dbPTM

ORC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ORC2_HUMAN
UniProt AC	Q13416
Protein Name	Origin recognition complex subunit 2
Gene Name	ORC2
Organism	Homo sapiens (Human).
Sequence Length	577
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. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3..
Protein Sequence	MSKPELKEDKMLEVHFVGDDDVLNHILDREGGAKLKKERAQLLVNPKKIIKKPEYDLEEDDQEVLKDQNYVEIMGRDVQESLKNGSATGGGNKVYSFQNRKHSEKMAKLASELAKTPQKSVSFSLKNDPEITINVPQSSKGHSASDKVQPKNNDKSEFLSTAPRSLRKRLIVPRSHSDSESEYSASNSEDDEGVAQEHEEDTNAVIFSQKIQAQNRVVSAPVGKETPSKRMKRDKTSDLVEEYFEAHSSSKVLTSDRTLQKLKRAKLDQQTLRNLLSKVSPSFSAELKQLNQQYEKLFHKWMLQLHLGFNIVLYGLGSKRDLLERFRTTMLQDSIHVVINGFFPGISVKSVLNSITEEVLDHMGTFRSILDQLDWIVNKFKEDSSLELFLLIHNLDSQMLRGEKSQQIIGQLSSLHNIYLIASIDHLNAPLMWDHAKQSLFNWLWYETTTYSPYTEETSYENSLLVKQSGSLPLSSLTHVLRSLTPNARGIFRLLIKYQLDNQDNPSYIGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGTDGVEYLLIPVDNGTLTDFLEKEEEEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	Acetylation	AQLLVNPKKIIKKPE HHHHCCHHHHHCCCC	51.94	25953088
55	Phosphorylation	KIIKKPEYDLEEDDQ HHHCCCCCCCCCCCH	34.06	27642862
70	Phosphorylation	EVLKDQNYVEIMGRD HHHHCCCCEEECCCC	8.20	28796482
81	Phosphorylation	MGRDVQESLKNGSAT CCCCHHHHHHCCCCC	27.79	27134283
93	Acetylation	SATGGGNKVYSFQNR CCCCCCCCEEEECCH	45.91	26051181
95	Phosphorylation	TGGGNKVYSFQNRKH CCCCCCEEEECCHHH	12.84	23186163
96	Phosphorylation	GGGNKVYSFQNRKHS CCCCCEEEECCHHHH	24.28	23917254
103	Phosphorylation	SFQNRKHSEKMAKLA EECCHHHHHHHHHHH	41.78	23882029
108	Acetylation	KHSEKMAKLASELAK HHHHHHHHHHHHHHC	40.88	25953088
111	O-linked_Glycosylation	EKMAKLASELAKTPQ HHHHHHHHHHHCCCC	43.51	30379171
111	Phosphorylation	EKMAKLASELAKTPQ HHHHHHHHHHHCCCC	43.51	30266825
116	Phosphorylation	LASELAKTPQKSVSF HHHHHHCCCCCCCEE	25.91	23927012
119	Acetylation	ELAKTPQKSVSFSLK HHHCCCCCCCEEECC	54.77	25953088
120	Phosphorylation	LAKTPQKSVSFSLKN HHCCCCCCCEEECCC	20.11	26074081
122	Phosphorylation	KTPQKSVSFSLKNDP CCCCCCCEEECCCCC	19.06	23401153
124	Phosphorylation	PQKSVSFSLKNDPEI CCCCCEEECCCCCCE	30.81	29978859
126	Sumoylation	KSVSFSLKNDPEITI CCCEEECCCCCCEEE	59.09	-
132	Phosphorylation	LKNDPEITINVPQSS CCCCCCEEEECCCCC	12.58	26434776
138	Phosphorylation	ITINVPQSSKGHSAS EEEECCCCCCCCCCC	28.13	25159151
139	Phosphorylation	TINVPQSSKGHSASD EEECCCCCCCCCCCC	37.09	21815630
147	Acetylation	KGHSASDKVQPKNND CCCCCCCCCCCCCCC	40.03	23749302
155	Ubiquitination	VQPKNNDKSEFLSTA CCCCCCCHHHHHHCC	54.75	-
156	Phosphorylation	QPKNNDKSEFLSTAP CCCCCCHHHHHHCCC	36.12	28555341
160	Phosphorylation	NDKSEFLSTAPRSLR CCHHHHHHCCCHHHH	28.04	21712546
