dbPTM

PDS5B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDS5B_HUMAN
UniProt AC	Q9NTI5
Protein Name	Sister chromatid cohesion protein PDS5 homolog B
Gene Name	PDS5B
Organism	Homo sapiens (Human).
Sequence Length	1447
Subcellular Localization	Nucleus .
Protein Description	Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells..
Protein Sequence	MAHSKTRTNDGKITYPPGVKEISDKISKEEMVRRLKMVVKTFMDMDQDSEEEKELYLNLALHLASDFFLKHPDKDVRLLVACCLADIFRIYAPEAPYTSPDKLKDIFMFITRQLKGLEDTKSPQFNRYFYLLENIAWVKSYNICFELEDSNEIFTQLYRTLFSVINNGHNQKVHMHMVDLMSSIICEGDTVSQELLDTVLVNLVPAHKNLNKQAYDLAKALLKRTAQAIEPYITNFFNQVLMLGKTSISDLSEHVFDLILELYNIDSHLLLSVLPQLEFKLKSNDNEERLQVVKLLAKMFGAKDSELASQNKPLWQCYLGRFNDIHVPIRLECVKFASHCLMNHPDLAKDLTEYLKVRSHDPEEAIRHDVIVSIVTAAKKDILLVNDHLLNFVRERTLDKRWRVRKEAMMGLAQIYKKYALQSAAGKDAAKQIAWIKDKLLHIYYQNSIDDRLLVERIFAQYMVPHNLETTERMKCLYYLYATLDLNAVKALNEMWKCQNLLRHQVKDLLDLIKQPKTDASVKAIFSKVMVITRNLPDPGKAQDFMKKFTQVLEDDEKIRKQLEVLVSPTCSCKQAEGCVREITKKLGNPKQPTNPFLEMIKFLLERIAPVHIDTESISALIKQVNKSIDGTADDEDEGVPTDQAIRAGLELLKVLSFTHPISFHSAETFESLLACLKMDDEKVAEAALQIFKNTGSKIEEDFPHIRSALLPVLHHKSKKGPPRQAKYAIHCIHAIFSSKETQFAQIFEPLHKSLDPSNLEHLITPLVTIGHIALLAPDQFAAPLKSLVATFIVKDLLMNDRLPGKKTTKLWVPDEEVSPETMVKIQAIKMMVRWLLGMKNNHSKSGTSTLRLLTTILHSDGDLTEQGKISKPDMSRLRLAAGSAIVKLAQEPCYHEIITLEQYQLCALAINDECYQVRQVFAQKLHKGLSRLRLPLEYMAICALCAKDPVKERRAHARQCLVKNINVRREYLKQHAAVSEKLLSLLPEYVVPYTIHLLAHDPDYVKVQDIEQLKDVKECLWFVLEILMAKNENNSHAFIRKMVENIKQTKDAQGPDDAKMNEKLYTVCDVAMNIIMSKSTTYSLESPKDPVLPARFFTQPDKNFSNTKNYLPPEMKSFFTPGKPKTTNVLGAVNKPLSSAGKQSQTKSSRMETVSNASSSSNPSSPGRIKGRLDSSEMDHSENEDYTMSSPLPGKKSDKRDDSDLVRSELEKPRGRKKTPVTEQEEKLGMDDLTKLVQEQKPKGSQRSRKRGHTASESDEQQWPEEKRLKEDILENEDEQNSPPKKGKRGRPPKPLGGGTPKEEPTMKTSKKGSKKKSGPPAPEEEEEEERQSGNTEQKSKSKQHRVSRRAQQRAESPESSAIESTQSTPQKGRGRPSKTPSPSQPKKNVRVGRSKQAATKENDSSEEVDVFQGSSPVDDIPQEETEEEEVSTVNVRRRSAKRERR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Acetylation	KTRTNDGKITYPPGV CCCCCCCCCCCCCCC	34.44	7366845
20	Acetylation	ITYPPGVKEISDKIS CCCCCCCHHHHHHCC	56.07	7366855
20	Ubiquitination	ITYPPGVKEISDKIS CCCCCCCHHHHHHCC	56.07	29967540
23	Phosphorylation	PPGVKEISDKISKEE CCCCHHHHHHCCHHH	33.66	22985185
25	Acetylation	GVKEISDKISKEEMV CCHHHHHHCCHHHHH	41.93	25953088
27	Phosphorylation	KEISDKISKEEMVRR HHHHHHCCHHHHHHH	39.49	22798277
28	Ubiquitination	EISDKISKEEMVRRL HHHHHCCHHHHHHHH	62.25	29967540
36	Ubiquitination	EEMVRRLKMVVKTFM HHHHHHHHHHHHHHH	28.04	23000965
40	Ubiquitination	RRLKMVVKTFMDMDQ HHHHHHHHHHHCCCC	25.32	23000965
41	Phosphorylation	RLKMVVKTFMDMDQD HHHHHHHHHHCCCCC	16.75	22067460
49	Phosphorylation	FMDMDQDSEEEKELY HHCCCCCCHHHHHHH	41.07	-
53	Acetylation	DQDSEEEKELYLNLA CCCCHHHHHHHHHHH	57.19	12650223
61 (in isoform 5)	Ubiquitination	-	3.71	21890473
80	Ubiquitination	DKDVRLLVACCLADI CHHHHHHHHHHHHHH	4.54	21890473
91	Phosphorylation	LADIFRIYAPEAPYT HHHHHHHHCCCCCCC	16.31	-
98	Phosphorylation	YAPEAPYTSPDKLKD HCCCCCCCCHHHHHH	32.49	-
102	Acetylation	APYTSPDKLKDIFMF CCCCCHHHHHHHHHH	61.90	26822725
111	Phosphorylation	KDIFMFITRQLKGLE HHHHHHHHHHHCCCC	10.91	-
115	Ubiquitination	MFITRQLKGLEDTKS HHHHHHHCCCCCCCC	53.78	24816145
121	Ubiquitination	LKGLEDTKSPQFNRY HCCCCCCCCCHHHHH	72.90	22817900
121 (in isoform 1)	Ubiquitination	-	72.90	21890473
121 (in isoform 2)	Ubiquitination	-	72.90	21890473
121 (in isoform 3)	Ubiquitination	-	72.90	21890473
140	O-linked_Glycosylation	ENIAWVKSYNICFEL HHHHHHHHEEEEEEE	17.50	31492838
212	Acetylation	PAHKNLNKQAYDLAK HHCCCCCHHHHHHHH	39.20	7339641
215	Phosphorylation	KNLNKQAYDLAKALL CCCCHHHHHHHHHHH	14.70	-
219	Acetylation	KQAYDLAKALLKRTA HHHHHHHHHHHHHHH	47.03	7339651
231	Ubiquitination	RTAQAIEPYITNFFN HHHHHHHHHHHHHHH	21.51	21890473
283	Phosphorylation	QLEFKLKSNDNEERL HCEEEECCCCHHHHH	60.91	25954137
294	Ubiquitination	EERLQVVKLLAKMFG HHHHHHHHHHHHHHC	38.64	29967540
298	Acetylation	QVVKLLAKMFGAKDS HHHHHHHHHHCCCHH	34.43	25953088
312	Acetylation	SELASQNKPLWQCYL HHHHHCCCCCCEECC	33.57	26051181
312	Ubiquitination	SELASQNKPLWQCYL HHHHHCCCCCCEECC	33.57	29967540
335	Acetylation	PIRLECVKFASHCLM CEEHHHHHHHHHHHH	47.04	25953088
338	Phosphorylation	LECVKFASHCLMNHP HHHHHHHHHHHHHCH	20.19	26126808
349	Ubiquitination	MNHPDLAKDLTEYLK HHCHHHHHHHHHHHH	61.64	29967540
354	Phosphorylation	LAKDLTEYLKVRSHD HHHHHHHHHHHHCCC	13.44	-
356	Acetylation	KDLTEYLKVRSHDPE HHHHHHHHHHCCCHH	34.40	-
356	Ubiquitination	KDLTEYLKVRSHDPE HHHHHHHHHHCCCHH	34.40	23000965
356 (in isoform 1)	Ubiquitination	-	34.40	21890473
356 (in isoform 2)	Ubiquitination	-	34.40	21890473
356 (in isoform 3)	Ubiquitination	-	34.40	21890473
380	Ubiquitination	SIVTAAKKDILLVND HHHHHCCCCEEEECH	45.32	29967540
417	Acetylation	MGLAQIYKKYALQSA HHHHHHHHHHHHHHH	40.72	19608861
418	2-Hydroxyisobutyrylation	GLAQIYKKYALQSAA HHHHHHHHHHHHHHC	20.84	-
418	Ubiquitination	GLAQIYKKYALQSAA HHHHHHHHHHHHHHC	20.84	29967540
419	Phosphorylation	LAQIYKKYALQSAAG HHHHHHHHHHHHHCC	14.37	-
427	2-Hydroxyisobutyrylation	ALQSAAGKDAAKQIA HHHHHCCHHHHHHHH	39.19	-
427	Ubiquitination	ALQSAAGKDAAKQIA HHHHHCCHHHHHHHH	39.19	29967540
499 (in isoform 3)	Phosphorylation	-	39.62	28450419
507	Ubiquitination	NLLRHQVKDLLDLIK HHHHHHHHHHHHHHH	35.77	21890473
507 (in isoform 1)	Ubiquitination	-	35.77	21890473
507 (in isoform 2)	Ubiquitination	-	35.77	21890473
514	Acetylation	KDLLDLIKQPKTDAS HHHHHHHHCCCCCHH	68.77	26051181
514	Ubiquitination	KDLLDLIKQPKTDAS HHHHHHHHCCCCCHH	68.77	29967540
518	O-linked_Glycosylation	DLIKQPKTDASVKAI HHHHCCCCCHHHHHH	43.40	31492838
518	Phosphorylation	DLIKQPKTDASVKAI HHHHCCCCCHHHHHH	43.40	21712546
523	2-Hydroxyisobutyrylation	PKTDASVKAIFSKVM CCCCHHHHHHHHHEE	33.01	-
527	Phosphorylation	ASVKAIFSKVMVITR HHHHHHHHHEEEEEC	20.44	24719451
528	Acetylation	SVKAIFSKVMVITRN HHHHHHHHEEEEECC	24.49	26051181
533	Phosphorylation	FSKVMVITRNLPDPG HHHEEEEECCCCCCC	11.33	21712546
548	2-Hydroxyisobutyrylation	KAQDFMKKFTQVLED HHHHHHHHHHHHHCC	41.68	-
548	Acetylation	KAQDFMKKFTQVLED HHHHHHHHHHHHHCC	41.68	25953088
558	Acetylation	QVLEDDEKIRKQLEV HHHCCHHHHHHHHHH	55.60	25953088
558	Ubiquitination	QVLEDDEKIRKQLEV HHHCCHHHHHHHHHH	55.60	33845483
572	Phosphorylation	VLVSPTCSCKQAEGC HHCCCCCCCHHCCHH	27.16	20068231
574	Ubiquitination	VSPTCSCKQAEGCVR CCCCCCCHHCCHHHH	35.93	-
627	Ubiquitination	ALIKQVNKSIDGTAD HHHHHHHHHCCCCCC	50.35	29967540
628	Phosphorylation	LIKQVNKSIDGTADD HHHHHHHHCCCCCCC	22.25	-
693	Ubiquitination	EAALQIFKNTGSKIE HHHHHHHHHCCCCCH	56.05	29967540
698	Acetylation	IFKNTGSKIEEDFPH HHHHCCCCCHHHCHH	56.32	26051181
698	Ubiquitination	IFKNTGSKIEEDFPH HHHHCCCCCHHHCHH	56.32	29967540
717	Ubiquitination	LLPVLHHKSKKGPPR HHHHHCCCCCCCCHH	53.90	29967540
728	Phosphorylation	GPPRQAKYAIHCIHA CCHHHHHHHHHHHHH	17.50	-
787	Phosphorylation	QFAAPLKSLVATFIV HHHHHHHHHHHHHHH	35.44	-
795	Acetylation	LVATFIVKDLLMNDR HHHHHHHHHHHHCCC	37.53	26051181
802	Methylation	KDLLMNDRLPGKKTT HHHHHCCCCCCCCCC	37.47	-
810	Acetylation	LPGKKTTKLWVPDEE CCCCCCCEEECCCCC	45.65	25953088
810	Ubiquitination	LPGKKTTKLWVPDEE CCCCCCCEEECCCCC	45.65	29967540
813	Ubiquitination	KKTTKLWVPDEEVSP CCCCEEECCCCCCCH	6.58	23000965
827	Ubiquitination	PETMVKIQAIKMMVR HHHHHHHHHHHHHHH	31.17	21890473
844	Phosphorylation	LGMKNNHSKSGTSTL HCCCCCCCCCCHHHH	30.55	-
872	Ubiquitination	TEQGKISKPDMSRLR CCCCCCCCCCHHHHH	48.81	29967540
964	Acetylation	HARQCLVKNINVRRE HHHHHHHHHHHHCHH	38.88	25953088
974	Ubiquitination	NVRREYLKQHAAVSE HHCHHHHHHHHHHHH	38.85	29967540
985	Phosphorylation	AVSEKLLSLLPEYVV HHHHHHHHHCHHHHH	37.99	-
990	Phosphorylation	LLSLLPEYVVPYTIH HHHHCHHHHHHHHHH	12.57	-
1005	Phosphorylation	LLAHDPDYVKVQDIE HHHCCCCCCCCCCHH	13.93	-
1015	Ubiquitination	VQDIEQLKDVKECLW CCCHHHHCCHHHHHH	61.23	29967540
1050	Phosphorylation	MVENIKQTKDAQGPD HHHHHHHCCCCCCCC	26.37	19651622
1060	Acetylation	AQGPDDAKMNEKLYT CCCCCCHHHHHHHHH	49.61	26051181
1066	Phosphorylation	AKMNEKLYTVCDVAM HHHHHHHHHHHHHHH	14.27	23403867
1067	Phosphorylation	KMNEKLYTVCDVAMN HHHHHHHHHHHHHHH	25.70	23403867
1078	Phosphorylation	VAMNIIMSKSTTYSL HHHHHHHCCCCCCCC	17.04	24275748
1080	Phosphorylation	MNIIMSKSTTYSLES HHHHHCCCCCCCCCC	20.76	23403867
1081	Phosphorylation	NIIMSKSTTYSLESP HHHHCCCCCCCCCCC	33.23	23403867
1082	Phosphorylation	IIMSKSTTYSLESPK HHHCCCCCCCCCCCC	20.43	23403867
1083	Phosphorylation	IMSKSTTYSLESPKD HHCCCCCCCCCCCCC	16.02	24144214
1084	Phosphorylation	MSKSTTYSLESPKDP HCCCCCCCCCCCCCC	24.46	23403867
1087	Phosphorylation	STTYSLESPKDPVLP CCCCCCCCCCCCCCC	42.41	25159151
1089	Acetylation	TYSLESPKDPVLPAR CCCCCCCCCCCCCCH	81.56	26051181
1089	Ubiquitination	TYSLESPKDPVLPAR CCCCCCCCCCCCCCH	81.56	23000965
1103	Acetylation	RFFTQPDKNFSNTKN HHCCCCCCCCCCCCC	67.58	88031
1103	Ubiquitination	RFFTQPDKNFSNTKN HHCCCCCCCCCCCCC	67.58	21890473
1103 (in isoform 1)	Ubiquitination	-	67.58	21890473
1103 (in isoform 2)	Ubiquitination	-	67.58	21890473
1109	Ubiquitination	DKNFSNTKNYLPPEM CCCCCCCCCCCCHHH	48.09	29967540
1118	Phosphorylation	YLPPEMKSFFTPGKP CCCHHHHHCCCCCCC	25.04	30266825
1121	Phosphorylation	PEMKSFFTPGKPKTT HHHHHCCCCCCCCCC	29.17	30266825
1124	Acetylation	KSFFTPGKPKTTNVL HHCCCCCCCCCCCHH	44.54	25953088
1127	Phosphorylation	FTPGKPKTTNVLGAV CCCCCCCCCCHHHHH	31.93	29396449
1128	Phosphorylation	TPGKPKTTNVLGAVN CCCCCCCCCHHHHHC	29.47	29396449
1136	Acetylation	NVLGAVNKPLSSAGK CHHHHHCCCCHHCCC	40.51	19608861
1139	Phosphorylation	GAVNKPLSSAGKQSQ HHHCCCCHHCCCCCC	27.03	22167270
1140	Phosphorylation	AVNKPLSSAGKQSQT HHCCCCHHCCCCCCC	49.04	22167270
1143	Acetylation	KPLSSAGKQSQTKSS CCCHHCCCCCCCCCC	46.63	26051181
1145	Phosphorylation	LSSAGKQSQTKSSRM CHHCCCCCCCCCCCC	43.21	29214152
1147	Phosphorylation	SAGKQSQTKSSRMET HCCCCCCCCCCCCHH	37.83	21712546
1149	Phosphorylation	GKQSQTKSSRMETVS CCCCCCCCCCCHHHH	26.94	26074081
1150	Phosphorylation	KQSQTKSSRMETVSN CCCCCCCCCCHHHHC	36.88	26074081
1154	Phosphorylation	TKSSRMETVSNASSS CCCCCCHHHHCCCCC	21.64	23927012
1156	Phosphorylation	SSRMETVSNASSSSN CCCCHHHHCCCCCCC	33.81	23927012
1159	Phosphorylation	METVSNASSSSNPSS CHHHHCCCCCCCCCC	34.70	23927012
1160	Phosphorylation	ETVSNASSSSNPSSP HHHHCCCCCCCCCCC	35.06	23927012
1160 (in isoform 2)	Phosphorylation	-	35.06	21406692
1161	Phosphorylation	TVSNASSSSNPSSPG HHHCCCCCCCCCCCC	31.47	29255136
1161 (in isoform 2)	Phosphorylation	-	31.47	21406692
1162	Phosphorylation	VSNASSSSNPSSPGR HHCCCCCCCCCCCCC	55.50	29255136
1165	Phosphorylation	ASSSSNPSSPGRIKG CCCCCCCCCCCCCCC	54.11	29255136
1165 (in isoform 2)	Phosphorylation	-	54.11	21406692
1166	Phosphorylation	SSSSNPSSPGRIKGR CCCCCCCCCCCCCCC	32.41	19664994
1166 (in isoform 2)	Phosphorylation	-	32.41	21406692
1176	Phosphorylation	RIKGRLDSSEMDHSE CCCCCCCCCCCCCCC	32.56	22167270
1176 (in isoform 2)	Phosphorylation	-	32.56	21406692
1177	Phosphorylation	IKGRLDSSEMDHSEN CCCCCCCCCCCCCCC	36.29	22167270
1177 (in isoform 2)	Phosphorylation	-	36.29	21406692
1182	Phosphorylation	DSSEMDHSENEDYTM CCCCCCCCCCCCCCC	37.54	22167270
1182 (in isoform 2)	Phosphorylation	-	37.54	21406692
1187	Phosphorylation	DHSENEDYTMSSPLP CCCCCCCCCCCCCCC	9.73	22167270
1188	Phosphorylation	HSENEDYTMSSPLPG CCCCCCCCCCCCCCC	23.93	23927012
1188 (in isoform 2)	Phosphorylation	-	23.93	21406692
1190	Phosphorylation	ENEDYTMSSPLPGKK CCCCCCCCCCCCCCC	22.47	23401153
1190 (in isoform 2)	Phosphorylation	-	22.47	21406692
1191	Phosphorylation	NEDYTMSSPLPGKKS CCCCCCCCCCCCCCC	21.45	23927012
1191 (in isoform 2)	Phosphorylation	-	21.45	21406692
1196	Acetylation	MSSPLPGKKSDKRDD CCCCCCCCCCCCCCC	47.35	25953088
1198	Phosphorylation	SPLPGKKSDKRDDSD CCCCCCCCCCCCCHH	52.42	22210691
1204	Phosphorylation	KSDKRDDSDLVRSEL CCCCCCCHHHHHHHH	36.81	25849741
1209	Phosphorylation	DDSDLVRSELEKPRG CCHHHHHHHHCCCCC	38.77	25159151
1213	Acetylation	LVRSELEKPRGRKKT HHHHHHCCCCCCCCC	53.27	83035809
1220	Phosphorylation	KPRGRKKTPVTEQEE CCCCCCCCCCCHHHH	26.48	25159151
1223	Phosphorylation	GRKKTPVTEQEEKLG CCCCCCCCHHHHHHC	32.90	23403867
1228	Acetylation	PVTEQEEKLGMDDLT CCCHHHHHHCHHHHH	49.98	12656425
1231	Sulfoxidation	EQEEKLGMDDLTKLV HHHHHHCHHHHHHHH	5.40	21406390
1235	Phosphorylation	KLGMDDLTKLVQEQK HHCHHHHHHHHHHHC	29.35	19664994
1242	Acetylation	TKLVQEQKPKGSQRS HHHHHHHCCCCCCCC	48.20	25953088
1246	Phosphorylation	QEQKPKGSQRSRKRG HHHCCCCCCCCHHCC	28.66	23401153
1249	Phosphorylation	KPKGSQRSRKRGHTA CCCCCCCCHHCCCCC	34.22	27174698
1255	Phosphorylation	RSRKRGHTASESDEQ CCHHCCCCCCCCHHH	34.40	22167270
1255 (in isoform 2)	Phosphorylation	-	34.40	21406692
1257	Phosphorylation	RKRGHTASESDEQQW HHCCCCCCCCHHHCC	38.50	22167270
1257 (in isoform 2)	Phosphorylation	-	38.50	21406692
1259	Phosphorylation	RGHTASESDEQQWPE CCCCCCCCHHHCCCH	43.91	22167270
1259 (in isoform 2)	Phosphorylation	-	43.91	21406692
1283	Phosphorylation	ENEDEQNSPPKKGKR HCCCCCCCCCCCCCC	42.12	19664994
1283 (in isoform 2)	Phosphorylation	-	42.12	21406692
1301	Phosphorylation	PKPLGGGTPKEEPTM CCCCCCCCCCCCCCC	34.17	25159151
1307	Phosphorylation	GTPKEEPTMKTSKKG CCCCCCCCCCCCCCC	34.28	27251275
1309	Acetylation	PKEEPTMKTSKKGSK CCCCCCCCCCCCCCC	52.72	25953088
1319	Phosphorylation	KKGSKKKSGPPAPEE CCCCCCCCCCCCCHH	66.47	23401153
1334	Phosphorylation	EEEEERQSGNTEQKS HHHHHHHCCCCCHHH	39.99	23401153
1337	Phosphorylation	EERQSGNTEQKSKSK HHHHCCCCCHHHHHH	43.23	26657352
1341	Phosphorylation	SGNTEQKSKSKQHRV CCCCCHHHHHHHHHH	41.68	26657352
1343	Phosphorylation	NTEQKSKSKQHRVSR CCCHHHHHHHHHHHH	44.64	26657352
1344	Methylation	TEQKSKSKQHRVSRR CCHHHHHHHHHHHHH	54.59	-
1349	Phosphorylation	KSKQHRVSRRAQQRA HHHHHHHHHHHHHHH	18.92	-
1358	Phosphorylation	RAQQRAESPESSAIE HHHHHHHCCCCHHHH	32.74	19664994
1358 (in isoform 2)	Phosphorylation	-	32.74	21406692
1361	Phosphorylation	QRAESPESSAIESTQ HHHHCCCCHHHHCCC	28.58	29255136
1361 (in isoform 2)	Phosphorylation	-	28.58	21406692
1362	Phosphorylation	RAESPESSAIESTQS HHHCCCCHHHHCCCC	31.44	29255136
1366	Phosphorylation	PESSAIESTQSTPQK CCCHHHHCCCCCCCC	26.15	29255136
1366 (in isoform 2)	Phosphorylation	-	26.15	21406692
1367	Phosphorylation	ESSAIESTQSTPQKG CCHHHHCCCCCCCCC	17.47	29255136
1369	Phosphorylation	SAIESTQSTPQKGRG HHHHCCCCCCCCCCC	41.99	29255136
1370	Phosphorylation	AIESTQSTPQKGRGR HHHCCCCCCCCCCCC	21.66	29255136
1379	Phosphorylation	QKGRGRPSKTPSPSQ CCCCCCCCCCCCCCC	48.04	22167270
1379 (in isoform 2)	Phosphorylation	-	48.04	25849741
1380	Acetylation	KGRGRPSKTPSPSQP CCCCCCCCCCCCCCC	68.11	25953088
1381	Phosphorylation	GRGRPSKTPSPSQPK CCCCCCCCCCCCCCC	33.08	22167270
1381 (in isoform 2)	Phosphorylation	-	33.08	25849741
1383	Phosphorylation	GRPSKTPSPSQPKKN CCCCCCCCCCCCCCC	42.27	22167270
1383 (in isoform 2)	Phosphorylation	-	42.27	25849741
1385	Phosphorylation	PSKTPSPSQPKKNVR CCCCCCCCCCCCCCC	64.55	30266825
1385 (in isoform 2)	Phosphorylation	-	64.55	25849741
1396	Phosphorylation	KNVRVGRSKQAATKE CCCCCCCCCCCCCCC	24.16	30624053
1401	Phosphorylation	GRSKQAATKENDSSE CCCCCCCCCCCCCCC	41.74	25921289
1406	Phosphorylation	AATKENDSSEEVDVF CCCCCCCCCCCCCCC	51.75	30266825
1407	Phosphorylation	ATKENDSSEEVDVFQ CCCCCCCCCCCCCCC	40.41	30266825
1416	Phosphorylation	EVDVFQGSSPVDDIP CCCCCCCCCCCCCCC	22.23	28102081
1417	Phosphorylation	VDVFQGSSPVDDIPQ CCCCCCCCCCCCCCH	35.45	28102081
1427	Phosphorylation	DDIPQEETEEEEVST CCCCHHHCCCHHHHH	48.20	28464451
1433	Phosphorylation	ETEEEEVSTVNVRRR HCCCHHHHHHHHHHH	29.89	27251275
1434	Phosphorylation	TEEEEVSTVNVRRRS CCCHHHHHHHHHHHH	22.67	27251275
1441	Phosphorylation	TVNVRRRSAKRERR- HHHHHHHHHHHHCC-	36.01	26074081

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
1370	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PDS5B_HUMAN !!

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 PDS5B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC1A_HUMAN	SMC1A	physical	17113138
STAG1_HUMAN	STAG1	physical	17113138
STAG2_HUMAN	STAG2	physical	17113138
SMC3_HUMAN	SMC3	physical	17113138
RAD21_HUMAN	RAD21	physical	17112726
WFDC5_HUMAN	WFDC5	physical	17112726
SMC1A_HUMAN	SMC1A	physical	15855230
SMC3_HUMAN	SMC3	physical	15855230
RAD21_HUMAN	RAD21	physical	15855230
STAG1_HUMAN	STAG1	physical	15855230
STAG2_HUMAN	STAG2	physical	15855230
A4_HUMAN	APP	physical	21832049
BRCA2_HUMAN	BRCA2	physical	22293751
RAD51_HUMAN	RAD51	physical	22293751
PALB2_HUMAN	PALB2	physical	22293751
CDC45_HUMAN	CDC45	physical	22293751
PCNA_HUMAN	PCNA	physical	22293751
RAD21_HUMAN	RAD21	physical	22293751
SMC3_HUMAN	SMC3	physical	22293751
PDS5A_HUMAN	PDS5A	physical	26344197
SMC3_HUMAN	SMC3	physical	26344197
STAG1_HUMAN	STAG1	physical	26344197
WAPL_HUMAN	WAPAL	physical	17113138

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 PDS5B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-1136, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-1162; SER-1166;SER-1176; SER-1182; SER-1191; SER-1257; SER-1283; SER-1358 ANDTHR-1370, AND MASS SPECTROMETRY.	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-1162; SER-1165;SER-1166; SER-1358; SER-1361 AND THR-1370, AND MASS SPECTROMETRY.	19413330 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358 AND THR-1367, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358 AND THR-1370, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1257 AND SER-1383, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"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-1257; SER-1283; SER-1319AND SER-1334, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; SER-1182;SER-1283; THR-1301; SER-1358 AND THR-1370, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166 AND SER-1358, ANDMASS SPECTROMETRY.	15302935 [Abstract]
"Complete sequencing and characterization of 21,243 full-length humancDNAs."; Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; Nat. Genet. 36:40-45(2004). Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).	14702039 [Abstract]