dbPTM

PABP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PABP1_HUMAN
UniProt AC	P11940
Protein Name	Polyadenylate-binding protein 1
Gene Name	PABPC1
Organism	Homo sapiens (Human).
Sequence Length	636
Subcellular Localization	Cytoplasm . Nucleus . Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661). Shuttles between the cytoplasm and the nucleus (PubMed:9582337).
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 binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability. [PubMed: 25480299 Positively regulates the replication of dengue virus (DENV)]
Protein Sequence	MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNPSAPSY -------CCCCCCCC	17.54	19413330
32	Phosphorylation	AMLYEKFSPAGPILS HHHHHHCCCCCCEEE	25.55	21815630
39	Phosphorylation	SPAGPILSIRVCRDM CCCCCEEEEEEEHHH	14.74	21406692
51	Phosphorylation	RDMITRRSLGYAYVN HHHHHHCCCEEEEEE	23.90	25159151
54	Phosphorylation	ITRRSLGYAYVNFQQ HHHCCCEEEEEEECC	10.47	21082442
56	Phosphorylation	RRSLGYAYVNFQQPA HCCCEEEEEEECCCC	6.35	20090780
71	Phosphorylation	DAERALDTMNFDVIK HHHHHHHHCCCEEEC	18.18	20860994
72	Sulfoxidation	AERALDTMNFDVIKG HHHHHHHCCCEEECC	4.73	21406390
78	Acetylation	TMNFDVIKGKPVRIM HCCCEEECCEEEEEE	61.81	23749302
78	Ubiquitination	TMNFDVIKGKPVRIM HCCCEEECCEEEEEE	61.81	21890473
78 (in isoform 1)	Ubiquitination	-	61.81	21890473
78 (in isoform 2)	Ubiquitination	-	61.81	21890473
80	Ubiquitination	NFDVIKGKPVRIMWS CCEEECCEEEEEEEE	35.02	21890473
80 (in isoform 1)	Ubiquitination	-	35.02	21890473
80 (in isoform 2)	Ubiquitination	-	35.02	21890473
87	Phosphorylation	KPVRIMWSQRDPSLR EEEEEEEECCCHHHH	9.65	23186163
92	Phosphorylation	MWSQRDPSLRKSGVG EEECCCHHHHHCCCC	45.13	23403867
95	Acetylation	QRDPSLRKSGVGNIF CCCHHHHHCCCCCEE	57.78	22004688
95	Malonylation	QRDPSLRKSGVGNIF CCCHHHHHCCCCCEE	57.78	26320211
95	Ubiquitination	QRDPSLRKSGVGNIF CCCHHHHHCCCCCEE	57.78	21906983
95 (in isoform 1)	Ubiquitination	-	57.78	21890473
95 (in isoform 2)	Ubiquitination	-	57.78	21890473
96	Phosphorylation	RDPSLRKSGVGNIFI CCHHHHHCCCCCEEE	32.07	30266825
104	Acetylation	GVGNIFIKNLDKSID CCCCEEECCCCHHCC	40.48	23749302
104	Malonylation	GVGNIFIKNLDKSID CCCCEEECCCCHHCC	40.48	26320211
104	Ubiquitination	GVGNIFIKNLDKSID CCCCEEECCCCHHCC	40.48	21890473
104 (in isoform 1)	Ubiquitination	-	40.48	21890473
104 (in isoform 2)	Ubiquitination	-	40.48	21890473
108	Acetylation	IFIKNLDKSIDNKAL EEECCCCHHCCCHHH	53.10	19608861
108	Malonylation	IFIKNLDKSIDNKAL EEECCCCHHCCCHHH	53.10	26320211
108	Ubiquitination	IFIKNLDKSIDNKAL EEECCCCHHCCCHHH	53.10	22053931
108 (in isoform 1)	Ubiquitination	-	53.10	21890473
108 (in isoform 2)	Ubiquitination	-	53.10	21890473
113	Ubiquitination	LDKSIDNKALYDTFS CCHHCCCHHHHHHHH	35.70	21906983
113 (in isoform 1)	Ubiquitination	-	35.70	21890473
113 (in isoform 2)	Ubiquitination	-	35.70	21890473
116	Phosphorylation	SIDNKALYDTFSAFG HCCCHHHHHHHHHHC	20.14	17360941
120	Phosphorylation	KALYDTFSAFGNILS HHHHHHHHHHCCCCE	25.44	21712546
127	Phosphorylation	SAFGNILSCKVVCDE HHHCCCCEEEEEECC	14.22	21712546
128	Glutathionylation	AFGNILSCKVVCDEN HHCCCCEEEEEECCC	3.30	22555962
128	S-palmitoylation	AFGNILSCKVVCDEN HHCCCCEEEEEECCC	3.30	29575903
129	Acetylation	FGNILSCKVVCDENG HCCCCEEEEEECCCC	34.03	26051181
129	Ubiquitination	FGNILSCKVVCDENG HCCCCEEEEEECCCC	34.03	21906983
129 (in isoform 1)	Ubiquitination	-	34.03	21890473
129 (in isoform 2)	Ubiquitination	-	34.03	21890473
138	Acetylation	VCDENGSKGYGFVHF EECCCCCEEEEEEEE	58.51	26051181
138	Ubiquitination	VCDENGSKGYGFVHF EECCCCCEEEEEEEE	58.51	-
140	Phosphorylation	DENGSKGYGFVHFET CCCCCEEEEEEEEEC	15.89	28152594
157	Acetylation	AAERAIEKMNGMLLN HHHHHHHHHHCCCCC	31.39	25953088
157	Ubiquitination	AAERAIEKMNGMLLN HHHHHHHHHHCCCCC	31.39	21890473
157 (in isoform 1)	Ubiquitination	-	31.39	21890473
157 (in isoform 2)	Ubiquitination	-	31.39	21890473
158	Sulfoxidation	AERAIEKMNGMLLND HHHHHHHHHCCCCCC	3.21	21406390
166	Methylation	NGMLLNDRKVFVGRF HCCCCCCCEEEEECC	35.64	-
167	Sumoylation	GMLLNDRKVFVGRFK CCCCCCCEEEEECCC	42.77	-
167	Sumoylation	GMLLNDRKVFVGRFK CCCCCCCEEEEECCC	42.77	-
167	Ubiquitination	GMLLNDRKVFVGRFK CCCCCCCEEEEECCC	42.77	-
167 (in isoform 1)	Ubiquitination	-	42.77	21890473
167 (in isoform 2)	Ubiquitination	-	42.77	21890473
188	Acetylation	AELGARAKEFTNVYI HHHHHHHHHHHCEEE	48.05	22004688
188	Malonylation	AELGARAKEFTNVYI HHHHHHHHHHHCEEE	48.05	26320211
188	Methylation	AELGARAKEFTNVYI HHHHHHHHHHHCEEE	48.05	19826687
188	Ubiquitination	AELGARAKEFTNVYI HHHHHHHHHHHCEEE	48.05	21890473
188 (in isoform 1)	Ubiquitination	-	48.05	21890473
188 (in isoform 2)	Ubiquitination	-	48.05	21890473
191	Phosphorylation	GARAKEFTNVYIKNF HHHHHHHHCEEECCC	25.51	28152594
194	Phosphorylation	AKEFTNVYIKNFGED HHHHHCEEECCCCCC	14.30	28152594
196	Acetylation	EFTNVYIKNFGEDMD HHHCEEECCCCCCCC	28.65	19826697
196	Ubiquitination	EFTNVYIKNFGEDMD HHHCEEECCCCCCCC	28.65	21890473
196 (in isoform 1)	Ubiquitination	-	28.65	21890473
196 (in isoform 2)	Ubiquitination	-	28.65	21890473
202	Sulfoxidation	IKNFGEDMDDERLKD ECCCCCCCCHHHHHH	6.43	21406390
208	Acetylation	DMDDERLKDLFGKFG CCCHHHHHHHHHHHC	59.62	25953088
208	Ubiquitination	DMDDERLKDLFGKFG CCCHHHHHHHHHHHC	59.62	21890473
208 (in isoform 1)	Ubiquitination	-	59.62	21890473
208 (in isoform 2)	Ubiquitination	-	59.62	21890473
213	Acetylation	RLKDLFGKFGPALSV HHHHHHHHHCCEEEE	39.55	19608861
213	Ubiquitination	RLKDLFGKFGPALSV HHHHHHHHHCCEEEE	39.55	21890473
213 (in isoform 1)	Ubiquitination	-	39.55	21890473
213 (in isoform 2)	Ubiquitination	-	39.55	21890473
219	Phosphorylation	GKFGPALSVKVMTDE HHHCCEEEEEEEECC	23.23	28450419
221	Acetylation	FGPALSVKVMTDESG HCCEEEEEEEECCCC	23.94	25953088
221	Ubiquitination	FGPALSVKVMTDESG HCCEEEEEEEECCCC	23.94	-
223	Sulfoxidation	PALSVKVMTDESGKS CEEEEEEEECCCCCC	3.03	30846556
224	Phosphorylation	ALSVKVMTDESGKSK EEEEEEEECCCCCCC	39.33	27362937
229	Acetylation	VMTDESGKSKGFGFV EEECCCCCCCCEEEE	59.27	25953088
229	Ubiquitination	VMTDESGKSKGFGFV EEECCCCCCCCEEEE	59.27	21906983
229 (in isoform 1)	Ubiquitination	-	59.27	21890473
229 (in isoform 2)	Ubiquitination	-	59.27	21890473
230	Phosphorylation	MTDESGKSKGFGFVS EECCCCCCCCEEEEE	41.35	27362937
231	Acetylation	TDESGKSKGFGFVSF ECCCCCCCCEEEEEE	62.84	26051181
231	Malonylation	TDESGKSKGFGFVSF ECCCCCCCCEEEEEE	62.84	26320211
231	Ubiquitination	TDESGKSKGFGFVSF ECCCCCCCCEEEEEE	62.84	21890473
231 (in isoform 1)	Ubiquitination	-	62.84	21890473
231 (in isoform 2)	Ubiquitination	-	62.84	21890473
237	Phosphorylation	SKGFGFVSFERHEDA CCCEEEEEEEEHHHH	21.09	21815630
240	Methylation	FGFVSFERHEDAQKA EEEEEEEEHHHHHHH	36.16	-
246	Acetylation	ERHEDAQKAVDEMNG EEHHHHHHHHHHHCC	52.69	25953088
246	Ubiquitination	ERHEDAQKAVDEMNG EEHHHHHHHHHHHCC	52.69	21906983
246 (in isoform 1)	Ubiquitination	-	52.69	21890473
246 (in isoform 2)	Ubiquitination	-	52.69	21890473
254	Acetylation	AVDEMNGKELNGKQI HHHHHCCEECCCEEE	54.76	26051181
254	Ubiquitination	AVDEMNGKELNGKQI HHHHHCCEECCCEEE	54.76	-
259	Acetylation	NGKELNGKQIYVGRA CCEECCCEEEEECCH	32.23	23236377
259	Ubiquitination	NGKELNGKQIYVGRA CCEECCCEEEEECCH	32.23	21890473
259 (in isoform 1)	Ubiquitination	-	32.23	21890473
259 (in isoform 2)	Ubiquitination	-	32.23	21890473
262	Phosphorylation	ELNGKQIYVGRAQKK ECCCEEEEECCHHHH	8.38	-
269	Ubiquitination	YVGRAQKKVERQTEL EECCHHHHHHHHHHH	36.93	-
279	Ubiquitination	RQTELKRKFEQMKQD HHHHHHHHHHHHHHH	52.22	22053931
279 (in isoform 1)	Ubiquitination	-	52.22	21890473
279 (in isoform 2)	Ubiquitination	-	52.22	21890473
284	Ubiquitination	KRKFEQMKQDRITRY HHHHHHHHHHHHHHH	49.06	22053931
284 (in isoform 1)	Ubiquitination	-	49.06	21890473
284 (in isoform 2)	Ubiquitination	-	49.06	21890473
291	Phosphorylation	KQDRITRYQGVNLYV HHHHHHHHHCCEEEE	10.85	28152594
297	Phosphorylation	RYQGVNLYVKNLDDG HHHCCEEEEEECCCC	12.27	28152594
299	Acetylation	QGVNLYVKNLDDGID HCCEEEEEECCCCCC	37.93	23954790
299	Methylation	QGVNLYVKNLDDGID HCCEEEEEECCCCCC	37.93	23161681
