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Protein

Cleavage and polyadenylation specificity factor subunit 1

Gene

CPSF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays 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. This subunit is involved in the RNA recognition step of the polyadenylation reaction.1 Publication

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • mRNA 3'-UTR AU-rich region binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-6784531. tRNA processing in the nucleus.
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 1
Alternative name(s):
Cleavage and polyadenylation specificity factor 160 kDa subunit
Short name:
CPSF 160 kDa subunit
Gene namesi
Name:CPSF1
Synonyms:CPSF160
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2324. CPSF1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26841.

Polymorphism and mutation databases

BioMutaiCPSF1.
DMDMi23503048.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14431443Cleavage and polyadenylation specificity factor subunit 1PRO_0000074387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei756 – 7561PhosphoserineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ10570.
MaxQBiQ10570.
PaxDbiQ10570.
PeptideAtlasiQ10570.
PRIDEiQ10570.

PTM databases

iPTMnetiQ10570.
PhosphoSiteiQ10570.
SwissPalmiQ10570.

Expressioni

Gene expression databases

BgeeiQ10570.
CleanExiHS_CPSF1.
ExpressionAtlasiQ10570. baseline and differential.
GenevisibleiQ10570. HS.

Interactioni

Subunit structurei

Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with FIP1L1, PAPD4/GLD2 and SRRM1. Interacts with TUT1; the interaction is direct and mediates the recruitment of the CPSF complex on the 3'UTR of selected pre-mRNAs.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NPM1P067482EBI-347859,EBI-78579
RELQ048643EBI-347859,EBI-307352

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi118946. 57 interactions.
DIPiDIP-32694N.
IntActiQ10570. 19 interactions.
MINTiMINT-1601544.
STRINGi9606.ENSP00000339353.

Structurei

3D structure databases

ProteinModelPortaliQ10570.
SMRiQ10570. Positions 499-629, 1120-1439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi893 – 90816Nuclear localization signalSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the CPSF1 family.Curated

Phylogenomic databases

eggNOGiKOG1896. Eukaryota.
COG5161. LUCA.
GeneTreeiENSGT00550000075040.
HOGENOMiHOG000007904.
HOVERGENiHBG051105.
InParanoidiQ10570.
KOiK14401.
OMAiEIHTITI.
PhylomeDBiQ10570.
TreeFamiTF314322.

Family and domain databases

InterProiIPR004871. Cleavage/polyA-sp_fac_asu_C.
[Graphical view]
PfamiPF03178. CPSF_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10570-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYAVYKQAHP PTGLEFSMYC NFFNNSERNL VVAGTSQLYV YRLNRDAEAL
60 70 80 90 100
TKNDRSTEGK AHREKLELAA SFSFFGNVMS MASVQLAGAK RDALLLSFKD
110 120 130 140 150
AKLSVVEYDP GTHDLKTLSL HYFEEPELRD GFVQNVHTPR VRVDPDGRCA
160 170 180 190 200
AMLVYGTRLV VLPFRRESLA EEHEGLVGEG QRSSFLPSYI IDVRALDEKL
210 220 230 240 250
LNIIDLQFLH GYYEPTLLIL FEPNQTWPGR VAVRQDTCSI VAISLNITQK
260 270 280 290 300
VHPVIWSLTS LPFDCTQALA VPKPIGGVVV FAVNSLLYLN QSVPPYGVAL
310 320 330 340 350
NSLTTGTTAF PLRTQEGVRI TLDCAQATFI SYDKMVISLK GGEIYVLTLI
360 370 380 390 400
TDGMRSVRAF HFDKAAASVL TTSMVTMEPG YLFLGSRLGN SLLLKYTEKL
410 420 430 440 450
QEPPASAVRE AADKEEPPSK KKRVDATAGW SAAGKSVPQD EVDEIEVYGS
460 470 480 490 500
EAQSGTQLAT YSFEVCDSIL NIGPCANAAV GEPAFLSEEF QNSPEPDLEI
510 520 530 540 550
VVCSGHGKNG ALSVLQKSIR PQVVTTFELP GCYDMWTVIA PVRKEEEDNP
560 570 580 590 600
KGEGTEQEPS TTPEADDDGR RHGFLILSRE DSTMILQTGQ EIMELDTSGF
610 620 630 640 650
ATQGPTVFAG NIGDNRYIVQ VSPLGIRLLE GVNQLHFIPV DLGAPIVQCA
660 670 680 690 700
VADPYVVIMS AEGHVTMFLL KSDSYGGRHH RLALHKPPLH HQSKVITLCL
710 720 730 740 750
YRDLSGMFTT ESRLGGARDE LGGRSGPEAE GLGSETSPTV DDEEEMLYGD
760 770 780 790 800
SGSLFSPSKE EARRSSQPPA DRDPAPFRAE PTHWCLLVRE NGTMEIYQLP
810 820 830 840 850
DWRLVFLVKN FPVGQRVLVD SSFGQPTTQG EARREEATRQ GELPLVKEVL
860 870 880 890 900
LVALGSRQSR PYLLVHVDQE LLIYEAFPHD SQLGQGNLKV RFKKVPHNIN
910 920 930 940 950
FREKKPKPSK KKAEGGGAEE GAGARGRVAR FRYFEDIYGY SGVFICGPSP
960 970 980 990 1000
HWLLVTGRGA LRLHPMAIDG PVDSFAPFHN VNCPRGFLYF NRQGELRISV
1010 1020 1030 1040 1050
LPAYLSYDAP WPVRKIPLRC TAHYVAYHVE SKVYAVATST NTPCARIPRM
1060 1070 1080 1090 1100
TGEEKEFETI ERDERYIHPQ QEAFSIQLIS PVSWEAIPNA RIELQEWEHV
1110 1120 1130 1140 1150
TCMKTVSLRS EETVSGLKGY VAAGTCLMQG EEVTCRGRIL IMDVIEVVPE
1160 1170 1180 1190 1200
PGQPLTKNKF KVLYEKEQKG PVTALCHCNG HLVSAIGQKI FLWSLRASEL
1210 1220 1230 1240 1250
TGMAFIDTQL YIHQMISVKN FILAADVMKS ISLLRYQEES KTLSLVSRDA
1260 1270 1280 1290 1300
KPLEVYSVDF MVDNAQLGFL VSDRDRNLMV YMYLPEAKES FGGMRLLRRA
1310 1320 1330 1340 1350
DFHVGAHVNT FWRTPCRGAT EGLSKKSVVW ENKHITWFAT LDGGIGLLLP
1360 1370 1380 1390 1400
MQEKTYRRLL MLQNALTTML PHHAGLNPRA FRMLHVDRRT LQNAVRNVLD
1410 1420 1430 1440
GELLNRYLYL STMERSELAK KIGTTPDIIL DDLLETDRVT AHF
Length:1,443
Mass (Da):160,884
Last modified:September 19, 2002 - v2
Checksum:i7E1DF4D8A93487A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121T → P in AAC50293 (PubMed:7590244).Curated
Sequence conflicti1318 – 13181Missing in AAC50293 (PubMed:7590244).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37012 mRNA. Translation: AAC50293.1.
BC017232 mRNA. Translation: AAH17232.1.
CCDSiCCDS34966.1.
RefSeqiNP_037423.2. NM_013291.2.
UniGeneiHs.493202.

Genome annotation databases

EnsembliENST00000616140; ENSP00000484669; ENSG00000071894.
ENST00000620219; ENSP00000478145; ENSG00000071894.
GeneIDi29894.
KEGGihsa:29894.
UCSCiuc003zcj.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37012 mRNA. Translation: AAC50293.1.
BC017232 mRNA. Translation: AAH17232.1.
CCDSiCCDS34966.1.
RefSeqiNP_037423.2. NM_013291.2.
UniGeneiHs.493202.

3D structure databases

ProteinModelPortaliQ10570.
SMRiQ10570. Positions 499-629, 1120-1439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118946. 57 interactions.
DIPiDIP-32694N.
IntActiQ10570. 19 interactions.
MINTiMINT-1601544.
STRINGi9606.ENSP00000339353.

PTM databases

iPTMnetiQ10570.
PhosphoSiteiQ10570.
SwissPalmiQ10570.

Polymorphism and mutation databases

BioMutaiCPSF1.
DMDMi23503048.

Proteomic databases

EPDiQ10570.
MaxQBiQ10570.
PaxDbiQ10570.
PeptideAtlasiQ10570.
PRIDEiQ10570.

Protocols and materials databases

DNASUi29894.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000616140; ENSP00000484669; ENSG00000071894.
ENST00000620219; ENSP00000478145; ENSG00000071894.
GeneIDi29894.
KEGGihsa:29894.
UCSCiuc003zcj.3. human.

Organism-specific databases

CTDi29894.
GeneCardsiCPSF1.
HGNCiHGNC:2324. CPSF1.
MIMi606027. gene.
neXtProtiNX_Q10570.
PharmGKBiPA26841.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1896. Eukaryota.
COG5161. LUCA.
GeneTreeiENSGT00550000075040.
HOGENOMiHOG000007904.
HOVERGENiHBG051105.
InParanoidiQ10570.
KOiK14401.
OMAiEIHTITI.
PhylomeDBiQ10570.
TreeFamiTF314322.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-6784531. tRNA processing in the nucleus.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-77595. Processing of Intronless Pre-mRNAs.

Miscellaneous databases

ChiTaRSiCPSF1. human.
GeneWikiiCPSF1.
GenomeRNAii29894.
NextBioi52452.
PROiQ10570.
SOURCEiSearch...

Gene expression databases

BgeeiQ10570.
CleanExiHS_CPSF1.
ExpressionAtlasiQ10570. baseline and differential.
GenevisibleiQ10570. HS.

Family and domain databases

InterProiIPR004871. Cleavage/polyA-sp_fac_asu_C.
[Graphical view]
PfamiPF03178. CPSF_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3'-end formation."
    Murthy K.G., Manley J.L.
    Genes Dev. 9:2672-2683(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  3. "SRm160 splicing coactivator promotes transcript 3'-end cleavage."
    McCracken S., Lambermon M., Blencowe B.J.
    Mol. Cell. Biol. 22:148-160(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRRM1.
  4. "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase."
    Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.
    EMBO J. 23:616-626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRE-MRNA 3'-END PROCESSING, IDENTIFICATION IN THE CPSF COMPLEX, IDENTIFICATION IN A COMPLEX WITH FIP1L1 AND PAPOLA, INTERACTION WITH FIP1L1.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
    Laishram R.S., Anderson R.A.
    EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CPSF COMPLEX, INTERACTION WITH TUT1.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCPSF1_HUMAN
AccessioniPrimary (citable) accession number: Q10570
Secondary accession number(s): Q96AF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 19, 2002
Last modified: May 11, 2016
This is version 145 of the entry and version 2 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.