CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012085
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Origin recognition complex subunit 1 
Protein Synonyms/Alias
 Replication control protein 1 
Gene Name
 ORC1 
Gene Synonyms/Alias
 ORC1L; PARC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
99FCEVPACKRHLLGRKubiquitination[1, 2]
149DVVPTNLKNEKTLFVubiquitination[1]
163VKLSWNEKKFRPLSSubiquitination[1]
164KLSWNEKKFRPLSSEubiquitination[1]
178ELFAELNKPQESAAKubiquitination[1, 3]
185KPQESAAKCQKPVRAubiquitination[3]
188ESAAKCQKPVRAKSKubiquitination[3]
195KPVRAKSKSAESPSWubiquitination[3]
326RTRIAASKTIDIREEacetylation[4, 5]
402LRFLGNSKSDQEEKEubiquitination[6]
586VYVQILQKLTGQKATubiquitination[1]
603HAAELLAKQFCTRGSubiquitination[1, 2]
859DDVLYALKDE*****ubiquitination[6]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. 
Sequence Annotation
 DOMAIN 45 171 BAH.
 NP_BIND 534 541 ATP (Potential).
 REGION 501 861 Necessary and sufficient for ORC complex
 BINDING 93 93 Histone H4K20me2 (By similarity).
 MOD_RES 203 203 Phosphothreonine.
 MOD_RES 273 273 Phosphoserine.
 MOD_RES 287 287 Phosphoserine.
 MOD_RES 326 326 N6-acetyllysine.
 MOD_RES 337 337 Phosphothreonine.
 MOD_RES 340 340 Phosphoserine.
 MOD_RES 417 417 Phosphoserine.
 MOD_RES 420 420 Phosphoserine.
 MOD_RES 478 478 Phosphoserine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Disease mutation; DNA replication; DNA-binding; Dwarfism; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 861 AA 
Protein Sequence
MAHYPTRLKT RKTYSWVGRP LLDRKLHYQT YREMCVKTEG CSTEIHIQIG QFVLIEGDDD 60
ENPYVAKLLE LFEDDSDPPP KKRARVQWFV RFCEVPACKR HLLGRKPGAQ EIFWYDYPAC 120
DSNINAETII GLVRVIPLAP KDVVPTNLKN EKTLFVKLSW NEKKFRPLSS ELFAELNKPQ 180
ESAAKCQKPV RAKSKSAESP SWTPAEHVAK RIESRHSASK SRQTPTHPLT PRARKRLELG 240
NLGNPQMSQQ TSCASLDSPG RIKRKVAFSE ITSPSKRSQP DKLQTLSPAL KAPEKTRETG 300
LSYTEDDKKA SPEHRIILRT RIAASKTIDI REERTLTPIS GGQRSSVVPS VILKPENIKK 360
RDAKEAKAQN EATSTPHRIR RKSSVLTMNR IRQQLRFLGN SKSDQEEKEI LPAAEISDSS 420
SDEEEASTPP LPRRAPRTVS RNLRSSLKSS LHTLTKVPKK SLKPRTPRCA APQIRSRSLA 480
AQEPASVLEE ARLRLHVSAV PESLPCREQE FQDIYNFVES KLLDHTGGCM YISGVPGTGK 540
TATVHEVIRC LQQAAQANDV PPFQYIEVNG MKLTEPHQVY VQILQKLTGQ KATANHAAEL 600
LAKQFCTRGS PQETTVLLVD ELDLLWTHKQ DIMYNLFDWP THKEARLVVL AIANTMDLPE 660
RIMMNRVSSR LGLTRMCFQP YTYSQLQQIL RSRLKHLKAF EDDAIQLVAR KVAALSGDAR 720
RCLDICRRAT EICEFSQQKP DSPGLVTIAH SMEAVDEMFS SSYITAIKNS SVLEQSFLRA 780
ILAEFRRSGL EEATFQQIYS QHVALCRMEG LPYPTMSETM AVCSHLGSCR LLLVEPSRND 840
LLLRVRLNVS QDDVLYALKD E 861 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0006270; P:DNA replication initiation; TAS:ProtInc.
 GO:0000083; P:regulation of transcription involved in G1/S phase of mitotic cell cycle; TAS:Reactome. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003959; ATPase_AAA_core.
 IPR001025; BAH_dom.
 IPR015163; Cdc6_C_dom.
 IPR020793; ORC1.
 IPR027417; P-loop_NTPase.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00004; AAA
 PF01426; BAH
 PF09079; Cdc6_C 
SMART
 SM00382; AAA
 SM00439; BAH
 SM01074; Cdc6_C 
PROSITE
 PS51038; BAH 
PRINTS