PDS5A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDS5A_HUMAN
• UniProt AC: Q29RF7
• Protein Name: Sister chromatid cohesion protein PDS5 homolog A
• Gene Name: PDS5A {ECO:0000312|HGNC:HGNC:29088}
• Organism: Homo sapiens (Human).
• Sequence Length: 1337
• Subcellular Localization: Nucleus . Associated with chromatin through most of the cell cycle. Dissociates from chromatin in late prophase, reassociates during late telophase.
• Protein Description: Probable 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..
• Protein Sequence: MDFTAQPKPATALCGVVSADGKIAYPPGVKEITDKITTDEMIKRLKMVVKTFMDMDQDSEDEKQQYLPLALHLASEFFLRNPNKDVRLLVACCLADIFRIYAPEAPYTSHDKLKDIFLFITRQLKGLEDTKSPQFNRYFYLLENLAWVKSYNICFELEDCNEIFIQLFRTLFSVINNSHNKKVQMHMLDLMSSIIMEGDGVTQELLDSILINLIPAHKNLNKQSFDLAKVLLKRTVQTIEACIANFFNQVLVLGRSSVSDLSEHVFDLIQELFAIDPHLLLSVMPQLEFKLKSNDGEERLAVVRLLAKLFGSKDSDLATQNRPLWQCFLGRFNDIHVPVRLESVKFASHCLMNHPDLAKDLTEYLKVRSHDPEEAIRHDVIVTIITAAKRDLALVNDQLLGFVRERTLDKRWRVRKEAMMGLAQLYKKYCLHGEAGKEAAEKVSWIKDKLLHIYYQNSIDDKLLVEKIFAQYLVPHNLETEERMKCLYYLYASLDPNAVKALNEMWKCQNMLRSHVRELLDLHKQPTSEANCSAMFGKLMTIAKNLPDPGKAQDFVKKFNQVLGDDEKLRSQLELLISPTCSCKQADICVREIARKLANPKQPTNPFLEMVKFLLERIAPVHIDSEAISALVKLMNKSIEGTADDEEEGVSPDTAIRSGLELLKVLSFTHPTSFHSAETYESLLQCLRMEDDKVAEAAIQIFRNTGHKIETDLPQIRSTLIPILHQKAKRGTPHQAKQAVHCIHAIFTNKEVQLAQIFEPLSRSLNADVPEQLITPLVSLGHISMLAPDQFASPMKSVVANFIVKDLLMNDRSTGEKNGKLWSPDEEVSPEVLAKVQAIKLLVRWLLGMKNNQSKSANSTLRLLSAMLVSEGDLTEQKRISKSDMSRLRLAAGSAIMKLAQEPCYHEIITPEQFQLCALVINDECYQVRQIFAQKLHKALVKLLLPLEYMAIFALCAKDPVKERRAHARQCLLKNISIRREYIKQNPMATEKLLSLLPEYVVPYMIHLLAHDPDFTRSQDVDQLRDIKECLWFMLEVLMTKNENNSHAFMKKMAENIKLTRDAQSPDESKTNEKLYTVCDVALCVINSKSALCNADSPKDPVLPMKFFTQPEKDFCNDKSYISEETRVLLLTGKPKPAGVLGAVNKPLSATGRKPYVRSTGTETGSNINVNSELNPSTGNRSREQSSEAAETGVSENEENPVRIISVTPVKNIDPVKNKEINSDQATQGNISSDRGKKRTVTAAGAENIQQKTDEKVDESGPPAPSKPRRGRRPKSESQGNATKNDDLNKPINKGRKRAAVGQESPGGLEAGNAKAPKLQDLAKKAAPAERQIDLQR

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	-------MDFTAQPK -------CCCCCCCC	41.96	19413330
11	Phosphorylation	TAQPKPATALCGVVS CCCCCCCCEECCEEE	28.79	21406692
18	Phosphorylation	TALCGVVSADGKIAY CEECCEEECCCCEEC	20.45	21406692
30	Ubiquitination	IAYPPGVKEITDKIT EECCCCHHHHHCCCC	49.68	-
35	Acetylation	GVKEITDKITTDEMI CHHHHHCCCCHHHHH	33.05	25953088
35	Ubiquitination	GVKEITDKITTDEMI CHHHHHCCCCHHHHH	33.05	-
38	Phosphorylation	EITDKITTDEMIKRL HHHCCCCHHHHHHHH	33.17	24719451
43	Acetylation	ITTDEMIKRLKMVVK CCHHHHHHHHHHHHH	50.82	25953088
43	Ubiquitination	ITTDEMIKRLKMVVK CCHHHHHHHHHHHHH	50.82	21906983
43 (in isoform 1)	Ubiquitination	-	50.82	21890473
43 (in isoform 3)	Ubiquitination	-	50.82	21890473
50	Ubiquitination	KRLKMVVKTFMDMDQ HHHHHHHHHHHCCCC	25.32	21906983
50 (in isoform 1)	Ubiquitination	-	25.32	21890473
50 (in isoform 3)	Ubiquitination	-	25.32	21890473
51	Phosphorylation	RLKMVVKTFMDMDQD HHHHHHHHHHCCCCC	16.75	22067460
59	Phosphorylation	FMDMDQDSEDEKQQY HHCCCCCCHHHHHHH	41.12	29449344
101	Phosphorylation	LADIFRIYAPEAPYT HHHHHHHHCCCCCCC	16.31	-
107	Phosphorylation	IYAPEAPYTSHDKLK HHCCCCCCCCHHHHH	28.11	-
108	Phosphorylation	YAPEAPYTSHDKLKD HCCCCCCCCHHHHHH	20.66	-
109	Phosphorylation	APEAPYTSHDKLKDI CCCCCCCCHHHHHHH	24.68	-
131	Ubiquitination	LKGLEDTKSPQFNRY CCCCCCCCCCHHHHH	72.90	-
131 (in isoform 1)	Ubiquitination	-	72.90	21890473
131 (in isoform 3)	Ubiquitination	-	72.90	21890473
181	Acetylation	VINNSHNKKVQMHML HHCCCCCHHHHHHHH	49.23	26051181
192	Phosphorylation	MHMLDLMSSIIMEGD HHHHHHHHHHHHCCC	26.19	22067460
193	Phosphorylation	HMLDLMSSIIMEGDG HHHHHHHHHHHCCCC	11.36	22067460
222	Ubiquitination	PAHKNLNKQSFDLAK HHCCCCCHHCCHHHH	50.95	-
229	Acetylation	KQSFDLAKVLLKRTV HHCCHHHHHHHHHHH	40.49	26051181
292	Ubiquitination	PQLEFKLKSNDGEER CCCEEEECCCCHHHH	48.05	21906983
292 (in isoform 1)	Ubiquitination	-	48.05	21890473
292 (in isoform 3)	Ubiquitination	-	48.05	21890473
308	Acetylation	AVVRLLAKLFGSKDS HHHHHHHHHHCCCCH	44.30	25953088
308	Ubiquitination	AVVRLLAKLFGSKDS HHHHHHHHHHCCCCH	44.30	21890473
348	Phosphorylation	LESVKFASHCLMNHP HHHHHHHHHHHHHCH	20.19	23898821
359	Ubiquitination	MNHPDLAKDLTEYLK HHCHHHHHHHHHHHH	61.64	-
364	Phosphorylation	LAKDLTEYLKVRSHD HHHHHHHHHHHHCCC	13.44	-
366	Acetylation	KDLTEYLKVRSHDPE HHHHHHHHHHCCCHH	34.40	23749302
366	Ubiquitination	KDLTEYLKVRSHDPE HHHHHHHHHHCCCHH	34.40	-
366 (in isoform 1)	Ubiquitination	-	34.40	21890473
366 (in isoform 3)	Ubiquitination	-	34.40	21890473
389	Acetylation	VTIITAAKRDLALVN HHHHHHCHHHHHHHC	43.94	30592171
426	Phosphorylation	MMGLAQLYKKYCLHG HHHHHHHHHHHHHHC	8.05	-
427	Acetylation	MGLAQLYKKYCLHGE HHHHHHHHHHHHHCH	45.95	23749302
428	Ubiquitination	GLAQLYKKYCLHGEA HHHHHHHHHHHHCHH	27.86	-
442	Ubiquitination	AGKEAAEKVSWIKDK HHHHHHHHHHHHHHH	36.52	-
449	Acetylation	KVSWIKDKLLHIYYQ HHHHHHHHHHHHHHC	48.20	26051181
462	Acetylation	YQNSIDDKLLVEKIF HCCCCCHHHHHHHHH	39.72	25953088
507	Acetylation	KALNEMWKCQNMLRS HHHHHHHHHHHHHHH	25.32	26051181
507	Ubiquitination	KALNEMWKCQNMLRS HHHHHHHHHHHHHHH	25.32	-
514	Phosphorylation	KCQNMLRSHVRELLD HHHHHHHHHHHHHHH	23.52	29759185
524	Acetylation	RELLDLHKQPTSEAN HHHHHHHHCCCCHHH	66.33	26051181
524	Ubiquitination	RELLDLHKQPTSEAN HHHHHHHHCCCCHHH	66.33	-
541	Phosphorylation	AMFGKLMTIAKNLPD HHHHHHHHHHHCCCC	28.37	24719451
544	Acetylation	GKLMTIAKNLPDPGK HHHHHHHHCCCCCCH	55.99	25953088
544	Ubiquitination	GKLMTIAKNLPDPGK HHHHHHHHCCCCCCH	55.99	-
557	Acetylation	GKAQDFVKKFNQVLG CHHHHHHHHHHHHHC	52.20	23749302
558	Acetylation	KAQDFVKKFNQVLGD HHHHHHHHHHHHHCC	44.22	25953088
558	Ubiquitination	KAQDFVKKFNQVLGD HHHHHHHHHHHHHCC	44.22	-
568	Acetylation	QVLGDDEKLRSQLEL HHHCCHHHHHHHHHH	57.08	26051181
568	Ubiquitination	QVLGDDEKLRSQLEL HHHCCHHHHHHHHHH	57.08	21906983
568 (in isoform 1)	Ubiquitination	-	57.08	21890473
568 (in isoform 3)	Ubiquitination	-	57.08	21890473
601	Ubiquitination	ARKLANPKQPTNPFL HHHHCCCCCCCCHHH	69.58	-
633	Ubiquitination	EAISALVKLMNKSIE HHHHHHHHHHHHCCC	42.75	-
637	Ubiquitination	ALVKLMNKSIEGTAD HHHHHHHHCCCCCCC	38.55	21906983
637 (in isoform 1)	Ubiquitination	-	38.55	21890473
708	Ubiquitination	IFRNTGHKIETDLPQ HHHHCCCCCCCCCHH	43.51	-
727	Acetylation	LIPILHQKAKRGTPH HHHHHHHHHHCCCHH	45.16	25953088
727	Ubiquitination	LIPILHQKAKRGTPH HHHHHHHHHHCCCHH	45.16	-
729	Ubiquitination	PILHQKAKRGTPHQA HHHHHHHHCCCHHHH	59.40	-
762	Phosphorylation	AQIFEPLSRSLNADV HHHHHHHHHHCCCCC	30.45	21712546
793	Phosphorylation	LAPDQFASPMKSVVA CCCHHCCCCCHHHHH	27.15	25159151
805	Acetylation	VVANFIVKDLLMNDR HHHHHHHHHHHHCCC	37.53	26051181
805	Ubiquitination	VVANFIVKDLLMNDR HHHHHHHHHHHHCCC	37.53	-
809	Sulfoxidation	FIVKDLLMNDRSTGE HHHHHHHHCCCCCCC	6.79	21406390
812	Methylation	KDLLMNDRSTGEKNG HHHHHCCCCCCCCCC	30.98	115493395
813	Phosphorylation	DLLMNDRSTGEKNGK HHHHCCCCCCCCCCC	43.56	28509920
814	Phosphorylation	LLMNDRSTGEKNGKL HHHCCCCCCCCCCCC	50.70	28509920
820	Acetylation	STGEKNGKLWSPDEE CCCCCCCCCCCCCCC	57.06	25953088
820	Ubiquitination	STGEKNGKLWSPDEE CCCCCCCCCCCCCCC	57.06	-
823	Phosphorylation	EKNGKLWSPDEEVSP CCCCCCCCCCCCCCH	32.67	27067055
835	Acetylation	VSPEVLAKVQAIKLL CCHHHHHHHHHHHHH	30.62	26051181
835	Ubiquitination	VSPEVLAKVQAIKLL CCHHHHHHHHHHHHH	30.62	-
840	Acetylation	LAKVQAIKLLVRWLL HHHHHHHHHHHHHHH	38.49	26051181
855	Ubiquitination	GMKNNQSKSANSTLR CCCCCCCCCHHHHHH	43.77	-
865	Phosphorylation	NSTLRLLSAMLVSEG HHHHHHHHHHHHCCC	19.07	22067460
870	Phosphorylation	LLSAMLVSEGDLTEQ HHHHHHHCCCCCCCC	31.72	22067460
875	Phosphorylation	LVSEGDLTEQKRISK HHCCCCCCCCCCCCH	40.90	-
