CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018779
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 
Protein Synonyms/Alias
 ATP-dependent RNA helicase DHX38; DEAH box protein 38 
Gene Name
 DHX38 
Gene Synonyms/Alias
 DDX38; KIAA0224; PRP16 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
260RDRSVRGKYSDDTPLacetylation[1]
425DGRIVFTKQPEPVIPubiquitination[2, 3]
434PEPVIPVKDATSDLAubiquitination[2]
504VDYRTEQKFADHMKRubiquitination[2]
510QKFADHMKRKSEASSubiquitination[2]
521EASSEFAKKKSILEQacetylation[1, 4]
717PVDILFSKTPQEDYVubiquitination[5]
793LQAKIFQKAPDGVRKubiquitination[6]
829DSGYCKLKVFNPRIGubiquitination[2]
875LYTQSAYKNELLTTTubiquitination[2]
1049REVRAQLKDIMVQQRubiquitination[2]
1166QENRRRAKEEASAMEubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [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] 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
Functional Description
 Probable ATP-binding RNA helicase involved in pre-mRNA splicing. 
Sequence Annotation
 DOMAIN 542 705 Helicase ATP-binding.
 DOMAIN 727 902 Helicase C-terminal.
 NP_BIND 555 562 ATP (By similarity).
 MOTIF 652 655 DEAH box.
 MOD_RES 2 2 N-acetylglycine.
 MOD_RES 199 199 Phosphoserine.
 MOD_RES 260 260 N6-acetyllysine.
 MOD_RES 1194 1194 Phosphoserine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; Helicase; Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1227 AA 
Protein Sequence
MGDTSEDASI HRLEGTDLDC QVGGLICKSK SAASEQHVFK APAPRPSLLG LDLLASLKRR 60
EREEKDDGED KKKSKVSSYK DWEESKDDQK DAEEEGGDQA GQNIRKDRHY RSARVETPSH 120
PGGVSEEFWE RSRQRERERR EHGVYASSKE EKDWKKEKSR DRDYDRKRDR DERDRSRHSS 180
RSERDGGSER SSRRNEPESP RHRPKDAATP SRSTWEEEDS GYGSSRRSQW ESPSPTPSYR 240
DSERSHRLST RDRDRSVRGK YSDDTPLPTP SYKYNEWADD RRHLGSTPRL SRGRGRREEG 300
EEGISFDTEE ERQQWEDDQR QADRDWYMMD EGYDEFHNPL AYSSEDYVRR REQHLHKQKQ 360
KRISAQRRQI NEDNERWETN RMLTSGVVHR LEVDEDFEED NAAKVHLMVH NLVPPFLDGR 420
IVFTKQPEPV IPVKDATSDL AIIARKGSQT VRKHREQKER KKAQHKHWEL AGTKLGDIMG 480
VKKEEEPDKA VTEDGKVDYR TEQKFADHMK RKSEASSEFA KKKSILEQRQ YLPIFAVQQE 540
LLTIIRDNSI VIVVGETGSG KTTQLTQYLH EDGYTDYGMI GCTQPRRVAA MSVAKRVSEE 600
MGGNLGEEVG YAIRFEDCTS ENTLIKYMTD GILLRESLRE ADLDHYSAII MDEAHERSLN 660
TDVLFGLLRE VVARRSDLKL IVTSATMDAE KFAAFFGNVP IFHIPGRTFP VDILFSKTPQ 720
EDYVEAAVKQ SLQVHLSGAP GDILIFMPGQ EDIEVTSDQI VEHLEELENA PALAVLPIYS 780
QLPSDLQAKI FQKAPDGVRK CIVATNIAET SLTVDGIMFV IDSGYCKLKV FNPRIGMDAL 840
QIYPISQANA NQRSGRAGRT GPGQCFRLYT QSAYKNELLT TTVPEIQRTN LANVVLLLKS 900
LGVQDLLQFH FMDPPPEDNM LNSMYQLWIL GALDNTGGLT STGRLMVEFP LDPALSKMLI 960
VSCDMGCSSE ILLIVSMLSV PAIFYRPKGR EEESDQIREK FAVPESDHLT YLNVYLQWKN 1020
NNYSTIWCND HFIHAKAMRK VREVRAQLKD IMVQQRMSLA SCGTDWDIVR KCICAAYFHQ 1080
AAKLKGIGEY VNIRTGMPCH LHPTSSLFGM GYTPDYIVYH ELVMTTKEYM QCVTAVDGEW 1140
LAELGPMFYS VKQAGKSRQE NRRRAKEEAS AMEEEMALAE EQLRARRQEQ EKRSPLGSVR 1200
STKIYTPGRK EQGEPMTPRR TPARFGL 1227 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 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:0031124; P:mRNA 3'-end processing; TAS:Reactome.
 GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
 GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
 GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR002464; DNA/RNA_helicase_DEAH_CS.
 IPR011709; DUF1605.
 IPR007502; Helicase-assoc_dom.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00270; DEAD
 PF04408; HA2
 PF00271; Helicase_C
 PF07717; OB_NTP_bind 
SMART
 SM00487; DEXDc
 SM00847; HA2
 SM00490; HELICc 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS