dbPTM

TISB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TISB_HUMAN
UniProt AC	Q07352
Protein Name	mRNA decay activator protein ZFP36L1 {ECO:0000305}
Gene Name	ZFP36L1 {ECO:0000312\|HGNC:HGNC:1107}
Organism	Homo sapiens (Human).
Sequence Length	338
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasmic granule . Cytoplasm, P-body . Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner (By similarity). Component of cytoplasmic stress granules (PubMed:15967811). Localizes in processing bodies
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: 12198173]
Protein Sequence	MTTTLVSATIFDLSEVLCKGNKMLNYSAPSAGGCLLDRKAVGTPAGGGFPRRHSVTLPSSKFHQNQLLSSLKGEPAPALSSRDSRFRDRSFSEGGERLLPTQKQPGGGQVNSSRYKTELCRPFEENGACKYGDKCQFAHGIHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRALAGARDLSADRPRLQHSFSFAGFPSAAATAAATGLLDSPTSITPPPILSADDLLGSPTLPDGTNNPFAFSSQELASLFAPSMGLPGGGSPTTFLFRPMSESPHMFDSPPSPQDSLSDQEGYLSSSSSSHSGSDSPTLDNSRRLPIFSRLSISDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26	Phosphorylation	KGNKMLNYSAPSAGG HCCCCCCCCCCCCCC	11.40	27642862
27	Phosphorylation	GNKMLNYSAPSAGGC CCCCCCCCCCCCCCC	32.41	25159151
30	Phosphorylation	MLNYSAPSAGGCLLD CCCCCCCCCCCCEEC	38.98	-
43	Phosphorylation	LDRKAVGTPAGGGFP ECCCCCCCCCCCCCC	11.90	28985074
54	Phosphorylation	GGFPRRHSVTLPSSK CCCCCCCCEECCCCH	18.26	29255136
56	Phosphorylation	FPRRHSVTLPSSKFH CCCCCCEECCCCHHH	35.65	30266825
59	Phosphorylation	RHSVTLPSSKFHQNQ CCCEECCCCHHHHHH	49.63	23403867
60	Phosphorylation	HSVTLPSSKFHQNQL CCEECCCCHHHHHHH	37.08	23403867
61	Ubiquitination	SVTLPSSKFHQNQLL CEECCCCHHHHHHHH	51.72	-
69	Phosphorylation	FHQNQLLSSLKGEPA HHHHHHHHHCCCCCC	42.06	25159151
70	Phosphorylation	HQNQLLSSLKGEPAP HHHHHHHHCCCCCCC	33.79	26434776
72	Ubiquitination	NQLLSSLKGEPAPAL HHHHHHCCCCCCCCC	64.28	21906983
72	Sumoylation	NQLLSSLKGEPAPAL HHHHHHCCCCCCCCC	64.28	-
80	Phosphorylation	GEPAPALSSRDSRFR CCCCCCCCCCCHHHC	25.98	24732914
81	Phosphorylation	EPAPALSSRDSRFRD CCCCCCCCCCHHHCC	40.74	21406692
84	Phosphorylation	PALSSRDSRFRDRSF CCCCCCCHHHCCCCC	32.01	28555341
90	Phosphorylation	DSRFRDRSFSEGGER CHHHCCCCCCCCCCC	37.10	15538381
91	Ubiquitination	SRFRDRSFSEGGERL HHHCCCCCCCCCCCC	8.86	-
92	Phosphorylation	RFRDRSFSEGGERLL HHCCCCCCCCCCCCC	36.26	23401153
96	Phosphorylation	RSFSEGGERLLPTQK CCCCCCCCCCCCCCC	51.52	27251275
101	Phosphorylation	GGERLLPTQKQPGGG CCCCCCCCCCCCCCC	48.66	22199227
103	Ubiquitination	ERLLPTQKQPGGGQV CCCCCCCCCCCCCCC	62.02	21906983
103	Acetylation	ERLLPTQKQPGGGQV CCCCCCCCCCCCCCC	62.02	7354879
108	Ubiquitination	TQKQPGGGQVNSSRY CCCCCCCCCCCCCHH	33.89	-
112	Phosphorylation	PGGGQVNSSRYKTEL CCCCCCCCCHHCCEE	19.82	-
115	Phosphorylation	GQVNSSRYKTELCRP CCCCCCHHCCEECCC	24.98	19658100
116	Ubiquitination	QVNSSRYKTELCRPF CCCCCHHCCEECCCC	34.12	-
123	Phosphorylation	KTELCRPFEENGACK CCEECCCCCCCCCCC	10.72	20166139
125	Phosphorylation	ELCRPFEENGACKYG EECCCCCCCCCCCCC	62.43	-
130	Ubiquitination	FEENGACKYGDKCQF CCCCCCCCCCCCCHH	52.30	-
134	Ubiquitination	GACKYGDKCQFAHGI CCCCCCCCCHHHCCH	26.10	-
139	Phosphorylation	GDKCQFAHGIHELRS CCCCHHHCCHHHHHH	36.71	27251275
141	Sumoylation	KCQFAHGIHELRSLT CCHHHCCHHHHHHHH	1.31	-
141	Ubiquitination	KCQFAHGIHELRSLT CCHHHCCHHHHHHHH	1.31	-
146	Phosphorylation	HGIHELRSLTRHPKY CCHHHHHHHHCCHHH	46.87	27251275
148	Phosphorylation	IHELRSLTRHPKYKT HHHHHHHHCCHHHHH	28.33	27251275
154	Ubiquitination	LTRHPKYKTELCRTF HHCCHHHHHHHHHHH	41.47	-
159	Phosphorylation	KYKTELCRTFHTIGF HHHHHHHHHHCEECC	53.72	15538381
160	Phosphorylation	YKTELCRTFHTIGFC HHHHHHHHHCEECCC	20.83	-
161	Phosphorylation	KTELCRTFHTIGFCP HHHHHHHHCEECCCC	2.18	18326031
163	Phosphorylation	ELCRTFHTIGFCPYG HHHHHHCEECCCCCC	20.71	-
169	Phosphorylation	HTIGFCPYGPRCHFI CEECCCCCCCCCEEE	40.73	28152594
172	Methylation	GFCPYGPRCHFIHNA CCCCCCCCCEEECCH	23.37	-
172	Ubiquitination	GFCPYGPRCHFIHNA CCCCCCCCCEEECCH	23.37	-
184	Phosphorylation	HNAEERRALAGARDL CCHHHHHHHHCCCCC	14.16	-
185	Ubiquitination	NAEERRALAGARDLS CHHHHHHHHCCCCCC	4.24	-
192	Phosphorylation	LAGARDLSADRPRLQ HHCCCCCCCCCCCCE	32.20	30266825
199	Ubiquitination	SADRPRLQHSFSFAG CCCCCCCEECCCCCC	31.30	-
201	Phosphorylation	DRPRLQHSFSFAGFP CCCCCEECCCCCCCH	15.04	-
203	Ubiquitination	PRLQHSFSFAGFPSA CCCEECCCCCCCHHH	19.73	-
203	Phosphorylation	PRLQHSFSFAGFPSA CCCEECCCCCCCHHH	19.73	17030608
215	Phosphorylation	PSAAATAAATGLLDS HHHHHHHHHHCCCCC	10.95	27251275
223	Ubiquitination	ATGLLDSPTSITPPP HHCCCCCCCCCCCCC	29.81	-
241	Methylation	ADDLLGSPTLPDGTN HHHHCCCCCCCCCCC	35.83	-
261	Phosphorylation	SSQELASLFAPSMGL CHHHHHHHHCHHHCC	3.36	27251275
272	Phosphorylation	SMGLPGGGSPTTFLF HHCCCCCCCCCEEEE	36.05	18326031
283	Phosphorylation	TFLFRPMSESPHMFD EEEEEECCCCCCCCC	37.29	-
314	Phosphorylation	SSSSSSHSGSDSPTL CCCCCCCCCCCCCCC	41.77	24275569
316	Phosphorylation	SSSSHSGSDSPTLDN CCCCCCCCCCCCCCC	37.62	24275569
318	Phosphorylation	SSHSGSDSPTLDNSR CCCCCCCCCCCCCCC	22.83	24275569
331	Phosphorylation	SRRLPIFSRLSISDD CCCCCCCEEEECCCC	32.79	23927012
334	Phosphorylation	LPIFSRLSISDD--- CCCCEEEECCCC---	20.95	23927012
336	Phosphorylation	IFSRLSISDD----- CCEEEECCCC-----	32.14	30266825
352	Phosphorylation	--------------------- ---------------------		-
383	Phosphorylation	---------------------------------------------------- ----------------------------------------------------		-
385	Phosphorylation	------------------------------------------------------ ------------------------------------------------------		-
387	Phosphorylation	-------------------------------------------------------- --------------------------------------------------------		-
400	Phosphorylation	--------------------------------------------------------------------- ---------------------------------------------------------------------		-
403	Phosphorylation	------------------------------------------------------------------------ ------------------------------------------------------------------------		25106868
405	Phosphorylation	-------------------------------------------------------------------------- --------------------------------------------------------------------------		17081983

