GDLPLSPSAFSAAPG CCCCCCHHHHCCCCC	38.27	16262601
233	Phosphorylation	PLSPSAFSAAPGTPL CCCHHHHCCCCCCCC	24.20	16262601
234	Phosphorylation	LSPSAFSAAPGTPLA CCHHHHCCCCCCCCC	15.95	16262601
236	Phosphorylation	PSAFSAAPGTPLARR HHHHCCCCCCCCCCC	47.08	-
238	Phosphorylation	AFSAAPGTPLARRDP HHCCCCCCCCCCCCC	17.67	16262601
239	Phosphorylation	FSAAPGTPLARRDPT HCCCCCCCCCCCCCC	29.91	-
244	Phosphorylation	GTPLARRDPTPVCCP CCCCCCCCCCCCCCC	45.96	-
252	Phosphorylation	PTPVCCPSCRRATPI CCCCCCCCCCCCCCE	13.31	16262601
257	Phosphorylation	CPSCRRATPISVWGP CCCCCCCCCEEEEEC	21.24	21815630
258	Phosphorylation	PSCRRATPISVWGPL CCCCCCCCEEEEECC	18.84	-
260	Phosphorylation	CRRATPISVWGPLGG CCCCCCEEEEECCCC	17.02	28450419
263	Phosphorylation	ATPISVWGPLGGLVR CCCEEEEECCCCCEE	12.85	-
271	Phosphorylation	PLGGLVRTPSVQSLG CCCCCEECCCHHHCC	16.67	16262601
273	Phosphorylation	GGLVRTPSVQSLGSD CCCEECCCHHHCCCC	31.98	16262601
276	Phosphorylation	VRTPSVQSLGSDPDE EECCCHHHCCCCHHH	32.32	16262601
277	Phosphorylation	RTPSVQSLGSDPDEY ECCCHHHCCCCHHHH	4.21	-
279	Phosphorylation	PSVQSLGSDPDEYAS CCHHHCCCCHHHHHH	51.79	16262601
282	Phosphorylation	QSLGSDPDEYASSGS HHCCCCHHHHHHCCC	67.54	16262601
284	Phosphorylation	LGSDPDEYASSGSSL CCCCHHHHHHCCCCC	21.11	16262601
285	Phosphorylation	GSDPDEYASSGSSLG CCCHHHHHHCCCCCC	8.65	-
290	Phosphorylation	EYASSGSSLGGSDSP HHHHCCCCCCCCCCC	34.26	-
294	Phosphorylation	SGSSLGGSDSPVFEA CCCCCCCCCCCCEEC	32.87	16262601
296	Phosphorylation	SSLGGSDSPVFEAGV CCCCCCCCCCEECCC	25.35	16262601
300	Phosphorylation	GSDSPVFEAGVFAPP CCCCCCEECCCCCCC	44.76	-
302	Phosphorylation	DSPVFEAGVFAPPQP CCCCEECCCCCCCCC	14.10	16262601
323	Phosphorylation	LPIFNRISVSE---- CCCCCCCCCCC----	19.16	23644599
325	Phosphorylation	IFNRISVSE------ CCCCCCCCC------	30.69	23090842
329	Phosphorylation	ISVSE---------- CCCCC----------		-
331	Phosphorylation	VSE------------ CCC------------		-

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
60	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
186	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
228	S	Phosphorylation	Kinase	MAPK1	P28482	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
60	S	Phosphorylation	26926077
Phosphorylated by MAPKAPK2 at Ser-60 and Ser-186; phosphorylation increases its stability and cytoplasmic localization, promotes binding to 14-3-3 adapter proteins and inhibits the recruitment of cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase complexes to the mRNA decay machinery, thereby inhibiting ZFP36-induced ARE-containing mRNA deadenylation and decay processes.
60	S	Phosphorylation	26926077
Phosphorylation at Ser-60 may participate in the PKM-mediated degradation of ZFP36 in a p38 MAPK-dependent manner.
66	S	Phosphorylation	16262601
Phosphorylated at Ser-66 and Ser-93; these phosphorylations increase in a SH3KBP1-dependent manner.
93	S	Phosphorylation	20221403
Phosphorylated at Ser-66 and Ser-93; these phosphorylations increase in a SH3KBP1-dependent manner.
186	S	Phosphorylation	16262601
Dephosphorylated by serine/threonine phosphatase 2A at Ser-186 (By similarity).
186	S	Phosphorylation	16262601
Phosphorylated by MAPKAPK2 at Ser-60 and Ser-186; phosphorylation increases its stability and cytoplasmic localization, promotes binding to 14-3-3 adapter proteins and inhibits the recruitment of cytoplasmic CCR4-NOT and PAN2-PAN3 deadenylase complexes to the mRNA decay machinery, thereby inhibiting ZFP36-induced ARE-containing mRNA deadenylation and decay processes.

