Tag | Content |
---|
CPLM ID | CPLM-022619 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cleavage and polyadenylation specificity factor subunit 3 |
Protein Synonyms/Alias | Cleavage and polyadenylation specificity factor 73 kDa subunit; CPSF 73 kDa subunit; mRNA 3'-end-processing endonuclease CPSF-73 |
Gene Name | Cpsf3 |
Gene Synonyms/Alias | Cpsf73 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
---|
295 | AMNDKIRKQININNP | ubiquitination | [1] | 348 | FESWCTDKRNGVIIA | ubiquitination | [1] | 381 | ITTMSGQKLPLKMSV | ubiquitination | [1] | 487 | RVSGILVKRNFNYHI | ubiquitination | [1] | 545 | EELEIQEKPALKVFK | ubiquitination | [1] |
|
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] |
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. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP- dependent protein that induces both the 3' endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. |
Sequence Annotation | ACT_SITE 396 396 Proton donor (Potential). METAL 71 71 Zinc 1 (By similarity). METAL 73 73 Zinc 1 (By similarity). METAL 75 75 Zinc 2 (By similarity). METAL 76 76 Zinc 2 (By similarity). METAL 158 158 Zinc 1 (By similarity). METAL 179 179 Zinc 1 (By similarity). METAL 179 179 Zinc 2 (By similarity). METAL 418 418 Zinc 2 (By similarity). MOD_RES 2 2 N-acetylserine (By similarity). MOD_RES 681 681 Phosphothreonine (By similarity). CROSSLNK 462 462 Glycyl lysine isopeptide (Lys-Gly) CROSSLNK 465 465 Glycyl lysine isopeptide (Lys-Gly) CROSSLNK 545 545 Glycyl lysine isopeptide (Lys-Gly) |
Keyword | Acetylation; Complete proteome; Endonuclease; Hydrolase; Isopeptide bond; Metal-binding; mRNA processing; Nuclease; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding; Ubl conjugation; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 684 AA |
Protein Sequence | MSAIPAEESD QLLIRPLGAG QEVGRSCIIL EFKGRKIMLD CGIHPGLEGM DALPYIDLID 60 PAEIDLLLIS HFHLDHCGAL PWFLQKTSFK GRTFMTHATK AIYRWLLSDY VKVSNISADD 120 MLYTETDLEE SMDKIETINF HEVKEVAGIK FWCYHAGHVL GAAMFMIEIA GVKLLYTGDF 180 SRQEDRHLMA AEIPNIKPDI LIIESTYGTH IHEKREEREA RFCNTVHDIV NRGGRGLIPV 240 FALGRAQELL LILDEYWQNH PELHDIPIYY ASSLAKKCMA VYQTYVNAMN DKIRKQININ 300 NPFVFKHISN LKSMDHFDDI GPSVVMASPG MIQNGLSREL FESWCTDKRN GVIIAGYCVE 360 GTLAKHIMSE PEEITTMSGQ KLPLKMSVDY ISFSAHTDYQ QTSEFIRALK PPHVILVHGE 420 QNEMARLKAA LIREYEDNDE VHIEVHNPRN TEAVTLNFRG EKLAKVMGFL ADKKPEQGQR 480 VSGILVKRNF NYHILSPCDL SNYTDLAMST VKQTQAIPYT GPFYLLYYQL QKLTGDVEEL 540 EIQEKPALKV FKSITVVQEP GMVVLEWLAN PSNDMYADTV TTVILEVQSN PKIRKGAVQK 600 VSKKLEMHVY SKRLEVMLQD IFGEDCVSVK DDSVLSVTVD GKTANINLET RAVECEEGSE 660 DDESLREMVE LAAQRLYEAL TPVH 684 |
Gene Ontology | GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:UniProtKB. GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW. GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB. GO:0004521; F:endoribonuclease activity; IDA:UniProtKB. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0003723; F:RNA binding; IDA:UniProtKB. GO:0006398; P:histone mRNA 3'-end processing; IDA:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |