dbPTM

RAD50_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAD50_HUMAN
UniProt AC	Q92878
Protein Name	DNA repair protein RAD50
Gene Name	RAD50
Organism	Homo sapiens (Human).
Sequence Length	1312
Subcellular Localization	Nucleus . Chromosome, telomere . Localizes to discrete nuclear foci after treatment with genotoxic agents.
Protein Description	Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point. [PubMed: 11741547]
Protein Sequence	MSRIEKMSILGVRSFGIEDKDKQIITFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRLQFRDVNGELIAVQRSMVCTQKSKKTEFKTLEGVITRTKHGEKVSLSSKCAEIDREMISSLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVKEYQMELKYLKQYKEKACEIRDQITSKEAQLTSSKEIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALDSRKKQMEKDNSELEEKMEKVFQGTDEQLNDLYHNHQRTVREKERKLVDCHRELEKLNKESRLLNQEKSELLVEQGRLQLQADRHQEHIRARDSLIQSLATQLELDGFERGPFSERQIKNFHKLVRERQEGEAKTANQLMNDFAEKETLKQKQIDEIRDKKTGLGRIIELKSEILSKKQNELKNVKYELQQLEGSSDRILELDQELIKAERELSKAEKNSNVETLKMEVISLQNEKADLDRTLRKLDQEMEQLNHHTTTRTQMEMLTKDKADKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASSEQNKNHINNELKRKEEQLSSYEDKLFDVCGSQDFESDLDRLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLVPMRQSIIDLKEKEIPELRNKLQNVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGIDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSTTNELKSEKLQISTNLQRRQQLEEQTVELSTEVQSLYREIKDAKEQVSPLETTLEKFQQEKEELINKKNTSNKIAQDKLNDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNKVIAQLSECEKHKEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRNEELKEVEEERKQHLKEMGQMQVLQMKSEHQKLEENIDNIKRNHNLALGRQKGYEEEIIHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRIKKNIDQCSEIVKCSVSSLGFNVH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5 (in isoform 2)	Phosphorylation	-	41.41	27794612
6	Ubiquitination	--MSRIEKMSILGVR --CCHHHHCCCCEEE	35.26	-
6	Malonylation	--MSRIEKMSILGVR --CCHHHHCCCCEEE	35.26	26320211
6	Acetylation	--MSRIEKMSILGVR --CCHHHHCCCCEEE	35.26	25953088
20	Methylation	RSFGIEDKDKQIITF ECCCCCCCCCCEEEE	54.77	23644510
36 (in isoform 3)	Ubiquitination	-	13.40	21890473
48 (in isoform 3)	Ubiquitination	-	2.53	21890473
51	Phosphorylation	TIIECLKYICTGDFP HHHHHHHHHHHCCCC	6.57	21406692
54	Phosphorylation	ECLKYICTGDFPPGT HHHHHHHHCCCCCCC	30.17	21406692
61	Phosphorylation	TGDFPPGTKGNTFVH HCCCCCCCCCCCCCC	41.37	21406692
62	Ubiquitination	GDFPPGTKGNTFVHD CCCCCCCCCCCCCCC	56.96	21890473
62 (in isoform 1)	Ubiquitination	-	56.96	21890473
68 (in isoform 2)	Ubiquitination	-	41.27	21890473
71	Ubiquitination	NTFVHDPKVAQETDV CCCCCCCCCCCCCCC	57.15	-
71	Acetylation	NTFVHDPKVAQETDV CCCCCCCCCCCCCCC	57.15	26051181
72 (in isoform 3)	Ubiquitination	-	8.93	21890473
91 (in isoform 3)	Ubiquitination	-	30.82	21890473
103 (in isoform 3)	Ubiquitination	-	27.85	21890473
108	Acetylation	VCTQKSKKTEFKTLE HCCCCCCCCCCEEEE	61.45	25953088
112	Ubiquitination	KSKKTEFKTLEGVIT CCCCCCCEEEEEEEE	46.07	-
112	Acetylation	KSKKTEFKTLEGVIT CCCCCCCEEEEEEEE	46.07	25953088
125 (in isoform 3)	Acetylation	-	50.43	-
126	Ubiquitination	TRTKHGEKVSLSSKC ECCCCCCEEECCHHH	41.54	-
128	Phosphorylation	TKHGEKVSLSSKCAE CCCCCEEECCHHHHH	33.33	21712546
130	Phosphorylation	HGEKVSLSSKCAEID CCCEEECCHHHHHHC	21.90	21712546
132	Ubiquitination	EKVSLSSKCAEIDRE CEEECCHHHHHHCHH	33.80	-
156 (in isoform 3)	Ubiquitination	-	2.37	21890473
170	Acetylation	NWPLSEGKALKQKFD CCCCCCCHHHHHHHH	46.63	26051181
175	Ubiquitination	EGKALKQKFDEIFSA CCHHHHHHHHHHHHH	53.87	21890473
175	Acetylation	EGKALKQKFDEIFSA CCHHHHHHHHHHHHH	53.87	27452117
175 (in isoform 1)	Ubiquitination	-	53.87	21890473
181 (in isoform 2)	Ubiquitination	-	34.10	21890473
187	Ubiquitination	FSATRYIKALETLRQ HHHHHHHHHHHHHHH	37.67	21890473
187 (in isoform 1)	Ubiquitination	-	37.67	21890473
193	Methylation	IKALETLRQVRQTQG HHHHHHHHHHHHHCC	40.13	115490107
193 (in isoform 2)	Ubiquitination	-	40.13	21890473
198	Phosphorylation	TLRQVRQTQGQKVKE HHHHHHHHCCHHHHH	24.89	-
204	Malonylation	QTQGQKVKEYQMELK HHCCHHHHHHHHHHH	58.71	32601280
204	Acetylation	QTQGQKVKEYQMELK HHCCHHHHHHHHHHH	58.71	26051181
206	Phosphorylation	QGQKVKEYQMELKYL CCHHHHHHHHHHHHH	13.87	30177828
211	Ubiquitination	KEYQMELKYLKQYKE HHHHHHHHHHHHHHH	34.92	21890473
211	Acetylation	KEYQMELKYLKQYKE HHHHHHHHHHHHHHH	34.92	26051181
211 (in isoform 1)	Ubiquitination	-	34.92	21890473
212	Phosphorylation	EYQMELKYLKQYKEK HHHHHHHHHHHHHHH	31.58	30177828
217 (in isoform 2)	Ubiquitination	-	50.69	21890473
217	Ubiquitination	LKYLKQYKEKACEIR HHHHHHHHHHHHHHH	50.69	-
230	Ubiquitination	IRDQITSKEAQLTSS HHHHHCCCHHHHCCC	48.71	21906983
230	Acetylation	IRDQITSKEAQLTSS HHHHHCCCHHHHCCC	48.71	26051181
230 (in isoform 1)	Ubiquitination	-	48.71	21890473
236 (in isoform 2)	Ubiquitination	-	48.26	21890473
238	Ubiquitination	EAQLTSSKEIVKSYE HHHHCCCHHHHHHHH	51.75	-
242	Ubiquitination	TSSKEIVKSYENELD CCCHHHHHHHHHCCH	53.64	21906983
242 (in isoform 1)	Ubiquitination	-	53.64	21890473
248 (in isoform 2)	Ubiquitination	-	14.33	21890473
252	Ubiquitination	ENELDPLKNRLKEIE HHCCHHHHHHHHHHH	45.47	-
252	Acetylation	ENELDPLKNRLKEIE HHCCHHHHHHHHHHH	45.47	26051181
256	Ubiquitination	DPLKNRLKEIEHNLS HHHHHHHHHHHHHHH	54.10	-
256	Acetylation	DPLKNRLKEIEHNLS HHHHHHHHHHHHHHH	54.10	26051181
263	Phosphorylation	KEIEHNLSKIMKLDN HHHHHHHHHHHHHHH	26.00	25159151
264	Acetylation	EIEHNLSKIMKLDNE HHHHHHHHHHHHHHH	50.41	23236377
264	Malonylation	EIEHNLSKIMKLDNE HHHHHHHHHHHHHHH	50.41	26320211
267	Acetylation	HNLSKIMKLDNEIKA HHHHHHHHHHHHHHH	57.04	25953088
273	Ubiquitination	MKLDNEIKALDSRKK HHHHHHHHHHHHHHH	36.40	-
280	Ubiquitination	KALDSRKKQMEKDNS HHHHHHHHHHHHCCH	54.49	-
284	Acetylation	SRKKQMEKDNSELEE HHHHHHHHCCHHHHH	57.79	26051181
295	Ubiquitination	ELEEKMEKVFQGTDE HHHHHHHHHHCCCHH	44.87	21890473
295 (in isoform 1)	Ubiquitination	-	44.87	21890473
301 (in isoform 2)	Ubiquitination	-	48.76	21890473
308	Phosphorylation	DEQLNDLYHNHQRTV HHHHHHHHHHHHHHH	11.93	-
322 (in isoform 3)	Ubiquitination	-	5.00	21890473
336	Phosphorylation	LEKLNKESRLLNQEK HHHHHHHHHHHCHHH	29.82	29978859
343	Ubiquitination	SRLLNQEKSELLVEQ HHHHCHHHHHHHHHH	39.19	-
343	Acetylation	SRLLNQEKSELLVEQ HHHHCHHHHHHHHHH	39.19	26051181
359	Methylation	RLQLQADRHQEHIRA CHHHHHHHHHHHHHH	36.08	115490123
397 (in isoform 3)	Phosphorylation	-	31.75	-
398	Acetylation	RQIKNFHKLVRERQE HHHHHHHHHHHHHHH	44.53	25953088
418 (in isoform 3)	Phosphorylation	-	8.86	-
421 (in isoform 3)	Phosphorylation	-	53.20	-
446	Ubiquitination	LGRIIELKSEILSKK CHHHHHHHHHHHHHH	33.00	-
446	Acetylation	LGRIIELKSEILSKK CHHHHHHHHHHHHHH	33.00	26051181
453	Acetylation	KSEILSKKQNELKNV HHHHHHHHHHHHHHH	55.79	7823307
461	Acetylation	QNELKNVKYELQQLE HHHHHHHHHHHHHHC	42.26	25953088
461	Ubiquitination	QNELKNVKYELQQLE HHHHHHHHHHHHHHC	42.26	21890473
461	Malonylation	QNELKNVKYELQQLE HHHHHHHHHHHHHHC	42.26	26320211
461 (in isoform 1)	Ubiquitination	-	42.26	21890473
467 (in isoform 2)	Ubiquitination	-	5.33	21890473
470	Phosphorylation	ELQQLEGSSDRILEL HHHHHCCCCHHHHHH	21.49	25849741
471	Phosphorylation	LQQLEGSSDRILELD HHHHCCCCHHHHHHH	41.59	30266825
473	Methylation	QLEGSSDRILELDQE HHCCCCHHHHHHHHH	37.02	115490131
483	Ubiquitination	ELDQELIKAERELSK HHHHHHHHHHHHHHH	57.74	-
483	Acetylation	ELDQELIKAERELSK HHHHHHHHHHHHHHH	57.74	26051181
493	Acetylation	RELSKAEKNSNVETL HHHHHHHHCCCHHHH	71.22	25953088
496 (in isoform 3)	Phosphorylation	-	45.07	-
501 (in isoform 3)	Phosphorylation	-	40.20	-
501	Acetylation	NSNVETLKMEVISLQ CCCHHHHHHEEHHHH	40.20	26051181
520	Ubiquitination	DLDRTLRKLDQEMEQ HHHHHHHHHHHHHHH	60.57	-
536	Phosphorylation	NHHTTTRTQMEMLTK HCCCCHHHHHHHHHC	30.12	20068231
542	Phosphorylation	RTQMEMLTKDKADKD HHHHHHHHCCCCCHH	35.57	20068231
551 (in isoform 3)	Phosphorylation	-	51.42	-
557	Phosphorylation	EQIRKIKSRHSDELT HHHHHHHHHCHHHHH	38.40	20068231
560	Phosphorylation	RKIKSRHSDELTSLL HHHHHHCHHHHHHHH	31.50	20068231
564	Phosphorylation	SRHSDELTSLLGYFP HHCHHHHHHHHCCCC	18.45	20068231
573	Acetylation	LLGYFPNKKQLEDWL HHCCCCCHHHHHHHH	41.98	26051181
585	Acetylation	DWLHSKSKEINQTRD HHHHHCCHHHHHHHH	67.37	23749302
599	Ubiquitination	DRLAKLNKELASSEQ HHHHHHHHHHHCCHH	65.62	-
616	Ubiquitination	NHINNELKRKEEQLS HHHHHHHHHHHHHHH	56.07	-
623	Phosphorylation	KRKEEQLSSYEDKLF HHHHHHHHHHHHHHH	30.48	-
624	Phosphorylation	RKEEQLSSYEDKLFD HHHHHHHHHHHHHHH	40.93	-
635	Phosphorylation	KLFDVCGSQDFESDL HHHHHHCCCCHHHHH	22.81	29255136
640	Phosphorylation	CGSQDFESDLDRLKE HCCCCHHHHHHHHHH	43.39	22617229
690	Phosphorylation	VCQRVFQTEAELQEV HHHHHHHCHHHHHHH	26.21	19664994