882	Acetylation	TEQKRISKSDMSRLR CCCCCCCHHHHHHHH	48.37	11925317
882	Ubiquitination	TEQKRISKSDMSRLR CCCCCCCHHHHHHHH	48.37	-
883	Phosphorylation	EQKRISKSDMSRLRL CCCCCCHHHHHHHHH	31.58	-
886	Phosphorylation	RISKSDMSRLRLAAG CCCHHHHHHHHHHHH	32.90	22210691
894	Phosphorylation	RLRLAAGSAIMKLAQ HHHHHHHHHHHHHHC	15.19	21406692
938	Ubiquitination	IFAQKLHKALVKLLL HHHHHHHHHHHHHHH	54.58	-
949	Phosphorylation	KLLLPLEYMAIFALC HHHHCHHHHHHHHHH	10.26	-
974	Acetylation	HARQCLLKNISIRRE HHHHHHHHHHHHCHH	39.01	19608861
974	Ubiquitination	HARQCLLKNISIRRE HHHHHHHHHHHHCHH	39.01	21890473
977	Phosphorylation	QCLLKNISIRREYIK HHHHHHHHHCHHHHH	21.31	24719451
982	Phosphorylation	NISIRREYIKQNPMA HHHHCHHHHHHCCCH	16.17	24719451
984	Ubiquitination	SIRREYIKQNPMATE HHCHHHHHHCCCHHH	43.02	-
1046	Phosphorylation	MTKNENNSHAFMKKM HHCCCCCCHHHHHHH	27.98	28787133
1058	Ubiquitination	KKMAENIKLTRDAQS HHHHHHCCCCCCCCC	56.22	-
1060	Phosphorylation	MAENIKLTRDAQSPD HHHHCCCCCCCCCCC	22.85	25867546
1065	Phosphorylation	KLTRDAQSPDESKTN CCCCCCCCCCCCCCC	35.72	28985074
1069	Phosphorylation	DAQSPDESKTNEKLY CCCCCCCCCCCCHHH	52.76	23312004
1070	Acetylation	AQSPDESKTNEKLYT CCCCCCCCCCCHHHH	54.01	26051181
1071	Phosphorylation	QSPDESKTNEKLYTV CCCCCCCCCCHHHHH	58.87	23312004
1079	S-nitrosocysteine	NEKLYTVCDVALCVI CCHHHHHHHHHEEEC	2.41	-
1079	S-nitrosylation	NEKLYTVCDVALCVI CCHHHHHHHHHEEEC	2.41	19483679
1084	S-nitrosocysteine	TVCDVALCVINSKSA HHHHHHEEECCCCCC	1.76	-
1084	S-nitrosylation	TVCDVALCVINSKSA HHHHHHEEECCCCCC	1.76	19483679
1090	Phosphorylation	LCVINSKSALCNADS EEECCCCCCCCCCCC	26.71	28450419
1097	Phosphorylation	SALCNADSPKDPVLP CCCCCCCCCCCCCCC	31.29	23401153
1099	Acetylation	LCNADSPKDPVLPMK CCCCCCCCCCCCCCC	77.83	26051181
1105	Sulfoxidation	PKDPVLPMKFFTQPE CCCCCCCCCEECCCC	5.31	21406390
1106	Acetylation	KDPVLPMKFFTQPEK CCCCCCCCEECCCCH	35.07	-
1106	Ubiquitination	KDPVLPMKFFTQPEK CCCCCCCCEECCCCH	35.07	-
1113	Acetylation	KFFTQPEKDFCNDKS CEECCCCHHCCCCCC	63.89	23749302
1113	Ubiquitination	KFFTQPEKDFCNDKS CEECCCCHHCCCCCC	63.89	-
1119	Acetylation	EKDFCNDKSYISEET CHHCCCCCCCCCCCC	31.03	26051181
1119	Ubiquitination	EKDFCNDKSYISEET CHHCCCCCCCCCCCC	31.03	-
1120	Phosphorylation	KDFCNDKSYISEETR HHCCCCCCCCCCCCE	30.48	28555341
1134	Acetylation	RVLLLTGKPKPAGVL EEEEECCCCCCCCEE	44.63	25953088
1134	Ubiquitination	RVLLLTGKPKPAGVL EEEEECCCCCCCCEE	44.63	-
1136	Ubiquitination	LLLTGKPKPAGVLGA EEECCCCCCCCEECC	51.49	-
1146	Acetylation	GVLGAVNKPLSATGR CEECCCCCCCCCCCC	40.51	19608861
1146	Ubiquitination	GVLGAVNKPLSATGR CEECCCCCCCCCCCC	40.51	-
1149	Phosphorylation	GAVNKPLSATGRKPY CCCCCCCCCCCCCCC	32.10	29978859
1151	Phosphorylation	VNKPLSATGRKPYVR CCCCCCCCCCCCCEE	33.86	29978859
1159	Phosphorylation	GRKPYVRSTGTETGS CCCCCEECCCCCCCC	22.57	25159151
1160	Phosphorylation	RKPYVRSTGTETGSN CCCCEECCCCCCCCC	37.24	25159151
1162	Phosphorylation	PYVRSTGTETGSNIN CCEECCCCCCCCCCC	30.38	25159151
1164	Phosphorylation	VRSTGTETGSNINVN EECCCCCCCCCCCCC	45.83	23186163
1166	Phosphorylation	STGTETGSNINVNSE CCCCCCCCCCCCCCC	41.79	18669648
1172	Phosphorylation	GSNINVNSELNPSTG CCCCCCCCCCCCCCC	38.90	23312004
1177	Phosphorylation	VNSELNPSTGNRSRE CCCCCCCCCCCCCHH	48.12	21712546
1178	Phosphorylation	NSELNPSTGNRSREQ CCCCCCCCCCCCHHH	39.47	21712546
1182	Phosphorylation	NPSTGNRSREQSSEA CCCCCCCCHHHHHHH	44.14	28176443
1186	Phosphorylation	GNRSREQSSEAAETG CCCCHHHHHHHHHHC	25.95	28176443
1187	Phosphorylation	NRSREQSSEAAETGV CCCHHHHHHHHHHCC	30.83	28176443
1192	Phosphorylation	QSSEAAETGVSENEE HHHHHHHHCCCCCCC	37.85	28176443
1195	Phosphorylation	EAAETGVSENEENPV HHHHHCCCCCCCCCE	35.73	29255136
1206	Phosphorylation	ENPVRIISVTPVKNI CCCEEEEEEEECCCC	19.98	30266825
1208	Phosphorylation	PVRIISVTPVKNIDP CEEEEEEEECCCCCC	18.64	29255136
1211	Acetylation	IISVTPVKNIDPVKN EEEEEECCCCCCCCC	49.76	19608861
1211	Ubiquitination	IISVTPVKNIDPVKN EEEEEECCCCCCCCC	49.76	21890473
1219	Acetylation	NIDPVKNKEINSDQA CCCCCCCCCCCCCCC	55.01	23749302
1219	Ubiquitination	NIDPVKNKEINSDQA CCCCCCCCCCCCCCC	55.01	2190698
1219 (in isoform 1)	Ubiquitination	-	55.01	21890473
1223	Phosphorylation	VKNKEINSDQATQGN CCCCCCCCCCCCCCC	36.44	21815630
1227	Phosphorylation	EINSDQATQGNISSD CCCCCCCCCCCCCCH	31.23	25262027
1232	Phosphorylation	QATQGNISSDRGKKR CCCCCCCCCHHCCCC	30.13	25159151
1233	Phosphorylation	ATQGNISSDRGKKRT CCCCCCCCHHCCCCE	27.77	25159151
1235	Methylation	QGNISSDRGKKRTVT CCCCCCHHCCCCEEE	61.86	115386725
1240	Phosphorylation	SDRGKKRTVTAAGAE CHHCCCCEEEHHCHH	30.96	29759185
1242	Phosphorylation	RGKKRTVTAAGAENI HCCCCEEEHHCHHHH	15.35	29759185
1253	Phosphorylation	AENIQQKTDEKVDES HHHHHHHHCCCCCCC	45.08	29759185
1256	Acetylation	IQQKTDEKVDESGPP HHHHHCCCCCCCCCC	58.77	26051181
1260	Phosphorylation	TDEKVDESGPPAPSK HCCCCCCCCCCCCCC	52.73	28555341
1266	Phosphorylation	ESGPPAPSKPRRGRR CCCCCCCCCCCCCCC	58.35	25867546
1267	Acetylation	SGPPAPSKPRRGRRP CCCCCCCCCCCCCCC	41.29	23749302
1276	Phosphorylation	RRGRRPKSESQGNAT CCCCCCCCCCCCCCC	45.20	26657352
1278	Phosphorylation	GRRPKSESQGNATKN CCCCCCCCCCCCCCC	50.94	28450419
1283	Phosphorylation	SESQGNATKNDDLNK CCCCCCCCCCCCCCC	34.09	28176443
1284	Acetylation	ESQGNATKNDDLNKP CCCCCCCCCCCCCCC	56.84	26051181
1290	Acetylation	TKNDDLNKPINKGRK CCCCCCCCCCCCCCC	55.35	19608861
1294	Acetylation	DLNKPINKGRKRAAV CCCCCCCCCCCCCCC	61.89	133681
1305	Phosphorylation	RAAVGQESPGGLEAG CCCCCCCCCCCHHCC	22.43	19664994
1315	Acetylation	GLEAGNAKAPKLQDL CHHCCCCCCHHHHHH	70.04	25953088
1315	Ubiquitination	GLEAGNAKAPKLQDL CHHCCCCCCHHHHHH	70.04	-
1318	Acetylation	AGNAKAPKLQDLAKK CCCCCCHHHHHHHHH	64.74	25953088

