CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017378
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Activating signal cointegrator 1 complex subunit 3 
Protein Synonyms/Alias
 ASC-1 complex subunit p200; ASC1p200; Helicase, ATP binding 1; Trip4 complex subunit p200 
Gene Name
 ASCC3 
Gene Synonyms/Alias
 HELIC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
18RSFSNVTKQDNYNEEubiquitination[1, 2, 3]
30NEEVADLKIKRSKLHubiquitination[1]
78KDILHAAKQIVGTDNubiquitination[1]
197KTISLDYKKFLNEHLubiquitination[1, 4]
198TISLDYKKFLNEHLQubiquitination[2]
213EACTPELKPVEKTNGubiquitination[2, 5, 6]
236KYLNSTLKEMTEVPRubiquitination[1, 7, 8, 9]
312ALQDNCKKILGENAKubiquitination[2]
319KILGENAKPNYGCQVubiquitination[2]
334TIQSEQEKQLMKQYRubiquitination[2]
423SAFIAGAKMILPEGIubiquitination[1, 2, 3, 7, 9]
436GIQRENNKLYEEVRIubiquitination[1, 2]
540IVYVAPMKALAAEMTubiquitination[2]
572TGDMQLSKSEILRTQacetylation[6, 10, 11, 12]
572TGDMQLSKSEILRTQubiquitination[1, 2, 6]
587MLVTTPEKWDVVTRKubiquitination[2]
594KWDVVTRKSVGDVALubiquitination[2]
693LGIKCANKMQQLNNMubiquitination[2]
710VCYENVLKQVKAGHQubiquitination[2]
740MSLIERAKNCGHIPFubiquitination[2]
761HDYVLAEKQVQRSRNubiquitination[2, 5]
834GTQIYAAKRGSFVDLubiquitination[1]
860AGRPQFDKFGEGIIIubiquitination[7, 9]
938LAYGISHKAYQIDPTubiquitination[1, 5, 7, 8, 9]
960LVIEVGRKLDKAQMIubiquitination[2]
1017DIFAIVSKAEEFDQIubiquitination[1]
1025AEEFDQIKVREEEIEubiquitination[1, 3]
1150EKKLTVDKLKDMRKDubiquitination[2]
1369AIFRVFNKYPTSKAVubiquitination[2]
1374FNKYPTSKAVYIAPLubiquitination[5]
1382AVYIAPLKALVRERMubiquitination[1, 2, 3, 5, 7, 8, 9]
1399WKVRIEEKLGKKVIEacetylation[6]
1403IEEKLGKKVIELTGDubiquitination[2]
1416GDVTPDMKSIAKADLubiquitination[1, 2, 3]
1420PDMKSIAKADLIVTTubiquitination[1]
1430LIVTTPEKWDGVSRSubiquitination[1]
1482FISSHTEKPVRIVGLubiquitination[1, 2, 3]
1543PRMASMNKPAFQAIRubiquitination[2, 5]
1609TVRDSNLKLTLAFGImethylation[13]
1671GTEYYDGKTRRYVDFubiquitination[1]
2097HFGFHKGKPESCAVTubiquitination[2, 6]
Reference
 [1] 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]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] 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]
 [6] 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]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [10] 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]
 [11] 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]
 [12] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [13] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510
Functional Description
 3'-5' DNA helicase involved in repair of alkylated DNA. Promotes DNA unwinding to generate single-stranded substrate needed for ALKHB3, enabling ALKHB3 to process alkylated N3- methylcytosine (3mC) within double-stranded regions. Enhances NF- kappa-B, SRF and AP1 transactivation. 
Sequence Annotation
 DOMAIN 486 669 Helicase ATP-binding 1.
 DOMAIN 728 914 Helicase C-terminal 1.
 DOMAIN 978 1287 SEC63 1.
 DOMAIN 1336 1511 Helicase ATP-binding 2.
 DOMAIN 1544 1739 Helicase C-terminal 2.
 DOMAIN 1812 2176 SEC63 2.
 NP_BIND 499 506 ATP (Potential).
 NP_BIND 1349 1356 ATP (Potential).
 MOTIF 611 614 DEVH box.
 MOTIF 1453 1456 DEIH box.
 MOD_RES 572 572 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2202 AA 
Protein Sequence
MALPRLTGAL RSFSNVTKQD NYNEEVADLK IKRSKLHEQV LDLGLTWKKI IKFLNEKLEK 60
SKMQSINEDL KDILHAAKQI VGTDNGREAI ESGAAFLFMT FHLKDSVGHK ETKAIKQMFG 120
PFPSSSATAA CNATNRIISH FSQDDLTALV QMTEKEHGDR VFFGKNLAFS FDMHDLDHFD 180
ELPINGETQK TISLDYKKFL NEHLQEACTP ELKPVEKTNG SFLWCEVEKY LNSTLKEMTE 240
VPRVEDLCCT LYDMLASIKS GDELQDELFE LLGPEGLELI EKLLQNRITI VDRFLNSSND 300
HRFQALQDNC KKILGENAKP NYGCQVTIQS EQEKQLMKQY RREEKRIARR EKKAGEDLEV 360
SEGLMCFDPK ELRIQREQAL LNARSVPILS RQRDADVEKI HYPHVYDSQA EAMKTSAFIA 420
GAKMILPEGI QRENNKLYEE VRIPYSEPMP LSFEEKPVYI QDLDEIGQLA FKGMKRLNRI 480
QSIVFETAYN TNENMLICAP TGAGKTNIAM LTVLHEIRQH FQQGVIKKNE FKIVYVAPMK 540
ALAAEMTDYF SRRLEPLGII VKELTGDMQL SKSEILRTQM LVTTPEKWDV VTRKSVGDVA 600
LSQIVRLLIL DEVHLLHEDR GPVLESIVAR TLRQVESTQS MIRILGLSAT LPNYLDVATF 660
LHVNPYIGLF FFDGRFRPVP LGQTFLGIKC ANKMQQLNNM DEVCYENVLK QVKAGHQVMV 720
FVHARNATVR TAMSLIERAK NCGHIPFFFP TQGHDYVLAE KQVQRSRNKQ VRELFPDGFS 780
IHHAGMLRQD RNLVENLFSN GHIKVLVCTA TLAWGVNLPA HAVIIKGTQI YAAKRGSFVD 840
LGILDVMQIF GRAGRPQFDK FGEGIIITTH DKLSHYLTLL TQRNPIESQF LESLADNLNA 900
EIALGTVTNV EEAVKWISYT YLYVRMRANP LAYGISHKAY QIDPTLRKHR EQLVIEVGRK 960
LDKAQMIRFE ERTGYFSSTD LGRTASHYYI KYNTIETFNE LFDAHKTEGD IFAIVSKAEE 1020
FDQIKVREEE IEELDTLLSN FCELSTPGGV ENSYGKINIL LQTYISRGEM DSFSLISDSA 1080
YVAQNAARIV RALFEIALRK RWPTMTYRLL NLSKVIDKRL WGWASPLRQF SILPPHILTR 1140
LEEKKLTVDK LKDMRKDEIG HILHHVNIGL KVKQCVHQIP SVMMEASIQP ITRTVLRVTL 1200
SIYADFTWND QVHGTVGEPW WIWVEDPTND HIYHSEYFLA LKKQVISKEA QLLVFTIPIF 1260
EPLPSQYYIR AVSDRWLGAE AVCIINFQHL ILPERHPPHT ELLDLQPLPI TALGCKAYEA 1320
LYNFSHFNPV QTQIFHTLYH TDCNVLLGAP TGSGKTVAAE LAIFRVFNKY PTSKAVYIAP 1380
LKALVRERMD DWKVRIEEKL GKKVIELTGD VTPDMKSIAK ADLIVTTPEK WDGVSRSWQN 1440
RNYVQQVTIL IIDEIHLLGE ERGPVLEVIV SRTNFISSHT EKPVRIVGLS TALANARDLA 1500
DWLNIKQMGL FNFRPSVRPV PLEVHIQGFP GQHYCPRMAS MNKPAFQAIR SHSPAKPVLI 1560
FVSSRRQTRL TALELIAFLA TEEDPKQWLN MDEREMENII ATVRDSNLKL TLAFGIGMHH 1620
AGLHERDRKT VEELFVNCKV QVLIATSTLA WGVNFPAHLV IIKGTEYYDG KTRRYVDFPI 1680
TDVLQMMGRA GRPQFDDQGK AVILVHDIKK DFYKKFLYEP FPVESSLLGV LSDHLNAEIA 1740
GGTITSKQDA LDYITWTYFF RRLIMNPSYY NLGDVSHDSV NKFLSHLIEK SLIELELSYC 1800
IEIGEDNRSI EPLTYGRIAS YYYLKHQTVK MFKDRLKPEC STEELLSILS DAEEYTDLPV 1860
RHNEDHMNSE LAKCLPIESN PHSFDSPHTK AHLLLQAHLS RAMLPCPDYD TDTKTVLDQA 1920
LRVCQAMLDV AANQGWLVTV LNITNLIQMV IQGRWLKDSS LLTLPNIENH HLHLFKKWKP 1980
IMKGPHARGR TSIESLPELI HACGGKDHVF SSMVESELHA AKTKQAWNFL SHLPVINVGI 2040
SVKGSWDDLV EGHNELSVST LTADKRDDNK WIKLHADQEY VLQVSLQRVH FGFHKGKPES 2100
CAVTPRFPKS KDEGWFLILG EVDKRELIAL KRVGYIRNHH VASLSFYTPE IPGRYIYTLY 2160
FMSDCYLGLD QQYDIYLNVT QASLSAQVNT KVSDSLTDLA LK 2202 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; TAS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IDA:UniProtKB.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008283; P:cell proliferation; IMP:UniProtKB.
 GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR004179; Sec63-dom. 
Pfam
 PF00270; DEAD
 PF00271; Helicase_C
 PF02889; Sec63 
SMART
 SM00382; AAA
 SM00487; DEXDc
 SM00490; HELICc
 SM00611; SEC63
 SM00973; Sec63 
PROSITE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS