CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001593
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pre-mRNA-splicing factor SLU7 
Protein Synonyms/Alias
 hSlu7 
Gene Name
 SLU7 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
103SSSGEWYKRGVKENSubiquitination[1]
107EWYKRGVKENSIITKubiquitination[1]
166LMFDYDGKRDRWNGYubiquitination[1, 2, 3]
180YNPEEHMKIVEEYAKubiquitination[4]
187KIVEEYAKVDLAKRTubiquitination[4]
199KRTLKAQKLQEELASubiquitination[1, 3]
273RIREDIAKYLRNLDPubiquitination[1]
288NSAYYDPKTRAMRENubiquitination[1, 2, 3]
302NPYANAGKNPDEVSYacetylation[3]
302NPYANAGKNPDEVSYubiquitination[1, 3, 4, 5, 6]
349HLQADPTKLELLYKSubiquitination[3]
355TKLELLYKSFKVKKEubiquitination[7, 8]
369EDFKEQQKESILEKYubiquitination[1]
526EKKHEKLKKALNAEEubiquitination[2]
527KKHEKLKKALNAEEAubiquitination[2]
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] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'- splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation. 
Sequence Annotation
 ZN_FING 118 135 CCHC-type.
 MOTIF 129 169 Bipartite nuclear localization signal.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 215 215 Phosphoserine.
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 235 235 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Spliceosome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 586 AA 
Protein Sequence
MSATVVDAVN AAPLSGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA EVDEEGKDIN 60
PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE WYKRGVKENS IITKYRKGAC 120
ENCGAMTHKK KDCFERPRRV GAKFTGTNIA PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK 180
IVEEYAKVDL AKRTLKAQKL QEELASGKLV EQANSPKHQW GEEEPNSQME KDHNSEDEDE 240
DKYADDIDMP GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA 300
GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL ELLYKSFKVK 360
KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY SRHGTVIKGQ ERAVACSKYE 420
EDVKIHNHTH IWGSYWKEGR WGYKCCHSFF KYSYCTGEAG KEIVNSEECI INEITGEESV 480
KKPQTLMELH QEKLKEEKKK KKKKKKKHRK SSSDSDDEEK KHEKLKKALN AEEARLLHVK 540
ETMQIDERKR PYNSMYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ 586 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; IDA:HGNC.
 GO:0030532; C:small nuclear ribonucleoprotein complex; IDA:HGNC.
 GO:0030628; F:pre-mRNA 3'-splice site binding; IDA:HGNC.
 GO:0000386; F:second spliceosomal transesterification activity; IDA:HGNC.
 GO:0008270; F:zinc ion binding; IDA:HGNC.
 GO:0000380; P:alternative mRNA splicing, via spliceosome; IDA:HGNC.
 GO:0033554; P:cellular response to stress; IDA:UniProtKB.
 GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
 GO:0000389; P:mRNA 3'-splice site recognition; IDA:HGNC. 
Interpro
 IPR021715; Slu7.
 IPR001878; Znf_CCHC. 
Pfam
 PF11708; Slu7 
SMART
 SM00343; ZnF_C2HC 
PROSITE
 PS50158; ZF_CCHC 
PRINTS