dbPTM

MCM10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM10_HUMAN
UniProt AC	Q7L590
Protein Name	Protein MCM10 homolog
Gene Name	MCM10
Organism	Homo sapiens (Human).
Sequence Length	875
Subcellular Localization	Nucleus . Colocalizes with ORC2 in nuclei foci. Associated with chromatin in S phase. From early to mid-S phase located in discrete nuclear foci. In early S phase, several hundred foci appeared throughout the nucleus. In mid-S phase, the foci appeare
Protein Description	Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication. Key effector of the RBBP6 and ZBTB38-mediated regulation of DNA-replication and common fragile sites stability; acts as a direct target of transcriptional repression by ZBTB38. [PubMed: 24726359]
Protein Sequence	MDEEEDNLSLLTALLEENESALDCNSEENNFLTRENGEPDAFDELFDADGDGESYTEEADDGETGETRDEKENLATLFGDMEDLTDEEEVPASQSTENRVLPAPAPRREKTNEELQEELRNLQEQMKALQEQLKVTTIKQTASPARLQKSPVEKSPRPPLKERRVQRIQESTCFSAELDVPALPRTKRVARTPKASPPDPKSSSSRMTSAPSQPLQTISRNKPSGITRGQIVGTPGSSGETTQPICVEAFSGLRLRRPRVSSTEMNKKMTGRKLIRLSQIKEKMAREKLEEIDWVTFGVILKKVTPQSVNSGKTFSIWKLNDLRDLTQCVSLFLFGEVHKALWKTEQGTVVGILNANPMKPKDGSEEVCLSIDHPQKVLIMGEALDLGTCKAKKKNGEPCTQTVNLRDCEYCQYHVQAQYKKLSAKRADLQSTFSGGRIPKKFARRGTSLKERLCQDGFYYGGVSSASYAASIAAAVAPKKKIQTTLSNLVVKGTNLIIQETRQKLGIPQKSLSCSEEFKELMDLPTCGARNLKQHLAKATASGIMGSPKPAIKSISASALLKQQKQRMLEMRRRKSEEIQKRFLQSSSEVESPAVPSSSRQPPAQPPRTGSEFPRLEGAPATMTPKLGRGVLEGDDVLFYDESPPPRPKLSALAEAKKLAAITKLRAKGQVLTKTNPNSIKKKQKDPQDILEVKERVEKNTMFSSQAEDELEPARKKRREQLAYLESEEFQKILKAKSKHTGILKEAEAEMQERYFEPLVKKEQMEEKMRNIREVKCRVVTCKTCAYTHFKLLETCVSEQHEYHWHDGVKRFFKCPCGNRSISLDRLPNKHCSNCGLYKWERDGMLKEKTGPKIGGETLLPRGEEHAKFLNSLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26	Phosphorylation	ESALDCNSEENNFLT CCHHCCCCHHCCEEE	53.25	25159151
54	Phosphorylation	DADGDGESYTEEADD CCCCCCCCCCEECCC	42.77	30576142
55	Phosphorylation	ADGDGESYTEEADDG CCCCCCCCCEECCCC	17.54	30576142
56	Phosphorylation	DGDGESYTEEADDGE CCCCCCCCEECCCCC	36.31	30576142
67	Phosphorylation	DDGETGETRDEKENL CCCCCCCCHHHHHHH	44.77	30576142
76	Phosphorylation	DEKENLATLFGDMED HHHHHHHHHHCCHHH	26.28	30266825
85	Phosphorylation	FGDMEDLTDEEEVPA HCCHHHCCCCCCCCC	54.40	17525332
93	Phosphorylation	DEEEVPASQSTENRV CCCCCCCCCCCCCCC	20.70	17525332
95	Phosphorylation	EEVPASQSTENRVLP CCCCCCCCCCCCCCC	34.88	30266825
96	Phosphorylation	EVPASQSTENRVLPA CCCCCCCCCCCCCCC	29.64	30266825
110	Ubiquitination	APAPRREKTNEELQE CCCCCCHHCHHHHHH	55.64	29967540
127	Ubiquitination	RNLQEQMKALQEQLK HHHHHHHHHHHHHHC	45.71	29967540
134	Sumoylation	KALQEQLKVTTIKQT HHHHHHHCHHHHHCC	36.91	-