161	Phosphorylation	DKSEFLSTAPRSLRK CHHHHHHCCCHHHHH	42.71	21712546
165	Phosphorylation	FLSTAPRSLRKRLIV HHHCCCHHHHHCEEE	31.31	25056879
175	Phosphorylation	KRLIVPRSHSDSESE HCEEECCCCCCCCCC	22.67	17081983
177	Phosphorylation	LIVPRSHSDSESEYS EEECCCCCCCCCCCC	44.04	17081983
179	Phosphorylation	VPRSHSDSESEYSAS ECCCCCCCCCCCCCC	46.14	17081983
181	Phosphorylation	RSHSDSESEYSASNS CCCCCCCCCCCCCCC	45.87	17081983
183	Phosphorylation	HSDSESEYSASNSED CCCCCCCCCCCCCCC	20.86	24461736
184	Phosphorylation	SDSESEYSASNSEDD CCCCCCCCCCCCCCC	22.59	24461736
186	Phosphorylation	SESEYSASNSEDDEG CCCCCCCCCCCCCCC	34.64	24461736
188	Phosphorylation	SEYSASNSEDDEGVA CCCCCCCCCCCCCCC	39.65	21947279
202	Phosphorylation	AQEHEEDTNAVIFSQ CHHHHCCCCEEEEEH	28.49	17081983
208	Phosphorylation	DTNAVIFSQKIQAQN CCCEEEEEHHHHHCC	21.31	17081983
219	Phosphorylation	QAQNRVVSAPVGKET HHCCCEEECCCCCCC	24.81	30266825
226	Phosphorylation	SAPVGKETPSKRMKR ECCCCCCCCCHHHCC	36.03	29255136
228	Phosphorylation	PVGKETPSKRMKRDK CCCCCCCCHHHCCCC	40.07	30266825
235	Ubiquitination	SKRMKRDKTSDLVEE CHHHCCCCCHHHHHH	54.70	-
236	Phosphorylation	KRMKRDKTSDLVEEY HHHCCCCCHHHHHHH	31.59	21712546
237	Phosphorylation	RMKRDKTSDLVEEYF HHCCCCCHHHHHHHH	34.39	25159151
243	Phosphorylation	TSDLVEEYFEAHSSS CHHHHHHHHHHHCCC	8.00	28796482
248	Phosphorylation	EEYFEAHSSSKVLTS HHHHHHHCCCCCCCC	43.27	25159151
249	Phosphorylation	EYFEAHSSSKVLTSD HHHHHHCCCCCCCCH	25.06	24732914
250	Phosphorylation	YFEAHSSSKVLTSDR HHHHHCCCCCCCCHH	29.78	24732914
251	Ubiquitination	FEAHSSSKVLTSDRT HHHHCCCCCCCCHHH	43.12	-
254	Phosphorylation	HSSSKVLTSDRTLQK HCCCCCCCCHHHHHH	31.41	23186163
255	Phosphorylation	SSSKVLTSDRTLQKL CCCCCCCCHHHHHHH	22.42	25159151
258	Phosphorylation	KVLTSDRTLQKLKRA CCCCCHHHHHHHHHH	38.23	25159151
266	Ubiquitination	LQKLKRAKLDQQTLR HHHHHHHCCCHHHHH	57.54	-
266	Acetylation	LQKLKRAKLDQQTLR HHHHHHHCCCHHHHH	57.54	25953088
277	Phosphorylation	QTLRNLLSKVSPSFS HHHHHHHHHHCCCHH	33.89	23312004
278	Ubiquitination	TLRNLLSKVSPSFSA HHHHHHHHHCCCHHH	46.86	-
278	Acetylation	TLRNLLSKVSPSFSA HHHHHHHHHCCCHHH	46.86	25953088
280	Phosphorylation	RNLLSKVSPSFSAEL HHHHHHHCCCHHHHH	20.68	29255136
282	Phosphorylation	LLSKVSPSFSAELKQ HHHHHCCCHHHHHHH	25.07	30266825
284	Phosphorylation	SKVSPSFSAELKQLN HHHCCCHHHHHHHHH	25.77	30266825
288	Ubiquitination	PSFSAELKQLNQQYE CCHHHHHHHHHHHHH	44.22	-
475	Phosphorylation	QSGSLPLSSLTHVLR ECCCCCHHHHHHHHH	22.74	-
483	Phosphorylation	SLTHVLRSLTPNARG HHHHHHHHCCCCCHH	32.22	22817900
528	Phosphorylation	REAFLVNSDLTLRAQ HHHHCCCCCCHHHHH	26.90	20068231
531	Phosphorylation	FLVNSDLTLRAQLTE HCCCCCCHHHHHHHH	21.13	20068231
549	Ubiquitination	HKLIRTKKGTDGVEY CCCEEECCCCCCCEE	67.44	-

