dbPTM

PABP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PABP1_MOUSE
UniProt AC	P29341
Protein Name	Polyadenylate-binding protein 1
Gene Name	Pabpc1
Organism	Mus musculus (Mouse).
Sequence Length	636
Subcellular Localization	Cytoplasm . Nucleus . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus (By similarity).
Protein Description	Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (By similarity). By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (By similarity)..
Protein Sequence	MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKELFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPSLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNPSAPSY -------CCCCCCCC	17.54	-
28	Phosphorylation	DVTEAMLYEKFSPAG CCHHHHHHHHCCCCC	12.18	18563927
39	Phosphorylation	SPAGPILSIRVCRDM CCCCCEEEEEEEHHH	14.74	22006019
51	Phosphorylation	RDMITRRSLGYAYVN HHHHHHCCCEEEEEE	23.90	26643407
54	Phosphorylation	ITRRSLGYAYVNFQQ HHHCCCEEEEEEECC	10.47	23984901
56	Phosphorylation	RRSLGYAYVNFQQPA HCCCEEEEEEECCCC	6.35	23984901
78	Acetylation	TMNFDVIKGKPVRIM HCCCEEECCEEEEEE	61.81	23864654
78	Malonylation	TMNFDVIKGKPVRIM HCCCEEECCEEEEEE	61.81	26320211
78	Ubiquitination	TMNFDVIKGKPVRIM HCCCEEECCEEEEEE	61.81	27667366
80	Acetylation	NFDVIKGKPVRIMWS CCEEECCEEEEEEEE	35.02	23864654
80	Ubiquitination	NFDVIKGKPVRIMWS CCEEECCEEEEEEEE	35.02	-
87	Phosphorylation	KPVRIMWSQRDPSLR EEEEEEEECCCHHHH	9.65	26060331
92	Phosphorylation	MWSQRDPSLRKSGVG EEECCCHHHHHCCCC	45.13	26060331
95	Ubiquitination	QRDPSLRKSGVGNIF CCCHHHHHCCCCCEE	57.78	22790023
96	Phosphorylation	RDPSLRKSGVGNIFI CCHHHHHCCCCCEEE	32.07	23684622
104	Acetylation	GVGNIFIKNLDKSID CCCCEEECCCCHHCC	40.48	23236377
104	Malonylation	GVGNIFIKNLDKSID CCCCEEECCCCHHCC	40.48	26320211
104	Ubiquitination	GVGNIFIKNLDKSID CCCCEEECCCCHHCC	40.48	27667366
108	Malonylation	IFIKNLDKSIDNKAL EEECCCCHHCCCHHH	53.10	26320211
108	Ubiquitination	IFIKNLDKSIDNKAL EEECCCCHHCCCHHH	53.10	27667366
109	Phosphorylation	FIKNLDKSIDNKALY EECCCCHHCCCHHHH	34.54	27681418
116	Phosphorylation	SIDNKALYDTFSAFG HCCCHHHHHHHHHHC	20.14	26745281
118	Phosphorylation	DNKALYDTFSAFGNI CCHHHHHHHHHHCCC	13.11	25367039
128	Glutathionylation	AFGNILSCKVVCDEN HHCCCCEEEEEECCC	3.30	24333276
129	Ubiquitination	FGNILSCKVVCDENG HCCCCEEEEEECCCC	34.03	-
132	Glutathionylation	ILSCKVVCDENGSKG CCEEEEEECCCCCEE	6.43	24333276
138	Ubiquitination	VCDENGSKGYGFVHF EECCCCCEEEEEEEE	58.51	22790023
157	Ubiquitination	AAERAIEKMNGMLLN HHHHHHHHHHCCCCC	31.39	22790023
167	Ubiquitination	GMLLNDRKVFVGRFK CCCCCCCEEEEECCC	42.77	27667366
188	Malonylation	AELGARAKEFTNVYI HHHHHHHHHHHCEEE	48.05	26320211
188	Ubiquitination	AELGARAKEFTNVYI HHHHHHHHHHHCEEE	48.05	-
194	Phosphorylation	AKEFTNVYIKNFGED HHHHHCEEECCCCCC	14.30	29514104
196	Ubiquitination	EFTNVYIKNFGEDMD HHHCEEECCCCCCCC	28.65	22790023
208	Acetylation	DMDDERLKELFGKFG CCCHHHHHHHHHHHC	59.60	23954790
213	Acetylation	RLKELFGKFGPALSV HHHHHHHHHCCEEEE	39.55	23806337
213	Ubiquitination	RLKELFGKFGPALSV HHHHHHHHHCCEEEE	39.55	22790023
219	Phosphorylation	GKFGPALSVKVMTDE HHHCCEEEEEEEECC	23.23	21454597
227	Phosphorylation	VKVMTDESGKSKGFG EEEEECCCCCCCCEE	55.09	21454597
229	Acetylation	VMTDESGKSKGFGFV EEECCCCCCCCEEEE	59.27	7612969
229	Ubiquitination	VMTDESGKSKGFGFV EEECCCCCCCCEEEE	59.27	-
230	Phosphorylation	MTDESGKSKGFGFVS EECCCCCCCCEEEEE	41.35	21454597
231	Ubiquitination	TDESGKSKGFGFVSF ECCCCCCCCEEEEEE	62.84	22790023
237	Phosphorylation	SKGFGFVSFERHEDA CCCEEEEEEEEHHHH	21.09	29514104
246	Ubiquitination	ERHEDAQKAVDEMNG EEHHHHHHHHHHHCC	52.69	-
254	Acetylation	AVDEMNGKELNGKQI HHHHHCCEECCCEEE	54.76	23954790
259	Ubiquitination	NGKELNGKQIYVGRA CCEECCCEEEEECCH	32.23	22790023
262	Phosphorylation	ELNGKQIYVGRAQKK ECCCEEEEECCHHHH	8.38	25367039
277	Ubiquitination	VERQTELKRKFEQMK HHHHHHHHHHHHHHH	47.51	27667366
279	Ubiquitination	RQTELKRKFEQMKQD HHHHHHHHHHHHHHH	52.22	27667366
284	Ubiquitination	KRKFEQMKQDRITRY HHHHHHHHHHHHHHH	49.06	22790023
291	Phosphorylation	KQDRITRYQGVNLYV HHHHHHHHHCCEEEE	10.85	29514104
297	Phosphorylation	RYQGVNLYVKNLDDG HHHCCEEEEEECCCC	12.27	-
299	Acetylation	QGVNLYVKNLDDGID HCCEEEEEECCCCCC	37.93	23236377
299	Methylation	QGVNLYVKNLDDGID HCCEEEEEECCCCCC	37.93	-
299	Ubiquitination	QGVNLYVKNLDDGID HCCEEEEEECCCCCC	37.93	22790023
312	Malonylation	IDDERLRKEFSPFGT CCHHHHHHHCCCCCC	68.64	26320211
312	Ubiquitination	IDDERLRKEFSPFGT CCHHHHHHHCCCCCC	68.64	27667366
315	Phosphorylation	ERLRKEFSPFGTITS HHHHHHCCCCCCEEE	22.02	26824392
319	Phosphorylation	KEFSPFGTITSAKVM HHCCCCCCEEEEEEE	22.82	23984901
333	Ubiquitination	MMEGGRSKGFGFVCF EECCCCCCCCEEEEE	57.82	22790023
339	Glutathionylation	SKGFGFVCFSSPEEA CCCCEEEEECCHHHH	2.27	24333276
339	S-palmitoylation	SKGFGFVCFSSPEEA CCCCEEEEECCHHHH	2.27	28526873
341	Phosphorylation	GFGFVCFSSPEEATK CCEEEEECCHHHHHH	39.60	26643407
342	Phosphorylation	FGFVCFSSPEEATKA CEEEEECCHHHHHHH	18.97	26745281
347	Phosphorylation	FSSPEEATKAVTEMN ECCHHHHHHHHHHHC	23.86	28066266
348	Ubiquitination	SSPEEATKAVTEMNG CCHHHHHHHHHHHCC	48.16	22790023
361	Acetylation	NGRIVATKPLYVALA CCEEEEEHHHHHHHH	24.24	23806337
361	Succinylation	NGRIVATKPLYVALA CCEEEEEHHHHHHHH	24.24	23806337
361	Ubiquitination	NGRIVATKPLYVALA CCEEEEEHHHHHHHH	24.24	27667366
364	Phosphorylation	IVATKPLYVALAQRK EEEEHHHHHHHHHCH	7.69	25177544
379	Phosphorylation	EERQAHLTNQYMQRM HHHHHHHHHHHHHHH	15.48	25367039
382	Phosphorylation	QAHLTNQYMQRMASV HHHHHHHHHHHHHHC	9.40	25367039
385	Methylation	LTNQYMQRMASVRAV HHHHHHHHHHHCCCC	13.20	-
388	Phosphorylation	QYMQRMASVRAVPNP HHHHHHHHCCCCCCC	11.64	24719451
419	Methylation	AIPQTQNRAAYYPPS EECCCCCCCCCCCHH	15.69	24129315
426	Phosphorylation	RAAYYPPSQIAQLRP CCCCCCHHHHHHCCC	29.70	24719451
432	Dimethylation	PSQIAQLRPSPRWTA HHHHHHCCCCCCCCC	19.98	-
432	Methylation	PSQIAQLRPSPRWTA HHHHHHCCCCCCCCC	19.98	54557789
434	Phosphorylation	QIAQLRPSPRWTAQG HHHHCCCCCCCCCCC	22.21	-
436	Methylation	AQLRPSPRWTAQGAR HHCCCCCCCCCCCCC	47.95	54557805
455	Dimethylation	QNMPGAIRPAAPRPP CCCCCCCCCCCCCCC	17.80	-