134	Sumoylation	KALQEQLKVTTIKQT HHHHHHHCHHHHHCC	36.91	-
134	Ubiquitination	KALQEQLKVTTIKQT HHHHHHHCHHHHHCC	36.91	-
139	Sumoylation	QLKVTTIKQTASPAR HHCHHHHHCCCCCHH	39.23	-
139	Sumoylation	QLKVTTIKQTASPAR HHCHHHHHCCCCCHH	39.23	-
139	Ubiquitination	QLKVTTIKQTASPAR HHCHHHHHCCCCCHH	39.23	32015554
141	Phosphorylation	KVTTIKQTASPARLQ CHHHHHCCCCCHHHC	24.89	26074081
143	Phosphorylation	TTIKQTASPARLQKS HHHHCCCCCHHHCCC	23.60	26074081
143 (in isoform 2)	Phosphorylation	-	23.60	25159151
150	Phosphorylation	SPARLQKSPVEKSPR CCHHHCCCCCCCCCC	22.63	27251275
150 (in isoform 2)	Phosphorylation	-	22.63	25159151
154 (in isoform 2)	Phosphorylation	-	67.03	20873877
155	Phosphorylation	QKSPVEKSPRPPLKE CCCCCCCCCCCCCHH	16.79	-
192	Phosphorylation	RTKRVARTPKASPPD CCCCCCCCCCCCCCC	21.28	26055452
196	Phosphorylation	VARTPKASPPDPKSS CCCCCCCCCCCCCCC	42.99	28985074
203	Phosphorylation	SPPDPKSSSSRMTSA CCCCCCCCCCCCCCC	38.16	25332170
205	Phosphorylation	PDPKSSSSRMTSAPS CCCCCCCCCCCCCCC	28.19	25332170
208	Phosphorylation	KSSSSRMTSAPSQPL CCCCCCCCCCCCCCC	22.19	29888752
209	Phosphorylation	SSSSRMTSAPSQPLQ CCCCCCCCCCCCCCC	28.92	29888752
212	Phosphorylation	SRMTSAPSQPLQTIS CCCCCCCCCCCCCCC	44.11	29888752
217	Phosphorylation	APSQPLQTISRNKPS CCCCCCCCCCCCCCC	28.71	29888752
219	Phosphorylation	SQPLQTISRNKPSGI CCCCCCCCCCCCCCC	32.94	29888752
221	Ubiquitination	PLQTISRNKPSGITR CCCCCCCCCCCCCCC	54.52	29967540
222	Ubiquitination	LQTISRNKPSGITRG CCCCCCCCCCCCCCC	39.18	29967540
234	Phosphorylation	TRGQIVGTPGSSGET CCCEEECCCCCCCCC	17.37	27050516
238	Phosphorylation	IVGTPGSSGETTQPI EECCCCCCCCCCCCE	46.71	21712546
261	Phosphorylation	RLRRPRVSSTEMNKK CCCCCCCCCCHHHHH	32.59	28985074
278	Phosphorylation	GRKLIRLSQIKEKMA HHHHHHHHHHHHHHH	21.73	24719451
296	Phosphorylation	LEEIDWVTFGVILKK HHHCCCEEEEEEEEE	15.49	18452278
302	Ubiquitination	VTFGVILKKVTPQSV EEEEEEEEECCCCCC	33.79	29967540
303	Ubiquitination	TFGVILKKVTPQSVN EEEEEEEECCCCCCC	48.14	29967540
305	Phosphorylation	GVILKKVTPQSVNSG EEEEEECCCCCCCCC	25.21	30266825
308	Phosphorylation	LKKVTPQSVNSGKTF EEECCCCCCCCCCCE	25.19	30266825
311	Phosphorylation	VTPQSVNSGKTFSIW CCCCCCCCCCCEEEE	39.24	30266825
312	Ubiquitination	TPQSVNSGKTFSIWK CCCCCCCCCCEEEEE	28.02	23000965
313	Sumoylation	PQSVNSGKTFSIWKL CCCCCCCCCEEEEEE	46.33	-
313	Acetylation	PQSVNSGKTFSIWKL CCCCCCCCCEEEEEE	46.33	26051181
313	Sumoylation	PQSVNSGKTFSIWKL CCCCCCCCCEEEEEE	46.33	-
313	Ubiquitination	PQSVNSGKTFSIWKL CCCCCCCCCEEEEEE	46.33	23000965
314	Phosphorylation	QSVNSGKTFSIWKLN CCCCCCCCEEEEEEC	26.58	-
316	Phosphorylation	VNSGKTFSIWKLNDL CCCCCCEEEEEECCH	32.54	25137130
318	Ubiquitination	SGKTFSIWKLNDLRD CCCCEEEEEECCHHH	9.63	23000965
319	Acetylation	GKTFSIWKLNDLRDL CCCEEEEEECCHHHH	35.42	25953088
319	Ubiquitination	GKTFSIWKLNDLRDL CCCEEEEEECCHHHH	35.42	23000965
359	Ubiquitination	GILNANPMKPKDGSE EEEECCCCCCCCCCC	13.40	29967540
360	Ubiquitination	ILNANPMKPKDGSEE EEECCCCCCCCCCCE	50.61	29967540
362	Sumoylation	NANPMKPKDGSEEVC ECCCCCCCCCCCEEE	70.02	-
362	Sumoylation	NANPMKPKDGSEEVC ECCCCCCCCCCCEEE	70.02	-
395	Ubiquitination	GTCKAKKKNGEPCTQ HCCCCCHHCCCCCCE	70.27	-
435	Phosphorylation	ADLQSTFSGGRIPKK HHHHCHHCCCCCCHH	40.19	25159151
448	Phosphorylation	KKFARRGTSLKERLC HHHHCCCCCHHHHHC	29.13	27251275
449	Phosphorylation	KFARRGTSLKERLCQ HHHCCCCCHHHHHCC	40.02	27251275
460	Phosphorylation	RLCQDGFYYGGVSSA HHCCCCCCCCCCCHH	13.51	-
461	Phosphorylation	LCQDGFYYGGVSSAS HCCCCCCCCCCCHHH	12.73	28985074
468	Phosphorylation	YGGVSSASYAASIAA CCCCCHHHHHHHHHH	19.77	28985074
469	Phosphorylation	GGVSSASYAASIAAA CCCCHHHHHHHHHHH	13.10	28985074
472	Phosphorylation	SSASYAASIAAAVAP CHHHHHHHHHHHHCC	12.46	-
481	Ubiquitination	AAAVAPKKKIQTTLS HHHHCCHHHHHHHHH	54.79	33845483
482	Sumoylation	AAVAPKKKIQTTLSN HHHCCHHHHHHHHHH	46.29	-
482	Sumoylation	AAVAPKKKIQTTLSN HHHCCHHHHHHHHHH	46.29	-
482	Ubiquitination	AAVAPKKKIQTTLSN HHHCCHHHHHHHHHH	46.29	33845483
485	Phosphorylation	APKKKIQTTLSNLVV CCHHHHHHHHHHHHH	32.93	29978859
486	Phosphorylation	PKKKIQTTLSNLVVK CHHHHHHHHHHHHHC	16.29	29978859
488	Phosphorylation	KKIQTTLSNLVVKGT HHHHHHHHHHHHCCC	26.48	29978859
492	Ubiquitination	TTLSNLVVKGTNLII HHHHHHHHCCCCEEE	5.51	32015554
493	Sumoylation	TLSNLVVKGTNLIIQ HHHHHHHCCCCEEEH	53.16	28112733
493	Ubiquitination	TLSNLVVKGTNLIIQ HHHHHHHCCCCEEEH	53.16	32015554
495	Phosphorylation	SNLVVKGTNLIIQET HHHHHCCCCEEEHHH	22.57	27461979
504	Ubiquitination	LIIQETRQKLGIPQK EEEHHHHHHHCCCHH	53.39	29967540
505	Ubiquitination	IIQETRQKLGIPQKS EEHHHHHHHCCCHHH	45.44	29967540
510	Ubiquitination	RQKLGIPQKSLSCSE HHHHCCCHHHCCCCH	46.15	32015554
511	Sumoylation	QKLGIPQKSLSCSEE HHHCCCHHHCCCCHH	48.27	-
511	Sumoylation	QKLGIPQKSLSCSEE HHHCCCHHHCCCCHH	48.27	-
511	Ubiquitination	QKLGIPQKSLSCSEE HHHCCCHHHCCCCHH	48.27	32015554
514	Phosphorylation	GIPQKSLSCSEEFKE CCCHHHCCCCHHHHH	23.76	25159151
519	Ubiquitination	SLSCSEEFKELMDLP HCCCCHHHHHHHCCC	6.99	29967540
520	Ubiquitination	LSCSEEFKELMDLPT CCCCHHHHHHHCCCC	53.90	29967540
533	Ubiquitination	PTCGARNLKQHLAKA CCCCCHHHHHHHHHH	4.75	29967540
534	Sumoylation	TCGARNLKQHLAKAT CCCCHHHHHHHHHHH	38.94	-
534	Sumoylation	TCGARNLKQHLAKAT CCCCHHHHHHHHHHH	38.94	-
534	Ubiquitination	TCGARNLKQHLAKAT CCCCHHHHHHHHHHH	38.94	29967540
538	Ubiquitination	RNLKQHLAKATASGI HHHHHHHHHHHHHCC	9.41	29967540
539	Ubiquitination	NLKQHLAKATASGIM HHHHHHHHHHHHCCC	53.26	29967540
541	Phosphorylation	KQHLAKATASGIMGS HHHHHHHHHHCCCCC	22.20	-
543	Phosphorylation	HLAKATASGIMGSPK HHHHHHHHCCCCCCH	25.21	27050516
548	Phosphorylation	TASGIMGSPKPAIKS HHHCCCCCCHHHHHH	16.63	25159151
554	Acetylation	GSPKPAIKSISASAL CCCHHHHHHCCHHHH	43.79	26051181
554	Methylation	GSPKPAIKSISASAL CCCHHHHHHCCHHHH	43.79	115972877
557	Phosphorylation	KPAIKSISASALLKQ HHHHHHCCHHHHHHH	24.22	20068231
559	Phosphorylation	AIKSISASALLKQQK HHHHCCHHHHHHHHH	16.80	20068231
562	Ubiquitination	SISASALLKQQKQRM HCCHHHHHHHHHHHH	4.75	29967540
563	Ubiquitination	ISASALLKQQKQRML CCHHHHHHHHHHHHH	52.08	29967540
566	Ubiquitination	SALLKQQKQRMLEMR HHHHHHHHHHHHHHH	37.06	-
587	Phosphorylation	IQKRFLQSSSEVESP HHHHHHHCCCCCCCC	37.67	25072903
588	Phosphorylation	QKRFLQSSSEVESPA HHHHHHCCCCCCCCC	19.98	25072903
589	Phosphorylation	KRFLQSSSEVESPAV HHHHHCCCCCCCCCC	51.40	25072903
593	Phosphorylation	QSSSEVESPAVPSSS HCCCCCCCCCCCCCC	24.28	21815630
598	Phosphorylation	VESPAVPSSSRQPPA CCCCCCCCCCCCCCC	34.05	25072903
599	Phosphorylation	ESPAVPSSSRQPPAQ CCCCCCCCCCCCCCC	24.38	25072903
600	Phosphorylation	SPAVPSSSRQPPAQP CCCCCCCCCCCCCCC	38.99	25072903
610	Phosphorylation	PPAQPPRTGSEFPRL CCCCCCCCCCCCCCC	51.32	-
612	Phosphorylation	AQPPRTGSEFPRLEG CCCCCCCCCCCCCCC	35.14	-
623	Phosphorylation	RLEGAPATMTPKLGR CCCCCCCCCCCCCCC	22.10	30001349
624	Sulfoxidation	LEGAPATMTPKLGRG CCCCCCCCCCCCCCC	7.02	21406390
625	Phosphorylation	EGAPATMTPKLGRGV CCCCCCCCCCCCCCC	16.96	23403867
626	Ubiquitination	GAPATMTPKLGRGVL CCCCCCCCCCCCCCC	21.03	22817900
626 (in isoform 2)	Ubiquitination	-	21.03	21906983
627	Sumoylation	APATMTPKLGRGVLE CCCCCCCCCCCCCCC	55.17	-
627	Sumoylation	APATMTPKLGRGVLE CCCCCCCCCCCCCCC	55.17	28112733
627	Ubiquitination	APATMTPKLGRGVLE CCCCCCCCCCCCCCC	55.17	22817900
627 (in isoform 1)	Ubiquitination	-	55.17	21906983
641	Phosphorylation	EGDDVLFYDESPPPR CCCCEEEECCCCCCC	18.03	30576142
644	Phosphorylation	DVLFYDESPPPRPKL CEEEECCCCCCCCHH	39.55	30266825
649	Ubiquitination	DESPPPRPKLSALAE CCCCCCCCHHHHHHH	47.95	29967540
650	Ubiquitination	ESPPPRPKLSALAEA CCCCCCCHHHHHHHH	57.25	29967540
652	Phosphorylation	PPPRPKLSALAEAKK CCCCCHHHHHHHHHH	27.62	26074081
657	Ubiquitination	KLSALAEAKKLAAIT HHHHHHHHHHHHHHH	14.53	29967540
658	Ubiquitination	LSALAEAKKLAAITK HHHHHHHHHHHHHHH	39.56	29967540
659	Ubiquitination	SALAEAKKLAAITKL HHHHHHHHHHHHHHH	50.86	29967540
664	Phosphorylation	AKKLAAITKLRAKGQ HHHHHHHHHHHHCCC	21.21	-
665	Sumoylation	KKLAAITKLRAKGQV HHHHHHHHHHHCCCE	29.84	-
665	Acetylation	KKLAAITKLRAKGQV HHHHHHHHHHHCCCE	29.84	25953088
665	Sumoylation	KKLAAITKLRAKGQV HHHHHHHHHHHCCCE	29.84	-
665	Ubiquitination	KKLAAITKLRAKGQV HHHHHHHHHHHCCCE	29.84	-
669	Sumoylation	AITKLRAKGQVLTKT HHHHHHHCCCEEECC	43.36	-
669	Sumoylation	AITKLRAKGQVLTKT HHHHHHHCCCEEECC	43.36	-
674	Ubiquitination	RAKGQVLTKTNPNSI HHCCCEEECCCCCCC	36.65	29967540
675	Sumoylation	AKGQVLTKTNPNSIK HCCCEEECCCCCCCC	41.99	-
675	Sumoylation	AKGQVLTKTNPNSIK HCCCEEECCCCCCCC	41.99	-
675	Ubiquitination	AKGQVLTKTNPNSIK HCCCEEECCCCCCCC	41.99	29967540
676	O-linked_Glycosylation	KGQVLTKTNPNSIKK CCCEEECCCCCCCCC	51.15	30379171
682	Sumoylation	KTNPNSIKKKQKDPQ CCCCCCCCCCCCCHH	54.46	-
682	Sumoylation	KTNPNSIKKKQKDPQ CCCCCCCCCCCCCHH	54.46	-
685	Ubiquitination	PNSIKKKQKDPQDIL CCCCCCCCCCHHHHH	65.35	29967540
686	Ubiquitination	NSIKKKQKDPQDILE CCCCCCCCCHHHHHH	79.03	29967540
694	Ubiquitination	DPQDILEVKERVEKN CHHHHHHHHHHHHHH	7.56	29967540
695	Sumoylation	PQDILEVKERVEKNT HHHHHHHHHHHHHHC	30.35	-
695	Sumoylation	PQDILEVKERVEKNT HHHHHHHHHHHHHHC	30.35	-
695	Ubiquitination	PQDILEVKERVEKNT HHHHHHHHHHHHHHC	30.35	29967540
702	Phosphorylation	KERVEKNTMFSSQAE HHHHHHHCCCCCCCC	30.57	-
705	Phosphorylation	VEKNTMFSSQAEDEL HHHHCCCCCCCCCCC	15.66	-
706	Phosphorylation	EKNTMFSSQAEDELE HHHCCCCCCCCCCCH	23.34	-
725	Phosphorylation	KRREQLAYLESEEFQ HHHHHHHHHCHHHHH	21.42	20068231
728	Phosphorylation	EQLAYLESEEFQKIL HHHHHHCHHHHHHHH	39.57	20068231
732	Ubiquitination	YLESEEFQKILKAKS HHCHHHHHHHHHHHH	34.85	29967540
733	Ubiquitination	LESEEFQKILKAKSK HCHHHHHHHHHHHHC	56.16	29967540
739	Phosphorylation	QKILKAKSKHTGILK HHHHHHHHCCCCCCH	34.23	29396449
739	Ubiquitination	QKILKAKSKHTGILK HHHHHHHHCCCCCCH	34.23	29967540
740	Ubiquitination	KILKAKSKHTGILKE HHHHHHHCCCCCCHH	44.47	29967540
745	Ubiquitination	KSKHTGILKEAEAEM HHCCCCCCHHHHHHH	4.31	29967540
746	Sumoylation	SKHTGILKEAEAEMQ HCCCCCCHHHHHHHH	53.62	-
746	Sumoylation	SKHTGILKEAEAEMQ HCCCCCCHHHHHHHH	53.62	-
746	Ubiquitination	SKHTGILKEAEAEMQ HCCCCCCHHHHHHHH	53.62	29967540
756	Phosphorylation	EAEMQERYFEPLVKK HHHHHHHHHHHHHCH	16.13	27642862
761	Ubiquitination	ERYFEPLVKKEQMEE HHHHHHHHCHHHHHH	14.07	29967540
762	Sumoylation	RYFEPLVKKEQMEEK HHHHHHHCHHHHHHH	59.27	-
762	Sumoylation	RYFEPLVKKEQMEEK HHHHHHHCHHHHHHH	59.27	28112733
762	Ubiquitination	RYFEPLVKKEQMEEK HHHHHHHCHHHHHHH	59.27	29967540
763	Sumoylation	YFEPLVKKEQMEEKM HHHHHHCHHHHHHHH	45.78	28112733
763	Ubiquitination	YFEPLVKKEQMEEKM HHHHHHCHHHHHHHH	45.78	-
769	Sumoylation	KKEQMEEKMRNIREV CHHHHHHHHHHHHHC	29.83	-
769	Sumoylation	KKEQMEEKMRNIREV CHHHHHHHHHHHHHC	29.83	-
777	Acetylation	MRNIREVKCRVVTCK HHHHHHCEEEEEECC	16.15	12436479
810	Ubiquitination	EYHWHDGVKRFFKCP CEECCCCCEEEEECC	5.11	29967540
811	Ubiquitination	YHWHDGVKRFFKCPC EECCCCCEEEEECCC	49.36	29967540
815	Ubiquitination	DGVKRFFKCPCGNRS CCCEEEEECCCCCCE	34.26	-
824	Phosphorylation	PCGNRSISLDRLPNK CCCCCEEECCCCCCC	26.01	25159151
827	Methylation	NRSISLDRLPNKHCS CCEEECCCCCCCCCC	58.29	115482797
830	Ubiquitination	ISLDRLPNKHCSNCG EECCCCCCCCCCCCC	51.82	29967540
831	Ubiquitination	SLDRLPNKHCSNCGL ECCCCCCCCCCCCCC	44.01	29967540
854	Sumoylation	LKEKTGPKIGGETLL CCCCCCCCCCCCCCC	56.16	-
854	Sumoylation	LKEKTGPKIGGETLL CCCCCCCCCCCCCCC	56.16	-
854	Ubiquitination	LKEKTGPKIGGETLL CCCCCCCCCCCCCCC	56.16	-
868	Ubiquitination	LPRGEEHAKFLNSLK CCCHHHHHHHHHHCC	13.94	29967540
869	Sumoylation	PRGEEHAKFLNSLK- CCHHHHHHHHHHCC-	52.90	-
869	Sumoylation	PRGEEHAKFLNSLK- CCHHHHHHHHHHCC-	52.90	-
869	Ubiquitination	PRGEEHAKFLNSLK- CCHHHHHHHHHHCC-	52.90	29967540

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
-	K	Ubiquitination	E3 ubiquitin ligase	DCAF1	Q9Y4B6	PMID:22570418

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM10_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 MCM10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CEP70_HUMAN	CEP70	physical	16189514
CEP72_HUMAN	CEP72	physical	16189514
DPPA2_HUMAN	DPPA2	physical	16189514
ZBT8A_HUMAN	ZBTB8A	physical	16189514
MCM7_HUMAN	MCM7	physical	11095689
ORC2_HUMAN	ORC2	physical	11095689
DDB1_HUMAN	DDB1	physical	22570418
RBX1_HUMAN	RBX1	physical	22570418
CUL4A_HUMAN	CUL4A	physical	22570418
A4_HUMAN	APP	physical	21832049
ORC3_HUMAN	ORC3	physical	15232106
CDN2A_HUMAN	CDKN2A	physical	15232106
ARF_HUMAN	CDKN2A	physical	15232106
CDN1A_HUMAN	CDKN1A	physical	15232106
TRI37_HUMAN	TRIM37	physical	19447967
MCM7_HUMAN	MCM7	physical	26186194
MCM6_HUMAN	MCM6	physical	26186194
MCMBP_HUMAN	MCMBP	physical	26186194
MCM4_HUMAN	MCM4	physical	26186194
SIR1_HUMAN	SIRT1	physical	26344197
DCAF1_HUMAN	VPRBP	physical	26032416
DDB1_HUMAN	DDB1	physical	26032416
MCMBP_HUMAN	MCMBP	physical	28514442
MCM4_HUMAN	MCM4	physical	28514442
MCM6_HUMAN	MCM6	physical	28514442
MCM7_HUMAN	MCM7	physical	28514442

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 MCM10_HUMAN

Related Literatures of Post-Translational Modification

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 THR-85 AND SER-93, AND MASSSPECTROMETRY.	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 THR-85 AND SER-93, AND MASSSPECTROMETRY.	17525332 [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-85, AND MASSSPECTROMETRY.	19690332 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-627, AND MASSSPECTROMETRY.	17370265 [Abstract]