PABP1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PABP1_RAT
• UniProt AC: Q9EPH8
• Protein Name: Polyadenylate-binding protein 1
• Gene Name: Pabpc1
• Organism: Rattus norvegicus (Rat).
• 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)..
• Protein Sequence: MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKELFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAATAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPSLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNPSAPSY -------CCCCCCCC	17.54	-
39	Phosphorylation	SPAGPILSIRVCRDM CCCCCEEEEEEEHHH	14.74	23984901
51	Phosphorylation	RDMITRRSLGYAYVN HHHHHHCCCEEEEEE	23.90	23984901
54	Phosphorylation	ITRRSLGYAYVNFQQ HHHCCCEEEEEEECC	10.47	23984901
71	Phosphorylation	DAERALDTMNFDVIK HHHHHHHHCCCEEEC	18.18	23984901
78	Acetylation	TMNFDVIKGKPVRIM HCCCEEECCEEEEEE	61.81	22902405
96	Phosphorylation	RDPSLRKSGVGNIFI CCHHHHHCCCCCEEE	32.07	28432305
104	Acetylation	GVGNIFIKNLDKSID CCCCEEECCCCHHCC	40.48	22902405
108	Acetylation	IFIKNLDKSIDNKAL EEECCCCHHCCCHHH	53.10	22638159
118	Phosphorylation	DNKALYDTFSAFGNI CCHHHHHHHHHHCCC	13.11	23984901
120	Phosphorylation	KALYDTFSAFGNILS HHHHHHHHHHCCCCE	25.44	23984901
157	Acetylation	AAERAIEKMNGMLLN HHHHHHHHHHCCCCC	31.39	21670749
188	Ubiquitination	AELGARAKEFTNVYI HHHHHHHHHHHCEEE	48.05	-
188	Acetylation	AELGARAKEFTNVYI HHHHHHHHHHHCEEE	48.05	22902405
191	Phosphorylation	GARAKEFTNVYIKNF HHHHHHHHCEEECCC	25.51	25575281
194	Phosphorylation	AKEFTNVYIKNFGED HHHHHCEEECCCCCC	14.30	25575281
219	Phosphorylation	GKFGPALSVKVMTDE HHHCCEEEEEEEECC	23.23	23984901
227	Phosphorylation	VKVMTDESGKSKGFG EEEEECCCCCCCCEE	55.09	26022182
237	Phosphorylation	SKGFGFVSFERHEDA CCCEEEEEEEEHHHH	21.09	27097102
259	Acetylation	NGKELNGKQIYVGRA CCEECCCEEEEECCH	32.23	22902405
262	Phosphorylation	ELNGKQIYVGRAQKK ECCCEEEEECCHHHH	8.38	30181290
284	Ubiquitination	KRKFEQMKQDRITRY HHHHHHHHHHHHHHH	49.06	-
299	Methylation	QGVNLYVKNLDDGID HCCEEEEEECCCCCC	37.93	-
315	Phosphorylation	ERLRKEFSPFGTITS HHHHHHCCCCCCEEE	22.02	28432305
319	Phosphorylation	KEFSPFGTITSAKVM HHCCCCCCEEEEEEE	22.82	23984901
321	Phosphorylation	FSPFGTITSAKVMME CCCCCCEEEEEEEEC	23.59	23984901
322	Phosphorylation	SPFGTITSAKVMMEG CCCCCEEEEEEEECC	23.42	23984901
341	Phosphorylation	GFGFVCFSSPEEATK CCEEEEECCHHHHHH	39.60	23984901
342	Phosphorylation	FGFVCFSSPEEATKA CEEEEECCHHHHHHH	18.97	23984901
364	Phosphorylation	IVATKPLYVALAQRK EEEEHHHHHHHHHCH	7.69	-
385	Methylation	LTNQYMQRMASVRAV HHHHHHHHHHHCCCC	13.20	26494653
419	Methylation	AIPQTQNRAAYYPPS EECCCCCCCCCCCHH	15.69	18966553
432	Methylation	PSQIAQLRPSPRWTA HHHHHHCCCCCCCCC	19.98	-
436	Methylation	AQLRPSPRWTAQGAR HHCCCCCCCCCCCCC	47.95	-
455	Methylation	QNMPGAIRPAAPRPP CCCCCCCCCCCCCCC	17.80	-
460	Methylation	AIRPAAPRPPFSTMR CCCCCCCCCCCCCCC	46.96	-
475	Methylation	PASSQVPRVMSTQRV CCHHCCCCEEECCCC	37.60	-
481	Methylation	PRVMSTQRVANTSTQ CCEEECCCCCCCCCC	29.60	-
493	Methylation	STQTMGPRPAAAATA CCCCCCCCHHHHHHC	27.97	-
493	Asymmetric dimethylarginine	STQTMGPRPAAAATA CCCCCCCCHHHHHHC	27.97	-
506	Methylation	TAATPAVRTVPQYKY HCCCCCCCCCCHHHH	31.92	-
512	Acetylation	VRTVPQYKYAAGVRN CCCCCHHHHCCCCCC	24.14	-
518	Methylation	YKYAAGVRNPQQHLN HHHCCCCCCHHHHCC	48.47	-
599	Phosphorylation	ELLHMLESPESLRSK HHHHHHCCHHHHHHH	29.97	22673903
629	Phosphorylation	AAQKAVNSATGVPTV HHHHHHHHHCCCCCC	22.17	23984901
631	Phosphorylation	QKAVNSATGVPTV-- HHHHHHHCCCCCC--	38.23	23984901

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PABP1_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
493	R	Methylation	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.

Oops, there are no SNP-PTM records of PABP1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

Drug and Disease Associations

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