dbPTM

ORC6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ORC6_HUMAN
UniProt AC	Q9Y5N6
Protein Name	Origin recognition complex subunit 6
Gene Name	ORC6
Organism	Homo sapiens (Human).
Sequence Length	252
Subcellular Localization	Nucleus.
Protein Description	Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Does not bind histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3..
Protein Sequence	MGSELIGRLAPRLGLAEPDMLRKAEEYLRLSRVKCVGLSARTTETSSAVMCLDLAASWMKCPLDRAYLIKLSGLNKETYQSCLKSFECLLGLNSNIGIRDLAVQFSCIEAVNMASKILKSYESSLPQTQQVDLDLSRPLFTSAALLSACKILKLKVDKNKMVATSGVKKAIFDRLCKQLEKIGQQVDREPGDVATPPRKRKKIVVEAPAKEMEKVEEMPHKPQKDEDLTQDYEEWKRKILENAASAQKATAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Ubiquitination	AEPDMLRKAEEYLRL CCHHHHHHHHHHHHH	57.07	-
34	Ubiquitination	YLRLSRVKCVGLSAR HHHHHCCEECEECCC	23.30	-
65	Methylation	WMKCPLDRAYLIKLS HHCCCCCHHHHHHHH	32.58	115486047
67	Phosphorylation	KCPLDRAYLIKLSGL CCCCCHHHHHHHHCC	15.17	22817900
70	Ubiquitination	LDRAYLIKLSGLNKE CCHHHHHHHHCCCHH	33.72	-
72	Phosphorylation	RAYLIKLSGLNKETY HHHHHHHHCCCHHHH	35.91	29978859
76	Acetylation	IKLSGLNKETYQSCL HHHHCCCHHHHHHHH	57.38	26051181
76	Ubiquitination	IKLSGLNKETYQSCL HHHHCCCHHHHHHHH	57.38	-
78	Phosphorylation	LSGLNKETYQSCLKS HHCCCHHHHHHHHHH	28.59	29978859
79	Phosphorylation	SGLNKETYQSCLKSF HCCCHHHHHHHHHHH	10.26	29978859
81	Phosphorylation	LNKETYQSCLKSFEC CCHHHHHHHHHHHHH	15.82	29978859
119	Ubiquitination	NMASKILKSYESSLP HHHHHHHHHHHHCCC	55.24	-
168	Acetylation	MVATSGVKKAIFDRL CCCCHHHHHHHHHHH	39.76	7682077
168	Ubiquitination	MVATSGVKKAIFDRL CCCCHHHHHHHHHHH	39.76	-
177	Ubiquitination	AIFDRLCKQLEKIGQ HHHHHHHHHHHHHHH	63.61	-
181	Ubiquitination	RLCKQLEKIGQQVDR HHHHHHHHHHHCCCC	61.81	-
195	Phosphorylation	REPGDVATPPRKRKK CCCCCCCCCCCCCCC	33.40	19664994
202	Ubiquitination	TPPRKRKKIVVEAPA CCCCCCCCEEEECCH	44.78	-
210	Sumoylation	IVVEAPAKEMEKVEE EEEECCHHHHHHHHC	57.44	28112733
210	Ubiquitination	IVVEAPAKEMEKVEE EEEECCHHHHHHHHC	57.44	-
210	Acetylation	IVVEAPAKEMEKVEE EEEECCHHHHHHHHC	57.44	26051181
214	Acetylation	APAKEMEKVEEMPHK CCHHHHHHHHCCCCC	54.35	22361695
221	Acetylation	KVEEMPHKPQKDEDL HHHCCCCCCCCCCCH	43.18	7826271
229	Phosphorylation	PQKDEDLTQDYEEWK CCCCCCHHHCHHHHH	31.54	17525332
232	Phosphorylation	DEDLTQDYEEWKRKI CCCHHHCHHHHHHHH	13.11	28796482
236	Ubiquitination	TQDYEEWKRKILENA HHCHHHHHHHHHHHH	47.28	-
238	Ubiquitination	DYEEWKRKILENAAS CHHHHHHHHHHHHHH	48.17	-
245	Phosphorylation	KILENAASAQKATAE HHHHHHHHHHHHHCC	28.90	25159151
248	Ubiquitination	ENAASAQKATAE--- HHHHHHHHHHCC---	47.63	21906983

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
195	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ORC6_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 ORC6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC7_HUMAN	CDC7	physical	12614612
ORC4_HUMAN	ORC4	physical	12614612
MCM4_HUMAN	MCM4	physical	12614612
MCM5_HUMAN	MCM5	physical	12614612
CDC45_HUMAN	CDC45	physical	12614612
RFA1_HUMAN	RPA1	physical	12614612
ORC2_HUMAN	ORC2	physical	12614612
ORC3_HUMAN	ORC3	physical	12614612
XRCC5_HUMAN	XRCC5	physical	15910003
XRCC6_HUMAN	XRCC6	physical	15910003
ORC3_HUMAN	ORC3	physical	15910003
ORC2_HUMAN	ORC2	physical	15910003
A4_HUMAN	APP	physical	21832049
MCM2_HUMAN	MCM2	physical	15232106
CDC6_HUMAN	CDC6	physical	15232106
LHX4_HUMAN	LHX4	physical	25416956
LRWD1_HUMAN	LRWD1	physical	26186194
SFPQ_HUMAN	SFPQ	physical	26186194
PSPC1_HUMAN	PSPC1	physical	26186194
BICD2_HUMAN	BICD2	physical	26186194
ORC2_HUMAN	ORC2	physical	26186194
ARP10_HUMAN	ACTR10	physical	26186194
CREB1_HUMAN	CREB1	physical	26186194
DCTN6_HUMAN	DCTN6	physical	26186194
PPIL4_HUMAN	PPIL4	physical	26186194
ORC2_HUMAN	ORC2	physical	28514442
BICD2_HUMAN	BICD2	physical	28514442
LRWD1_HUMAN	LRWD1	physical	28514442
DCTN6_HUMAN	DCTN6	physical	28514442
CREB1_HUMAN	CREB1	physical	28514442
PPIL4_HUMAN	PPIL4	physical	28514442
PSPC1_HUMAN	PSPC1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613803	Meier-Gorlin syndrome 3 (MGORS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ORC6_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-195, 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-229, 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 THR-195, AND MASSSPECTROMETRY.	17081983 [Abstract]