UIMC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UIMC1_HUMAN
• UniProt AC: Q96RL1
• Protein Name: BRCA1-A complex subunit RAP80
• Gene Name: UIMC1
• Organism: Homo sapiens (Human).
• Sequence Length: 719
• Subcellular Localization: Nucleus . Localizes at sites of DNA damage at double-strand breaks (DSBs).
• Protein Description: Ubiquitin-binding protein. [PubMed: 24627472 Specifically recognizes and binds 'Lys-63'-linked ubiquitin]
• Protein Sequence: MPRRKKKVKEVSESRNLEKKDVETTSSVSVKRKRRLEDAFIVISDSDGEEPKEENGLQKTKTKQSNRAKCLAKRKIAQMTEEEQFALALKMSEQEAREVNSQEEEEEELLRKAIAESLNSCRPSDASATRSRPLATGPSSQSHQEKTTDSGLTEGIWQLVPPSLFKGSHISQGNEAEEREEPWDHTEKTEEEPVSGSSGSWDQSSQPVFENVNVKSFDRCTGHSAEHTQCGKPQESTGRGSAFLKAVQGSGDTSRHCLPTLADAKGLQDTGGTVNYFWGIPFCPDGVDPNQYTKVILCQLEVYQKSLKMAQRQLLNKKGFGEPVLPRPPSLIQNECGQGEQASEKNECISEDMGDEDKEERQESRASDWHSKTKDFQESSIKSLKEKLLLEEEPTTSHGQSSQGIVEETSEEGNSVPASQSVAALTSKRSLVLMPESSAEEITVCPETQLSSSETFDLEREVSPGSRDILDGVRIIMADKEVGNKEDAEKEVAISTFSSSNQVSCPLCDQCFPPTKIERHAMYCNGLMEEDTVLTRRQKEAKTKSDSGTAAQTSLDIDKNEKCYLCKSLVPFREYQCHVDSCLQLAKADQGDGPEGSGRACSTVEGKWQQRLKNPKEKGHSEGRLLSFLEQSEHKTSDADIKSSETGAFRVPSPGMEEAGCSREMQSSFTRRDLNESPVKSFVSISEATDCLVDFKKQVTVQPGSRTRTKAGRGRRRKF

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
9	Sumoylation	PRRKKKVKEVSESRN CCCHHHHHHHHHHCC	62.37	-
9	Sumoylation	PRRKKKVKEVSESRN CCCHHHHHHHHHHCC	62.37	-
9	Ubiquitination	PRRKKKVKEVSESRN CCCHHHHHHHHHHCC	62.37	21906983
9 (in isoform 1)	Ubiquitination	-	62.37	21890473
9 (in isoform 2)	Ubiquitination	-	62.37	21890473
9 (in isoform 5)	Ubiquitination	-	62.37	21890473
12	Phosphorylation	KKKVKEVSESRNLEK HHHHHHHHHHCCCCC	30.83	25159151
19	Ubiquitination	SESRNLEKKDVETTS HHHCCCCCCCCCCCC	58.39	-
20	Sumoylation	ESRNLEKKDVETTSS HHCCCCCCCCCCCCC	58.60	-
20	Sumoylation	ESRNLEKKDVETTSS HHCCCCCCCCCCCCC	58.60	28112733
20	Ubiquitination	ESRNLEKKDVETTSS HHCCCCCCCCCCCCC	58.60	21906983
20 (in isoform 1)	Ubiquitination	-	58.60	21890473
20 (in isoform 2)	Ubiquitination	-	58.60	21890473
20 (in isoform 5)	Ubiquitination	-	58.60	21890473
24	Phosphorylation	LEKKDVETTSSVSVK CCCCCCCCCCCCCCC	31.65	28450419
25	Phosphorylation	EKKDVETTSSVSVKR CCCCCCCCCCCCCCC	12.90	28450419
26	Phosphorylation	KKDVETTSSVSVKRK CCCCCCCCCCCCCCC	35.84	28450419
27	Phosphorylation	KDVETTSSVSVKRKR CCCCCCCCCCCCCCC	19.13	25159151
29	Phosphorylation	VETTSSVSVKRKRRL CCCCCCCCCCCCCCC	24.70	23401153
31	Sumoylation	TTSSVSVKRKRRLED CCCCCCCCCCCCCCC	44.70	-
31	Sumoylation	TTSSVSVKRKRRLED CCCCCCCCCCCCCCC	44.70	28112733
31	Ubiquitination	TTSSVSVKRKRRLED CCCCCCCCCCCCCCC	44.70	21890473
31 (in isoform 1)	Ubiquitination	-	44.70	21890473
31 (in isoform 2)	Ubiquitination	-	44.70	21890473
31 (in isoform 5)	Ubiquitination	-	44.70	21890473
44	Phosphorylation	EDAFIVISDSDGEEP CCCEEEEECCCCCCC	21.84	25159151
46	Phosphorylation	AFIVISDSDGEEPKE CEEEEECCCCCCCCH	40.50	23927012
59	Ubiquitination	KEENGLQKTKTKQSN CHHCCCCCCCCCHHH	57.96	-
75	Sumoylation	AKCLAKRKIAQMTEE HHHHHHHHHHHCCHH	41.51	-
75	Sumoylation	AKCLAKRKIAQMTEE HHHHHHHHHHHCCHH	41.51	28112733
75	Ubiquitination	AKCLAKRKIAQMTEE HHHHHHHHHHHCCHH	41.51	21906983
75 (in isoform 1)	Ubiquitination	-	41.51	21890473
75 (in isoform 2)	Ubiquitination	-	41.51	21890473
75 (in isoform 5)	Ubiquitination	-	41.51	21890473
90	Sumoylation	EQFALALKMSEQEAR HHHHHHHHHHHHHHH	34.47	-
90	Sumoylation	EQFALALKMSEQEAR HHHHHHHHHHHHHHH	34.47	28112733
90	Ubiquitination	EQFALALKMSEQEAR HHHHHHHHHHHHHHH	34.47	906983
90 (in isoform 1)	Ubiquitination	-	34.47	21890473
90 (in isoform 2)	Ubiquitination	-	34.47	21890473
90 (in isoform 5)	Ubiquitination	-	34.47	21890473
97	Methylation	KMSEQEAREVNSQEE HHHHHHHHHHCCHHH	47.87	115490305
101	Phosphorylation	QEAREVNSQEEEEEE HHHHHHCCHHHHHHH	44.11	29255136
110 (in isoform 4)	Ubiquitination	-	6.29	21906983
112	Ubiquitination	EEEELLRKAIAESLN HHHHHHHHHHHHHHH	44.08	-
115 (in isoform 4)	Ubiquitination	-	12.75	21906983
124	Phosphorylation	SLNSCRPSDASATRS HHHHCCCCCCCCCCC	26.85	28555341
127	Phosphorylation	SCRPSDASATRSRPL HCCCCCCCCCCCCCC	34.85	28555341
129	Phosphorylation	RPSDASATRSRPLAT CCCCCCCCCCCCCCC	27.04	26714015
131	Phosphorylation	SDASATRSRPLATGP CCCCCCCCCCCCCCC	33.62	28176443
136	Phosphorylation	TRSRPLATGPSSQSH CCCCCCCCCCCCCCC	58.26	29116813
137 (in isoform 3)	Ubiquitination	-	17.93	21890473
139	Phosphorylation	RPLATGPSSQSHQEK CCCCCCCCCCCCCCC	42.21	28176443
140	Phosphorylation	PLATGPSSQSHQEKT CCCCCCCCCCCCCCC	38.54	23401153
142	Phosphorylation	ATGPSSQSHQEKTTD CCCCCCCCCCCCCCC	29.14	28176443
146	Ubiquitination	SSQSHQEKTTDSGLT CCCCCCCCCCCCCCC	50.59	-
147	Phosphorylation	SQSHQEKTTDSGLTE CCCCCCCCCCCCCCC	34.77	-
163	Phosphorylation	IWQLVPPSLFKGSHI HHHCCCHHHHCCCCC	40.13	24719451
166	Sumoylation	LVPPSLFKGSHISQG CCCHHHHCCCCCCCC	65.87	-
166	Ubiquitination	LVPPSLFKGSHISQG CCCHHHHCCCCCCCC	65.87	-
167 (in isoform 3)	Ubiquitination	-	19.68	21890473
168	Phosphorylation	PPSLFKGSHISQGNE CHHHHCCCCCCCCCC	20.45	20363803
171	Phosphorylation	LFKGSHISQGNEAEE HHCCCCCCCCCCHHH	26.98	29255136
175 (in isoform 4)	Ubiquitination	-	65.37	21906983
188	Sumoylation	EPWDHTEKTEEEPVS CCCCCCCCCCCCCCC	63.49	28112733
188	Ubiquitination	EPWDHTEKTEEEPVS CCCCCCCCCCCCCCC	63.49	-
189	Phosphorylation	PWDHTEKTEEEPVSG CCCCCCCCCCCCCCC	42.25	23186163
190 (in isoform 4)	Ubiquitination	-	72.01	21906983
195	Phosphorylation	KTEEEPVSGSSGSWD CCCCCCCCCCCCCCC	43.61	25159151
197	Phosphorylation	EEEPVSGSSGSWDQS CCCCCCCCCCCCCCC	24.82	25159151
198	Phosphorylation	EEPVSGSSGSWDQSS CCCCCCCCCCCCCCC	40.13	25159151
200	Phosphorylation	PVSGSSGSWDQSSQP CCCCCCCCCCCCCCC	29.45	25159151
204	Phosphorylation	SSGSWDQSSQPVFEN CCCCCCCCCCCCEEC	28.59	29116813