299	Ubiquitination	QGVNLYVKNLDDGID HCCEEEEEECCCCCC	37.93	21890473
299 (in isoform 1)	Ubiquitination	-	37.93	21890473
299 (in isoform 2)	Ubiquitination	-	37.93	21890473
309	Methylation	DDGIDDERLRKEFSP CCCCCHHHHHHHCCC	46.95	-
312	Acetylation	IDDERLRKEFSPFGT CCHHHHHHHCCCCCC	68.64	22004688
312	Malonylation	IDDERLRKEFSPFGT CCHHHHHHHCCCCCC	68.64	26320211
312	Ubiquitination	IDDERLRKEFSPFGT CCHHHHHHHCCCCCC	68.64	21890473
312 (in isoform 1)	Ubiquitination	-	68.64	21890473
312 (in isoform 2)	Ubiquitination	-	68.64	21890473
315	Phosphorylation	ERLRKEFSPFGTITS HHHHHHCCCCCCEEE	22.02	30266825
319	Phosphorylation	KEFSPFGTITSAKVM HHCCCCCCEEEEEEE	22.82	30266825
321	Phosphorylation	FSPFGTITSAKVMME CCCCCCEEEEEEEEC	23.59	29255136
322	Phosphorylation	SPFGTITSAKVMMEG CCCCCEEEEEEEECC	23.42	29255136
324	Acetylation	FGTITSAKVMMEGGR CCCEEEEEEEECCCC	30.36	25953088
324	Ubiquitination	FGTITSAKVMMEGGR CCCEEEEEEEECCCC	30.36	-
333	Acetylation	MMEGGRSKGFGFVCF EECCCCCCCCEEEEE	57.82	26051181
333	Malonylation	MMEGGRSKGFGFVCF EECCCCCCCCEEEEE	57.82	26320211
333	Ubiquitination	MMEGGRSKGFGFVCF EECCCCCCCCEEEEE	57.82	21890473
333 (in isoform 1)	Ubiquitination	-	57.82	21890473
333 (in isoform 2)	Ubiquitination	-	57.82	21890473
339	Glutathionylation	SKGFGFVCFSSPEEA CCCCEEEEECCHHHH	2.27	22555962
339	S-palmitoylation	SKGFGFVCFSSPEEA CCCCEEEEECCHHHH	2.27	29575903
341	Phosphorylation	GFGFVCFSSPEEATK CCEEEEECCHHHHHH	39.60	25159151
342	Phosphorylation	FGFVCFSSPEEATKA CEEEEECCHHHHHHH	18.97	25159151
347	Phosphorylation	FSSPEEATKAVTEMN ECCHHHHHHHHHHHC	23.86	24732914
348	Acetylation	SSPEEATKAVTEMNG CCHHHHHHHHHHHCC	48.16	26051181
348	Ubiquitination	SSPEEATKAVTEMNG CCHHHHHHHHHHHCC	48.16	21906983
348 (in isoform 1)	Ubiquitination	-	48.16	21890473
348 (in isoform 2)	Ubiquitination	-	48.16	21890473
360	Phosphorylation	MNGRIVATKPLYVAL HCCEEEEEHHHHHHH	23.46	28152594
361	Acetylation	NGRIVATKPLYVALA CCEEEEEHHHHHHHH	24.24	22004688
361	Ubiquitination	NGRIVATKPLYVALA CCEEEEEHHHHHHHH	24.24	21890473
361 (in isoform 1)	Ubiquitination	-	24.24	21890473
361 (in isoform 2)	Ubiquitination	-	24.24	21890473
364	Phosphorylation	IVATKPLYVALAQRK EEEEHHHHHHHHHCH	7.69	27273156
379	Phosphorylation	EERQAHLTNQYMQRM HHHHHHHHHHHHHHH	15.48	21945579
382	Phosphorylation	QAHLTNQYMQRMASV HHHHHHHHHHHHHHC	9.40	21945579
383	Sulfoxidation	AHLTNQYMQRMASVR HHHHHHHHHHHHHCC	1.15	28465586
385	Methylation	LTNQYMQRMASVRAV HHHHHHHHHHHCCCC	13.20	24129315
388	Phosphorylation	QYMQRMASVRAVPNP HHHHHHHHCCCCCCC	11.64	26074081
390	Methylation	MQRMASVRAVPNPVI HHHHHHCCCCCCCCC	27.63	97818475
400	Phosphorylation	PNPVINPYQPAPPSG CCCCCCCCCCCCCCC	23.73	-
408	Phosphorylation	QPAPPSGYFMAAIPQ CCCCCCCCEEEEECC	8.43	20068231
416	Phosphorylation	FMAAIPQTQNRAAYY EEEEECCCCCCCCCC	23.58	20068231
419	Dimethylation	AIPQTQNRAAYYPPS EECCCCCCCCCCCHH	15.69	-
419	Methylation	AIPQTQNRAAYYPPS EECCCCCCCCCCCHH	15.69	24129315
422	Phosphorylation	QTQNRAAYYPPSQIA CCCCCCCCCCHHHHH	18.60	23917254
426	Phosphorylation	RAAYYPPSQIAQLRP CCCCCCHHHHHHCCC	29.70	24719451
432	Dimethylation	PSQIAQLRPSPRWTA HHHHHHCCCCCCCCC	19.98	-
432	Methylation	PSQIAQLRPSPRWTA HHHHHHCCCCCCCCC	19.98	24129315
434	Phosphorylation	QIAQLRPSPRWTAQG HHHHCCCCCCCCCCC	22.21	30301811
436	Dimethylation	AQLRPSPRWTAQGAR HHCCCCCCCCCCCCC	47.95	-
436	Methylation	AQLRPSPRWTAQGAR HHCCCCCCCCCCCCC	47.95	24129315
443	Dimethylation	RWTAQGARPHPFQNM CCCCCCCCCCCCCCC	36.56	-
443	Methylation	RWTAQGARPHPFQNM CCCCCCCCCCCCCCC	36.56	30762749
455	Dimethylation	QNMPGAIRPAAPRPP CCCCCCCCCCCCCCC	17.80	-
455	Methylation	QNMPGAIRPAAPRPP CCCCCCCCCCCCCCC	17.80	11850402
460	Dimethylation	AIRPAAPRPPFSTMR CCCCCCCCCCCCCCC	46.96	-
460	Methylation	AIRPAAPRPPFSTMR CCCCCCCCCCCCCCC	46.96	11850402
467	Dimethylation	RPPFSTMRPASSQVP CCCCCCCCCCHHCCC	24.58	-
467	Methylation	RPPFSTMRPASSQVP CCCCCCCCCCHHCCC	24.58	30762743
470	Phosphorylation	FSTMRPASSQVPRVM CCCCCCCHHCCCCEE	24.80	20873877
475	Dimethylation	PASSQVPRVMSTQRV CCHHCCCCEEECCCC	37.60	-
475	Methylation	PASSQVPRVMSTQRV CCHHCCCCEEECCCC	37.60	18600837
478	Phosphorylation	SQVPRVMSTQRVANT HCCCCEEECCCCCCC	20.66	24719451
481	Methylation	PRVMSTQRVANTSTQ CCEEECCCCCCCCCC	29.60	24129315
485	O-linked_Glycosylation	STQRVANTSTQTMGP ECCCCCCCCCCCCCC	24.34	28510447
485	Phosphorylation	STQRVANTSTQTMGP ECCCCCCCCCCCCCC	24.34	20860994
486	Phosphorylation	TQRVANTSTQTMGPR CCCCCCCCCCCCCCC	20.51	20860994
487	Phosphorylation	QRVANTSTQTMGPRP CCCCCCCCCCCCCCH	26.48	20860994
489	Phosphorylation	VANTSTQTMGPRPAA CCCCCCCCCCCCHHH	24.96	20860994
490	Sulfoxidation	ANTSTQTMGPRPAAA CCCCCCCCCCCHHHH	5.10	21406390
493	Asymmetric dimethylarginine	STQTMGPRPAAAAAA CCCCCCCCHHHHHHH	27.97	-
493	Methylation	STQTMGPRPAAAAAA CCCCCCCCHHHHHHH	27.97	24129315
502	Phosphorylation	AAAAAAATPAVRTVP HHHHHHCCCCCCCCC	13.67	21406692
506	Methylation	AAATPAVRTVPQYKY HHCCCCCCCCCHHHH	31.92	24129315
511	Phosphorylation	AVRTVPQYKYAAGVR CCCCCCHHHHCCCCC	10.41	-
512	Acetylation	VRTVPQYKYAAGVRN CCCCCHHHHCCCCCC	24.14	19608861
512	Methylation	VRTVPQYKYAAGVRN CCCCCHHHHCCCCCC	24.14	22638171
512	Ubiquitination	VRTVPQYKYAAGVRN CCCCCHHHHCCCCCC	24.14	21890473
512 (in isoform 1)	Ubiquitination	-	24.14	21890473
518	Methylation	YKYAAGVRNPQQHLN HHHCCCCCCHHHHCC	48.47	24129315
531 (in isoform 2)	Ubiquitination	-	12.19	21890473
536 (in isoform 2)	Ubiquitination	-	10.34	21890473
546	Phosphorylation	VQGQEPLTASMLASA ECCCCCCCHHHHHCC	27.66	28555341
573	Sulfoxidation	LFPLIQAMHPTLAGK HHHHHHHHCHHHHHH	1.92	31801345
591	Phosphorylation	MLLEIDNSELLHMLE EEEEECCHHHHHHHC	26.35	24732914
599	Phosphorylation	ELLHMLESPESLRSK HHHHHHCCHHHHHHH	29.97	25159151
602	Phosphorylation	HMLESPESLRSKVDE HHHCCHHHHHHHHHH	32.25	24732914
606	Acetylation	SPESLRSKVDEAVAV CHHHHHHHHHHHHHH	47.47	22004688
606	Ubiquitination	SPESLRSKVDEAVAV CHHHHHHHHHHHHHH	47.47	-
620	Acetylation	VLQAHQAKEAAQKAV HHHHHHHHHHHHHHH	41.12	23236377
620	Malonylation	VLQAHQAKEAAQKAV HHHHHHHHHHHHHHH	41.12	26320211
620	Succinylation	VLQAHQAKEAAQKAV HHHHHHHHHHHHHHH	41.12	23954790
620	Ubiquitination	VLQAHQAKEAAQKAV HHHHHHHHHHHHHHH	41.12	21890473
620 (in isoform 1)	Ubiquitination	-	41.12	21890473
625	Acetylation	QAKEAAQKAVNSATG HHHHHHHHHHHHHCC	49.96	25953088
625	Ubiquitination	QAKEAAQKAVNSATG HHHHHHHHHHHHHCC	49.96	2190698
625 (in isoform 1)	Ubiquitination	-	49.96	21890473
629	Phosphorylation	AAQKAVNSATGVPTV HHHHHHHHHCCCCCC	22.17	30108239
631	Phosphorylation	QKAVNSATGVPTV-- HHHHHHHCCCCCC--	38.23	30108239
635	O-linked_Glycosylation	NSATGVPTV------ HHHCCCCCC------	36.12	28510447
635	Phosphorylation	NSATGVPTV------ HHHCCCCCC------	36.12	28985074

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
-	K	Ubiquitination	E3 ubiquitin ligase	MKRN1	Q9UHC7	PMID:31640799

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
493	R	Methylation
Arg-493 is dimethylated, probably to asymmetric dimethylarginine.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAN3_HUMAN	PAN3	physical	18056425
ERF1_HUMAN	ETF1	physical	18056425
PAIP2_HUMAN	PAIP2	physical	11438674
PAIP1_HUMAN	PAIP1	physical	9548260
IF4A1_HUMAN	EIF4A1	physical	9548260
ERF3B_HUMAN	GSPT2	physical	10358005
ERF3A_HUMAN	GSPT1	physical	10358005
IF4G1_HUMAN	EIF4G1	physical	9857202
IF4G3_HUMAN	EIF4G3	physical	9857202
NUCL_HUMAN	NCL	physical	20221403
TTP_HUMAN	ZFP36	physical	20221403
TNR6B_HUMAN	TNRC6B	physical	21063388
TNR6A_HUMAN	TNRC6A	physical	20181956
ATX2_HUMAN	ATXN2	physical	20181956
PAIP1_HUMAN	PAIP1	physical	14685257
PAIP2_HUMAN	PAIP2	physical	14685257
ERF3A_HUMAN	GSPT1	physical	14685257
PABP1_HUMAN	PABPC1	physical	20096703
UBR5_HUMAN	UBR5	physical	20096703
PAIP2_HUMAN	PAIP2	physical	20096703
PAN2_HUMAN	PAN2	physical	17785442
PAN3_HUMAN	PAN3	physical	17785442
PABP1_HUMAN	PABPC1	physical	17785442
PAIP2_HUMAN	PAIP2	physical	17785442
TOB1_HUMAN	TOB1	physical	17785442
CAF1A_HUMAN	CHAF1A	physical	17785442
CNOT6_HUMAN	CNOT6	physical	17785442
BRCA1_HUMAN	BRCA1	physical	16782705
ROA1_HUMAN	HNRNPA1	physical	22939629
U520_HUMAN	SNRNP200	physical	22939629
SNW1_HUMAN	SNW1	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL13_HUMAN	RPL13	physical	22939629
RALY_HUMAN	RALY	physical	22939629
SMD3_HUMAN	SNRPD3	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
PRPF3_HUMAN	PRPF3	physical	22939629
SNRPA_HUMAN	SNRPA	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
HBB_HUMAN	HBB	physical	21145460
UBP10_HUMAN	USP10	physical	23230274
U2AF1_HUMAN	U2AF1	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
ATX2_HUMAN	ATXN2	physical	15663938
HBB_HUMAN	HBB	physical	18447585
PAIP2_HUMAN	PAIP2	physical	23964095
APEX1_HUMAN	APEX1	physical	22863883
DHX15_HUMAN	DHX15	physical	22863883
PDIA1_HUMAN	P4HB	physical	22863883
PSMD9_HUMAN	PSMD9	physical	22863883
TMOD3_HUMAN	TMOD3	physical	22863883
THIC_HUMAN	ACAT2	physical	26344197
CSTF2_HUMAN	CSTF2	physical	26344197
DD19A_HUMAN	DDX19A	physical	26344197
EF1G_HUMAN	EEF1G	physical	26344197
FPPS_HUMAN	FDPS	physical	26344197
G3BP1_HUMAN	G3BP1	physical	26344197
G3BP2_HUMAN	G3BP2	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
HSP7C_HUMAN	HSPA8	physical	26344197
KIN17_HUMAN	KIN	physical	26344197
LC7L2_HUMAN	LUC7L2	physical	26344197
MIF_HUMAN	MIF	physical	26344197
MSI2H_HUMAN	MSI2	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
ORC4_HUMAN	ORC4	physical	26344197
PAPOA_HUMAN	PAPOLA	physical	26344197
PAPOB_HUMAN	PAPOLB	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197
PLRG1_HUMAN	PLRG1	physical	26344197
PPCE_HUMAN	PREP	physical	26344197
PRP8_HUMAN	PRPF8	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL39_HUMAN	RPL39	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RLA0_HUMAN	RPLP0	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
PAIRB_HUMAN	SERBP1	physical	26344197
SF3A1_HUMAN	SF3A1	physical	26344197
SUMO1_HUMAN	SUMO1	physical	26344197
HNRPQ_HUMAN	SYNCRIP	physical	26344197
1433G_HUMAN	YWHAG	physical	26344197
TTP_HUMAN	ZFP36	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 PABP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-319, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND MASS SPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-493, AND MASS SPECTROMETRY.	15782174 [Abstract]
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-96; SER-315 AND SER-342,AND MASS SPECTROMETRY.	18669648 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-319, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, AND MASSSPECTROMETRY.	15592455 [Abstract]

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