dbPTM

MCM3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM3_HUMAN
UniProt AC	P25205
Protein Name	DNA replication licensing factor MCM3
Gene Name	MCM3
Organism	Homo sapiens (Human).
Sequence Length	808
Subcellular Localization	Nucleus.
Protein Description	Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for DNA replication and cell proliferation..
Protein Sequence	MAGTVVLDDVELREAQRDYLDFLDDEEDQGIYQSKVRELISDNQYRLIVNVNDLRRKNEKRANRLLNNAFEELVAFQRALKDFVASIDATYAKQYEEFYVGLEGSFGSKHVSPRTLTSCFLSCVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERRYSDLTTLVAFPSSSVYPTKDEENNPLETEYGLSVYKDHQTITIQEMPEKAPAGQLPRSVDVILDDDLVDKAKPGDRVQVVGTYRCLPGKKGGYTSGTFRTVLIACNVKQMSKDAQPSFSAEDIAKIKKFSKTRSKDIFDQLAKSLAPSIHGHDYVKKAILCLLLGGVERDLENGSHIRGDINILLIGDPSVAKSQLLRYVLCTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEQDREISDHVLRMHRYRAPGEQDGDAMPLGSAVDILATDDPNFSQEDQQDTQIYEKHDNLLHGTKKKKEKMVSAAFMKKYIHVAKIIKPVLTQESATYIAEEYSRLRSQDSMSSDTARTSPVTARTLETLIRLATAHAKARMSKTVDLQDAEEAVELVQYAYFKKVLEKEKKRKKRSEDESETEDEEEKSQEDQEQKRKRRKTRQPDAKDGDSYDPYDFSDTEEEMPQVHTPKTADSQETKESQKVELSESRLKAFKVALLDVFREAHAQSIGMNRLTESINRDSEEPFSSVEIQAALSKMQDDNQVMVSEGIIFLI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGTVVLDD ------CCCEEEECH	23.51	22223895
4	Phosphorylation	----MAGTVVLDDVE ----CCCEEEECHHH	9.63	23401153
19	Phosphorylation	LREAQRDYLDFLDDE HHHHHHHHHHHCCCC	15.45	22817900
32	Phosphorylation	DEEDQGIYQSKVREL CCCCCCCCHHHHHHH	17.35	22817900
34	Phosphorylation	EDQGIYQSKVRELIS CCCCCCHHHHHHHHC	19.02	-
35	Ubiquitination	DQGIYQSKVRELISD CCCCCHHHHHHHHCC	29.77	21906983
45	Phosphorylation	ELISDNQYRLIVNVN HHHCCCCEEEEEEHH	17.40	-
55	Methylation	IVNVNDLRRKNEKRA EEEHHHHHHHHHHHH	50.84	115482835
64	Phosphorylation	KNEKRANRLLNNAFE HHHHHHHHHHHHHHH	39.30	-
77	Phosphorylation	FEELVAFQRALKDFV HHHHHHHHHHHHHHH	21.72	-
80	Ubiquitination	LVAFQRALKDFVASI HHHHHHHHHHHHHHC	6.27	-
80	Ubiquitination	LVAFQRALKDFVASI HHHHHHHHHHHHHHC	6.27	-
81	2-Hydroxyisobutyrylation	VAFQRALKDFVASID HHHHHHHHHHHHHCC	48.40	-
81	Acetylation	VAFQRALKDFVASID HHHHHHHHHHHHHCC	48.40	26051181
81	Ubiquitination	VAFQRALKDFVASID HHHHHHHHHHHHHCC	48.40	-
86	Phosphorylation	ALKDFVASIDATYAK HHHHHHHHCCHHHHH	18.72	28152594
90	Phosphorylation	FVASIDATYAKQYEE HHHHCCHHHHHHCCE	21.92	28152594
91	Phosphorylation	VASIDATYAKQYEEF HHHCCHHHHHHCCEE	17.33	28152594
100	Methylation	KQYEEFYVGLEGSFG HHCCEEEECCCCCCC	9.53	-
112	Phosphorylation	SFGSKHVSPRTLTSC CCCCCCCCHHHHHHH	14.37	21658608
126	Ubiquitination	CFLSCVVCVEGIVTK HHHHHHHHHHCHHHH	0.85	-
126	Ubiquitination	CFLSCVVCVEGIVTK HHHHHHHHHHCHHHH	0.85	-
135	Phosphorylation	EGIVTKCSLVRPKVV HCHHHHCCCCCCCCE	31.30	24719451
140	Ubiquitination	KCSLVRPKVVRSVHY HCCCCCCCCEEEEEE	42.68	-
144	Phosphorylation	VRPKVVRSVHYCPAT CCCCCEEEEEECCCC	11.13	23401153
147	Nitration	KVVRSVHYCPATKKT CCEEEEEECCCCHHH	9.66	-
147	Phosphorylation	KVVRSVHYCPATKKT CCEEEEEECCCCHHH	9.66	28152594
148	S-nitrosocysteine	VVRSVHYCPATKKTI CEEEEEECCCCHHHH	0.82	-
148	S-nitrosylation	VVRSVHYCPATKKTI CEEEEEECCCCHHHH	0.82	19483679
151	Phosphorylation	SVHYCPATKKTIERR EEEECCCCHHHHHHH	20.44	27080861
152	2-Hydroxyisobutyrylation	VHYCPATKKTIERRY EEECCCCHHHHHHHH	50.45	-
152	Acetylation	VHYCPATKKTIERRY EEECCCCHHHHHHHH	50.45	25953088
152	Ubiquitination	VHYCPATKKTIERRY EEECCCCHHHHHHHH	50.45	-
154	O-linked_Glycosylation	YCPATKKTIERRYSD ECCCCHHHHHHHHCC	29.62	28510447
154	Phosphorylation	YCPATKKTIERRYSD ECCCCHHHHHHHHCC	29.62	21406692
157	Phosphorylation	ATKKTIERRYSDLTT CCHHHHHHHHCCCCE	38.70	-
159	Phosphorylation	KKTIERRYSDLTTLV HHHHHHHHCCCCEEE	16.86	21712546
160	Phosphorylation	KTIERRYSDLTTLVA HHHHHHHCCCCEEEE	25.08	25159151
163	Phosphorylation	ERRYSDLTTLVAFPS HHHHCCCCEEEECCC	24.07	25159151
164	Phosphorylation	RRYSDLTTLVAFPSS HHHCCCCEEEECCCC	26.91	22617229
170	Phosphorylation	TTLVAFPSSSVYPTK CEEEECCCCCCCCCC	28.88	20873877
171	Phosphorylation	TLVAFPSSSVYPTKD EEEECCCCCCCCCCC	24.86	20873877
172	Phosphorylation	LVAFPSSSVYPTKDE EEECCCCCCCCCCCC	29.97	20873877
174	Phosphorylation	AFPSSSVYPTKDEEN ECCCCCCCCCCCCCC	13.72	20873877
176	Phosphorylation	PSSSVYPTKDEENNP CCCCCCCCCCCCCCC	33.18	20873877
177	Ubiquitination	SSSVYPTKDEENNPL CCCCCCCCCCCCCCC	59.65	-
185	Ubiquitination	DEENNPLETEYGLSV CCCCCCCEEECEEEE	40.63	-
185	Ubiquitination	DEENNPLETEYGLSV CCCCCCCEEECEEEE	40.63	-
186	Phosphorylation	EENNPLETEYGLSVY CCCCCCEEECEEEEE	42.04	27080861
188	Phosphorylation	NNPLETEYGLSVYKD CCCCEEECEEEEEEC	30.68	27080861
189	Phosphorylation	NPLETEYGLSVYKDH CCCEEECEEEEEECC	12.78	27251275
191	Phosphorylation	LETEYGLSVYKDHQT CEEECEEEEEECCCE	21.02	27080861
193	Phosphorylation	TEYGLSVYKDHQTIT EECEEEEEECCCEEE	13.81	27080861
197	Ubiquitination	LSVYKDHQTITIQEM EEEEECCCEEEEEEC	44.74	-
198	Phosphorylation	SVYKDHQTITIQEMP EEEECCCEEEEEECC	19.37	-
199	Phosphorylation	VYKDHQTITIQEMPE EEECCCEEEEEECCC	2.28	-
204	Phosphorylation	QTITIQEMPEKAPAG CEEEEEECCCCCCCC	2.73	-
205	Phosphorylation	TITIQEMPEKAPAGQ EEEEEECCCCCCCCC	38.90	19651622
207	Acetylation	TIQEMPEKAPAGQLP EEEECCCCCCCCCCC	54.52	26051181
207	Ubiquitination	TIQEMPEKAPAGQLP EEEECCCCCCCCCCC	54.52	21906983
208	Phosphorylation	IQEMPEKAPAGQLPR EEECCCCCCCCCCCC	9.49	-
209	Phosphorylation	QEMPEKAPAGQLPRS EECCCCCCCCCCCCC	48.25	20068231
216	Phosphorylation	PAGQLPRSVDVILDD CCCCCCCCEEEEECH	22.26	21601212
222	Sumoylation	RSVDVILDDDLVDKA CCEEEEECHHHHCCC	35.93	-
222	Ubiquitination	RSVDVILDDDLVDKA CCEEEEECHHHHCCC	35.93	-
228	Ubiquitination	LDDDLVDKAKPGDRV ECHHHHCCCCCCCEE	51.32	-
230	Ubiquitination	DDLVDKAKPGDRVQV HHHHCCCCCCCEEEE	56.10	-
234	Methylation	DKAKPGDRVQVVGTY CCCCCCCEEEEEEEE	27.04	16188073
240	Phosphorylation	DRVQVVGTYRCLPGK CEEEEEEEEECCCCC	9.00	-