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
54	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
54	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
90	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
92	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
92	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
92	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
92	S	Phosphorylation	Kinase	PKB_GROUP	-	PhosphoELM
203	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
203	S	Phosphorylation	Kinase	MAPKAPK2	P49137	Uniprot
334	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
334	S	Phosphorylation	Kinase	RPS6KA1	Q15418	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
54	S	Phosphorylation	18326031
MAPKAPK2-mediated phosphorylations at Ser-54, Ser-92 and Ser-203 do not impair ARE-containing RNA-binding.
54	S	Phosphorylation	18326031
Phosphorylated at Ser-54, Ser-92 and Ser-203 by MAPKAPK2; these phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization in a protein kinase AKT1-independent manner.
90	S	Phosphorylation	15538381
Ubiquitination leads to proteasomal degradation, a process inhibited by phosphorylations at Ser-90, Ser-92 and Ser-203.
90	S	ubiquitylation	15538381
Ubiquitination leads to proteasomal degradation, a process inhibited by phosphorylations at Ser-90, Ser-92 and Ser-203.
92	S	Phosphorylation	15538381
AKT1-mediated phosphorylation at Ser-92 does not impair ARE-containing RNA-binding.
92	S	Phosphorylation	15538381
MAPKAPK2-mediated phosphorylations at Ser-54, Ser-92 and Ser-203 do not impair ARE-containing RNA-binding.
92	S	Phosphorylation	15538381
Phosphorylated at Ser-54, Ser-92 and Ser-203 by MAPKAPK2; these phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization in a protein kinase AKT1-independent manner.
92	S	Phosphorylation	15538381
Phosphorylated by protein kinase AKT1 at Ser-92 and Ser-203 in response to insulin; these phosphorylations stabilize ZFP36L1, increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization.
92	S	Phosphorylation	15538381
Ubiquitination leads to proteasomal degradation, a process inhibited by phosphorylations at Ser-90, Ser-92 and Ser-203.
92	S	ubiquitylation	15538381
Ubiquitination leads to proteasomal degradation, a process inhibited by phosphorylations at Ser-90, Ser-92 and Ser-203.
203	S	Phosphorylation	17030608
MAPKAPK2-mediated phosphorylations at Ser-54, Ser-92 and Ser-203 do not impair ARE-containing RNA-binding.
203	S	Phosphorylation	17030608
Phosphorylated at Ser-54, Ser-92 and Ser-203 by MAPKAPK2; these phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization in a protein kinase AKT1-independent manner.
203	S	Phosphorylation	17030608
Phosphorylated by protein kinase AKT1 at Ser-92 and Ser-203 in response to insulin; these phosphorylations stabilize ZFP36L1, increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization.
203	S	Phosphorylation	17030608
Ubiquitination leads to proteasomal degradation, a process inhibited by phosphorylations at Ser-90, Ser-92 and Ser-203.
203	S	ubiquitylation	17030608
Ubiquitination leads to proteasomal degradation, a process inhibited by phosphorylations at Ser-90, Ser-92 and Ser-203.
334	S	Phosphorylation	25106868
Phosphorylated by RPS6KA1 at Ser-334 upon phorbol 12-myristate 13-acetate (PMA) treatment; this phosphorylation results in dissociation of the CCR4-NOT deadenylase complex and induces p38 MAPK-mediated stabilization of the low-density lipoprotein receptor LDLR mRNA.

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 TISB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MK14_HUMAN	MAPK14	physical	16189514
1433B_HUMAN	YWHAB	physical	17030608
CNOT6_HUMAN	CNOT6	physical	18326031
DCP2_HUMAN	DCP2	physical	18326031
EXOS2_HUMAN	EXOSC2	physical	18326031

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 TISB_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-334, AND MASSSPECTROMETRY.	19413330 [Abstract]

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