CPSF6
entrez
11052
canonical
uniprot
Q16630
canonical
ensembl
ENSG00000111605
resolver
ensp
ENSP00000266679
resolver
ensp
ENSP00000391774
resolver
ensp
ENSP00000556716
resolver
ensp
ENSP00000556717
resolver
ensp
ENSP00000611518
resolver
genesymbol
CPSF6
resolver
genesymbol_syn
CFIM68
resolver
hgnc
HGNC:13871
resolver
uniprot
A8K7K9
resolver
uniprot
Q53ES1
resolver
uniprot
Q9BSJ7
resolver
uniprot
Q9BW18
resolver
uniprot_entry
CPSF6_HUMAN
resolver
uniprot_sec
A8K7K9
resolver
uniprot_sec
Q53ES1
resolver
uniprot_sec
Q9BSJ7
resolver
uniprot_sec
Q9BW18
resolver
amino_acid_sequence
MADGVDHIDIYADVGEEFNQEAEYGGHDQIDLYDDVISPSANNGDAPEDRDYMDTLPPTVGDDVGKGAAPNVVYTYTGKRIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPCNKQFLSQFEMQSRKTTQSGQMSGEGKAGPPGGSSRAAFPQGGRGRGRFPGAVPGGDRFPGPAGPGGPPPPFPAGQTPPRPPLGPPGPPGPPGPPPPGQVLPPPLAGPPNRGDRPPPPVLFPGQPFGQPPLGPLPPGPPPPVPGYGPPPGPPPPQQGPPPPPGPFPPRPPGPLGPPLTLAPPPHLPGPPPGAPPPAPHVNPAFFPPPTNSGMPTSDSRGPPPTDPYGRPPPYDRGDYGPPGREMDTARTPLSEAEFEEIMNRNRAISSSAISRAVSDASAGDYGSAIETLVTAISLIKQSKVSADDRCKVLISSLQDCLHGIESKSYGSGSRRERSRERDHSRSREKSRRHKSRSRDRHDDYYRERSRERERHRDRDRDRDRERDREREYRHR
uniprot
proteins
function
FUNCTION: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:14690600, PubMed:29276085, PubMed:8626397, PubMed:9659921). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:14690600, PubMed:8626397, PubMed:9659921). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:20695905, PubMed:29276085). CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery (PubMed:15169763, PubMed:21295486, PubMed:29276085). Plays a role in mRNA export (PubMed:19864460). {ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:23187700, ECO:0000269|PubMed:29276085, ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.; FUNCTION: (Microbial infection) Binds HIV-1 capsid-nucleocapsid (HIV-1 CA-NC) complexes and might thereby promote the integration of the virus in the nucleus of dividing cells (in vitro). {ECO:0000269|PubMed:24130490}.
uniprot
proteins
mass_dalton
59210
uniprot
proteins
mutagenesis
MUTAGEN 84; /note="Y->A: Reduces affinity for UGUARNA by 40%; when associated with A-128."; /evidence="ECO:0000269|PubMed:21295486"; MUTAGEN 86; /note="G->V: Abolishes interaction with NUDT21/CPSF5; when associated with V-87."; /evidence="ECO:0000269|PubMed:15169763"; MUTAGEN 87; /note="N->V: Abolishes interaction with NUDT21/CPSF5; when associated with V-86."; /evidence="ECO:0000269|PubMed:15169763"; MUTAGEN 90..91; /note="WW->AA: Reduces affinity for UGUARNA by 70%. Strongly reduced affinity for UGUARNA; when associated with A-94."; /evidence="ECO:0000269|PubMed:21295486"; MUTAGEN 94; /note="D->A: Strongly reduced affinity for UGUARNA; when associated with 90-A-A-91."; /evidence="ECO:0000269|PubMed:21295486"; MUTAGEN 111; /note="E->A: Reduces affinity for UGUARNA by 85%."; /evidence="ECO:0000269|PubMed:21295486"; MUTAGEN 126; /note="F->A: Increases affinity for UGUARNA by 40%."; /evidence="ECO:0000269|PubMed:21295486"; MUTAGEN 128; /note="L->A: Reduces affinity for UGUARNA by 40%; when associated with A-84."; /evidence="ECO:0000269|PubMed:21295486"; MUTAGEN 202; /note="R->A: Decreased methylation in presence of PRMT5/WDR77. Loss of methylation in presence of PRMT5/WDR77 or PRMT1; when associated with A-204 and A-206."; /evidence="ECO:0000269|PubMed:20562214"; MUTAGEN 204; /note="R->A: Decreased methylation in presence of PRMT5/WDR77. Loss of methylation in presence of PRMT5/WDR77 or PRMT1; when associated with A-202 and A-206."; /evidence="ECO:0000269|PubMed:20562214"; MUTAGEN 206; /note="R->A: Loss of methylation in presence of PRMT5/WDR77 or PRMT1."; /evidence="ECO:0000269|PubMed:20562214
uniprot
proteins
post_translational_modification
PTM: Phosphorylated (PubMed:29276085). Phosphorylated in the Arg/Ser-rich domain by SRPK1, in vitro (PubMed:29276085). {ECO:0000269|PubMed:29276085}.; PTM: Symmetrically dimethylated on arginine residues in the GAR motif by PRMT5 in a WDR77- and CLNS1A-dependent manner (PubMed:20562214). Asymmetrically dimethylated on arginine residues in the GAR motif by PRMT1 (PubMed:20562214). {ECO:0000269|PubMed:20562214}.
uniprot
proteins
protein_family
RRM CPSF6/7 family
uniprot
proteins
pubmed
14561889
uniprot
proteins
pubmed
14690600
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15169763
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17267687
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19864460
uniprot
proteins
pubmed
20562214
uniprot
proteins
pubmed
20695905
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21295486
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23187700
uniprot
proteins
pubmed
24130490
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29276085
uniprot
proteins
pubmed
29507755
uniprot
proteins
pubmed
29997211
uniprot
proteins
pubmed
30916345
uniprot
proteins
pubmed
8626397
uniprot
proteins
pubmed
9659921
uniprot
proteins
sequence_length
551
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:30916345, ECO:0000269|PubMed:9659921}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17267687}. Nucleus speckle {ECO:0000269|PubMed:17267687}. Cytoplasm {ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:30916345}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460). Colocalizes with PSPC1 in punctate subnuclear structures often located adjacent to nuclear speckles, called paraspeckles, and corresponding to interchromatin granules-associated zones (IGAZs) (PubMed:17267687). Distribution in speckles and paraspeckles varies during the cell cycle (PubMed:17267687). Associates at sites of active transcription on nascent perichromatin fibrils (PFs) and perichromatin granules (PubMed:17267687). Nuclear import is mediated via interaction with TNPO3 independently of CPSF6 phosphorylation status (PubMed:30916345). {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:17267687, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:30916345}.
uniprot
proteins