CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-042004
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cleavage and polyadenylation specific factor 3, 73kDa, isoform CRA_b 
Protein Synonyms/Alias
 Cleavage and polyadenylation-specificity factor subunit 3 
Gene Name
 CPSF3 
Gene Synonyms/Alias
 hCG_1784298 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
240YASSLAKKCMAVYQTubiquitination[1]
255YVNAMNDKIRKQINIubiquitination[1]
258AMNDKIRKQININNPubiquitination[1, 2, 3, 4]
269INNPFVFKHISNLKSubiquitination[1, 2, 4]
275FKHISNLKSMDHFDDubiquitination[1, 5]
311FESWCTDKRNGVIIAubiquitination[1, 4]
344ITTMSGQKLPLKMSVubiquitination[1, 3, 5, 6]
373SEFIRALKPPHVILVubiquitination[1]
391QNEMARLKAALIREYubiquitination[1, 3, 4, 5, 6]
425TLNFRGEKLAKVMGFubiquitination[1]
428FRGEKLAKVMGFLADubiquitination[1]
436VMGFLADKKPEQGQRubiquitination[2, 4, 5, 7]
437MGFLADKKPEQGQRVubiquitination[1, 2, 3, 4]
450RVSGILVKRNFNYHIubiquitination[1, 2, 3, 4, 7]
508EELEIQEKPALKVFKubiquitination[1, 3, 5, 6]
512IQEKPALKVFKNITVubiquitination[1, 5]
515KPALKVFKNITVIQEubiquitination[1]
567AVQKVSKKLEMHVYSubiquitination[1, 4]
575LEMHVYSKRLEIMLQubiquitination[1]
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] 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]
 [3] 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]
 [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]
 [5] 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]
 [6] 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]
 [7] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 647 AA 
Protein Sequence
MLDCGIHPGL EGMDALPYID LIDPAEIDLL LISHFHLDHC GALPWFLQKT SFKGRTFMTH 60
ATKAIYRWLL SDYVKVSNIS ADDMLYTETD LEESMDKIET INFHEVKEVA GIKFWCYHAG 120
HVLGAAMFMI EIAGVKLLYT GDFSRQEDRH LMAAEIPNIK PDILIIESTY GTHIHEKREE 180
REARFCNTVH DIVNRGGRGL IPVFALGRAQ ELLLILDEYW QNHPELHDIP IYYASSLAKK 240
CMAVYQTYVN AMNDKIRKQI NINNPFVFKH ISNLKSMDHF DDIGPSVVMA SPGMMQSGLS 300
RELFESWCTD KRNGVIIAGY CVEGTLAKHI MSEPEEITTM SGQKLPLKMS VDYISFSAHT 360
DYQQTSEFIR ALKPPHVILV HGEQNEMARL KAALIREYED NDEVHIEVHN PRNTEAVTLN 420
FRGEKLAKVM GFLADKKPEQ GQRVSGILVK RNFNYHILSP CDLSNYTDLA MSTVKQTQAI 480
PYTGPFNLLC YQLQKLTGDV EELEIQEKPA LKVFKNITVI QEPGMVVLEW LANPSNDMYA 540
DTVTTVILEV QSNPKIRKGA VQKVSKKLEM HVYSKRLEIM LQDIFGEDCV SVKDDSILSV 600
TVDGKTANLN LETRTVECEE GSEDDESLRE MVELAAQRLY EALTPVH 647 
Gene Ontology
 GO:0008409; F:5'-3' exonuclease activity; IEA:Compara.
 GO:0004521; F:endoribonuclease activity; IEA:Compara.
 GO:0003723; F:RNA binding; IEA:Compara. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR022712; Beta_Casp.
 IPR021718; CPSF73-100_C.
 IPR011108; RMMBL. 
Pfam
 PF10996; Beta-Casp
 PF11718; CPSF73-100_C
 PF00753; Lactamase_B
 PF07521; RMMBL 
SMART
 SM01027; Beta-Casp
 SM01098; CPSF73-100_C
 SM00849; Lactamase_B 
PROSITE
  
PRINTS