CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001236
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 U5 small nuclear ribonucleoprotein 200 kDa helicase 
Protein Synonyms/Alias
 Activating signal cointegrator 1 complex subunit 3-like 1; BRR2 homolog; U5 snRNP-specific 200 kDa protein; U5-200KD 
Gene Name
 SNRNP200 
Gene Synonyms/Alias
 ASCC3L1; HELIC2; KIAA0788 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46EVLSLVGKLEGTRMGubiquitination[1]
284DDAIVSQKKADEVLEubiquitination[2]
285DAIVSQKKADEVLEIubiquitination[1]
358EADPELSKFLYQLHEubiquitination[3, 4]
426GSHFMANKRCQLPDGubiquitination[1, 3, 4, 5]
469LPVEKLPKYAQAGFEacetylation[6]
469LPVEKLPKYAQAGFEubiquitination[1, 3, 4, 7]
479QAGFEGFKTLNRIQSubiquitination[1, 3, 4, 5, 7]
487TLNRIQSKLYRAALEubiquitination[1]
557EMVGSFGKRLATYGIubiquitination[1, 2, 5, 7]
711MNEIVYEKIMEHAGKubiquitination[2]
745IRDMCLEKDTLGLFLubiquitination[1]
770RTEAEQCKNLELKDLubiquitination[1, 3, 4, 7, 8]
775QCKNLELKDLLPYGFubiquitination[1]
944GISHDDLKGDPLLDQacetylation[9]
944GISHDDLKGDPLLDQubiquitination[1, 2, 8, 10]
966TAALMLDKNNLVKYDubiquitination[1]
971LDKNNLVKYDKKTGNacetylation[6]
974NNLVKYDKKTGNFQVubiquitination[1]
975NLVKYDKKTGNFQVTubiquitination[1]
1025FSLSSEFKNITVREEubiquitination[2, 8]
1039EEKLELQKLLERVPIubiquitination[2, 3, 4, 7]
1049ERVPIPVKESIEEPSubiquitination[1, 2]
1134CPLRQFRKLPEEVVKubiquitination[1, 8]
1141KLPEEVVKKIEKKNFubiquitination[1]
1146VVKKIEKKNFPFERLubiquitination[1]
1176KMGKTIHKYVHLFPKacetylation[6]
1294RHLILPEKYPPPTELubiquitination[1]
1404FQDRLNKKVVLLTGEubiquitination[1, 7, 8]
1417GETSTDLKLLGKGNIubiquitination[1]
1421TDLKLLGKGNIIISTubiquitination[3, 4, 7]
1431IIISTPEKWDILSRRubiquitination[1, 2, 3, 4, 7, 8]
1544TRLLSMAKPVYHAITubiquitination[1, 3, 4, 7, 11]
1557ITKHSPKKPVIVFVPubiquitination[7]
1595RFLHCTEKDLIPYLEubiquitination[1, 7]
1603DLIPYLEKLSDSTLKubiquitination[2]
1711IMCQGSKKDFFKKFLubiquitination[1]
1961WSKDSYLKQLPHFTSubiquitination[3, 4]
2059IAPLFPQKREEGWWVubiquitination[1, 2, 8]
2080SNSLISIKRLTLQQKubiquitination[2, 3, 4]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 
Functional Description
 RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome. 
Sequence Annotation
 DOMAIN 490 673 Helicase ATP-binding 1.
 DOMAIN 684 921 Helicase C-terminal 1.
 DOMAIN 981 1286 SEC63 1.
 DOMAIN 1337 1512 Helicase ATP-binding 2.
 DOMAIN 1545 1753 Helicase C-terminal 2.
 DOMAIN 1812 2124 SEC63 2.
 NP_BIND 503 510 ATP.
 NP_BIND 1350 1357 ATP.
 MOTIF 615 618 DEIH box.
 MOTIF 1454 1457 DEVH box.
 MOD_RES 26 26 Phosphoserine.
 MOD_RES 225 225 Phosphoserine.
 MOD_RES 709 709 Phosphotyrosine (By similarity).
 MOD_RES 971 971 N6-acetyllysine; alternate.
 MOD_RES 2131 2131 Phosphothreonine.
 MOD_RES 2133 2133 Phosphoserine.
 MOD_RES 2135 2135 Phosphoserine.
 CROSSLNK 944 944 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 971 971 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1071 1071 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1199 1199 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 2091 2091 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; Helicase; Hydrolase; Isopeptide bond; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Retinitis pigmentosa; Spliceosome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2136 AA 
Protein Sequence
MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK 60
PQMQEERRAK RRKRDEDRHD INKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI 120
QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRKEIDLL LGQTDDTRYH VLVNLGKKIT 180
DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL 240
SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR 300
ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE AEKERIMGKM EADPELSKFL 360
YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS 420
HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT 480
LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY 540
IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG 600
GERTYTQLVR LIILDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED 660
VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ 720
VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY 780
GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR 840
WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM 900
LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA 960
ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL 1020
SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD 1080
MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV 1140
KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV 1200
ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH LITFFVPVFE 1260
PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALRNSAFESL 1320
YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA PTGSGKTICA EFAILRMLLQ SSEGRCVYIT 1380
PMEALAEQVY MDWYEKFQDR LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK 1440
QRKNVQNINL FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV 1500
AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI TKHSPKKPVI 1560
VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY LEKLSDSTLK ETLLNGVGYL 1620
HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP 1680
IYDVLQMVGH ANRPLQDDEG RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI 1740
VTKTIENKQD AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK 1800
CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS NAAEYENIPI 1860
RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS RMQLSAELQS DTEEILSKAI 1920
RLIQACVDVL SSNGWLSPAL AAMELAQMVT QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE 1980
SVFDIMEMED EERNALLQLT DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ 2040
LEREEEVTGP VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG 2100
AHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD 2136 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005682; C:U5 snRNP; IDA:HGNC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004004; F:ATP-dependent RNA helicase activity; IDA:UniProtKB.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0000354; P:cis assembly of pre-catalytic spliceosome; IC:HGNC. 
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