CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019333
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Splicing factor 45 
Protein Synonyms/Alias
 45 kDa-splicing factor; RNA-binding motif protein 17 
Gene Name
 RBM17 
Gene Synonyms/Alias
 SPF45 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21SKTEGWSKNFKLLQSacetylation[1]
34QSQLQVKKAALTQAKubiquitination[2]
245VAHKIMQKYGFREGQacetylation[3]
285IVGDATEKDASKKSDacetylation[4]
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] 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]
 [4] 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] 
Functional Description
 Splice factor that binds to the single stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia. 
Sequence Annotation
 DOMAIN 235 283 G-patch.
 DOMAIN 306 385 RRM.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 21 21 N6-acetyllysine.
 MOD_RES 71 71 Phosphothreonine.
 MOD_RES 155 155 Phosphoserine.
 MOD_RES 169 169 Phosphoserine.
 MOD_RES 222 222 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 401 AA 
Protein Sequence
MSLYDDLGVE TSDSKTEGWS KNFKLLQSQL QVKKAALTQA KSQRTKQSTV LAPVIDLKRG 60
GSSDDRQIVD TPPHVAAGLK DPVPSGFSAG EVLIPLADEY DPMFPNDYEK VVKRQREERQ 120
RQRELERQKE IEEREKRRKD RHEASGFARR PDPDSDEDED YERERRKRSM GGAAIAPPTS 180
LVEKDKELPR DFPYEEDSRP RSQSSKAAIP PPVYEEQDRP RSPTGPSNSF LANMGGTVAH 240
KIMQKYGFRE GQGLGKHEQG LSTALSVEKT SKRGGKIIVG DATEKDASKK SDSNPLTEIL 300
KCPTKVVLLR NMVGAGEVDE DLEVETKEEC EKYGKVGKCV IFEIPGAPDD EAVRIFLEFE 360
RVESAIKAVV DLNGRYFGGR VVKACFYNLD KFRVLDLAEQ V 401 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 
Interpro
 IPR000467; G_patch_dom.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR003954; RRM_dom_euk.
 IPR016967; Splicing_factor_SPF45. 
Pfam
 PF01585; G-patch 
SMART
 SM00443; G_patch
 SM00361; RRM_1 
PROSITE
 PS50174; G_PATCH
 PS50102; RRM 
PRINTS