205	Phosphorylation	SGSWDQSSQPVFENV CCCCCCCCCCCEECC	32.63	25159151
215	Ubiquitination	VFENVNVKSFDRCTG CEECCCCCCCCCCCC	39.95	21906983
215 (in isoform 1)	Ubiquitination	-	39.95	21890473
215 (in isoform 2)	Ubiquitination	-	39.95	21890473
218 (in isoform 4)	Ubiquitination	-	52.41	21906983
221	Phosphorylation	VKSFDRCTGHSAEHT CCCCCCCCCCCCCCC	38.53	28348404
224	Phosphorylation	FDRCTGHSAEHTQCG CCCCCCCCCCCCCCC	36.38	27794612
228	Phosphorylation	TGHSAEHTQCGKPQE CCCCCCCCCCCCCCC	19.63	27794612
232	Ubiquitination	AEHTQCGKPQESTGR CCCCCCCCCCCCCCC	51.67	-
236	Phosphorylation	QCGKPQESTGRGSAF CCCCCCCCCCCCHHH	30.80	25627689
237	Phosphorylation	CGKPQESTGRGSAFL CCCCCCCCCCCHHHH	30.10	25627689
239	Methylation	KPQESTGRGSAFLKA CCCCCCCCCHHHHHH	35.66	115490297
241	Phosphorylation	QESTGRGSAFLKAVQ CCCCCCCHHHHHHHC	17.94	25159151
245	Sumoylation	GRGSAFLKAVQGSGD CCCHHHHHHHCCCCC	39.81	-
245	Acetylation	GRGSAFLKAVQGSGD CCCHHHHHHHCCCCC	39.81	26051181
245	Methylation	GRGSAFLKAVQGSGD CCCHHHHHHHCCCCC	39.81	42366373
245	Sumoylation	GRGSAFLKAVQGSGD CCCHHHHHHHCCCCC	39.81	28112733
245	Ubiquitination	GRGSAFLKAVQGSGD CCCHHHHHHHCCCCC	39.81	21890473
245 (in isoform 1)	Ubiquitination	-	39.81	21890473
250	Phosphorylation	FLKAVQGSGDTSRHC HHHHHCCCCCCCCCH	19.19	28450419
253	Phosphorylation	AVQGSGDTSRHCLPT HHCCCCCCCCCHHCC	31.05	28450419
254	Phosphorylation	VQGSGDTSRHCLPTL HCCCCCCCCCHHCCH	25.43	30576142
260	Phosphorylation	TSRHCLPTLADAKGL CCCCHHCCHHHCCCC	22.94	26074081
265	Ubiquitination	LPTLADAKGLQDTGG HCCHHHCCCCCCCCC	61.78	-
273 (in isoform 4)	Ubiquitination	-	13.61	21906983
296 (in isoform 3)	Ubiquitination	-	3.20	21890473
304 (in isoform 3)	Ubiquitination	-	33.75	21890473
305	Ubiquitination	CQLEVYQKSLKMAQR EHHHHHHHHHHHHHH	39.82	-
308	Sumoylation	EVYQKSLKMAQRQLL HHHHHHHHHHHHHHH	39.00	-
308	Sumoylation	EVYQKSLKMAQRQLL HHHHHHHHHHHHHHH	39.00	-
308	Ubiquitination	EVYQKSLKMAQRQLL HHHHHHHHHHHHHHH	39.00	-
309 (in isoform 3)	Ubiquitination	-	4.69	21890473
314 (in isoform 2)	Ubiquitination	-	6.57	21890473
318	Ubiquitination	QRQLLNKKGFGEPVL HHHHHCCCCCCCCCC	59.40	-
319 (in isoform 2)	Ubiquitination	-	37.08	21890473
330	Phosphorylation	PVLPRPPSLIQNECG CCCCCCCHHHHCCCC	40.56	29255136
343	Phosphorylation	CGQGEQASEKNECIS CCCCCCCHHHCCHHC	49.12	29255136
350	Phosphorylation	SEKNECISEDMGDED HHHCCHHCCCCCCCC	38.92	30108239
350 (in isoform 3)	Ubiquitination	-	38.92	21890473
358	Ubiquitination	EDMGDEDKEERQESR CCCCCCCHHHHHHHH	60.47	-
364	Phosphorylation	DKEERQESRASDWHS CHHHHHHHHHHHHHH	25.47	24719451
372	Ubiquitination	RASDWHSKTKDFQES HHHHHHHHCCCHHHH	46.86	-
374	Ubiquitination	SDWHSKTKDFQESSI HHHHHHCCCHHHHHH	61.35	21906983
374 (in isoform 1)	Ubiquitination	-	61.35	21890473
378 (in isoform 2)	Ubiquitination	-	46.58	21890473
379	Phosphorylation	KTKDFQESSIKSLKE HCCCHHHHHHHHHHH	26.95	27732954
380	Phosphorylation	TKDFQESSIKSLKEK CCCHHHHHHHHHHHH	33.03	20068231
382	Sumoylation	DFQESSIKSLKEKLL CHHHHHHHHHHHHHH	52.24	-
382	Sumoylation	DFQESSIKSLKEKLL CHHHHHHHHHHHHHH	52.24	28112733
382	Ubiquitination	DFQESSIKSLKEKLL CHHHHHHHHHHHHHH	52.24	21890473
382 (in isoform 1)	Ubiquitination	-	52.24	21890473
383	Phosphorylation	FQESSIKSLKEKLLL HHHHHHHHHHHHHHC	42.90	20068231
387	Sumoylation	SIKSLKEKLLLEEEP HHHHHHHHHHCCCCC	42.73	28112733
387	Ubiquitination	SIKSLKEKLLLEEEP HHHHHHHHHHCCCCC	42.73	21906983
387 (in isoform 1)	Ubiquitination	-	42.73	21890473
393 (in isoform 2)	Ubiquitination	-	38.27	21890473
395	Phosphorylation	LLLEEEPTTSHGQSS HHCCCCCCCCCCCCC	44.18	30576142
396	Phosphorylation	LLEEEPTTSHGQSSQ HCCCCCCCCCCCCCC	29.46	17525332
397	Phosphorylation	LEEEPTTSHGQSSQG CCCCCCCCCCCCCCC	28.26	28450419
401	Phosphorylation	PTTSHGQSSQGIVEE CCCCCCCCCCCCEEE	29.26	30576142
402	Phosphorylation	TTSHGQSSQGIVEET CCCCCCCCCCCEEEE	25.25	17525332
402 (in isoform 3)	Ubiquitination	-	25.25	21890473
407 (in isoform 3)	Ubiquitination	-	54.35	21890473
409	Phosphorylation	SQGIVEETSEEGNSV CCCCEEEECCCCCCC	28.12	28450419
410	Phosphorylation	QGIVEETSEEGNSVP CCCEEEECCCCCCCC	36.61	28450419
415	Phosphorylation	ETSEEGNSVPASQSV EECCCCCCCCHHHHH	40.09	17525332
419	Phosphorylation	EGNSVPASQSVAALT CCCCCCHHHHHHHHH	19.54	17525332
421	Phosphorylation	NSVPASQSVAALTSK CCCCHHHHHHHHHCC	15.95	23312004
421 (in isoform 2)	Ubiquitination	-	15.95	21890473
426	Phosphorylation	SQSVAALTSKRSLVL HHHHHHHHCCCEEEE	27.72	27251275
427	Phosphorylation	QSVAALTSKRSLVLM HHHHHHHCCCEEEEC	27.24	27251275
428	Acetylation	SVAALTSKRSLVLMP HHHHHHCCCEEEECC	40.55	26051181
428	Sumoylation	SVAALTSKRSLVLMP HHHHHHCCCEEEECC	40.55	28112733
428	Ubiquitination	SVAALTSKRSLVLMP HHHHHHCCCEEEECC	40.55	21906983
428 (in isoform 1)	Ubiquitination	-	40.55	21890473
430	Phosphorylation	AALTSKRSLVLMPES HHHHCCCEEEECCCC	26.94	25627689
443	Phosphorylation	ESSAEEITVCPETQL CCCCCEEEECCCCCC	21.23	28348404
448	Phosphorylation	EITVCPETQLSSSET EEEECCCCCCCCCCC	21.69	28348404
451	Phosphorylation	VCPETQLSSSETFDL ECCCCCCCCCCCEEC	23.23	28348404
452	Phosphorylation	CPETQLSSSETFDLE CCCCCCCCCCCEECC	40.56	28102081
453	Phosphorylation	PETQLSSSETFDLER CCCCCCCCCCEECCC	36.96	28102081
455	Phosphorylation	TQLSSSETFDLEREV CCCCCCCCEECCCCC	25.13	28102081
463	Phosphorylation	FDLEREVSPGSRDIL EECCCCCCCCCCHHH	20.84	25159151
466	Phosphorylation	EREVSPGSRDILDGV CCCCCCCCCHHHHHE	30.11	30266825
466 (in isoform 3)	Ubiquitination	-	30.11	21890473
476 (in isoform 2)	Ubiquitination	-	0.99	21890473
480	Sumoylation	VRIIMADKEVGNKED EEEEECCCCCCCHHH	44.77	-
480	Sumoylation	VRIIMADKEVGNKED EEEEECCCCCCCHHH	44.77	-
480	Ubiquitination	VRIIMADKEVGNKED EEEEECCCCCCCHHH	44.77	21906983