243	Phosphorylation	QVVGTYRCLPGKKGG EEEEEEECCCCCCCC	3.66	-
248	Sumoylation	YRCLPGKKGGYTSGT EECCCCCCCCCCCCC	64.58	-
248	Acetylation	YRCLPGKKGGYTSGT EECCCCCCCCCCCCC	64.58	26051181
248	Ubiquitination	YRCLPGKKGGYTSGT EECCCCCCCCCCCCC	64.58	-
252	Ubiquitination	PGKKGGYTSGTFRTV CCCCCCCCCCCHHEE	24.77	-
252	Phosphorylation	PGKKGGYTSGTFRTV CCCCCCCCCCCHHEE	24.77	30108239
252	Ubiquitination	PGKKGGYTSGTFRTV CCCCCCCCCCCHHEE	24.77	-
253	Phosphorylation	GKKGGYTSGTFRTVL CCCCCCCCCCHHEEE	27.61	28450419
255	Phosphorylation	KGGYTSGTFRTVLIA CCCCCCCCHHEEEEE	15.09	28450419
258	Phosphorylation	YTSGTFRTVLIACNV CCCCCHHEEEEEECH	18.57	-
266	Sumoylation	VLIACNVKQMSKDAQ EEEEECHHHCCCCCC	26.71	-
266	Acetylation	VLIACNVKQMSKDAQ EEEEECHHHCCCCCC	26.71	25953088
266	Ubiquitination	VLIACNVKQMSKDAQ EEEEECHHHCCCCCC	26.71	21890473
269	Phosphorylation	ACNVKQMSKDAQPSF EECHHHCCCCCCCCC	25.53	22817901
270	Ubiquitination	CNVKQMSKDAQPSFS ECHHHCCCCCCCCCC	52.30	-
273	Ubiquitination	KQMSKDAQPSFSAED HHCCCCCCCCCCHHH	44.28	-
273	Ubiquitination	KQMSKDAQPSFSAED HHCCCCCCCCCCHHH	44.28	-
275	Ubiquitination	MSKDAQPSFSAEDIA CCCCCCCCCCHHHHH	21.54	-
275	Phosphorylation	MSKDAQPSFSAEDIA CCCCCCCCCCHHHHH	21.54	25159151
275	Ubiquitination	MSKDAQPSFSAEDIA CCCCCCCCCCHHHHH	21.54	-
277	Phosphorylation	KDAQPSFSAEDIAKI CCCCCCCCHHHHHHH	34.78	30576142
279	Methylation	AQPSFSAEDIAKIKK CCCCCCHHHHHHHHH	49.07	-
283	Acetylation	FSAEDIAKIKKFSKT CCHHHHHHHHHHCCC	56.23	26822725
283	Ubiquitination	FSAEDIAKIKKFSKT CCHHHHHHHHHHCCC	56.23	-
285	Acetylation	AEDIAKIKKFSKTRS HHHHHHHHHHCCCCC	47.24	25953088
290	Phosphorylation	KIKKFSKTRSKDIFD HHHHHCCCCCHHHHH	38.69	23312004
292	Phosphorylation	KKFSKTRSKDIFDQL HHHCCCCCHHHHHHH	39.65	20873877
293	Ubiquitination	KFSKTRSKDIFDQLA HHCCCCCHHHHHHHH	52.10	-
293	Acetylation	KFSKTRSKDIFDQLA HHCCCCCHHHHHHHH	52.10	-
293	Sumoylation	KFSKTRSKDIFDQLA HHCCCCCHHHHHHHH	52.10	-
293	Ubiquitination	KFSKTRSKDIFDQLA HHCCCCCHHHHHHHH	52.10	21890473
301	Ubiquitination	DIFDQLAKSLAPSIH HHHHHHHHHHCHHHC	55.37	21890473
303	Phosphorylation	FDQLAKSLAPSIHGH HHHHHHHHCHHHCCH	8.83	-
311	Ubiquitination	APSIHGHDYVKKAIL CHHHCCHHHHHHHHH	55.29	21890473
311	Sumoylation	APSIHGHDYVKKAIL CHHHCCHHHHHHHHH	55.29	-
311	Ubiquitination	APSIHGHDYVKKAIL CHHHCCHHHHHHHHH	55.29	-
312	Phosphorylation	PSIHGHDYVKKAILC HHHCCHHHHHHHHHH	14.43	-
314	Acetylation	IHGHDYVKKAILCLL HCCHHHHHHHHHHHH	30.20	26051181
315	Ubiquitination	HGHDYVKKAILCLLL CCHHHHHHHHHHHHH	30.52	-
315	Ubiquitination	HGHDYVKKAILCLLL CCHHHHHHHHHHHHH	30.52	-
320	Phosphorylation	VKKAILCLLLGGVER HHHHHHHHHHCCCHH	3.87	-
328	Ubiquitination	LLGGVERDLENGSHI HHCCCHHHCCCCCCC	44.84	-
333	Phosphorylation	ERDLENGSHIRGDIN HHHCCCCCCCCCCEE	27.59	20068231
337	Phosphorylation	ENGSHIRGDINILLI CCCCCCCCCEEEEEE	39.28	-
338	Ubiquitination	NGSHIRGDINILLIG CCCCCCCCEEEEEEC	22.40	21890473
338	Ubiquitination	NGSHIRGDINILLIG CCCCCCCCEEEEEEC	22.40	-
346	Ubiquitination	INILLIGDPSVAKSQ EEEEEECCHHHHHHH	25.88	21890473
346	Ubiquitination	INILLIGDPSVAKSQ EEEEEECCHHHHHHH	25.88	-
351	2-Hydroxyisobutyrylation	IGDPSVAKSQLLRYV ECCHHHHHHHHHHHH	36.26	-
351	Ubiquitination	IGDPSVAKSQLLRYV ECCHHHHHHHHHHHH	36.26	21890473
357	Phosphorylation	AKSQLLRYVLCTAPR HHHHHHHHHHHCCCC	9.57	-
359	Ubiquitination	SQLLRYVLCTAPRAI HHHHHHHHHCCCCCC	1.27	-
360	Ubiquitination	QLLRYVLCTAPRAIP HHHHHHHHCCCCCCC	1.86	-
360	Glutathionylation	QLLRYVLCTAPRAIP HHHHHHHHCCCCCCC	1.86	22555962
360	S-palmitoylation	QLLRYVLCTAPRAIP HHHHHHHHCCCCCCC	1.86	29575903
360	Ubiquitination	QLLRYVLCTAPRAIP HHHHHHHHCCCCCCC	1.86	-
369	Phosphorylation	APRAIPTTGRGSSGV CCCCCCCCCCCCCCC	21.37	21210654
371	Methylation	RAIPTTGRGSSGVGL CCCCCCCCCCCCCCC	39.46	115482827
373	Phosphorylation	IPTTGRGSSGVGLTA CCCCCCCCCCCCCEE	23.66	26033855
374	Phosphorylation	PTTGRGSSGVGLTAA CCCCCCCCCCCCEEE	40.08	26033855
379	Phosphorylation	GSSGVGLTAAVTTDQ CCCCCCCEEEEECCC	13.47	26033855
383	Phosphorylation	VGLTAAVTTDQETGE CCCEEEEECCCCCCC	21.67	-
384	Phosphorylation	GLTAAVTTDQETGER CCEEEEECCCCCCCH	29.14	-
396	Ubiquitination	GERRLEAGAMVLADR CCHHHHHHCEEEECC	12.58	21890473
396	Ubiquitination	GERRLEAGAMVLADR CCHHHHHHCEEEECC	12.58	-
413	Acetylation	VCIDEFDKMSDMDRT EEECCCCCCCCCCHH	45.70	26822725
413	Ubiquitination	VCIDEFDKMSDMDRT EEECCCCCCCCCCHH	45.70	-
416	Methylation	DEFDKMSDMDRTAIH CCCCCCCCCCHHHHH	39.23	-
419	Methylation	DKMSDMDRTAIHEVM CCCCCCCHHHHHHHH	21.30	115482843
428	Phosphorylation	AIHEVMEQGRVTIAK HHHHHHHCCCEEEEE	27.22	-
429	Phosphorylation	IHEVMEQGRVTIAKA HHHHHHCCCEEEEEC	16.84	-
435	2-Hydroxyisobutyrylation	QGRVTIAKAGIHARL CCCEEEEECCHHHHH	43.21	-
435	Acetylation	QGRVTIAKAGIHARL CCCEEEEECCHHHHH	43.21	25953088
435	Ubiquitination	QGRVTIAKAGIHARL CCCEEEEECCHHHHH	43.21	21890473
446	Glutathionylation	HARLNARCSVLAAAN HHHHHHHHHHHHHHC	2.83	22555962
456	Nitration	LAAANPVYGRYDQYK HHHHCCCCCCCCCCC	9.35	-
456	Phosphorylation	LAAANPVYGRYDQYK HHHHCCCCCCCCCCC	9.35	28152594
458	Ubiquitination	AANPVYGRYDQYKTP HHCCCCCCCCCCCCC	17.73	-
458	Ubiquitination	AANPVYGRYDQYKTP HHCCCCCCCCCCCCC	17.73	-
459	Phosphorylation	ANPVYGRYDQYKTPM HCCCCCCCCCCCCCH	11.75	27174698
462	Phosphorylation	VYGRYDQYKTPMENI CCCCCCCCCCCHHHC	17.58	27174698
463	Ubiquitination	YGRYDQYKTPMENIG CCCCCCCCCCHHHCC	40.28	21906983
464	Methylation	GRYDQYKTPMENIGL CCCCCCCCCHHHCCC	23.96	-
464	Phosphorylation	GRYDQYKTPMENIGL CCCCCCCCCHHHCCC	23.96	27174698
466	Sulfoxidation	YDQYKTPMENIGLQD CCCCCCCHHHCCCCH	8.13	21406390
474	Phosphorylation	ENIGLQDSLLSRFDL HHCCCCHHHHHHHHH	20.46	27174698
477	Phosphorylation	GLQDSLLSRFDLLFI CCCHHHHHHHHHHHH	35.87	27174698
480	Ubiquitination	DSLLSRFDLLFIMLD HHHHHHHHHHHHHHH	41.15	21890473
480	Ubiquitination	DSLLSRFDLLFIMLD HHHHHHHHHHHHHHH	41.15	-
508	Ubiquitination	VLRMHRYRAPGEQDG HHHHHCCCCCCCCCC	33.97	-
508	Ubiquitination	VLRMHRYRAPGEQDG HHHHHCCCCCCCCCC	33.97	-
519	Phosphorylation	EQDGDAMPLGSAVDI CCCCCCCCCCHHHHE	34.98	-
522	Phosphorylation	GDAMPLGSAVDILAT CCCCCCCHHHHEEEC	32.57	20873877
529	Phosphorylation	SAVDILATDDPNFSQ HHHHEEECCCCCCCH	37.17	28464451
535	Phosphorylation	ATDDPNFSQEDQQDT ECCCCCCCHHHHHCC	39.02	30576142
542	Phosphorylation	SQEDQQDTQIYEKHD CHHHHHCCHHHHHHH	16.72	20873877
545	Phosphorylation	DQQDTQIYEKHDNLL HHHCCHHHHHHHCCC	14.76	28464451
547	Acetylation	QDTQIYEKHDNLLHG HCCHHHHHHHCCCCC	39.01	-
555	Phosphorylation	HDNLLHGTKKKKEKM HHCCCCCCHHHHHHH	29.01	28555341
556	2-Hydroxyisobutyrylation	DNLLHGTKKKKEKMV HCCCCCCHHHHHHHH	68.16	-
556	Acetylation	DNLLHGTKKKKEKMV HCCCCCCHHHHHHHH	68.16	25953088
559	Acetylation	LHGTKKKKEKMVSAA CCCCHHHHHHHHHHH	72.02	7975523
561	Acetylation	GTKKKKEKMVSAAFM CCHHHHHHHHHHHHH	54.18	25953088
564	Phosphorylation	KKKEKMVSAAFMKKY HHHHHHHHHHHHHHH	15.47	23403867
569	Acetylation	MVSAAFMKKYIHVAK HHHHHHHHHHHHHHH	35.65	25953088
570	Ubiquitination	VSAAFMKKYIHVAKI HHHHHHHHHHHHHHH	37.33	-
574	Phosphorylation	FMKKYIHVAKIIKPV HHHHHHHHHHHHHHH	4.15	27251275
579	Acetylation	IHVAKIIKPVLTQES HHHHHHHHHHCCHHH	32.33	26051181
579	Ubiquitination	IHVAKIIKPVLTQES HHHHHHHHHHCCHHH	32.33	21890473
580	Phosphorylation	HVAKIIKPVLTQESA HHHHHHHHHCCHHHH	18.88	15210935
599	Phosphorylation	EEYSRLRSQDSMSSD HHHHHHHCCCCCCCC	42.82	-
601	Ubiquitination	YSRLRSQDSMSSDTA HHHHHCCCCCCCCCC	47.78	-
602	Phosphorylation	SRLRSQDSMSSDTAR HHHHCCCCCCCCCCC	16.96	25954137
604	Phosphorylation	LRSQDSMSSDTARTS HHCCCCCCCCCCCCC	29.07	25954137
605	Phosphorylation	RSQDSMSSDTARTSP HCCCCCCCCCCCCCC	30.27	25954137
606	Ubiquitination	SQDSMSSDTARTSPV CCCCCCCCCCCCCCC	36.76	-
607	Phosphorylation	QDSMSSDTARTSPVT CCCCCCCCCCCCCCH	21.71	25954137
610	Phosphorylation	MSSDTARTSPVTART CCCCCCCCCCCHHHH	34.61	29214152
611	Phosphorylation	SSDTARTSPVTARTL CCCCCCCCCCHHHHH	16.30	23917254
614	Acetylation	TARTSPVTARTLETL CCCCCCCHHHHHHHH	17.51	19608861
615	Ubiquitination	ARTSPVTARTLETLI CCCCCCHHHHHHHHH	11.60	-
615	Ubiquitination	ARTSPVTARTLETLI CCCCCCHHHHHHHHH	11.60	-
617	O-linked_Glycosylation	TSPVTARTLETLIRL CCCCHHHHHHHHHHH	26.87	28510447
617	Phosphorylation	TSPVTARTLETLIRL CCCCHHHHHHHHHHH	26.87	20068231
620	Phosphorylation	VTARTLETLIRLATA CHHHHHHHHHHHHHH	30.51	20068231
624	Ubiquitination	TLETLIRLATAHAKA HHHHHHHHHHHHHHH	3.83	21890473
624	Ubiquitination	TLETLIRLATAHAKA HHHHHHHHHHHHHHH	3.83	-
630	2-Hydroxyisobutyrylation	RLATAHAKARMSKTV HHHHHHHHHHHCCCC	27.02	-
651	Phosphorylation	EAVELVQYAYFKKVL HHHHHHHHHHHHHHH	8.86	-
656	Phosphorylation	VQYAYFKKVLEKEKK HHHHHHHHHHHHHHH	42.00	-
662	Phosphorylation	KKVLEKEKKRKKRSE HHHHHHHHHHHHCCC	69.79	20068231
668	Phosphorylation	EKKRKKRSEDESETE HHHHHHCCCCCCCCH	59.27	29255136
672	Phosphorylation	KKRSEDESETEDEEE HHCCCCCCCCHHHHH	63.24	29255136
674	Phosphorylation	RSEDESETEDEEEKS CCCCCCCCHHHHHHH	59.00	29255136
680	Ubiquitination	ETEDEEEKSQEDQEQ CCHHHHHHHHHHHHH	61.80	-
681	Phosphorylation	TEDEEEKSQEDQEQK CHHHHHHHHHHHHHH	41.92	17525332
694	Phosphorylation	QKRKRRKTRQPDAKD HHHHHHHHCCCCCCC	32.50	23403867
700	Ubiquitination	KTRQPDAKDGDSYDP HHCCCCCCCCCCCCC	70.40	-
704	Phosphorylation	PDAKDGDSYDPYDFS CCCCCCCCCCCCCCC	36.64	23927012
705	Phosphorylation	DAKDGDSYDPYDFSD CCCCCCCCCCCCCCC	26.19	23927012
708	Phosphorylation	DGDSYDPYDFSDTEE CCCCCCCCCCCCCCC	27.07	23927012
711	Phosphorylation	SYDPYDFSDTEEEMP CCCCCCCCCCCCCCC	40.50	19664994
713	Phosphorylation	DPYDFSDTEEEMPQV CCCCCCCCCCCCCCC	44.06	23927012
717	Phosphorylation	FSDTEEEMPQVHTPK CCCCCCCCCCCCCCC	2.96	17525332
719	Phosphorylation	DTEEEMPQVHTPKTA CCCCCCCCCCCCCCC	38.01	17525332
722	Phosphorylation	EEMPQVHTPKTADSQ CCCCCCCCCCCCCCH	27.85	19664994
725	Phosphorylation	PQVHTPKTADSQETK CCCCCCCCCCCHHCH	36.58	28176443
726	Phosphorylation	QVHTPKTADSQETKE CCCCCCCCCCHHCHH	22.15	17525332
728	Phosphorylation	HTPKTADSQETKESQ CCCCCCCCHHCHHHH	27.70	23401153
731	Phosphorylation	KTADSQETKESQKVE CCCCCHHCHHHHCEE	32.26	28450419
732	Sumoylation	TADSQETKESQKVEL CCCCHHCHHHHCEEC	55.40	-
732	Acetylation	TADSQETKESQKVEL CCCCHHCHHHHCEEC	55.40	26051181
732	Ubiquitination	TADSQETKESQKVEL CCCCHHCHHHHCEEC	55.40	21906983
733	Ubiquitination	ADSQETKESQKVELS CCCHHCHHHHCEECC	66.86	-
734	Phosphorylation	DSQETKESQKVELSE CCHHCHHHHCEECCH	36.54	17525332
736	Sumoylation	QETKESQKVELSESR HHCHHHHCEECCHHH	47.13	-
736	Acetylation	QETKESQKVELSESR HHCHHHHCEECCHHH	47.13	23236377
736	Ubiquitination	QETKESQKVELSESR HHCHHHHCEECCHHH	47.13	-
740	Phosphorylation	ESQKVELSESRLKAF HHHCEECCHHHHHHH	21.74	21815630
742	Phosphorylation	QKVELSESRLKAFKV HCEECCHHHHHHHHH	39.27	27050516
743	Methylation	KVELSESRLKAFKVA CEECCHHHHHHHHHH	35.84	115482851
748	Ubiquitination	ESRLKAFKVALLDVF HHHHHHHHHHHHHHH	31.30	21890473
749	Phosphorylation	SRLKAFKVALLDVFR HHHHHHHHHHHHHHH	3.52	20068231
750	Phosphorylation	RLKAFKVALLDVFRE HHHHHHHHHHHHHHH	11.73	17081983
753	Phosphorylation	AFKVALLDVFREAHA HHHHHHHHHHHHHHH	38.06	20068231
756	Phosphorylation	VALLDVFREAHAQSI HHHHHHHHHHHHHHH	39.79	19664994
758	Phosphorylation	LLDVFREAHAQSIGM HHHHHHHHHHHHHCH	10.08	20230923
762	Phosphorylation	FREAHAQSIGMNRLT HHHHHHHHHCHHHHH	23.15	22817901
767	Phosphorylation	AQSIGMNRLTESINR HHHHCHHHHHHHHCC	33.81	19664994
769	Phosphorylation	SIGMNRLTESINRDS HHCHHHHHHHHCCCC	25.17	22817901
770	Phosphorylation	IGMNRLTESINRDSE HCHHHHHHHHCCCCC	54.97	-
773	Phosphorylation	NRLTESINRDSEEPF HHHHHHHCCCCCCCC	51.49	17525332
776	Phosphorylation	TESINRDSEEPFSSV HHHHCCCCCCCCCHH	40.39	21406692
777	Ubiquitination	ESINRDSEEPFSSVE HHHCCCCCCCCCHHH	74.17	-
777	Sumoylation	ESINRDSEEPFSSVE HHHCCCCCCCCCHHH	74.17	-
777	Ubiquitination	ESINRDSEEPFSSVE HHHCCCCCCCCCHHH	74.17	-
779	Phosphorylation	INRDSEEPFSSVEIQ HCCCCCCCCCHHHHH	30.30	17525332
781	Acetylation	RDSEEPFSSVEIQAA CCCCCCCCHHHHHHH	44.16	-
781	Ubiquitination	RDSEEPFSSVEIQAA CCCCCCCCHHHHHHH	44.16	-
781	Phosphorylation	RDSEEPFSSVEIQAA CCCCCCCCHHHHHHH	44.16	21406692
781	Sumoylation	RDSEEPFSSVEIQAA CCCCCCCCHHHHHHH	44.16	-
781	Ubiquitination	RDSEEPFSSVEIQAA CCCCCCCCHHHHHHH	44.16	-
782	Phosphorylation	DSEEPFSSVEIQAAL CCCCCCCHHHHHHHH	24.93	21406692
785	Phosphorylation	EPFSSVEIQAALSKM CCCCHHHHHHHHHHC	2.94	-
787	Phosphorylation	FSSVEIQAALSKMQD CCHHHHHHHHHHCCC	18.94	-
788	Methylation	SSVEIQAALSKMQDD CHHHHHHHHHHCCCC	8.94	-
790	Phosphorylation	VEIQAALSKMQDDNQ HHHHHHHHHCCCCCC	22.73	21406692
793	Ubiquitination	QAALSKMQDDNQVMV HHHHHHCCCCCCEEE	59.65	21890473
793	Ubiquitination	QAALSKMQDDNQVMV HHHHHHCCCCCCEEE	59.65	-

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
160	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
160	S	Phosphorylation	Kinase	DAPK1	P53355	PSP
160	S	Phosphorylation	Kinase	DAPK-FAMILY	-	GPS
535	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
535	S	Phosphorylation	Kinase	ATR	Q13535	PSP
722	T	Phosphorylation	Kinase	CDK2	P24941	PSP
728	S	Phosphorylation	Kinase	ATM	Q62388	PSP
728	S	Phosphorylation	Kinase	ATR	Q9JKK8	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	KEAP1	Q14145	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM3_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 MCM3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM2_HUMAN	MCM2	physical	12614612
MCM5_HUMAN	MCM5	physical	12614612
CDC45_HUMAN	CDC45	physical	12614612
DBF4A_HUMAN	DBF4	physical	12614612
ORC5_HUMAN	ORC5	physical	12614612
ORC4_HUMAN	ORC4	physical	12614612
MCM7_HUMAN	MCM7	physical	12614612
GANP_HUMAN	MCM3AP	physical	10733502
GANP_HUMAN	MCM3AP	physical	9712829
MCM7_HUMAN	MCM7	physical	11779870
LZTR1_HUMAN	LZTR1	physical	20211142
SYF2_HUMAN	SYF2	physical	16951160
CCL2_HUMAN	CCL2	physical	21383955
HIF1A_HUMAN	HIF1A	physical	21658608
EPAS1_HUMAN	EPAS1	physical	21658608
CDK2_HUMAN	CDK2	physical	21965652
CCNE1_HUMAN	CCNE1	physical	21965652
MCM5_HUMAN	MCM5	physical	22939629
MCM7_HUMAN	MCM7	physical	22939629
MCM6_HUMAN	MCM6	physical	22939629
MCM4_HUMAN	MCM4	physical	22939629
RFA2_HUMAN	RPA2	physical	22939629
RFC4_HUMAN	RFC4	physical	22939629
RFC3_HUMAN	RFC3	physical	22939629
PUR1_HUMAN	PPAT	physical	22939629
MCM2_HUMAN	MCM2	physical	15232106
MCM5_HUMAN	MCM5	physical	15232106
MCM10_HUMAN	MCM10	physical	15232106
ORC4_HUMAN	ORC4	physical	15232106
FKBP4_HUMAN	FKBP4	physical	22863883
FKBP5_HUMAN	FKBP5	physical	22863883
HS90A_HUMAN	HSP90AA1	physical	22863883
SAE1_HUMAN	SAE1	physical	22863883
TPM3_HUMAN	TPM3	physical	22863883
SLD5_HUMAN	GINS4	physical	26344197
HNRPF_HUMAN	HNRNPF	physical	26344197
HNRH2_HUMAN	HNRNPH2	physical	26344197
HNRH3_HUMAN	HNRNPH3	physical	26344197
MCFD2_HUMAN	MCFD2	physical	26344197
MCM2_HUMAN	MCM2	physical	26344197
MCM7_HUMAN	MCM7	physical	26344197
MCMBP_HUMAN	MCMBP	physical	26344197
CNDD3_HUMAN	NCAPD3	physical	26344197
NUP62_HUMAN	NUP62	physical	26344197
NUP88_HUMAN	NUP88	physical	26344197
RPB4_HUMAN	POLR2D	physical	26344197
ZO2_HUMAN	TJP2	physical	26344197
1433G_HUMAN	YWHAG	physical	26344197
MCMBP_HUMAN	MCMBP	physical	28514442
MCM5_HUMAN	MCM5	physical	28514442
TSNAX_HUMAN	TSNAX	physical	28514442
MCM7_HUMAN	MCM7	physical	28514442
TIM_HUMAN	TIMELESS	physical	28514442
MCM4_HUMAN	MCM4	physical	28514442
YIPF3_HUMAN	YIPF3	physical	28514442
MCM2_HUMAN	MCM2	physical	28514442
MCM6_HUMAN	MCM6	physical	28514442
EAF1_HUMAN	EAF1	physical	27173435
FACD2_HUMAN	FANCD2	physical	23993743
MCM2_HUMAN	MCM2	physical	23993743
MCM5_HUMAN	MCM5	physical	23993743
MCM7_HUMAN	MCM7	physical	23993743

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 MCM3_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-704; TYR-708; SER-711; THR-713 AND THR-722, ANDMASS SPECTROMETRY.	19413330 [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-672; THR-674; TYR-708;SER-711; THR-713; THR-722 AND THR-725, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-711 AND THR-722, ANDMASS SPECTROMETRY.	19369195 [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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-704; TYR-708; SER-711; THR-713 AND THR-722, ANDMASS SPECTROMETRY.	19413330 [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-160; SER-668; SER-672;THR-674; SER-681; SER-711; THR-713 AND THR-722, 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-711 AND THR-722, ANDMASS SPECTROMETRY.	18691976 [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-672; THR-674; SER-681;SER-728 AND SER-734, AND MASS SPECTROMETRY.	17525332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704; SER-711 ANDTHR-713, AND MASS SPECTROMETRY.	17287340 [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-672 AND THR-674, 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-672; THR-674; SER-711;THR-713 AND THR-722, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Minichromosome maintenance proteins are direct targets of the ATM andATR checkpoint kinases."; Cortez D., Glick G., Elledge S.J.; Proc. Natl. Acad. Sci. U.S.A. 101:10078-10083(2004). Cited for: PHOSPHORYLATION AT SER-535, AND MUTAGENESIS OF SER-535.	15210935 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-713 AND THR-722, ANDMASS SPECTROMETRY.	17487921 [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 THR-713 AND THR-722, ANDMASS SPECTROMETRY.	15302935 [Abstract]