CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040025
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Helicase SKI2W 
Protein Synonyms/Alias
 Uncharacterized protein 
Gene Name
 SKIV2L 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
123FEPDVFQKQAILHLEubiquitination[1, 2]
158YAIALAQKHMTRTIYubiquitination[1, 2, 3]
170TIYTSPIKALSNQKFubiquitination[1, 2, 4]
176IKALSNQKFRDFRNTubiquitination[1, 2]
323SRGAFHTKGYYAAVEubiquitination[1, 2, 3, 5]
332YYAAVEAKKERMSKHubiquitination[5]
333YAAVEAKKERMSKHAubiquitination[1, 2]
338AKKERMSKHAQTFGAubiquitination[1]
346HAQTFGAKQPTHQGGubiquitination[1, 2, 3, 5]
404DLTTSSEKSEIHLFLubiquitination[1]
527GTVILLCKGRVPEMAubiquitination[1, 2]
543LHRMMMGKPSQLQSQubiquitination[1]
574LRVEDMMKRSFSEFPubiquitination[1]
587FPSRKDSKAHEQALAubiquitination[1, 5]
598QALAELTKRLGALEEubiquitination[1, 2, 3, 5]
644MESVNGLKSLSAGRVubiquitination[1, 3, 5]
686TTLVLCDKPLSQDPQubiquitination[1]
726PCDHTVVKLQPGDMAubiquitination[1]
738DMAAITTKVLRVNGEubiquitination[1, 2]
746VLRVNGEKILEDFSKubiquitination[1]
753KILEDFSKRQQPKFKubiquitination[1]
760KRQQPKFKKDPPLAAubiquitination[1]
761RQQPKFKKDPPLAAVubiquitination[1]
798PVNDLQLKDMSVVEGubiquitination[1, 2, 3, 5]
811EGGLRARKLEELIQGubiquitination[1]
833RFPAQYLKLRERMQIubiquitination[1, 3]
842RERMQIQKEMERLRFubiquitination[1]
882VDEAGTVKLAGRVACubiquitination[1, 2, 5, 6]
1032GEPVLGAKMETAATLubiquitination[1, 3, 5]
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] 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]
 [5] 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]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1053 AA 
Protein Sequence
MDFAPKDCPT PAPGLLSLSC MLEPLDLGGG DEDENEAVGQ PGGPRGDTVS ASPCSAPLAR 60
ASSLEDLVLK EASTAVSTPE APEPPSQEQW AIPVDATSPV GDFYRLIPQP AFQWAFEPDV 120
FQKQAILHLE RHDSVFVAAH TSAGKTVVAE YAIALAQKHM TRTIYTSPIK ALSNQKFRDF 180
RNTFGDVGLL TGDVQLHPEA SCLIMTTEIL RSMLYSGSDV IRDLEWVIFD EVHYINDVER 240
GVVWEEVLIM LPDHVSIILL SATVPNALEF ADWIGRLKRR QIYVISTVTR PVPLEHYLFT 300
GNSSKTQGEL FLLLDSRGAF HTKGYYAAVE AKKERMSKHA QTFGAKQPTH QGGPAQDRGV 360
YLSLLASLRT RAQLPVVVFT FSRGRCDEQA SGLTSLDLTT SSEKSEIHLF LQRCLARLRG 420
SDRQLPQVLH MSELLNRGLG VHHSGILPIL KEIVEMLFSR GLVKVLFATE TFAMGVNMPA 480
RTVVFDSMRK HDGSTFRDLL PGEYVQMAGR AGRRGLDPTG TVILLCKGRV PEMADLHRMM 540
MGKPSQLQSQ FRLTYTMILN LLRVDALRVE DMMKRSFSEF PSRKDSKAHE QALAELTKRL 600
GALEEPDMTG QLVDLPEYYS WGEELTETQH MIQRRIMESV NGLKSLSAGR VVVVKNQEHH 660
NALGVILQVS SNSTSRVFTT LVLCDKPLSQ DPQDRGPATA EVPYPDDLVG FKLFLPEGPC 720
DHTVVKLQPG DMAAITTKVL RVNGEKILED FSKRQQPKFK KDPPLAAVTT AVQELLRLAQ 780
AHPAGPPTLD PVNDLQLKDM SVVEGGLRAR KLEELIQGAQ CVHSPRFPAQ YLKLRERMQI 840
QKEMERLRFL LSDQSLLLLP EYHQRVEVLR TLGYVDEAGT VKLAGRVACA MSSHELLLTE 900
LMFDNALSTL RPEEIAALLS GLVCQSPGDA GDQLPNTLKQ GIERVRAVAK RIGEVQVACG 960
LNQTVEEFVG ELNFGLVEVV YEWARGMPFS ELAGLSGTPE GLVVRCIQRL AEMCRSLRGA 1020
ARLVGEPVLG AKMETAATLL RRDIVFAASL YTQ 1053 
Gene Ontology
 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. 
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