ORC1_HUMAN - dbPTM
ORC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ORC1_HUMAN
UniProt AC Q13415
Protein Name Origin recognition complex subunit 1
Gene Name ORC1
Organism Homo sapiens (Human).
Sequence Length 861
Subcellular Localization Nucleus.
Protein Description Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The 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..
Protein Sequence MAHYPTRLKTRKTYSWVGRPLLDRKLHYQTYREMCVKTEGCSTEIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPPKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDSNINAETIIGLVRVIPLAPKDVVPTNLKNEKTLFVKLSWNEKKFRPLSSELFAELNKPQESAAKCQKPVRAKSKSAESPSWTPAEHVAKRIESRHSASKSRQTPTHPLTPRARKRLELGNLGNPQMSQQTSCASLDSPGRIKRKVAFSEITSPSKRSQPDKLQTLSPALKAPEKTRETGLSYTEDDKKASPEHRIILRTRIAASKTIDIREERTLTPISGGQRSSVVPSVILKPENIKKRDAKEAKAQNEATSTPHRIRRKSSVLTMNRIRQQLRFLGNSKSDQEEKEILPAAEISDSSSDEEEASTPPLPRRAPRTVSRNLRSSLKSSLHTLTKVPKKSLKPRTPRCAAPQIRSRSLAAQEPASVLEEARLRLHVSAVPESLPCREQEFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVIRCLQQAAQANDVPPFQYIEVNGMKLTEPHQVYVQILQKLTGQKATANHAAELLAKQFCTRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVVLAIANTMDLPERIMMNRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHLKAFEDDAIQLVARKVAALSGDARRCLDICRRATEICEFSQQKPDSPGLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPSRNDLLLRVRLNVSQDDVLYALKDE
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
4Phosphorylation----MAHYPTRLKTR
----CCCCCCCCCCC		9.2124719451
25SumoylationGRPLLDRKLHYQTYR
CCCHHCCCCCHHHHH		39.00-
25SumoylationGRPLLDRKLHYQTYR
CCCHHCCCCCHHHHH		39.00-
25UbiquitinationGRPLLDRKLHYQTYR
CCCHHCCCCCHHHHH		39.00-
81UbiquitinationDDSDPPPKKRARVQW
CCCCCCCCHHHHHHH		61.74-
99AcetylationFCEVPACKRHLLGRK
HHCCHHHHHHHCCCC		44.9825953088
99UbiquitinationFCEVPACKRHLLGRK
HHCCHHHHHHHCCCC		44.98-
149UbiquitinationDVVPTNLKNEKTLFV
CCCCCCCCCCCEEEE		66.19-
152UbiquitinationPTNLKNEKTLFVKLS
CCCCCCCCEEEEEEE		60.98-
163UbiquitinationVKLSWNEKKFRPLSS
EEEEECCCHHCCCCH		54.74-
164UbiquitinationKLSWNEKKFRPLSSE
EEEECCCHHCCCCHH		40.19-
169PhosphorylationEKKFRPLSSELFAEL
CCHHCCCCHHHHHHC		25.1724732914
170PhosphorylationKKFRPLSSELFAELN
CHHCCCCHHHHHHCC		46.1024732914
178UbiquitinationELFAELNKPQESAAK
HHHHHCCCCHHHHHH		61.78-
182PhosphorylationELNKPQESAAKCQKP
HCCCCHHHHHHCCCC		28.4224732914
185UbiquitinationKPQESAAKCQKPVRA
CCHHHHHHCCCCHHC		36.59-
188UbiquitinationESAAKCQKPVRAKSK
HHHHHCCCCHHCCCC		55.75-
194PhosphorylationQKPVRAKSKSAESPS
CCCHHCCCCCCCCCC		30.7523312004
195UbiquitinationKPVRAKSKSAESPSW
CCHHCCCCCCCCCCC		53.64-
196PhosphorylationPVRAKSKSAESPSWT
CHHCCCCCCCCCCCC		44.3430266825
199PhosphorylationAKSKSAESPSWTPAE
CCCCCCCCCCCCHHH		24.7723401153
201PhosphorylationSKSAESPSWTPAEHV
CCCCCCCCCCHHHHH		53.5130266825
203PhosphorylationSAESPSWTPAEHVAK
CCCCCCCCHHHHHHH		19.5625159151
210AcetylationTPAEHVAKRIESRHS
CHHHHHHHHHHHHHH		53.4725953088
210UbiquitinationTPAEHVAKRIESRHS
CHHHHHHHHHHHHHH		53.47-
214PhosphorylationHVAKRIESRHSASKS
HHHHHHHHHHHCCCC		32.6824732914
217PhosphorylationKRIESRHSASKSRQT
HHHHHHHHCCCCCCC		32.8824719451
219PhosphorylationIESRHSASKSRQTPT
HHHHHHCCCCCCCCC		33.8924732914
221PhosphorylationSRHSASKSRQTPTHP
HHHHCCCCCCCCCCC		27.4224732914
224PhosphorylationSASKSRQTPTHPLTP
HCCCCCCCCCCCCCH		29.1029255136
226PhosphorylationSKSRQTPTHPLTPRA
CCCCCCCCCCCCHHH		39.2424732914
230PhosphorylationQTPTHPLTPRARKRL
CCCCCCCCHHHHHHH		18.3830266825
248PhosphorylationNLGNPQMSQQTSCAS
CCCCCCCCCCCCCCC		17.5626074081
251PhosphorylationNPQMSQQTSCASLDS
CCCCCCCCCCCCCCC		20.3825850435
252PhosphorylationPQMSQQTSCASLDSP
CCCCCCCCCCCCCCC		11.8925850435
255PhosphorylationSQQTSCASLDSPGRI
CCCCCCCCCCCCCCC		36.7229255136
258PhosphorylationTSCASLDSPGRIKRK
CCCCCCCCCCCCCCE		34.2529255136
269PhosphorylationIKRKVAFSEITSPSK
CCCEEEECCCCCCCC		20.5325159151
272PhosphorylationKVAFSEITSPSKRSQ
EEEECCCCCCCCCCC		30.4530266825
273PhosphorylationVAFSEITSPSKRSQP
EEECCCCCCCCCCCC		32.6030266825
275PhosphorylationFSEITSPSKRSQPDK
ECCCCCCCCCCCCCH		40.2330266825
276AcetylationSEITSPSKRSQPDKL
CCCCCCCCCCCCCHH		60.5025953088
278PhosphorylationITSPSKRSQPDKLQT
CCCCCCCCCCCHHHH		50.2129214152
285PhosphorylationSQPDKLQTLSPALKA
CCCCHHHHCCHHHCC		39.3730266825
287PhosphorylationPDKLQTLSPALKAPE
CCHHHHCCHHHCCCH		16.1223401153
299PhosphorylationAPEKTRETGLSYTED
CCHHHHHCCCCCCCC		39.8830266825
302PhosphorylationKTRETGLSYTEDDKK
HHHHCCCCCCCCCCC		31.2130266825
303PhosphorylationTRETGLSYTEDDKKA
HHHCCCCCCCCCCCC		21.1330266825
304PhosphorylationRETGLSYTEDDKKAS
HHCCCCCCCCCCCCC		29.5730266825
311PhosphorylationTEDDKKASPEHRIIL
CCCCCCCCHHHEEEE		39.4323401153
320PhosphorylationEHRIILRTRIAASKT
HHEEEEEEEHHHCCE		24.0028634120
326AcetylationRTRIAASKTIDIREE
EEEHHHCCEEECCCC		44.7819608861
335PhosphorylationIDIREERTLTPISGG
EECCCCCCCCCCCCC		37.9627067055
337PhosphorylationIREERTLTPISGGQR
CCCCCCCCCCCCCCC		20.2625159151
340PhosphorylationERTLTPISGGQRSSV
CCCCCCCCCCCCCCC		37.7725159151
345PhosphorylationPISGGQRSSVVPSVI
CCCCCCCCCCCCEEE		21.4325627689
346PhosphorylationISGGQRSSVVPSVIL
CCCCCCCCCCCEEEE		29.3525627689
350PhosphorylationQRSSVVPSVILKPEN
CCCCCCCEEEECHHH		15.3525159151
364AcetylationNIKKRDAKEAKAQNE
HCCHHHHHHHHHHHH		63.597826015
373PhosphorylationAKAQNEATSTPHRIR
HHHHHHHCCCCHHHH		27.2729396449
374PhosphorylationKAQNEATSTPHRIRR
HHHHHHCCCCHHHHH		47.1725262027
375PhosphorylationAQNEATSTPHRIRRK
HHHHHCCCCHHHHHH		20.8225159151
383PhosphorylationPHRIRRKSSVLTMNR
CHHHHHHHCHHHHHH		24.7023401153
384PhosphorylationHRIRRKSSVLTMNRI
HHHHHHHCHHHHHHH		24.9620873877
387PhosphorylationRRKSSVLTMNRIRQQ
HHHHCHHHHHHHHHH		15.3925159151
401PhosphorylationQLRFLGNSKSDQEEK
HHHHHCCCCCHHHHH		31.5728348404
402UbiquitinationLRFLGNSKSDQEEKE
HHHHCCCCCHHHHHH		63.15-
403PhosphorylationRFLGNSKSDQEEKEI
HHHCCCCCHHHHHHH		44.3323898821
417PhosphorylationILPAAEISDSSSDEE
HCCHHHCCCCCCCHH		23.9718669648
419PhosphorylationPAAEISDSSSDEEEA
CHHHCCCCCCCHHHH		25.5820068231
420PhosphorylationAAEISDSSSDEEEAS
HHHCCCCCCCHHHHC		46.9618669648
421PhosphorylationAEISDSSSDEEEAST
HHCCCCCCCHHHHCC		53.6618669648
427PhosphorylationSSDEEEASTPPLPRR
CCCHHHHCCCCCCCC		44.7318669648
428PhosphorylationSDEEEASTPPLPRRA
CCHHHHCCCCCCCCC		35.6520068231
445PhosphorylationTVSRNLRSSLKSSLH
HHHHHHHHHHHHHHH		43.0929214152
446PhosphorylationVSRNLRSSLKSSLHT
HHHHHHHHHHHHHHH		33.1224719451
448MethylationRNLRSSLKSSLHTLT
HHHHHHHHHHHHHHC		39.69115974473
448UbiquitinationRNLRSSLKSSLHTLT
HHHHHHHHHHHHHHC		39.69-
449PhosphorylationNLRSSLKSSLHTLTK
HHHHHHHHHHHHHCC		43.34-
450PhosphorylationLRSSLKSSLHTLTKV
HHHHHHHHHHHHCCC		23.6825159151
453PhosphorylationSLKSSLHTLTKVPKK
HHHHHHHHHCCCCHH		41.2225159151
455PhosphorylationKSSLHTLTKVPKKSL
HHHHHHHCCCCHHHC		31.02-
456UbiquitinationSSLHTLTKVPKKSLK
HHHHHHCCCCHHHCC		60.70-
461PhosphorylationLTKVPKKSLKPRTPR
HCCCCHHHCCCCCCC		47.99-
476PhosphorylationCAAPQIRSRSLAAQE
CCCHHHHHCHHHCCC		28.0524732914
478PhosphorylationAPQIRSRSLAAQEPA
CHHHHHCHHHCCCCH		24.4929255136
486PhosphorylationLAAQEPASVLEEARL
HHCCCCHHHHHHHHH		37.6424732914
515PhosphorylationEQEFQDIYNFVESKL
HHHHHHHHHHHHHHH		15.7327642862
540UbiquitinationSGVPGTGKTATVHEV
ECCCCCCCCHHHHHH		34.52-
586UbiquitinationVYVQILQKLTGQKAT
HHHHHHHHHHCCCCC		44.57-
591UbiquitinationLQKLTGQKATANHAA
HHHHHCCCCCHHHHH		49.39-
603AcetylationHAAELLAKQFCTRGS
HHHHHHHHHHHCCCC		43.8326051181
603UbiquitinationHAAELLAKQFCTRGS
HHHHHHHHHHHCCCC		43.83-
610PhosphorylationKQFCTRGSPQETTVL
HHHHCCCCCCCCEEE		21.8125159151
668PhosphorylationRIMMNRVSSRLGLTR
HHHHHHHHHHHCCCH		13.4020860994
669PhosphorylationIMMNRVSSRLGLTRM
HHHHHHHHHHCCCHH		28.7720860994
674PhosphorylationVSSRLGLTRMCFQPY
HHHHHCCCHHHCCCC		17.9820860994
698UbiquitinationRSRLKHLKAFEDDAI
HHHHHHHHHCCHHHH		51.23-
711UbiquitinationAIQLVARKVAALSGD
HHHHHHHHHHHHHCC		26.87-
730PhosphorylationLDICRRATEICEFSQ
HHHHHHHHHHHHHHH		24.8726074081
736PhosphorylationATEICEFSQQKPDSP
HHHHHHHHHCCCCCC		14.9226074081
850PhosphorylationLRVRLNVSQDDVLYA
EEEEECCCHHHHHHE		27.1520068231
856PhosphorylationVSQDDVLYALKDE--
CCHHHHHHEECCC--		15.1020068231
859UbiquitinationDDVLYALKDE-----
HHHHHEECCC-----		52.1921906983
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
258SPhosphorylationKinaseCDK1P06493
PhosphoELM
258SPhosphorylationKinaseCDK2P24941
PSP
273SPhosphorylationKinaseCDK1P06493
PhosphoELM
273SPhosphorylationKinaseCDK2P24941
PSP
375TPhosphorylationKinaseCDK1P06493
PhosphoELM
375TPhosphorylationKinaseCDK2P24941
PSP
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ORC1_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 ORC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCM2_HUMANMCM2physical
12614612
CDC7_HUMANCDC7physical
12614612
ORC2_HUMANORC2physical
12614612
ORC4_HUMANORC4physical
12614612
ORC5_HUMANORC5physical
12614612
MCM4_HUMANMCM4physical
12614612
MCM6_HUMANMCM6physical
12614612
MCM7_HUMANMCM7physical
12614612
CDC6_HUMANCDC6physical
12614612
CDC45_HUMANCDC45physical
12614612
KAT7_HUMANKAT7physical
10438470
CDC6_HUMANCDC6physical
9566895
ORC2_HUMANORC2physical
11779870
CCNA2_HUMANCCNA2physical
11931757
CDK2_HUMANCDK2physical
11931757
ORC2_HUMANORC2physical
11931757
CIRBP_HUMANCIRBPphysical
26496610
ORC2_HUMANORC2physical
26496610
ORC4_HUMANORC4physical
26496610
ORC5_HUMANORC5physical
26496610
RFC3_HUMANRFC3physical
26496610
SRP72_HUMANSRP72physical
26496610
ELOB_HUMANTCEB2physical
26496610
TRI26_HUMANTRIM26physical
26496610
ZN174_HUMANZNF174physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
CDIPT_HUMANCDIPTphysical
26496610
EXOS2_HUMANEXOSC2physical
26496610
SYHM_HUMANHARS2physical
26496610
PHF3_HUMANPHF3physical
26496610
ORC3_HUMANORC3physical
26496610
DIM1_HUMANDIMT1physical
26496610
LARP7_HUMANLARP7physical
26496610
DPOE3_HUMANPOLE3physical
26496610
PHIP_HUMANPHIPphysical
26496610
MRM3_HUMANRNMTL1physical
26496610
CHM1B_HUMANCHMP1Bphysical
26496610
RT15_HUMANMRPS15physical
26496610
RM11_HUMANMRPL11physical
26496610
ZN768_HUMANZNF768physical
26496610
PHF6_HUMANPHF6physical
26496610
DOT1L_HUMANDOT1Lphysical
26496610
LRWD1_HUMANLRWD1physical
26496610
ARP9_YEASTARP9physical
25453095
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
224690Meier-Gorlin syndrome 1 (MGORS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ORC1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-326, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-273 AND SER-287, ANDMASS SPECTROMETRY.
"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-196; THR-203; THR-337;SER-340; SER-417; SER-420; SER-421; SER-427 AND SER-478, AND MASSSPECTROMETRY.
"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-417; SER-419; SER-420AND SER-421, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory