CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013043
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Far upstream element-binding protein 2 
Protein Synonyms/Alias
 FUSE-binding protein 2; KH type-splicing regulatory protein; KSRP 
Gene Name
 Khsrp 
Gene Synonyms/Alias
 Fubp2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
72GGGPGIRKDAFADAVacetylation[1]
72GGGPGIRKDAFADAVubiquitination[2]
88RARQIAAKIGGDAATacetylation[1, 3, 4]
88RARQIAAKIGGDAATubiquitination[2]
110DFGFGGQKRQLEDGDubiquitination[2]
123GDQPDSKKLASQGDSubiquitination[2]
170RGGEQINKIQQDSGCacetylation[3]
170RGGEQINKIQQDSGCubiquitination[2]
204GAPESVQKAKMMLDDubiquitination[2]
252KAGLVIGKGGETIKQubiquitination[5]
258GKGGETIKQLQERAGubiquitination[2]
267LQERAGVKMILIQDGubiquitination[2]
282SQNTNVDKPLRIIGDubiquitination[2]
360AGVRIQFKQDDGTGPacetylation[3]
449GRGGENVKAINQQTGubiquitination[2]
489PQQIDHAKQLIEEKIacetylation[3]
629AWEEYYKKIGQQPQQubiquitination[5]
647PPQQDYTKAWEEYYKubiquitination[5]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] 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]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Binds to the dendritic targeting element and may play a role in mRNA trafficking. Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs (By similarity). 
Sequence Annotation
 DOMAIN 145 209 KH 1.
 DOMAIN 234 300 KH 2.
 DOMAIN 323 387 KH 3.
 DOMAIN 425 492 KH 4.
 REPEAT 572 583 1.
 REPEAT 618 629 2.
 REPEAT 644 655 3.
 REPEAT 674 685 4.
 REGION 572 685 4 X 12 AA imperfect repeats.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 101 101 Phosphothreonine (By similarity).
 MOD_RES 182 182 Phosphoserine.
 MOD_RES 194 194 Phosphoserine (By similarity).
 MOD_RES 275 275 Phosphoserine.
 MOD_RES 481 481 Phosphoserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; DNA-binding; mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 748 AA 
Protein Sequence
MSDYNTGGPP PGPPPPAGGG GGAAGAGGGP PPGPPGAGDR GGGGPGGGGP GGGGASGGPS 60
QPPGGGGPGI RKDAFADAVQ RARQIAAKIG GDAATTVNNN TPDFGFGGQK RQLEDGDQPD 120
SKKLASQGDS IGSQLGPIHP PPRTSMTEEY RVPDGMVGLI IGRGGEQINK IQQDSGCKVQ 180
ISPDSGGLPE RSVSLTGAPE SVQKAKMMLD DIVSRGRGGP PGQFHDNANG GQNGTVQEIM 240
IPAGKAGLVI GKGGETIKQL QERAGVKMIL IQDGSQNTNV DKPLRIIGDP YKVQQACEMV 300
MDILRERDQG GFGDRNEYGS RVGGGIDVPV PRHSVGVVIG RSGEMIKKIQ NDAGVRIQFK 360
QDDGTGPEKI AHIMGPPDRC EHAARIINDL LQSLRSGPPG PPGAPGMPPG GRGRGRGQGN 420
WGPPGGEMTF SIPTHKCGLV IGRGGENVKA INQQTGAFVE ISRQLPPNGD PNFKLFVIRG 480
SPQQIDHAKQ LIEEKIEGPL CPVGPGPGGP GPAGPMGPFN PGPFNQGPPG APPHAGGPPP 540
HQYPPQGWGN TYPQWQPPAP HDPNKAAAAA TDPNAAWAAY YSHYYQQPPG PVPGPAPAPA 600
APPAQGEPPQ PPPTGQSDYT KAWEEYYKKI GQQPQQPGAP PQQDYTKAWE EYYKKQAQVA 660
TGGGPGAPPG SQPDYSAAWA EYYRQQAAYY GQTPGPGGPQ PPPTQQGQQQ ASGNCHPPPP 720
PFSFQPPATV HPALVGSAGN PFPCGVCP 748 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR015096; DUF1897.
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1. 
Pfam
 PF09005; DUF1897
 PF00013; KH_1 
SMART
 SM00322; KH 
PROSITE
 PS00178; AA_TRNA_LIGASE_I
 PS50084; KH_TYPE_1 
PRINTS