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Protein

Cleavage and polyadenylation specificity factor subunit 7

Gene

CPSF7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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:8626397, PubMed:17024186, PubMed:29276085). 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:8626397, PubMed:17024186). 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). CPSF7 activates directly the mRNA 3'-processing machinery (PubMed:29276085). Binds to pA signals in RNA substrates (PubMed:8626397, PubMed:17024186).5 Publications

GO - Molecular functioni

GO - Biological processi

  • messenger ribonucleoprotein complex assembly Source: UniProtKB
  • mRNA 3'-end processing Source: Reactome
  • mRNA alternative polyadenylation Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • pre-mRNA cleavage required for polyadenylation Source: UniProtKB
  • protein heterotetramerization Source: UniProtKB
  • protein tetramerization Source: UniProtKB
  • termination of RNA polymerase II transcription Source: Reactome

Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing

Enzyme and pathway databases

ReactomeiR-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-77595 Processing of Intronless Pre-mRNAs

Names & Taxonomyi

Protein namesi
Recommended name:
Cleavage and polyadenylation specificity factor subunit 7Curated
Alternative name(s):
Cleavage and polyadenylation specificity factor 59 kDa subunit
Short name:
CPSF 59 kDa subunit
Cleavage factor Im complex 59 kDa subunit1 Publication
Short name:
CFIm591 Publication
Pre-mRNA cleavage factor Im 59 kDa subunit
Gene namesi
Name:CPSF7Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000149532.15
HGNCiHGNC:30098 CPSF7
neXtProtiNX_Q8N684

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi79869
OpenTargetsiENSG00000149532
PharmGKBiPA165543380

Polymorphism and mutation databases

BioMutaiCPSF7
DMDMi74759932

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000815271 – 471Cleavage and polyadenylation specificity factor subunit 7Add BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei203PhosphothreonineCombined sources1
Modified residuei205PhosphoserineBy similarity1
Cross-linki354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei413PhosphoserineCombined sources1
Modified residuei423PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated (PubMed:29276085).1 Publication
Asymmetrically dimethylated on arginine residues by PRMT1 (PubMed:20562214).1 Publication

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8N684
MaxQBiQ8N684
PaxDbiQ8N684
PeptideAtlasiQ8N684
PRIDEiQ8N684
ProteomicsDBi72138
72139 [Q8N684-2]
72140 [Q8N684-3]

PTM databases

iPTMnetiQ8N684
PhosphoSitePlusiQ8N684
SwissPalmiQ8N684

Miscellaneous databases

PMAP-CutDBiQ8N684

Expressioni

Gene expression databases

BgeeiENSG00000149532
ExpressionAtlasiQ8N684 baseline and differential
GenevisibleiQ8N684 HS

Organism-specific databases

HPAiHPA041094

Interactioni

Subunit structurei

Component of the cleavage factor Im (CFIm) complex which is an heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or an heterodimer of CPSF6 and CPSF7 (PubMed:8626397, PubMed:20695905, PubMed:23187700, Ref. 22). The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery (PubMed:29276085). Interacts with NUDT21/CPSF5 (PubMed:29276085). Interacts (via Arg/Ser-rich domain) with FIP1L1 (preferentially via unphosphorylated form and Arg/Glu/Asp-rich region); this interaction mediates, at least in part, the interaction between the CFIm and CPSF complexes and may be inhibited by CPSF7 hyper-phosphorylation (PubMed:29276085).5 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi122957, 105 interactors
CORUMiQ8N684
IntActiQ8N684, 60 interactors
MINTiQ8N684
STRINGi9606.ENSP00000345412

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi83 – 87Combined sources5
Helixi95 – 104Combined sources10
Beta strandi110 – 117Combined sources8
Turni119 – 121Combined sources3
Beta strandi124 – 133Combined sources10
Helixi135 – 144Combined sources10
Beta strandi156 – 159Combined sources4
Helixi162 – 176Combined sources15

3D structure databases

ProteinModelPortaliQ8N684
SMRiQ8N684
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N684

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 162RRMPROSITE-ProRule annotationAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni418 – 469Arg/Ser-rich domain1 PublicationAdd BLAST52

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi51 – 54Poly-Pro4
Compositional biasi218 – 329Pro-richAdd BLAST112
Compositional biasi418 – 469Arg-richAdd BLAST52

Domaini

Contains an Arg/Ser-rich domain composed of arginine-serine dipeptide repeats within the C-terminal region that is necessary and sufficient for activating mRNA 3'-processing (PubMed:29276085).1 Publication

Sequence similaritiesi

Belongs to the RRM CPSF6/7 family.Curated

Phylogenomic databases

eggNOGiKOG4849 Eukaryota
ENOG4111NBM LUCA
GeneTreeiENSGT00730000110905
HOGENOMiHOG000111137
HOVERGENiHBG056699
InParanoidiQ8N684
KOiK14398
OMAiEDRHDDY
OrthoDBiEOG091G0CVC
PhylomeDBiQ8N684
TreeFamiTF316430

Family and domain databases

CDDicd12644 RRM_CFIm59, 1 hit
Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR034772 CPSF6/7
IPR034770 CPSF7
IPR034773 CPSF7_RRM
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PANTHERiPTHR23204 PTHR23204, 1 hit
PTHR23204:SF2 PTHR23204:SF2, 1 hit
PfamiView protein in Pfam
PF00076 RRM_1, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 1 hit
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N684-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSEGVDLIDI YADEEFNQDP EFNNTDQIDL YDDVLTATSQ PSDDRSSSTE
60 70 80 90 100
PPPPVRQEPS PKPNNKTPAI LYTYSGLRNR RAAVYVGSFS WWTTDQQLIQ
110 120 130 140 150
VIRSIGVYDV VELKFAENRA NGQSKGYAEV VVASENSVHK LLELLPGKVL
160 170 180 190 200
NGEKVDVRPA TRQNLSQFEA QARKRECVRV PRGGIPPRAH SRDSSDSADG
210 220 230 240 250
RATPSENLVP SSARVDKPPS VLPYFNRPPS ALPLMGLPPP PIPPPPPLSS
260 270 280 290 300
SFGVPPPPPG IHYQHLMPPP PRLPPHLAVP PPGAIPPALH LNPAFFPPPN
310 320 330 340 350
ATVGPPPDTY MKASAPYNHH GSRDSGPPPS TVSEAEFEDI MKRNRAISSS
360 370 380 390 400
AISKAVSGAS AGDYSDAIET LLTAIAVIKQ SRVANDERCR VLISSLKDCL
410 420 430 440 450
HGIEAKSYSV GASGSSSRKR HRSRERSPSR SRESSRRHRD LLHNEDRHDD
460 470
YFQERNREHE RHRDRERDRH H
Length:471
Mass (Da):52,050
Last modified:October 1, 2002 - v1
Checksum:i69529E441D742CF9
GO
Isoform 2 (identifier: Q8N684-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     176-184: Missing.

Show »
Length:462
Mass (Da):51,096
Checksum:iA3E41F7CB8340247
GO
Isoform 3 (identifier: Q8N684-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGRPESAGGGSRGPFEGGGRARRAGGIFLTLSILRTRDLPSGAM

Show »
Length:514
Mass (Da):56,375
Checksum:i37D5BE0605F7A0FB
GO

Sequence cautioni

The sequence AAH18135 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14118 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAD97884 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti335A → V in CAD97884 (PubMed:17974005).Curated1
Sequence conflicti353S → F in CAD97884 (PubMed:17974005).Curated1
Sequence conflicti387E → D in BAB14118 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0389751M → MGRPESAGGGSRGPFEGGGR ARRAGGIFLTLSILRTRDLP SGAM in isoform 3. Curated1
Alternative sequenceiVSP_017194176 – 184Missing in isoform 2. 1 Publication9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ275970 mRNA Translation: CAC81661.1
AK022591 mRNA Translation: BAB14118.1 Different initiation.
AK096343 mRNA Translation: BAG53266.1
AL512759 mRNA Translation: CAC21678.1
BX537888 mRNA Translation: CAD97884.1 Different initiation.
AP003108 Genomic DNA No translation available.
BC018135 mRNA Translation: AAH18135.1 Different initiation.
CCDSiCCDS44619.1 [Q8N684-1]
CCDS44620.1 [Q8N684-2]
CCDS8006.2 [Q8N684-3]
RefSeqiNP_001129512.1, NM_001136040.2 [Q8N684-1]
NP_001136037.1, NM_001142565.1 [Q8N684-2]
NP_079087.3, NM_024811.3 [Q8N684-3]
XP_005274356.1, XM_005274299.4 [Q8N684-1]
XP_011543560.1, XM_011545258.2 [Q8N684-1]
XP_011543561.1, XM_011545259.2 [Q8N684-2]
UniGeneiHs.718984

Genome annotation databases

EnsembliENST00000340437; ENSP00000345412; ENSG00000149532 [Q8N684-3]
ENST00000394888; ENSP00000378352; ENSG00000149532 [Q8N684-1]
ENST00000439958; ENSP00000397203; ENSG00000149532 [Q8N684-2]
ENST00000448745; ENSP00000407394; ENSG00000149532 [Q8N684-2]
GeneIDi79869
KEGGihsa:79869
UCSCiuc001nrp.4 human [Q8N684-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiCPSF7_HUMAN
AccessioniPrimary (citable) accession number: Q8N684
Secondary accession number(s): B3KU04
, C9K0Q4, Q7Z3H9, Q9H025, Q9H9V1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 1, 2002
Last modified: July 18, 2018
This is version 155 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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