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
116	T	Phosphorylation	Kinase	CDK2	P24941	PSP
188	S	Phosphorylation	Kinase	PLK1	P53350	PSP
226	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ORC2_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 ORC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM2_HUMAN	MCM2	physical	12614612
DBF4A_HUMAN	DBF4	physical	12614612
ORC1_HUMAN	ORC1	physical	12614612
ORC2_HUMAN	ORC2	physical	12614612
ORC3_HUMAN	ORC3	physical	12614612
ORC4_HUMAN	ORC4	physical	12614612
ORC5_HUMAN	ORC5	physical	12614612
MCM4_HUMAN	MCM4	physical	12614612
MCM5_HUMAN	MCM5	physical	12614612
MCM6_HUMAN	MCM6	physical	12614612
MCM7_HUMAN	MCM7	physical	12614612
CDC6_HUMAN	CDC6	physical	12614612
RFA1_HUMAN	RPA1	physical	12614612
ORC3_HUMAN	ORC3	physical	11395502
ORC4_HUMAN	ORC4	physical	11395502
ORC5_HUMAN	ORC5	physical	11395502
ORC3_HUMAN	ORC3	physical	17525332
BRCA1_HUMAN	BRCA1	physical	17525332
ORC3_HUMAN	ORC3	physical	10402192
ORC3_HUMAN	ORC3	physical	11323433
ORC5_HUMAN	ORC5	physical	11323433
ORC4_HUMAN	ORC4	physical	11323433
ORC6_HUMAN	ORC6	physical	11323433
ORC1_HUMAN	ORC1	physical	11323433
ORC1_HUMAN	ORC1	physical	11931757
CCNA2_HUMAN	CCNA2	physical	11931757
MCM10_HUMAN	MCM10	physical	11095689
MCM3_HUMAN	MCM3	physical	11046155
MCM8_HUMAN	MCM8	physical	15684404
CCL2_HUMAN	CCL2	physical	21383955
CBX5_HUMAN	CBX5	physical	21383955
XRCC5_HUMAN	XRCC5	physical	15910003
XRCC6_HUMAN	XRCC6	physical	15910003
ORC3_HUMAN	ORC3	physical	15910003
ORC6_HUMAN	ORC6	physical	15910003
ORC3_HUMAN	ORC3	physical	12004060
ORC4_HUMAN	ORC4	physical	12004060
ORC5_HUMAN	ORC5	physical	12004060
ORC6_HUMAN	ORC6	physical	12004060
LRWD1_HUMAN	LRWD1	physical	22935713
ORC5_HUMAN	ORC5	physical	22939629
ORC3_HUMAN	ORC3	physical	22939629
MCM2_HUMAN	MCM2	physical	15232106
MCM10_HUMAN	MCM10	physical	15232106
ORC1_HUMAN	ORC1	physical	15232106
LRWD1_HUMAN	LRWD1	physical	20850016
ORC3_HUMAN	ORC3	physical	20850016
ORC4_HUMAN	ORC4	physical	20850016
ORC5_HUMAN	ORC5	physical	20850016
ORC1_HUMAN	ORC1	physical	20850016
MRCKB_HUMAN	CDC42BPB	physical	26344197
LRWD1_HUMAN	LRWD1	physical	26344197
PESC_HUMAN	PES1	physical	26344197
ORC1_HUMAN	ORC1	physical	26496610
ORC5_HUMAN	ORC5	physical	26496610
ORC3_HUMAN	ORC3	physical	26496610
LRWD1_HUMAN	LRWD1	physical	26496610
BRNP1_HUMAN	BRINP1	physical	26496610

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 ORC2_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-116 AND SER-280, ANDMASS SPECTROMETRY.	18669648 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, AND MASSSPECTROMETRY.	19413330 [Abstract]