CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000557
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cleavage and polyadenylation specificity factor subunit 2 
Protein Synonyms/Alias
 Cleavage and polyadenylation specificity factor 100 kDa subunit; CPSF 100 kDa subunit 
Gene Name
 Cpsf2 
Gene Synonyms/Alias
 Cpsf100; Mcpsf 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
138FSQIVNLKGKGHGLSubiquitination[1]
680MAQQKAMKSLFGEDEacetylation[2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Involved in the histone 3' end pre-mRNA processing (By similarity). 
Sequence Annotation
 MOD_RES 412 412 Phosphoserine.
 MOD_RES 419 419 Phosphoserine.
 MOD_RES 420 420 Phosphoserine.
 MOD_RES 423 423 Phosphoserine.
 MOD_RES 660 660 Phosphoserine (By similarity).  
Keyword
 Complete proteome; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 782 AA 
Protein Sequence
MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SVDIIDSLRK HVHQIDAVLL 60
SHPDPLHLGA LPFAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD 120
AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR 180
EIHLNGCSLE MLSRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA 240
GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN 300
NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK NSIILTYRTT 360
PGTLARFLID NPTEKVTEIE LRKRVKLEGK ELEEYVEKEK LKKEAAKKLE QSKEADIDSS 420
DESDVEEDVD QPSAHKTKHD LMMKGEGSRK GSFFKQAKKS YPMFPAPEER IKWDEYGEII 480
KPEDFLVPEL QATEEEKSKL ESGLTNGEEP MDQDLSDVPT KCVSATESIE IKARVTYIDY 540
EGRSDGDSIK KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT 600
SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE GELKDDGEDS 660
EMQVDAPSDS SAMAQQKAMK SLFGEDEKEL GEETEIIPTL EPLPPHEVPG HQSVFMNEPR 720
LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV RRTETGRIGL EGCLCQDFYR IRDLLYEQYA 780
IV 782 
Gene Ontology
 GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB.
 GO:0016787; F:hydrolase activity; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006398; P:histone mRNA 3'-end processing; ISS:UniProtKB.
 GO:0006379; P:mRNA cleavage; IEA:InterPro.
 GO:0006378; P:mRNA polyadenylation; IEA:InterPro. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR022712; Beta_Casp.
 IPR027075; CPSF2.
 IPR025069; Cpsf2_C.
 IPR011108; RMMBL. 
Pfam
 PF10996; Beta-Casp
 PF13299; CPSF100_C
 PF00753; Lactamase_B
 PF07521; RMMBL 
SMART
 SM01027; Beta-Casp
 SM00849; Lactamase_B 
PROSITE
  
PRINTS