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

Oops, there are no upstream regulatory protein records of PDS5A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDS5A_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PDS5A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAG1_HUMAN	STAG1	physical	11076961
STAG2_HUMAN	STAG2	physical	11076961
RAD21_HUMAN	RAD21	physical	17113138
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
PDS5B_HUMAN	PDS5B	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
WAPL_HUMAN	WAPAL	physical	21111234
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.

Related Literatures of Post-Translational Modification

Acetylation

"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 SER-1305, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-974; LYS-1146; LYS-1211 ANDLYS-1290, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-1195 AND SER-1305, ANDMASS SPECTROMETRY.
PubMed: 19690332

"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 SER-1305, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-1195; THR-1208 ANDSER-1305, AND MASS SPECTROMETRY.
PubMed: 18669648

"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 THR-1208; SER-1232 ANDSER-1305, AND MASS SPECTROMETRY.
PubMed: 18691976

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND MASSSPECTROMETRY.
PubMed: 19007248

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND MASSSPECTROMETRY.
PubMed: 17924679

"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 THR-1208 AND SER-1305, ANDMASS SPECTROMETRY.
PubMed: 16964243

"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-1305, AND MASSSPECTROMETRY.
PubMed: 17081983

"The status, quality, and expansion of the NIH full-length cDNAproject: the Mammalian Gene Collection (MGC).";
-
Genome Res. 14:2121-2127(2004).
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed: 15489334