699	Phosphorylation	AELQEVISDLQSKLR HHHHHHHHHHHHHHC	37.13	24732914
703	O-linked_Glycosylation	EVISDLQSKLRLAPD HHHHHHHHHHCCCHH	40.74	30379171
706 (in isoform 3)	Ubiquitination	-	32.32	21890473
711	Acetylation	KLRLAPDKLKSTESE HHCCCHHHHHCCHHH	57.67	25953088
713	Malonylation	RLAPDKLKSTESELK CCCHHHHHCCHHHHH	62.16	26320211
743	Ubiquitination	RQSIIDLKEKEIPEL CHHHHHCCCCCHHHH	64.09	-
753	Ubiquitination	EIPELRNKLQNVNRD CHHHHHHHHHHHHHH	45.04	-
753	Acetylation	EIPELRNKLQNVNRD CHHHHHHHHHHHHHH	45.04	25953088
773	Phosphorylation	NDIEEQETLLGTIMP HHHHHHHHHHCCCCC	27.29	29759185
777	Phosphorylation	EQETLLGTIMPEEES HHHHHHCCCCCHHHH	17.67	29759185
797	Dimethylation	TDVTIMERFQMELKD CCHHHHHHHHHHHHH	15.09	-
797	Methylation	TDVTIMERFQMELKD CCHHHHHHHHHHHHH	15.09	18963897
803	Acetylation	ERFQMELKDVERKIA HHHHHHHHHHHHHHH	46.55	26051181
808	Acetylation	ELKDVERKIAQQAAK HHHHHHHHHHHHHHH	28.96	25953088
815	Acetylation	KIAQQAAKLQGIDLD HHHHHHHHHCCCCHH	44.34	23236377
815	Malonylation	KIAQQAAKLQGIDLD HHHHHHHHHCCCCHH	44.34	26320211
820 (in isoform 3)	Acetylation	-	49.71	-
823	Methylation	LQGIDLDRTVQQVNQ HCCCCHHHHHHHHHH	44.06	115490115
824	Phosphorylation	QGIDLDRTVQQVNQE CCCCHHHHHHHHHHH	23.49	20873877
832	Acetylation	VQQVNQEKQEKQHKL HHHHHHHHHHHHHHH	54.73	26051181
838	Ubiquitination	EKQEKQHKLDTVSSK HHHHHHHHHHHHHHH	45.63	-
845	Ubiquitination	KLDTVSSKIELNRKL HHHHHHHHHHHHHHH	32.47	21890473
845 (in isoform 1)	Ubiquitination	-	32.47	21890473
851 (in isoform 2)	Ubiquitination	-	49.20	21890473
851	Ubiquitination	SKIELNRKLIQDQQE HHHHHHHHHHHHHHH	49.20	-
864	Ubiquitination	QEQIQHLKSTTNELK HHHHHHHHHHHHHHH	43.56	-
878	Phosphorylation	KSEKLQISTNLQRRQ HHHHHHHCHHHHHHH	9.78	23403867
879	Phosphorylation	SEKLQISTNLQRRQQ HHHHHHCHHHHHHHH	41.39	23403867
900	O-linked_Glycosylation	ELSTEVQSLYREIKD HHHHHHHHHHHHHHH	32.32	30379171
921	Ubiquitination	PLETTLEKFQQEKEE CHHHHHHHHHHHHHH	52.14	-
926	Acetylation	LEKFQQEKEELINKK HHHHHHHHHHHHCCC	52.75	26051181
932	Acetylation	EKEELINKKNTSNKI HHHHHHCCCCCCCHH	40.17	25953088
935	Phosphorylation	ELINKKNTSNKIAQD HHHCCCCCCCHHHHH	42.42	26074081
936	Phosphorylation	LINKKNTSNKIAQDK HHCCCCCCCHHHHHH	45.58	26074081
948	Acetylation	QDKLNDIKEKVKNIH HHHHHHHHHHHHHHH	55.11	26051181
959	Acetylation	KNIHGYMKDIENYIQ HHHHHHHHHHHHHHH	47.25	19608861
964	Phosphorylation	YMKDIENYIQDGKDD HHHHHHHHHHCCCCH	6.28	-
980 (in isoform 3)	Ubiquitination	-	11.11	21890473
982	Ubiquitination	QKETELNKVIAQLSE HHHHHHHHHHHHHHH	47.87	-
987 (in isoform 3)	Ubiquitination	-	3.26	21890473
988	Phosphorylation	NKVIAQLSECEKHKE HHHHHHHHHHHHHHH	28.28	29514088
992	Acetylation	AQLSECEKHKEKINE HHHHHHHHHHHHHHH	72.18	27452117
995 (in isoform 3)	Ubiquitination	-	59.91	21890473
1023	Phosphorylation	RWLQDNLTLRKRNEE HHHHHHCCHHHHHHH	30.67	24719451
1032	Acetylation	RKRNEELKEVEEERK HHHHHHHHHHHHHHH	64.09	12650513
1051 (in isoform 3)	Ubiquitination	-	2.01	21890473
1059	Ubiquitination	QMKSEHQKLEENIDN HHHHHHHHHHHHHHH	60.83	-
1059	Acetylation	QMKSEHQKLEENIDN HHHHHHHHHHHHHHH	60.83	26051181
1068	Ubiquitination	EENIDNIKRNHNLAL HHHHHHHHHHHCHHH	54.09	-
1068	Acetylation	EENIDNIKRNHNLAL HHHHHHHHHHHCHHH	54.09	26051181
1089	Ubiquitination	EEEIIHFKKELREPQ HHHHHHHHHHHCCCC	31.04	-
1089	Acetylation	EEEIIHFKKELREPQ HHHHHHHHHHHCCCC	31.04	25953088
1113	Phosphorylation	EMMIVMRTTELVNKD HHHHHHHHHHHHCCC	13.41	22817900
1114	Phosphorylation	MMIVMRTTELVNKDL HHHHHHHHHHHCCCC	19.56	22817900
1119	Ubiquitination	RTTELVNKDLDIYYK HHHHHHCCCCHHHHH	52.79	21890473
1119	Acetylation	RTTELVNKDLDIYYK HHHHHHCCCCHHHHH	52.79	26051181
1119 (in isoform 1)	Ubiquitination	-	52.79	21890473
1125	Phosphorylation	NKDLDIYYKTLDQAI CCCCHHHHHHHHHHH	9.61	22817900
1125 (in isoform 2)	Ubiquitination	-	9.61	21890473
1126	Ubiquitination	KDLDIYYKTLDQAIM CCCHHHHHHHHHHHH	26.16	21906983
1126 (in isoform 1)	Ubiquitination	-	26.16	21890473
1127	Phosphorylation	DLDIYYKTLDQAIMK CCHHHHHHHHHHHHH	21.31	20068231
1132 (in isoform 2)	Ubiquitination	-	2.28	21890473
1134	Ubiquitination	TLDQAIMKFHSMKME HHHHHHHHHHCCCHH	33.54	21890473
1134 (in isoform 1)	Ubiquitination	-	33.54	21890473
1140 (in isoform 2)	Ubiquitination	-	4.12	21890473
1145	Ubiquitination	MKMEEINKIIRDLWR CCHHHHHHHHHHHHH	45.21	-
1146 (in isoform 3)	Acetylation	-	2.43	-
1146 (in isoform 3)	Ubiquitination	-	2.43	21890473
1153	Phosphorylation	IIRDLWRSTYRGQDI HHHHHHHHHCCCCCC	20.43	30576142
1155	Phosphorylation	RDLWRSTYRGQDIEY HHHHHHHCCCCCCEE	17.62	30576142
1162	Phosphorylation	YRGQDIEYIEIRSDA CCCCCCEEEEEECCC	12.27	-
1167	Phosphorylation	IEYIEIRSDADENVS CEEEEEECCCCCCCC	42.69	30576142
1174	Phosphorylation	SDADENVSASDKRRN CCCCCCCCHHHCCCC	33.37	30576142
1178	Ubiquitination	ENVSASDKRRNYNYR CCCCHHHCCCCCCEE	51.25	-
1190	Ubiquitination	NYRVVMLKGDTALDM CEEEEEEECCCCCCC	36.32	21906983
1190 (in isoform 1)	Ubiquitination	-	36.32	21890473
1196 (in isoform 2)	Ubiquitination	-	23.44	21890473
1202	Phosphorylation	LDMRGRCSAGQKVLA CCCCCCCCHHHHHHH	33.79	28258704
1285	Acetylation	GRSEYVEKFYRIKKN CCHHHHHHHHHHHCC	37.34	23954790
1285	Ubiquitination	GRSEYVEKFYRIKKN CCHHHHHHHHHHHCC	37.34	19608861
1285	Malonylation	GRSEYVEKFYRIKKN CCHHHHHHHHHHHCC	37.34	26320211
1285 (in isoform 1)	Ubiquitination	-	37.34	21890473
1291 (in isoform 2)	Ubiquitination	-	57.68	21890473
1291	Ubiquitination	EKFYRIKKNIDQCSE HHHHHHHCCHHHHHH	57.68	-
1291	Acetylation	EKFYRIKKNIDQCSE HHHHHHHCCHHHHHH	57.68	26051181
1297	Phosphorylation	KKNIDQCSEIVKCSV HCCHHHHHHHHHHHH	25.40	20873877
1301	Ubiquitination	DQCSEIVKCSVSSLG HHHHHHHHHHHHHCC	26.84	-
1301	Acetylation	DQCSEIVKCSVSSLG HHHHHHHHHHHHHCC	26.84	26051181
1306	Phosphorylation	IVKCSVSSLGFNVH- HHHHHHHHCCCCCC-	30.29	27134283

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
635	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAD50_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 RAD50_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BLM_HUMAN	BLM	physical	10783165
MRE11_HUMAN	MRE11A	physical	11504724
ATM_HUMAN	ATM	physical	10783165
MLH1_HUMAN	MLH1	physical	10783165
MSH2_HUMAN	MSH2	physical	10783165
MSH6_HUMAN	MSH6	physical	10783165
RFC1_HUMAN	RFC1	physical	10783165
MRE11_HUMAN	MRE11A	physical	8756642
RINT1_HUMAN	RINT1	physical	11096100
MRE11_HUMAN	MRE11A	physical	9705271
NBN_HUMAN	NBN	physical	9705271
MDC1_HUMAN	MDC1	physical	12607003
MRE11_HUMAN	MRE11A	physical	12607003
NBN_HUMAN	NBN	physical	12607003
MRE11_HUMAN	MRE11A	physical	17500065
NBN_HUMAN	NBN	physical	17500065
GEMI2_HUMAN	GEMIN2	physical	20403813
DCR1B_HUMAN	DCLRE1B	physical	18469862
BRCA1_HUMAN	BRCA1	physical	16391231
NBN_HUMAN	NBN	physical	16391231
MRE11_HUMAN	MRE11A	physical	16391231
CTIP_HUMAN	RBBP8	physical	16391231
NBN_HUMAN	NBN	physical	15734743
MRE11_HUMAN	MRE11A	physical	15734743
TE2IP_HUMAN	TERF2IP	physical	22939629
TERF2_HUMAN	TERF2	physical	22939629
RBL2_HUMAN	RBL2	physical	16600870
RNF8_HUMAN	RNF8	physical	23115235
ILF2_HUMAN	ILF2	physical	20808282
MCM5_HUMAN	MCM5	physical	20808282
ILF3_HUMAN	ILF3	physical	20808282
BLM_HUMAN	BLM	physical	25084169
BRCA1_HUMAN	BRCA1	physical	25084169
CHAP1_HUMAN	CHAMP1	physical	26344197
SMC5_HUMAN	SMC5	physical	26344197
H31T_HUMAN	HIST3H3	physical	25823024
RAD50_HUMAN	RAD50	physical	28134932
CF161_HUMAN	C15orf26	physical	27173435
MRE11_HUMAN	MRE11A	physical	27173435
CC150_HUMAN	CCDC150	physical	27173435
FANCJ_HUMAN	BRIP1	physical	23530059
MRE11_HUMAN	MRE11A	physical	23530059
NBN_HUMAN	NBN	physical	23530059
SPTA1_HUMAN	SPTA1	physical	16889989
MCM9_HUMAN	MCM9	physical	26215093
MCM8_HUMAN	MCM8	physical	26215093
NBN_HUMAN	NBN	physical	26215093
MRE11_HUMAN	MRE11A	physical	26215093

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613078	Nijmegen breakage syndrome-like disorder (NBSLD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RAD50_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-959 AND LYS-1285, AND MASSSPECTROMETRY.	19608861 [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-635 AND THR-690, ANDMASS SPECTROMETRY.	18669648 [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-635, AND MASSSPECTROMETRY.	17525332 [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-635 AND SER-640, ANDMASS SPECTROMETRY.	17081983 [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-635 AND THR-690, ANDMASS SPECTROMETRY.	15302935 [Abstract]
"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 THR-690, AND MASSSPECTROMETRY.	19690332 [Abstract]