dbPTM

TTP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTP_MOUSE
UniProt AC	P22893
Protein Name	mRNA decay activator protein ZFP36 {ECO:0000305}
Gene Name	Zfp36 {ECO:0000303\|PubMed:7559666, ECO:0000312\|MGI:MGI:99180}
Organism	Mus musculus (Mouse).
Sequence Length	319
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasmic granule . Cytoplasm, P-body . Shuttles between nucleus and cytoplasm in a CRM1-dependent manner (PubMed:11796723, PubMed:11886850). Localized predominantly in the cytoplasm in a p38 MAPK- and YWHAB-dependent manner (
Protein Description	Zinc-finger RNA-binding protein that destabilizes numerous 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: 10330172]
Protein Sequence	MDLSAIYESLQSMSHDLSSDHGGTESLGGLWNINSDSIPSGVTSRLTGRSTSLVEGRSCGWVPPPPGFAPLAPRPGPELSPSPTSPTATPTTSSRYKTELCRTYSESGRCRYGAKCQFAHGLGELRQANRHPKYKTELCHKFYLQGRCPYGSRCHFIHNPTEDLALPGQPHVLRQSISFSGLPSGRRSSPPPPGFSGPSLSSCSFSPSSSPPPPGDLPLSPSAFSAAPGTPVTRRDPNQACCPSCRRSTTPSTIWGPLGGLARSPSAHSLGSDPDDYASSGSSLGGSDSPVFEAGVFGPPQTPAPPRRLPIFNRISVSE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
50	Phosphorylation	TSRLTGRSTSLVEGR HHHCCCCCCCCCCCC	24.56	26745281
51	Phosphorylation	SRLTGRSTSLVEGRS HHCCCCCCCCCCCCC	25.39	26745281
52	Phosphorylation	RLTGRSTSLVEGRSC HCCCCCCCCCCCCCC	31.50	26824392
58	Phosphorylation	TSLVEGRSCGWVPPP CCCCCCCCCCCCCCC	28.04	22817900
80	Phosphorylation	PRPGPELSPSPTSPT CCCCCCCCCCCCCCC	22.97	22817900
82	Phosphorylation	PGPELSPSPTSPTAT CCCCCCCCCCCCCCC	37.12	26824392
84	Phosphorylation	PELSPSPTSPTATPT CCCCCCCCCCCCCCC	52.23	26824392
85	Phosphorylation	ELSPSPTSPTATPTT CCCCCCCCCCCCCCC	24.52	26824392
87	Phosphorylation	SPSPTSPTATPTTSS CCCCCCCCCCCCCCH	42.82	19060867
89	Phosphorylation	SPTSPTATPTTSSRY CCCCCCCCCCCCHHH	24.52	29472430
91	Phosphorylation	TSPTATPTTSSRYKT CCCCCCCCCCHHHHH	34.65	25777480
92	Phosphorylation	SPTATPTTSSRYKTE CCCCCCCCCHHHHHH	26.38	25777480
93	Phosphorylation	PTATPTTSSRYKTEL CCCCCCCCHHHHHHE	18.46	25777480
94	Phosphorylation	TATPTTSSRYKTELC CCCCCCCHHHHHHEE	37.22	25777480
105	Phosphorylation	TELCRTYSESGRCRY HHEEECCCCCCCCCH	25.36	22817900
107	Phosphorylation	LCRTYSESGRCRYGA EEECCCCCCCCCHHC	26.12	28285833
176	Phosphorylation	QPHVLRQSISFSGLP CCCEEEEEEEECCCC	17.48	22942356
178	Phosphorylation	HVLRQSISFSGLPSG CEEEEEEEECCCCCC	20.71	26824392
180	Phosphorylation	LRQSISFSGLPSGRR EEEEEEECCCCCCCC	32.41	22942356
184	Phosphorylation	ISFSGLPSGRRSSPP EEECCCCCCCCCCCC	50.39	28833060
188	Phosphorylation	GLPSGRRSSPPPPGF CCCCCCCCCCCCCCC	45.92	25293948
189	Phosphorylation	LPSGRRSSPPPPGFS CCCCCCCCCCCCCCC	39.35	22942356
196	Phosphorylation	SPPPPGFSGPSLSSC CCCCCCCCCCCCCCC	56.56	25293948
199	Phosphorylation	PPGFSGPSLSSCSFS CCCCCCCCCCCCCCC	44.39	25293948
201	Phosphorylation	GFSGPSLSSCSFSPS CCCCCCCCCCCCCCC	33.37	25293948
202	Phosphorylation	FSGPSLSSCSFSPSS CCCCCCCCCCCCCCC	21.05	25293948
204	Phosphorylation	GPSLSSCSFSPSSSP CCCCCCCCCCCCCCC	30.61	25293948
206	Phosphorylation	SLSSCSFSPSSSPPP CCCCCCCCCCCCCCC	13.95	25293948
208	Phosphorylation	SSCSFSPSSSPPPPG CCCCCCCCCCCCCCC	42.10	25293948
209	Phosphorylation	SCSFSPSSSPPPPGD CCCCCCCCCCCCCCC	50.69	25293948
210	Phosphorylation	CSFSPSSSPPPPGDL CCCCCCCCCCCCCCC	45.85	25293948
220	Phosphorylation	PPGDLPLSPSAFSAA CCCCCCCCHHHHHCC	18.18	7768935
222	Phosphorylation	GDLPLSPSAFSAAPG CCCCCCHHHHHCCCC	38.27	25293948
225	Phosphorylation	PLSPSAFSAAPGTPV CCCHHHHHCCCCCCC	24.20	25293948
248	Phosphorylation	CCPSCRRSTTPSTIW CCCCCCCCCCCCCCC	19.79	23984901
249	Phosphorylation	CPSCRRSTTPSTIWG CCCCCCCCCCCCCCC	40.70	22817900
250	Phosphorylation	PSCRRSTTPSTIWGP CCCCCCCCCCCCCCC	19.25	27180971
252	Phosphorylation	CRRSTTPSTIWGPLG CCCCCCCCCCCCCCC	30.36	23984901
253	Phosphorylation	RRSTTPSTIWGPLGG CCCCCCCCCCCCCCC	23.19	22942356
264	Phosphorylation	PLGGLARSPSAHSLG CCCCCCCCCCHHHCC	20.01	22817900
266	Phosphorylation	GGLARSPSAHSLGSD CCCCCCCCHHHCCCC	39.60	22817900
269	Phosphorylation	ARSPSAHSLGSDPDD CCCCCHHHCCCCHHH	33.86	21183079
272	Phosphorylation	PSAHSLGSDPDDYAS CCHHHCCCCHHHHHC	51.79	21183079
277	Phosphorylation	LGSDPDDYASSGSSL CCCCHHHHHCCCCCC	18.76	-
289	Phosphorylation	SSLGGSDSPVFEAGV CCCCCCCCCCEECCC	25.35	22942356
316	Phosphorylation	LPIFNRISVSE---- CCCCCCEECCC----	19.16	26824392
318	Phosphorylation	IFNRISVSE------ CCCCEECCC------	30.69	22942356

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
52	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
52	S	Phosphorylation	Kinase	MAPKAPK3	Q3UMW7	PSP
52	S	Phosphorylation	Kinase	MAPK2	P49138	PhosphoELM
58	S	Phosphorylation	Kinase	MAPKAPK2	P49138	PSP
80	S	Phosphorylation	Kinase	MAPKAPK2	P49138	GPS
82	S	Phosphorylation	Kinase	MAPKAPK2	P49138	GPS
85	S	Phosphorylation	Kinase	MAPKAPK2	P49138	GPS
105	S	Phosphorylation	Kinase	MAPKAPK2	P49138	PSP
176	S	Phosphorylation	Kinase	MAPKAPK2	P49138	PSP
178	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
178	S	Phosphorylation	Kinase	MAPKAPK3	Q3UMW7	PSP
178	S	Phosphorylation	Kinase	MAPK2	P49138	PhosphoELM
220	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
220	S	Phosphorylation	Kinase	MAPK1	P63085	Uniprot
220	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
220	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
249	T	Phosphorylation	Kinase	MAPKAPK2	P49138	PSP
250	T	Phosphorylation	Kinase	MAPK2	P49138	PhosphoELM
264	S	Phosphorylation	Kinase	MAPKAPK2	P49138	PSP
266	S	Phosphorylation	Kinase	MAPKAPK2	P49138	PSP
316	S	Phosphorylation	Kinase	MAPK2	P49138	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
52	S	Phosphorylation	15014438
Phosphorylated by MAPKAPK2 at Ser-52 and Ser-178; 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.
52	S	Phosphorylation	15014438
Phosphorylation at Ser-52 may participate in the PKM-mediated degradation of ZFP36 in a p38 MAPK-dependent manner (By similarity).
58	S	Phosphorylation	7768935
Phosphorylated at Ser-58 and Ser-85; these phosphorylations increase in a SH3KBP1-dependent manner (By similarity).
85	S	Phosphorylation	14688255
Phosphorylated at Ser-58 and Ser-85; these phosphorylations increase in a SH3KBP1-dependent manner (By similarity).
178	S	Phosphorylation	11886850
Dephosphorylated by serine/threonine phosphatase 2A at Ser-178.
178	S	Phosphorylation	11886850
Phosphorylated by MAPKAPK2 at Ser-52 and Ser-178; 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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433B_MOUSE	Ywhab	physical	16702957
TNFA_MOUSE	Tnf	physical	22665488
CNOT7_HUMAN	CNOT7	physical	20595389
CNOT8_HUMAN	CNOT8	physical	20595389
PABP1_HUMAN	PABPC1	physical	20595389

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TTP_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sitesincluding Ser178, a site required for 14-3-3 binding."; Chrestensen C.A., Schroeder M.J., Shabanowitz J., Hunt D.F.,Pelo J.W., Worthington M.T., Sturgill T.W.; J. Biol. Chem. 279:10176-10184(2004). Cited for: FUNCTION, RNA-BINDING, PHOSPHORYLATION AT SER-52; SER-80; SER-82;SER-85; SER-178; THR-249 AND SER-316, AND MASS SPECTROMETRY.	14688255 [Abstract]
"Phosphorylation of tristetraprolin, a potential zinc fingertranscription factor, by mitogen stimulation in intact cells and bymitogen-activated protein kinase in vitro."; Taylor G.A., Thompson M.J., Lai W.S., Blackshear P.J.; J. Biol. Chem. 270:13341-13347(1995). Cited for: PHOSPHORYLATION AT SER-220.	7768935 [Abstract]

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