480 (in isoform 1)	Ubiquitination	-	44.77	21890473
481 (in isoform 3)	Ubiquitination	-	57.09	21890473
485	Sumoylation	ADKEVGNKEDAEKEV CCCCCCCHHHHHHHH	51.55	-
485	Sumoylation	ADKEVGNKEDAEKEV CCCCCCCHHHHHHHH	51.55	-
485	Ubiquitination	ADKEVGNKEDAEKEV CCCCCCCHHHHHHHH	51.55	21906983
485 (in isoform 1)	Ubiquitination	-	51.55	21890473
498	Phosphorylation	EVAISTFSSSNQVSC HHHHEECCCCCCEEC	32.71	-
509 (in isoform 3)	Ubiquitination	-	56.84	21890473
544	Sumoylation	RQKEAKTKSDSGTAA HHHHCCCCCCCCCCC	52.11	-
544	Sumoylation	RQKEAKTKSDSGTAA HHHHCCCCCCCCCCC	52.11	28112733
544	Ubiquitination	RQKEAKTKSDSGTAA HHHHCCCCCCCCCCC	52.11	21906983
544 (in isoform 1)	Ubiquitination	-	52.11	21890473
545	Phosphorylation	QKEAKTKSDSGTAAQ HHHCCCCCCCCCCCC	42.09	30576142
547	Phosphorylation	EAKTKSDSGTAAQTS HCCCCCCCCCCCCCE	45.17	30576142
549	Phosphorylation	KTKSDSGTAAQTSLD CCCCCCCCCCCCEEC	23.83	28555341
553	Phosphorylation	DSGTAAQTSLDIDKN CCCCCCCCEECCCCC	26.91	23312004
554	Phosphorylation	SGTAAQTSLDIDKNE CCCCCCCEECCCCCC	16.38	25159151
559	Sumoylation	QTSLDIDKNEKCYLC CCEECCCCCCCEEEE	68.30	-
559	Sumoylation	QTSLDIDKNEKCYLC CCEECCCCCCCEEEE	68.30	28112733
559	Ubiquitination	QTSLDIDKNEKCYLC CCEECCCCCCCEEEE	68.30	21906983
559 (in isoform 1)	Ubiquitination	-	68.30	21890473
562	Sumoylation	LDIDKNEKCYLCKSL ECCCCCCCEEEECCC	37.26	-
562	Sumoylation	LDIDKNEKCYLCKSL ECCCCCCCEEEECCC	37.26	25218447
562	Ubiquitination	LDIDKNEKCYLCKSL ECCCCCCCEEEECCC	37.26	-
564 (in isoform 3)	Ubiquitination	-	26.63	21890473
567	Ubiquitination	NEKCYLCKSLVPFRE CCCEEEECCCCCCCE	44.20	-
575	Phosphorylation	SLVPFREYQCHVDSC CCCCCCEEEEEHHHH	16.51	25690035
581	Phosphorylation	EYQCHVDSCLQLAKA EEEEEHHHHHHHHHH	18.68	25690035
587	Sumoylation	DSCLQLAKADQGDGP HHHHHHHHHHCCCCC	62.17	-
587	Sumoylation	DSCLQLAKADQGDGP HHHHHHHHHHCCCCC	62.17	28112733
587	Ubiquitination	DSCLQLAKADQGDGP HHHHHHHHHHCCCCC	62.17	21906983
587 (in isoform 1)	Ubiquitination	-	62.17	21890473
597	Phosphorylation	QGDGPEGSGRACSTV CCCCCCCCCCCCCCC	24.36	30576142
602	Phosphorylation	EGSGRACSTVEGKWQ CCCCCCCCCCCCHHH	34.21	23312004
603	Phosphorylation	GSGRACSTVEGKWQQ CCCCCCCCCCCHHHH	23.59	30576142
607	Sumoylation	ACSTVEGKWQQRLKN CCCCCCCHHHHHHCC	28.46	-
607	Acetylation	ACSTVEGKWQQRLKN CCCCCCCHHHHHHCC	28.46	26051181
607	Sumoylation	ACSTVEGKWQQRLKN CCCCCCCHHHHHHCC	28.46	28112733
607	Ubiquitination	ACSTVEGKWQQRLKN CCCCCCCHHHHHHCC	28.46	-
618	Ubiquitination	RLKNPKEKGHSEGRL HHCCHHHCCCCHHHH	68.96	-
627	Phosphorylation	HSEGRLLSFLEQSEH CCHHHHHHHHHHCCC	32.17	25159151
632	Phosphorylation	LLSFLEQSEHKTSDA HHHHHHHCCCCCCCC	32.09	23312004
635	Sumoylation	FLEQSEHKTSDADIK HHHHCCCCCCCCCCC	45.75	-
635	Sumoylation	FLEQSEHKTSDADIK HHHHCCCCCCCCCCC	45.75	28112733
635	Ubiquitination	FLEQSEHKTSDADIK HHHHCCCCCCCCCCC	45.75	-
636	Phosphorylation	LEQSEHKTSDADIKS HHHCCCCCCCCCCCC	33.47	28509920
637	Phosphorylation	EQSEHKTSDADIKSS HHCCCCCCCCCCCCC	35.29	28509920
642	Sumoylation	KTSDADIKSSETGAF CCCCCCCCCCCCCCE	48.77	28112733
642	Ubiquitination	KTSDADIKSSETGAF CCCCCCCCCCCCCCE	48.77	2190698
642 (in isoform 1)	Ubiquitination	-	48.77	21890473
643	Phosphorylation	TSDADIKSSETGAFR CCCCCCCCCCCCCEE	33.47	23403867
644	Phosphorylation	SDADIKSSETGAFRV CCCCCCCCCCCCEEC	33.89	28464451
646	Phosphorylation	ADIKSSETGAFRVPS CCCCCCCCCCEECCC	35.44	23403867
653	Phosphorylation	TGAFRVPSPGMEEAG CCCEECCCCCCHHHC	31.09	19664994
656	Sulfoxidation	FRVPSPGMEEAGCSR EECCCCCCHHHCCCH	4.83	21406390
661	Carbamidation	PGMEEAGCSREMQSS CCCHHHCCCHHHHHH	4.46	17322306
662	Phosphorylation	GMEEAGCSREMQSSF CCHHHCCCHHHHHHC	30.29	23927012
667	Phosphorylation	GCSREMQSSFTRRDL CCCHHHHHHCCCCCC	26.55	26074081
668	Phosphorylation	CSREMQSSFTRRDLN CCHHHHHHCCCCCCC	17.47	23401153
670	Phosphorylation	REMQSSFTRRDLNES HHHHHHCCCCCCCCC	27.09	26074081
677	Phosphorylation	TRRDLNESPVKSFVS CCCCCCCCCCCEEEE	33.64	29255136
680	Acetylation	DLNESPVKSFVSISE CCCCCCCCEEEEHHH	41.37	7681407
681	Phosphorylation	LNESPVKSFVSISEA CCCCCCCEEEEHHHH	30.99	23927012
684	Phosphorylation	SPVKSFVSISEATDC CCCCEEEEHHHHHCC	20.56	28464451
686	Phosphorylation	VKSFVSISEATDCLV CCEEEEHHHHHCCEE	17.42	24732914
689	Phosphorylation	FVSISEATDCLVDFK EEEHHHHHCCEEEEC	24.16	24732914
696	Acetylation	TDCLVDFKKQVTVQP HCCEEEECCCEEECC	37.52	24468251
696	Sumoylation	TDCLVDFKKQVTVQP HCCEEEECCCEEECC	37.52	28112733
696	Ubiquitination	TDCLVDFKKQVTVQP HCCEEEECCCEEECC	37.52	-
697	Sumoylation	DCLVDFKKQVTVQPG CCEEEECCCEEECCC	50.42	28112733
697	Ubiquitination	DCLVDFKKQVTVQPG CCEEEECCCEEECCC	50.42	-
700	Phosphorylation	VDFKKQVTVQPGSRT EEECCCEEECCCCCC	15.78	-
705	Phosphorylation	QVTVQPGSRTRTKAG CEEECCCCCCCCCCC	36.84	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
44	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
46	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
205	S	Phosphorylation	Kinase	ATM	Q13315	PSP
205	S	Phosphorylation	Kinase	ATR	Q13535	PSP
402	S	Phosphorylation	Kinase	ATM	Q13315	GPS
627	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
677	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UIMC1_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 UIMC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_HUMAN	UBC	physical	17525341
BRCA1_HUMAN	BRCA1	physical	17525341
BABA2_HUMAN	BRE	physical	17525341
BRCC3_HUMAN	BRCC3	physical	17525341
ALBU_HUMAN	ALB	physical	19615732
BARD1_HUMAN	BARD1	physical	19615732
BRCA1_HUMAN	BRCA1	physical	19615732
CAZA1_HUMAN	CAPZA1	physical	19615732
CAPZB_HUMAN	CAPZB	physical	19615732
CCNA2_HUMAN	CCNA2	physical	19615732
CDK1_HUMAN	CDK1	physical	19615732
ODO2_HUMAN	DLST	physical	19615732
FA7_HUMAN	F7	physical	19615732
NRDC_HUMAN	NRD1	physical	19615732
PUR4_HUMAN	PFAS	physical	19615732
RFC4_HUMAN	RFC4	physical	19615732
CSKP_HUMAN	CASK	physical	19615732
ULA1_HUMAN	NAE1	physical	19615732
CPNE1_HUMAN	CPNE1	physical	19615732
UBA3_HUMAN	UBA3	physical	19615732
CSN2_HUMAN	COPS2	physical	19615732
BAG5_HUMAN	BAG5	physical	19615732
BABA2_HUMAN	BRE	physical	19615732
ERP44_HUMAN	ERP44	physical	19615732
ABRX2_HUMAN	FAM175B	physical	19615732
BABA1_HUMAN	BABAM1	physical	19615732
SSU72_HUMAN	SSU72	physical	19615732
NOP53_HUMAN	GLTSCR2	physical	19615732
LIN7C_HUMAN	LIN7C	physical	19615732
WDR48_HUMAN	WDR48	physical	19615732
P5CR3_HUMAN	PYCRL	physical	19615732
BRCC3_HUMAN	BRCC3	physical	19615732
THNS1_HUMAN	THNSL1	physical	19615732
ABRX1_HUMAN	FAM175A	physical	19615732
DPY30_HUMAN	DPY30	physical	19615732
BRCC3_HUMAN	BRCC3	physical	18077395
MDC1_HUMAN	MDC1	physical	21857162
MDC1_HUMAN	MDC1	physical	21622030
BRCA1_HUMAN	BRCA1	physical	21622030
P53_HUMAN	TP53	physical	19433585
MDM2_HUMAN	MDM2	physical	19433585
ABRX1_HUMAN	FAM175A	physical	19261749
BABA2_HUMAN	BRE	physical	19261749
BABA1_HUMAN	BABAM1	physical	19261749
BRCC3_HUMAN	BRCC3	physical	19261749
BABA1_HUMAN	BABAM1	physical	19261746
BRCC3_HUMAN	BRCC3	physical	19261746
ABRX1_HUMAN	FAM175A	physical	19261748
BABA2_HUMAN	BRE	physical	19261748
BRCC3_HUMAN	BRCC3	physical	19261748
BABA1_HUMAN	BABAM1	physical	19261748
BRCA1_HUMAN	BRCA1	physical	19261748
SUMO2_HUMAN	SUMO2	physical	22689573
UBC_HUMAN	UBC	physical	22689573
BRCA1_HUMAN	BRCA1	physical	17621610
ABRX1_HUMAN	FAM175A	physical	17525340
BRCA1_HUMAN	BRCA1	physical	17525340
CTIP_HUMAN	RBBP8	physical	17525340
UBC_HUMAN	UBC	physical	22350954
ESR1_HUMAN	ESR1	physical	17311814
UBC_HUMAN	UBC	physical	19944020
ABRX1_HUMAN	FAM175A	physical	17643121
ECM29_HUMAN	KIAA0368	physical	20682791
UBC_HUMAN	UBC	physical	19536136
UBC_HUMAN	UBC	physical	19305427
ABRX1_HUMAN	FAM175A	physical	19305427
BRCC3_HUMAN	BRCC3	physical	19305427
BRCA1_HUMAN	BRCA1	physical	19305427
ABRX1_HUMAN	FAM175A	physical	19015238
BABA2_HUMAN	BRE	physical	19015238
BRCC3_HUMAN	BRCC3	physical	19015238
UBC_HUMAN	UBC	physical	19015238
H2A2C_HUMAN	HIST2H2AC	physical	19015238
H2B2E_HUMAN	HIST2H2BE	physical	19015238
CEP57_MOUSE	Cep57	physical	12954732
ABRX1_HUMAN	FAM175A	physical	17643122
SUMO2_HUMAN	SUMO2	physical	23211528
UBC_HUMAN	UBC	physical	23211528
BLM_HUMAN	BLM	physical	23708797
ELOA1_YEAST	ELA1	physical	23993092
ELOC_YEAST	ELC1	physical	23993092
UBC_HUMAN	UBC	physical	24627472
C1QBP_HUMAN	C1QBP	physical	23264621
HSP74_HUMAN	HSPA4	physical	23264621
BRCC3_HUMAN	BRCC3	physical	23264621
CDK1_HUMAN	CDK1	physical	23264621
RS6_HUMAN	RPS6	physical	23264621
ABRX1_HUMAN	FAM175A	physical	23264621
FANCG_HUMAN	FANCG	physical	25132264
H2A2C_HUMAN	HIST2H2AC	physical	25132264
UBC_HUMAN	UBC	physical	22605335
UBC_HUMAN	UBC	physical	17311814
UBC_HUMAN	UBC	physical	23823328
UBC_HUMAN	UBC	physical	23562397
UBC_HUMAN	UBC	physical	25756347
PARP1_HUMAN	PARP1	physical	25252691
BRCA1_HUMAN	BRCA1	physical	25252691
ABRX1_HUMAN	FAM175A	physical	25252691
SUMO2_HUMAN	SUMO2	physical	26719330
TRAIP_HUMAN	TRAIP	physical	26781088
RIOX2_HUMAN	MINA	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28842250
UBP13_HUMAN	USP13	physical	28569838
BRCA1_HUMAN	BRCA1	physical	28569838
ABRX1_HUMAN	FAM175A	physical	28569838
BABA1_HUMAN	BABAM1	physical	28569838

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

Phosphorylation

"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-44; SER-46; SER-627;SER-653 AND SER-677, AND MASS SPECTROMETRY.
PubMed: 18669648

"RAP80 responds to DNA damage induced by both ionizing radiation andUV irradiation and is phosphorylated at Ser 205.";
Yan J., Yang X.-P., Kim Y.-S., Jetten A.M.;
Cancer Res. 68:4269-4276(2008).
Cited for: PHOSPHORYLATION AT SER-205, AND MUTAGENESIS OF SER-205.
PubMed: 18519686

"Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damageresponse.";
Kim H., Chen J., Yu X.;
Science 316:1202-1205(2007).
Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION,UBIQUITIN-BINDING, PHOSPHORYLATION AT SER-101, AND MUTAGENESIS OFALA-88; SER-92; ALA-113 AND SER-117.
PubMed: 17525342

"RAP80 targets BRCA1 to specific ubiquitin structures at DNA damagesites.";
Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B.,Livingston D.M., Greenberg R.A.;
Science 316:1198-1202(2007).
Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION,UBIQUITIN-BINDING, AND PHOSPHORYLATION AT SER-101.
PubMed: 17525341

"Abraxas and RAP80 form a BRCA1 protein complex required for the DNAdamage response.";
Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S.,Elledge S.J.;
Science 316:1194-1198(2007).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140; SER-402AND SER-419, AND MUTAGENESIS OF ALA-88; SER-92; ALA-113 AND SER-117.
PubMed: 17525340

"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-140; SER-402; SER-415AND SER-419, AND MASS SPECTROMETRY.
PubMed: 17525332

"The ubiquitin-interacting motif containing protein RAP80 interactswith BRCA1 and functions in DNA damage repair response.";
Yan J., Kim Y.S., Yang X.-P., Li L.-P., Liao G., Xia F., Jetten A.M.;
Cancer Res. 67:6647-6656(2007).
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ALA-88 AND ALA-113, ANDPHOSPHORYLATION AT SER-205 AND SER-402.
PubMed: 17621610

"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-44 AND SER-46, AND MASSSPECTROMETRY.
PubMed: 17081983

"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-597; SER-653 ANDSER-677, AND MASS SPECTROMETRY.
PubMed: 15302935