CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007552
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Superkiller viralicidic activity 2-like 2 
Protein Synonyms/Alias
 ATP-dependent helicase SKIV2L2 
Gene Name
 SKIV2L2 
Gene Synonyms/Alias
 KIAA0052; Mtr4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
43GPPGSADKAGKRFDGacetylation[1]
51AGKRFDGKLQSESTNacetylation[2]
78TDEPIFGKKPRIEESacetylation[2]
78TDEPIFGKKPRIEESubiquitination[3]
79DEPIFGKKPRIEESIacetylation[4]
79DEPIFGKKPRIEESIubiquitination[3]
126EEDYLPLKPRVGKAAubiquitination[3, 5]
134PRVGKAAKEYPFILDubiquitination[3]
192VIFTSPIKALSNQKYubiquitination[3, 6, 7]
198IKALSNQKYREMYEEacetylation[2]
198IKALSNQKYREMYEEubiquitination[8]
358RDAGDLAKGDQKGRKubiquitination[8]
379SNVFKIVKMIMERNFacetylation[2]
379SNVFKIVKMIMERNFubiquitination[3]
397IIFSFSKKDCEAYALubiquitination[3]
408AYALQMTKLDFNTDEubiquitination[3]
417DFNTDEEKKMVEEVFubiquitination[8]
418FNTDEEKKMVEEVFSubiquitination[3]
449EHVLPLLKRGIGIHHubiquitination[8]
503VLFTNARKFDGKDFRubiquitination[3]
507NARKFDGKDFRWISSubiquitination[3]
587NPEYMLEKSFYQFQHubiquitination[3, 8]
606PGVVEKVKNSEEQYNubiquitination[3]
614NSEEQYNKIVIPNEEubiquitination[3, 8]
638QQLAKLGKEIEEYIHubiquitination[3]
748SVRLYIPKDLRPVDNacetylation[2]
748SVRLYIPKDLRPVDNubiquitination[3]
761DNRQSVLKSIQEVQKubiquitination[3, 6, 7]
768KSIQEVQKRFPDGIPubiquitination[3]
796GLKKVIQKVEAFEHRacetylation[2]
796GLKKVIQKVEAFEHRubiquitination[3]
833AQIAIDIKSAKRELKubiquitination[3]
852VLQMDELKCRKRVLRubiquitination[3]
873SSDVIEMKGRVACEIubiquitination[3, 8]
1022GNTELENKFAEGITKubiquitination[3, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [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] 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]
 [7] 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]
 [8] 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
 May be involved in pre-mRNA splicing. Associated with the RNA exosome complex and involved in the 3'processing of the 7S pre-RNA to the mature 5.8S rRNA. 
Sequence Annotation
 DOMAIN 148 304 Helicase ATP-binding.
 DOMAIN 405 577 Helicase C-terminal.
 NP_BIND 161 168 ATP (Potential).
 MOTIF 252 255 DEIH box.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 51 51 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; Helicase; Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; rRNA processing; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1042 AA 
Protein Sequence
MADAFGDELF SVFEGDSTTA AGTKKDKEKD KGKWKGPPGS ADKAGKRFDG KLQSESTNNG 60
KNKRDVDFEG TDEPIFGKKP RIEESITEDL SLADLMPRVK VQSVETVEGC THEVALPAEE 120
DYLPLKPRVG KAAKEYPFIL DAFQREAIQC VDNNQSVLVS AHTSAGKTVC AEYAIALALR 180
EKQRVIFTSP IKALSNQKYR EMYEEFQDVG LMTGDVTINP TASCLVMTTE ILRSMLYRGS 240
EVMREVAWVI FDEIHYMRDS ERGVVWEETI ILLPDNVHYV FLSATIPNAR QFAEWICHLH 300
KQPCHVIYTD YRPTPLQHYI FPAGGDGLHL VVDENGDFRE DNFNTAMQVL RDAGDLAKGD 360
QKGRKGGTKG PSNVFKIVKM IMERNFQPVI IFSFSKKDCE AYALQMTKLD FNTDEEKKMV 420
EEVFSNAIDC LSDEDKKLPQ VEHVLPLLKR GIGIHHGGLL PILKETIEIL FSEGLIKALF 480
ATETFAMGIN MPARTVLFTN ARKFDGKDFR WISSGEYIQM SGRAGRRGMD DRGIVILMVD 540
EKMSPTIGKQ LLKGSADPLN SAFHLTYNMV LNLLRVEEIN PEYMLEKSFY QFQHYRAIPG 600
VVEKVKNSEE QYNKIVIPNE ESVVIYYKIR QQLAKLGKEI EEYIHKPKYC LPFLQPGRLV 660
KVKNEGDDFG WGVVVNFSKK SNVKPNSGEL DPLYVVEVLL RCSKESLKNS ATEAAKPAKP 720
DEKGEMQVVP VLVHLLSAIS SVRLYIPKDL RPVDNRQSVL KSIQEVQKRF PDGIPLLDPI 780
DDMGIQDQGL KKVIQKVEAF EHRMYSHPLH NDPNLETVYT LCEKKAQIAI DIKSAKRELK 840
KARTVLQMDE LKCRKRVLRR LGFATSSDVI EMKGRVACEI SSADELLLTE MMFNGLFNDL 900
SAEQATALLS CFVFQENSSE MPKLTEQLAG PLRQMQECAK RIAKVSAEAK LEIDEETYLS 960
SFKPHLMDVV YTWATGATFA HICKMTDVFE GSIIRCMRRL EELLRQMCQA AKAIGNTELE 1020
NKFAEGITKI KRDIVFAASL YL 1042 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR012961; DSH_C.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR016438; RNA_helicase_ATP-dep_SK12/DOB1.
 IPR025696; rRNA_proc-arch_dom. 
Pfam
 PF00270; DEAD
 PF08148; DSHCT
 PF00271; Helicase_C
 PF13234; rRNA_proc-arch 
SMART
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS