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Q9UKF6

- CPSF3_HUMAN

UniProt

Q9UKF6 - CPSF3_HUMAN

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Protein
Cleavage and polyadenylation specificity factor subunit 3
Gene
CPSF3, CPSF73
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Cofactori

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711Zinc 1
Metal bindingi73 – 731Zinc 1
Metal bindingi75 – 751Zinc 2
Metal bindingi76 – 761Zinc 2
Metal bindingi158 – 1581Zinc 1
Metal bindingi179 – 1791Zinc 1
Metal bindingi179 – 1791Zinc 2
Active sitei396 – 3961Proton donor Reviewed prediction
Metal bindingi418 – 4181Zinc 2

GO - Molecular functioni

  1. 5'-3' exonuclease activity Source: UniProtKB
  2. RNA binding Source: UniProtKB
  3. endoribonuclease activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  2. RNA splicing Source: Reactome
  3. gene expression Source: Reactome
  4. histone mRNA 3'-end processing Source: UniProtKB
  5. mRNA 3'-end processing Source: Reactome
  6. mRNA cleavage Source: ProtInc
  7. mRNA export from nucleus Source: Reactome
  8. mRNA polyadenylation Source: ProtInc
  9. mRNA splicing, via spliceosome Source: Reactome
  10. termination of RNA polymerase II transcription Source: Reactome
  11. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Cleavage and polyadenylation specificity factor subunit 3 (EC:3.1.27.-)
Alternative name(s):
Cleavage and polyadenylation specificity factor 73 kDa subunit
Short name:
CPSF 73 kDa subunit
mRNA 3'-end-processing endonuclease CPSF-73
Gene namesi
Name:CPSF3
Synonyms:CPSF73
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2326. CPSF3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. mRNA cleavage and polyadenylation specificity factor complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731H → A: Inhibits histone 3'-end processing. 2 Publications
Mutagenesisi75 – 762DH → KA: Loss of histone 3'-end processing. 2 Publications
Mutagenesisi75 – 751D → A: Inhibits histone 3'-end processing. 2 Publications
Mutagenesisi76 – 761H → A: Inhibits histone 3'-end processing. 2 Publications
Mutagenesisi334 – 3341S → A: Does not inhibit histone 3'-end processing. 2 Publications
Mutagenesisi396 – 3961H → A: Inhibits histone 3'-end processing. 2 Publications
Mutagenesisi462 – 4621K → R: Reduced sumoylation; when associated with R-465 and R-545. 2 Publications
Mutagenesisi465 – 4651K → R: Reduced sumoylation; when associated with R-462 and R-545. 2 Publications
Mutagenesisi545 – 5451K → R: Reduced sumoylation; when associated with R-462 and R-465. 2 Publications

Organism-specific databases

PharmGKBiPA26843.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 684683Cleavage and polyadenylation specificity factor subunit 3
PRO_0000074400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Cross-linki462 – 462Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki465 – 465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki545 – 545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei681 – 6811Phosphothreonine1 Publication

Post-translational modificationi

Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UKF6.
PaxDbiQ9UKF6.
PeptideAtlasiQ9UKF6.
PRIDEiQ9UKF6.

PTM databases

PhosphoSiteiQ9UKF6.

Expressioni

Gene expression databases

ArrayExpressiQ9UKF6.
BgeeiQ9UKF6.
CleanExiHS_CPSF3.
GenevestigatoriQ9UKF6.

Organism-specific databases

HPAiHPA034657.

Interactioni

Subunit structurei

Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF2, CSTF2 and SYMPK. Interacts with TUT1; the interaction is direct and mediates the recruitment of the CPSF complex on the 3'UTR of pre-mRNAs. Interacts with WDR33.4 Publications

Protein-protein interaction databases

BioGridi119680. 23 interactions.
DIPiDIP-42501N.
IntActiQ9UKF6. 8 interactions.
MINTiMINT-1742891.
STRINGi9606.ENSP00000238112.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 2516
Beta strandi27 – 326
Beta strandi35 – 395
Helixi49 – 524
Helixi56 – 583
Helixi61 – 633
Beta strandi66 – 683
Helixi74 – 774
Helixi80 – 867
Beta strandi91 – 966
Helixi97 – 11014
Helixi125 – 1317
Helixi132 – 1343
Beta strandi135 – 1384
Beta strandi144 – 1463
Beta strandi149 – 1557
Beta strandi163 – 1697
Beta strandi172 – 1765
Beta strandi186 – 1883
Beta strandi199 – 2046
Turni206 – 2094
Helixi215 – 23117
Beta strandi235 – 2395
Beta strandi242 – 2454
Helixi246 – 25914
Helixi261 – 2633
Beta strandi268 – 2714
Helixi275 – 28410
Turni285 – 2873
Beta strandi307 – 3104
Helixi314 – 3163
Beta strandi321 – 3288
Helixi335 – 34410
Beta strandi351 – 3544
Helixi363 – 3675
Beta strandi372 – 3754
Beta strandi381 – 3833
Beta strandi386 – 3905
Helixi399 – 40911
Beta strandi412 – 4198
Helixi421 – 43515
Beta strandi444 – 4463
Beta strandi454 – 4585

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I7TX-ray2.10A1-459[»]
2I7VX-ray2.10A1-459[»]
ProteinModelPortaliQ9UKF6.
SMRiQ9UKF6. Positions 7-459.

Miscellaneous databases

EvolutionaryTraceiQ9UKF6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1236.
HOGENOMiHOG000203394.
HOVERGENiHBG051107.
InParanoidiQ9UKF6.
KOiK14403.
OMAiEISFSAH.
OrthoDBiEOG7BW0HT.
PhylomeDBiQ9UKF6.
TreeFamiTF105643.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
IPR022712. Beta_Casp.
IPR021718. CPSF73-100_C.
IPR011108. RMMBL.
[Graphical view]
PfamiPF10996. Beta-Casp. 1 hit.
PF11718. CPSF73-100_C. 1 hit.
PF00753. Lactamase_B. 1 hit.
PF07521. RMMBL. 1 hit.
[Graphical view]
SMARTiSM01027. Beta-Casp. 1 hit.
SM01098. CPSF73-100_C. 1 hit.
SM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UKF6-1 [UniParc]FASTAAdd to Basket

« Hide

MSAIPAEESD QLLIRPLGAG QEVGRSCIIL EFKGRKIMLD CGIHPGLEGM    50
DALPYIDLID PAEIDLLLIS HFHLDHCGAL PWFLQKTSFK GRTFMTHATK 100
AIYRWLLSDY VKVSNISADD MLYTETDLEE SMDKIETINF HEVKEVAGIK 150
FWCYHAGHVL GAAMFMIEIA GVKLLYTGDF SRQEDRHLMA AEIPNIKPDI 200
LIIESTYGTH IHEKREEREA RFCNTVHDIV NRGGRGLIPV FALGRAQELL 250
LILDEYWQNH PELHDIPIYY ASSLAKKCMA VYQTYVNAMN DKIRKQININ 300
NPFVFKHISN LKSMDHFDDI GPSVVMASPG MMQSGLSREL FESWCTDKRN 350
GVIIAGYCVE GTLAKHIMSE PEEITTMSGQ KLPLKMSVDY ISFSAHTDYQ 400
QTSEFIRALK PPHVILVHGE QNEMARLKAA LIREYEDNDE VHIEVHNPRN 450
TEAVTLNFRG EKLAKVMGFL ADKKPEQGQR VSGILVKRNF NYHILSPCDL 500
SNYTDLAMST VKQTQAIPYT GPFNLLCYQL QKLTGDVEEL EIQEKPALKV 550
FKNITVIQEP GMVVLEWLAN PSNDMYADTV TTVILEVQSN PKIRKGAVQK 600
VSKKLEMHVY SKRLEIMLQD IFGEDCVSVK DDSILSVTVD GKTANLNLET 650
RTVECEEGSE DDESLREMVE LAAQRLYEAL TPVH 684
Length:684
Mass (Da):77,486
Last modified:May 1, 2000 - v1
Checksum:iF8AA24EA6FB78377
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti142 – 1421E → G.1 Publication
Corresponds to variant rs17850770 [ dbSNP | Ensembl ].
VAR_037646
Natural varianti578 – 5781D → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_035873

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF171877 mRNA. Translation: AAF00224.1.
AC080162 Genomic DNA. Translation: AAY14858.1.
CH471053 Genomic DNA. Translation: EAX00989.1.
BC011654 mRNA. Translation: AAH11654.1.
BC020211 mRNA. Translation: AAH20211.1.
AF017269 mRNA. Translation: AAB70268.1.
CCDSiCCDS1664.1.
RefSeqiNP_057291.1. NM_016207.3.
UniGeneiHs.515972.

Genome annotation databases

EnsembliENST00000238112; ENSP00000238112; ENSG00000119203.
GeneIDi51692.
KEGGihsa:51692.
UCSCiuc002qzo.2. human.

Polymorphism databases

DMDMi18203503.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF171877 mRNA. Translation: AAF00224.1 .
AC080162 Genomic DNA. Translation: AAY14858.1 .
CH471053 Genomic DNA. Translation: EAX00989.1 .
BC011654 mRNA. Translation: AAH11654.1 .
BC020211 mRNA. Translation: AAH20211.1 .
AF017269 mRNA. Translation: AAB70268.1 .
CCDSi CCDS1664.1.
RefSeqi NP_057291.1. NM_016207.3.
UniGenei Hs.515972.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I7T X-ray 2.10 A 1-459 [» ]
2I7V X-ray 2.10 A 1-459 [» ]
ProteinModelPortali Q9UKF6.
SMRi Q9UKF6. Positions 7-459.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119680. 23 interactions.
DIPi DIP-42501N.
IntActi Q9UKF6. 8 interactions.
MINTi MINT-1742891.
STRINGi 9606.ENSP00000238112.

PTM databases

PhosphoSitei Q9UKF6.

Polymorphism databases

DMDMi 18203503.

Proteomic databases

MaxQBi Q9UKF6.
PaxDbi Q9UKF6.
PeptideAtlasi Q9UKF6.
PRIDEi Q9UKF6.

Protocols and materials databases

DNASUi 51692.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000238112 ; ENSP00000238112 ; ENSG00000119203 .
GeneIDi 51692.
KEGGi hsa:51692.
UCSCi uc002qzo.2. human.

Organism-specific databases

CTDi 51692.
GeneCardsi GC02P009514.
HGNCi HGNC:2326. CPSF3.
HPAi HPA034657.
MIMi 606029. gene.
neXtProti NX_Q9UKF6.
PharmGKBi PA26843.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1236.
HOGENOMi HOG000203394.
HOVERGENi HBG051107.
InParanoidi Q9UKF6.
KOi K14403.
OMAi EISFSAH.
OrthoDBi EOG7BW0HT.
PhylomeDBi Q9UKF6.
TreeFami TF105643.

Enzyme and pathway databases

Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi CPSF3. human.
EvolutionaryTracei Q9UKF6.
GeneWikii CPSF3.
GenomeRNAii 51692.
NextBioi 55702.
PROi Q9UKF6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UKF6.
Bgeei Q9UKF6.
CleanExi HS_CPSF3.
Genevestigatori Q9UKF6.

Family and domain databases

Gene3Di 3.60.15.10. 1 hit.
InterProi IPR001279. Beta-lactamas-like.
IPR022712. Beta_Casp.
IPR021718. CPSF73-100_C.
IPR011108. RMMBL.
[Graphical view ]
Pfami PF10996. Beta-Casp. 1 hit.
PF11718. CPSF73-100_C. 1 hit.
PF00753. Lactamase_B. 1 hit.
PF07521. RMMBL. 1 hit.
[Graphical view ]
SMARTi SM01027. Beta-Casp. 1 hit.
SM01098. CPSF73-100_C. 1 hit.
SM00849. Lactamase_B. 1 hit.
[Graphical view ]
SUPFAMi SSF56281. SSF56281. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Homo sapiens mRNA for CPSF (cleavage and polyadenylation specificity factor) 73 kDa subunit."
    Yu S., Chen W., Pang X., Dong X., Wang H.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Hepatoma.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT GLY-142.
    Tissue: Brain and Uterus.
  5. "H. sapiens mRNA for the 73 kDa subunit of CPSF (cleavage and polyadenylation specificity factor, partial cds)."
    Pusch W.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 120-498.
  6. "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.
  7. "Evidence that polyadenylation factor CPSF-73 is the mRNA 3' processing endonuclease."
    Ryan K., Calvo O., Manley J.L.
    RNA 10:565-573(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex."
    Vethantham V., Rao N., Manley J.L.
    Mol. Cell. Biol. 27:8848-8858(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-462; LYS-465 AND LYS-545, MUTAGENESIS OF LYS-462; LYS-465 AND LYS-545.
  9. "Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation."
    Kolev N.G., Yario T.A., Benson E., Steitz J.A.
    EMBO Rep. 9:1013-1018(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CPSF2; CSTF2 AND SYMPK, MUTAGENESIS OF HIS-73; ASP-75; HIS-76; SER-334 AND HIS-396.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Molecular architecture of the human pre-mRNA 3' processing complex."
    Shi Y., Di Giammartino D.C., Taylor D., Sarkeshik A., Rice W.J., Yates J.R. III, Frank J., Manley J.L.
    Mol. Cell 33:365-376(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WDR33.
  12. "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.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease."
    Mandel C.R., Kaneko S., Zhang H., Gebauer D., Vethantham V., Manley J.L., Tong L.
    Nature 444:953-956(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-459 IN COMPLEX WITH ZINC IONS, FUNCTION, MUTAGENESIS OF 75-ASP-HIS-76.
  17. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-578.

Entry informationi

Entry nameiCPSF3_HUMAN
AccessioniPrimary (citable) accession number: Q9UKF6
Secondary accession number(s): O14769, Q53RS2, Q96F36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 117 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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