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 TTP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CC85B_HUMAN	CCDC85B	physical	16189514
NU214_HUMAN	NUP214	physical	14766228
1433F_HUMAN	YWHAH	physical	11886850
HDAC1_HUMAN	HDAC1	physical	19738286
HDAC3_HUMAN	HDAC3	physical	19738286
HDAC7_HUMAN	HDAC7	physical	19738286
SH3K1_HUMAN	SH3KBP1	physical	20221403
NUCL_HUMAN	NCL	physical	20221403
PABP1_HUMAN	PABPC1	physical	20221403
HSP74_HUMAN	HSPA4	physical	20221403
M3K4_HUMAN	MAP3K4	physical	20221403
LN28A_HUMAN	LIN28A	physical	22210895
A4_HUMAN	APP	physical	21832049
DCP2_HUMAN	DCP2	physical	16364915
EDC3_HUMAN	EDC3	physical	16364915
EDC4_HUMAN	EDC4	physical	16364915
DCP1A_HUMAN	DCP1A	physical	16364915
1433T_HUMAN	YWHAQ	physical	15014438
TNFA_HUMAN	TNF	physical	15014438
TRAF2_HUMAN	TRAF2	physical	25056949
PP2AA_HUMAN	PPP2CA	physical	17170118
1433B_HUMAN	YWHAB	physical	17170118
PRR5L_HUMAN	PRR5L	physical	21964062
DNJB1_HUMAN	DNAJB1	physical	21964062
DCP1B_HUMAN	DCP1B	physical	21964062
XRN1_HUMAN	XRN1	physical	21964062
DHX36_HUMAN	DHX36	physical	21964062
CCL3_HUMAN	CCL3	physical	21784977
DUS2_HUMAN	DUSP2	physical	21784977
ZEB2_HUMAN	ZEB2	physical	21784977
ROA2_HUMAN	HNRNPA2B1	physical	21784977
TNFA_HUMAN	TNF	physical	21784977
COMD6_HUMAN	COMMD6	physical	21784977
MED30_HUMAN	MED30	physical	21784977
KLHL2_HUMAN	KLHL2	physical	21784977
VATE1_HUMAN	ATP6V1E1	physical	21784977
PP2AB_HUMAN	PPP2CB	physical	21784977
METL9_HUMAN	METTL9	physical	21784977
SPY2_HUMAN	SPRY2	physical	21784977
STK40_HUMAN	STK40	physical	21784977
RGS16_HUMAN	RGS16	physical	21784977
TANK_HUMAN	TANK	physical	21784977
TFR1_HUMAN	TFRC	physical	23102618
1433B_HUMAN	YWHAB	physical	14688255
CNOT6_HUMAN	CNOT6	physical	21078877
CNO6L_HUMAN	CNOT6L	physical	21078877
CNOT8_HUMAN	CNOT8	physical	21078877
CNOT7_HUMAN	CNOT7	physical	21078877
PAN2_HUMAN	PAN2	physical	21078877

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 TTP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-186, AND MASSSPECTROMETRY.	18669648 [Abstract]
"MK2-induced tristetraprolin:14-3-3 complexes prevent stress granuleassociation and ARE-mRNA decay."; Stoecklin G., Stubbs T., Kedersha N., Wax S., Rigby W.F.,Blackwell T.K., Anderson P.; EMBO J. 23:1313-1324(2004). Cited for: PHOSPHORYLATION AT SER-60 AND SER-186 BY MAPKAPK2, SUBCELLULARLOCATION, RNA-BINDING, FUNCTION, AND MUTAGENESIS OF SER-60 ANDSER-186.	15014438 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92, AND MASSSPECTROMETRY.	19369195 [Abstract]

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