ORC3_HUMAN - dbPTM
ORC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ORC3_HUMAN
UniProt AC Q9UBD5
Protein Name Origin recognition complex subunit 3
Gene Name ORC3
Organism Homo sapiens (Human).
Sequence Length 711
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, H3K27me3 and H4K20me3..
Protein Sequence MATSSMSKGCFVFKPNSKKRKISLPIEDYFNKGKNEPEDSKLRFETYQLIWQQMKSENERLQEELNKNLFDNLIEFLQKSHSGFQKNSRDLGGQIKLREIPTAALVLGVNVTDHDLTFGSLTEALQNNVTPYVVSLQAKDCPDMKHFLQKLISQLMDCCVDIKSKEEESVHVTQRKTHYSMDSLSSWYMTVTQKTDPKMLSKKRTTSSQWQSPPVVVILKDMESFATKVLQDFIIISSQHLHEFPLILIFGIATSPIIIHRLLPHAVSSLLCIELFQSLSCKEHLTTVLDKLLLTTQFPFKINEKVLQVLTNIFLYHDFSVQNFIKGLQLSLLEHFYSQPLSVLCCNLPEAKRRINFLSNNQCENIRRLPSFRRYVEKQASEKQVALLTNERYLKEETQLLLENLHVYHMNYFLVLRCLHKFTSSLPKYPLGRQIRELYCTCLEKNIWDSEEYASVLQLLRMLAKDELMTILEKCFKVFKSYCENHLGSTAKRIEEFLAQFQSLDETKEEEDASGSQPKGLQKTDLYHLQKSLLEMKELRRSKKQTKFEVLRENVVNFIDCLVREYLLPPETQPLHEVVYFSAAHALREHLNAAPRIALHTALNNPYYYLKNEALKSEEGCIPNIAPDICIAYKLHLECSRLINLVDWSEAFATVVTAAEKMDANSATSEEMNEIIHARFIRAVSELELLGFIKPTKQKTDHVARLTWGGC
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 Orthologous
Protein Cluster
14AcetylationSKGCFVFKPNSKKRK
CCCEEEECCCCCCCE
37.6825953088
20UbiquitinationFKPNSKKRKISLPIE
ECCCCCCCEEECCHH
45.3222817900
21AcetylationKPNSKKRKISLPIED
CCCCCCCEEECCHHH
45.597682003
22UbiquitinationPNSKKRKISLPIEDY
CCCCCCEEECCHHHH
6.2522817900
23PhosphorylationNSKKRKISLPIEDYF
CCCCCEEECCHHHHC
31.0025159151
29PhosphorylationISLPIEDYFNKGKNE
EECCHHHHCCCCCCC
9.03-
32UbiquitinationPIEDYFNKGKNEPED
CHHHHCCCCCCCCCH
62.4521906983
32 (in isoform 1)Ubiquitination-62.4521890473
32 (in isoform 2)Ubiquitination-62.4521890473
34AcetylationEDYFNKGKNEPEDSK
HHHCCCCCCCCCHHH
60.807682013
34UbiquitinationEDYFNKGKNEPEDSK
HHHCCCCCCCCCHHH
60.8022817900
34 (in isoform 2)Ubiquitination-60.80-
41AcetylationKNEPEDSKLRFETYQ
CCCCCHHHHHHHHHH
56.887682023
41UbiquitinationKNEPEDSKLRFETYQ
CCCCCHHHHHHHHHH
56.8822817900
41 (in isoform 1)Ubiquitination-56.8821890473
41 (in isoform 2)Ubiquitination-56.8821890473
46PhosphorylationDSKLRFETYQLIWQQ
HHHHHHHHHHHHHHH
17.5424719451
47PhosphorylationSKLRFETYQLIWQQM
HHHHHHHHHHHHHHH
8.3024719451
55UbiquitinationQLIWQQMKSENERLQ
HHHHHHHHHHHHHHH
50.7221906983
55 (in isoform 1)Ubiquitination-50.7221890473
55 (in isoform 2)Ubiquitination-50.7221890473
56PhosphorylationLIWQQMKSENERLQE
HHHHHHHHHHHHHHH
40.0724719451
86UbiquitinationKSHSGFQKNSRDLGG
HHCCCCCCCCCCCCC
55.4129967540
88PhosphorylationHSGFQKNSRDLGGQI
CCCCCCCCCCCCCCE
33.9222985185
96UbiquitinationRDLGGQIKLREIPTA
CCCCCCEEEEECCCC
33.3429967540
110UbiquitinationAALVLGVNVTDHDLT
CEEEECCCCCCCCCC
29.2222817900
112UbiquitinationLVLGVNVTDHDLTFG
EEECCCCCCCCCCHH
23.5522817900
145AcetylationAKDCPDMKHFLQKLI
CCCCCCHHHHHHHHH
38.2923749302
153PhosphorylationHFLQKLISQLMDCCV
HHHHHHHHHHHHHHH
27.9129083192
163UbiquitinationMDCCVDIKSKEEESV
HHHHHHCCCCCCCCE
51.5222817900
164PhosphorylationDCCVDIKSKEEESVH
HHHHHCCCCCCCCEE
45.7129083192
165UbiquitinationCCVDIKSKEEESVHV
HHHHCCCCCCCCEEC
65.2322817900
165 (in isoform 1)Ubiquitination-65.2321890473
165 (in isoform 2)Ubiquitination-65.2321890473
183PhosphorylationKTHYSMDSLSSWYMT
CCEECHHHHHHCEEE
22.8524275569
185PhosphorylationHYSMDSLSSWYMTVT
EECHHHHHHCEEEEC
23.8324275569
188PhosphorylationMDSLSSWYMTVTQKT
HHHHHHCEEEECCCC
5.7124275569
198UbiquitinationVTQKTDPKMLSKKRT
ECCCCCHHHHCCCCC
56.1129967540
205PhosphorylationKMLSKKRTTSSQWQS
HHHCCCCCCCCCCCC
39.6522199227
206PhosphorylationMLSKKRTTSSQWQSP
HHCCCCCCCCCCCCC
30.3422199227
207PhosphorylationLSKKRTTSSQWQSPP
HCCCCCCCCCCCCCC
21.6622199227
208PhosphorylationSKKRTTSSQWQSPPV
CCCCCCCCCCCCCCE
33.0917525332
212PhosphorylationTTSSQWQSPPVVVIL
CCCCCCCCCCEEEEE
28.3620068231
235UbiquitinationKVLQDFIIISSQHLH
HHHHHHHHHCCCCHH
2.2322817900
240UbiquitinationFIIISSQHLHEFPLI
HHHHCCCCHHCCCEE
30.9722817900
285UbiquitinationSLSCKEHLTTVLDKL
CCCCHHHHHHHHHHH
4.5021890473
287UbiquitinationSCKEHLTTVLDKLLL
CCHHHHHHHHHHHHH
25.9822817900
292UbiquitinationLTTVLDKLLLTTQFP
HHHHHHHHHHHCCCC
4.7722817900
325UbiquitinationDFSVQNFIKGLQLSL
CCCHHHHHHHHHHHH
4.5422817900
330UbiquitinationNFIKGLQLSLLEHFY
HHHHHHHHHHHHHHH
4.7222817900
337UbiquitinationLSLLEHFYSQPLSVL
HHHHHHHHCCCCCHH
14.3321890473
340UbiquitinationLEHFYSQPLSVLCCN
HHHHHCCCCCHHHCC
22.2122817900
345UbiquitinationSQPLSVLCCNLPEAK
CCCCCHHHCCCHHHH
1.0422817900
365UbiquitinationLSNNQCENIRRLPSF
CCCCCCCHHHCCHHH
40.4729967540
375PhosphorylationRLPSFRRYVEKQASE
CCHHHHHHHHHHCCH
14.54-
375UbiquitinationRLPSFRRYVEKQASE
CCHHHHHHHHHHCCH
14.5421890473
376UbiquitinationLPSFRRYVEKQASEK
CHHHHHHHHHHCCHH
7.6022817900
378UbiquitinationSFRRYVEKQASEKQV
HHHHHHHHHCCHHHH
40.9122817900
380UbiquitinationRRYVEKQASEKQVAL
HHHHHHHCCHHHHHH
30.6321890473
383AcetylationVEKQASEKQVALLTN
HHHHCCHHHHHHHHC
47.8025953088
383UbiquitinationVEKQASEKQVALLTN
HHHHCCHHHHHHHHC
47.8021906983
383 (in isoform 1)Ubiquitination-47.8021890473
383 (in isoform 2)Ubiquitination-47.8021890473
388UbiquitinationSEKQVALLTNERYLK
CHHHHHHHHCHHHHH
3.3129967540
390UbiquitinationKQVALLTNERYLKEE
HHHHHHHCHHHHHHH
31.5521890473
394UbiquitinationLLTNERYLKEETQLL
HHHCHHHHHHHHHHH
7.6329967540
404UbiquitinationETQLLLENLHVYHMN
HHHHHHHHHCHHHHH
35.1027667366
421AcetylationLVLRCLHKFTSSLPK
HHHHHHHHHHHCCCC
37.0725953088
423PhosphorylationLRCLHKFTSSLPKYP
HHHHHHHHHCCCCCC
23.3920068231
424PhosphorylationRCLHKFTSSLPKYPL
HHHHHHHHCCCCCCC
32.7720068231
425PhosphorylationCLHKFTSSLPKYPLG
HHHHHHHCCCCCCCH
45.7120068231
428UbiquitinationKFTSSLPKYPLGRQI
HHHHCCCCCCCHHHH
65.8721890473
428UbiquitinationKFTSSLPKYPLGRQI
HHHHCCCCCCCHHHH
65.8722817900
428 (in isoform 1)Ubiquitination-65.8721890473
428 (in isoform 2)Ubiquitination-65.8721890473
432UbiquitinationSLPKYPLGRQIRELY
CCCCCCCHHHHHHHH
18.2321890473
456UbiquitinationDSEEYASVLQLLRML
CHHHHHHHHHHHHHH
2.7627667366
466UbiquitinationLLRMLAKDELMTILE
HHHHHHHHHHHHHHH
48.9722817900
467UbiquitinationLRMLAKDELMTILEK
HHHHHHHHHHHHHHH
39.4722817900
468UbiquitinationRMLAKDELMTILEKC
HHHHHHHHHHHHHHH
5.4221963094
470UbiquitinationLAKDELMTILEKCFK
HHHHHHHHHHHHHHH
34.7321890473
471UbiquitinationAKDELMTILEKCFKV
HHHHHHHHHHHHHHH
2.6621890473
473UbiquitinationDELMTILEKCFKVFK
HHHHHHHHHHHHHHH
43.8822817900
480AcetylationEKCFKVFKSYCENHL
HHHHHHHHHHHHHCC
43.4326051181
480UbiquitinationEKCFKVFKSYCENHL
HHHHHHHHHHHHHCC
43.4329967540
481UbiquitinationKCFKVFKSYCENHLG
HHHHHHHHHHHHCCC
24.4522817900
482UbiquitinationCFKVFKSYCENHLGS
HHHHHHHHHHHCCCH
12.3622817900
485UbiquitinationVFKSYCENHLGSTAK
HHHHHHHHCCCHHHH
31.9321890473
486UbiquitinationFKSYCENHLGSTAKR
HHHHHHHCCCHHHHH
14.8521890473
492UbiquitinationNHLGSTAKRIEEFLA
HCCCHHHHHHHHHHH
54.73-
492 (in isoform 2)Ubiquitination-54.73-
494UbiquitinationLGSTAKRIEEFLAQF
CCHHHHHHHHHHHHH
6.1527667366
495UbiquitinationGSTAKRIEEFLAQFQ
CHHHHHHHHHHHHHH
46.8927667366
503PhosphorylationEFLAQFQSLDETKEE
HHHHHHHCCCCCCCC
38.7923401153
503 (in isoform 2)Phosphorylation-38.79-
507PhosphorylationQFQSLDETKEEEDAS
HHHCCCCCCCCCCCC
43.3428355574
508UbiquitinationFQSLDETKEEEDASG
HHCCCCCCCCCCCCC
62.1729967540
508 (in isoform 2)Phosphorylation-62.17-
509UbiquitinationQSLDETKEEEDASGS
HCCCCCCCCCCCCCC
74.2227667366
510UbiquitinationSLDETKEEEDASGSQ
CCCCCCCCCCCCCCC
63.8327667366
514PhosphorylationTKEEEDASGSQPKGL
CCCCCCCCCCCCCCC
51.8329523821
515 (in isoform 2)Phosphorylation-31.8326714015
516PhosphorylationEEEDASGSQPKGLQK
CCCCCCCCCCCCCCH
40.5917525332
517 (in isoform 2)Phosphorylation-47.4526714015
519UbiquitinationDASGSQPKGLQKTDL
CCCCCCCCCCCHHHH
65.6922817900
520UbiquitinationASGSQPKGLQKTDLY
CCCCCCCCCCHHHHH
39.7721963094
523UbiquitinationSQPKGLQKTDLYHLQ
CCCCCCCHHHHHHHH
49.3921890473
523UbiquitinationSQPKGLQKTDLYHLQ
CCCCCCCHHHHHHHH
49.3922817900
523 (in isoform 1)Ubiquitination-49.3921890473
524UbiquitinationQPKGLQKTDLYHLQK
CCCCCCHHHHHHHHH
20.4821890473
524 (in isoform 2)Ubiquitination-20.4821890473
525UbiquitinationPKGLQKTDLYHLQKS
CCCCCHHHHHHHHHH
52.8722817900
527PhosphorylationGLQKTDLYHLQKSLL
CCCHHHHHHHHHHHH
11.8625159151
531UbiquitinationTDLYHLQKSLLEMKE
HHHHHHHHHHHHHHH
49.8129967540
532PhosphorylationDLYHLQKSLLEMKEL
HHHHHHHHHHHHHHH
25.8129214152
532UbiquitinationDLYHLQKSLLEMKEL
HHHHHHHHHHHHHHH
25.8129967540
532 (in isoform 2)Ubiquitination-25.81-
537UbiquitinationQKSLLEMKELRRSKK
HHHHHHHHHHHHCCC
44.1929967540
538UbiquitinationKSLLEMKELRRSKKQ
HHHHHHHHHHHCCCC
46.3129967540
543AcetylationMKELRRSKKQTKFEV
HHHHHHCCCCCHHHH
47.277265723
547UbiquitinationRRSKKQTKFEVLREN
HHCCCCCHHHHHHHH
36.7127667366
548UbiquitinationRSKKQTKFEVLRENV
HCCCCCHHHHHHHHH
9.9727667366
558UbiquitinationLRENVVNFIDCLVRE
HHHHHHHHHHHHHHH
3.1721963094
559UbiquitinationRENVVNFIDCLVREY
HHHHHHHHHHHHHHH
2.8521963094
561GlutathionylationNVVNFIDCLVREYLL
HHHHHHHHHHHHHCC
3.0222555962
563UbiquitinationVNFIDCLVREYLLPP
HHHHHHHHHHHCCCC
5.7022817900
564UbiquitinationNFIDCLVREYLLPPE
HHHHHHHHHHCCCCC
17.5622817900
573UbiquitinationYLLPPETQPLHEVVY
HCCCCCCCCHHHHHH
36.5721963094
574UbiquitinationLLPPETQPLHEVVYF
CCCCCCCCHHHHHHH
43.0021963094
578UbiquitinationETQPLHEVVYFSAAH
CCCCHHHHHHHHHHH
2.7022817900
579UbiquitinationTQPLHEVVYFSAAHA
CCCHHHHHHHHHHHH
3.4822817900
607PhosphorylationHTALNNPYYYLKNEA
HHHHCCHHHHHCHHH
13.5817360941
611UbiquitinationNNPYYYLKNEALKSE
CCHHHHHCHHHHHCC
36.3021906983
611 (in isoform 1)Ubiquitination-36.3021890473
612UbiquitinationNPYYYLKNEALKSEE
CHHHHHCHHHHHCCC
36.8621963094
612 (in isoform 2)Ubiquitination-36.8621890473
616UbiquitinationYLKNEALKSEEGCIP
HHCHHHHHCCCCCCC
63.9722817900
617UbiquitinationLKNEALKSEEGCIPN
HCHHHHHCCCCCCCC
41.5522817900
617 (in isoform 2)Ubiquitination-41.55-
685PhosphorylationARFIRAVSELELLGF
HHHHHHHHHHHHHCC
35.16-
694UbiquitinationLELLGFIKPTKQKTD
HHHHCCCCCCCCCCC
44.362190698
694 (in isoform 1)Ubiquitination-44.3621890473
695 (in isoform 2)Ubiquitination-39.7621890473
699UbiquitinationFIKPTKQKTDHVARL
CCCCCCCCCCCCCCC
58.43-
700 (in isoform 2)Ubiquitination-28.92-

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

Oops, there are no upstream regulatory protein records of ORC3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ORC3_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 ORC3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ORC2_HUMANORC2physical
12614612
ORC5_HUMANORC5physical
12614612
ORC6_HUMANORC6physical
12614612
MCM4_HUMANMCM4physical
12614612
MCM7_HUMANMCM7physical
12614612
ORC4_HUMANORC4physical
11395502
ORC5_HUMANORC5physical
11395502
BRCA1_HUMANBRCA1physical
17525332
ORC2_HUMANORC2physical
10402192
ORC4_HUMANORC4physical
11323433
ORC6_HUMANORC6physical
11323433
ORC5_HUMANORC5physical
11323433
XRCC5_HUMANXRCC5physical
15910003
XRCC6_HUMANXRCC6physical
15910003
ORC2_HUMANORC2physical
15910003
ORC6_HUMANORC6physical
15910003
A4_HUMANAPPphysical
21832049
ORC5_HUMANORC5physical
22939629
ORC6_HUMANORC6physical
15232106
MCM7_HUMANMCM7physical
15232106
ORC1_HUMANORC1physical
15232106
ORC4_HUMANORC4physical
15232106
ORC2_HUMANORC2physical
26344197

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 ORC3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-23, AND MASSSPECTROMETRY.
"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-208 AND SER-516, ANDMASS SPECTROMETRY.

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