455	Methylation	QNMPGAIRPAAPRPP CCCCCCCCCCCCCCC	17.80	140923
460	Methylation	AIRPAAPRPPFSTMR CCCCCCCCCCCCCCC	46.96	-
475	Dimethylation	PASSQVPRVMSTQRV CCHHCCCCEEECCCC	37.60	-
475	Methylation	PASSQVPRVMSTQRV CCHHCCCCEEECCCC	37.60	24129315
478	Phosphorylation	SQVPRVMSTQRVANT HCCCCEEECCCCCCC	20.66	24719451
479	Phosphorylation	QVPRVMSTQRVANTS CCCCEEECCCCCCCC	11.42	20469934
481	Methylation	PRVMSTQRVANTSTQ CCEEECCCCCCCCCC	29.60	-
493	Asymmetric dimethylarginine	STQTMGPRPAAAAAA CCCCCCCCHHHHHHH	27.97	-
493	Methylation	STQTMGPRPAAAAAA CCCCCCCCHHHHHHH	27.97	24129315
502	Phosphorylation	AAAAAAATPAVRTVP HHHHHHCCCCCCCCC	13.67	28066266
506	Methylation	AAATPAVRTVPQYKY HHCCCCCCCCCHHHH	31.92	24129315
512	Acetylation	VRTVPQYKYAAGVRN CCCCCHHHHCCCCCC	24.14	23806337
512	Malonylation	VRTVPQYKYAAGVRN CCCCCHHHHCCCCCC	24.14	26320211
512	Ubiquitination	VRTVPQYKYAAGVRN CCCCCHHHHCCCCCC	24.14	27667366
518	Methylation	YKYAAGVRNPQQHLN HHHCCCCCCHHHHCC	48.47	-
531	Phosphorylation	LNAQPQVTMQQPAVH CCCCCCEEECCCCEE	12.19	28285833
546	Phosphorylation	VQGQEPLTASMLASA ECCCCCCCHHHHHCC	27.66	30352176
591	Phosphorylation	MLLEIDNSELLHMLE EEEEECCHHHHHHHC	26.35	25293948
599	Phosphorylation	ELLHMLESPESLRSK HHHHHHCCHHHHHHH	29.97	26643407
602	Phosphorylation	HMLESPESLRSKVDE HHHCCHHHHHHHHHH	32.25	25293948
620	Acetylation	VLQAHQAKEAAQKAV HHHHHHHHHHHHHHH	41.12	22826441
620	Malonylation	VLQAHQAKEAAQKAV HHHHHHHHHHHHHHH	41.12	26320211
620	Ubiquitination	VLQAHQAKEAAQKAV HHHHHHHHHHHHHHH	41.12	-
625	Malonylation	QAKEAAQKAVNSATG HHHHHHHHHHHHHCC	49.96	26320211
625	Ubiquitination	QAKEAAQKAVNSATG HHHHHHHHHHHHHCC	49.96	-
629	Phosphorylation	AAQKAVNSATGVPTV HHHHHHHHHCCCCCC	22.17	25619855
631	Phosphorylation	QKAVNSATGVPTV-- HHHHHHHCCCCCC--	38.23	25619855
635	Phosphorylation	NSATGVPTV------ HHHCCCCCC------	36.12	25619855

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 PABP1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
493	R	Methylation		24129315
Arg-493 is dimethylated, probably to asymmetric dimethylarginine (By similarity).

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 PABP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CETN2_HUMAN	CETN2	physical	26496610
IF4G1_HUMAN	EIF4G1	physical	26496610
RS23_HUMAN	RPS23	physical	26496610
PABP4_HUMAN	PABPC4	physical	26496610
PAIP1_HUMAN	PAIP1	physical	26496610
LAR4B_HUMAN	LARP4B	physical	26496610
LARP1_HUMAN	LARP1	physical	26496610
SND1_HUMAN	SND1	physical	26496610
RT18B_HUMAN	MRPS18B	physical	26496610
ASCC1_HUMAN	ASCC1	physical	26496610
ZCCHV_HUMAN	ZC3HAV1	physical	26496610
VKOR1_HUMAN	VKORC1	physical	26496610
LARP4_HUMAN	LARP4	physical	26496610
DJC21_HUMAN	DNAJC21	physical	26496610

Drug and Disease Associations

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

Regulatory Network of PABP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, AND MASSSPECTROMETRY.	17947660 [Abstract]

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