SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O95639

- CPSF4_HUMAN

UniProt

O95639 - CPSF4_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cleavage and polyadenylation specificity factor subunit 4

Gene
CPSF4, CPSF30, NAR, NEB1
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. CPSF4 binds RNA polymers with a preference for poly(U).2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri35 – 6127C3H1-type 1Add
BLAST
Zinc fingeri62 – 8928C3H1-type 2Add
BLAST
Zinc fingeri90 – 11728C3H1-type 3Add
BLAST
Zinc fingeri118 – 14225C3H1-type 4Add
BLAST
Zinc fingeri143 – 16927C3H1-type 5Add
BLAST
Zinc fingeri243 – 26018CCHC-typeAdd
BLAST

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. modification by virus of host mRNA processing Source: Reactome
  2. modulation by virus of host morphology or physiology Source: Reactome
  3. modulation by virus of host process Source: Reactome
  4. mRNA processing Source: UniProtKB-KW
  5. viral life cycle Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, mRNA processing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_6173. Inhibition of Host mRNA Processing and RNA Silencing.

Names & Taxonomyi

Protein namesi
Recommended name:
Cleavage and polyadenylation specificity factor subunit 4
Alternative name(s):
Cleavage and polyadenylation specificity factor 30 kDa subunit
Short name:
CPSF 30 kDa subunit
NS1 effector domain-binding protein 1
Short name:
Neb-1
No arches homolog
Gene namesi
Name:CPSF4
Synonyms:CPSF30, NAR, NEB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:2327. CPSF4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26844.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Cleavage and polyadenylation specificity factor subunit 4PRO_0000074402Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021Phosphoserine2 Publications
Modified residuei212 – 2121Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95639.
PaxDbiO95639.
PRIDEiO95639.

PTM databases

PhosphoSiteiO95639.

Expressioni

Gene expression databases

ArrayExpressiO95639.
BgeeiO95639.
CleanExiHS_CPSF4.
GenevestigatoriO95639.

Organism-specific databases

HPAiHPA049094.

Interactioni

Subunit structurei

Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with FIP1L1. Association with influenza A virus NS1 blocks processing of pre-mRNAs, thereby preventing nuclear export of host cell mRNAs.3 Publications

Protein-protein interaction databases

BioGridi116104. 9 interactions.
DIPiDIP-48675N.
IntActiO95639. 7 interactions.
MINTiMINT-1429837.
STRINGi9606.ENSP00000292476.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 724
Helixi79 – 813
Beta strandi82 – 854
Turni90 – 923
Helixi97 – 1026
Beta strandi111 – 1133
Beta strandi122 – 1254

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9NNMR-A61-126[»]
2RHKX-ray1.95C/D61-121[»]
ProteinModelPortaliO95639.
SMRiO95639. Positions 61-126.

Miscellaneous databases

EvolutionaryTraceiO95639.

Family & Domainsi

Sequence similaritiesi

Belongs to the CPSF4/YTH1 family.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5084.
HOGENOMiHOG000212457.
HOVERGENiHBG051108.
InParanoidiO95639.
KOiK14404.
OMAiPLDQVTC.
OrthoDBiEOG7XH6QD.
PhylomeDBiO95639.
TreeFamiTF314871.

Family and domain databases

Gene3Di4.10.1000.10. 2 hits.
4.10.60.10. 1 hit.
InterProiIPR000571. Znf_CCCH.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00642. zf-CCCH. 2 hits.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 1 hit.
SM00356. ZnF_C3H1. 5 hits.
[Graphical view]
SUPFAMiSSF57756. SSF57756. 1 hit.
PROSITEiPS50103. ZF_C3H1. 5 hits.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95639-1) [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

MQEIIASVDH IKFDLEIAVE QQLGAQPLPF PGMDKSGAAV CEFFLKAACG    50
KGGMCPFRHI SGEKTVVCKH WLRGLCKKGD QCEFLHEYDM TKMPECYFYS 100
KFGECSNKEC PFLHIDPESK IKDCPWYDRG FCKHGPLCRH RHTRRVICVN 150
YLVGFCPEGP SCKFMHPRFE LPMGTTEQPP LPQQTQPPAK QSNNPPLQRS 200
SSLIQLTSQN SSPNQQRTPQ VIGVMQSQNS SAGNRGPRPL EQVTCYKCGE 250
KGHYANRCTK GHLAFLSGQ 269
Length:269
Mass (Da):30,255
Last modified:May 1, 1999 - v1
Checksum:i49444E3EB840464A
GO
Isoform 2 (identifier: O95639-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     191-215: Missing.

Note: No experimental confirmation available.

Show »
Length:244
Mass (Da):27,547
Checksum:i0DF72BE36CF97106
GO
Isoform 3 (identifier: O95639-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     191-216: Missing.

Note: May be due to a competing acceptor splice site. No experimental confirmation available.

Show »
Length:243
Mass (Da):27,419
Checksum:i3535FE5A0D525C8F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei191 – 21626Missing in isoform 3. VSP_008602Add
BLAST
Alternative sequencei191 – 21525Missing in isoform 2. VSP_008601Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U79569 mRNA. Translation: AAD00321.1.
CR542161 mRNA. Translation: CAG46958.1.
EF191081 Genomic DNA. Translation: ABN05292.1.
CH236956 Genomic DNA. Translation: EAL23878.1.
CH471091 Genomic DNA. Translation: EAW76667.1.
CH471091 Genomic DNA. Translation: EAW76668.1.
BC003101 mRNA. Translation: AAH03101.1.
BC050738 mRNA. Translation: AAH50738.1.
CCDSiCCDS47652.1. [O95639-2]
CCDS5664.1. [O95639-1]
RefSeqiNP_001075028.1. NM_001081559.1. [O95639-2]
NP_006684.1. NM_006693.2. [O95639-1]
UniGeneiHs.489287.

Genome annotation databases

EnsembliENST00000292476; ENSP00000292476; ENSG00000160917. [O95639-1]
ENST00000436336; ENSP00000395311; ENSG00000160917. [O95639-2]
GeneIDi10898.
KEGGihsa:10898.
UCSCiuc003uqi.3. human. [O95639-2]
uc003uqj.3. human. [O95639-1]
uc003uqk.3. human. [O95639-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U79569 mRNA. Translation: AAD00321.1 .
CR542161 mRNA. Translation: CAG46958.1 .
EF191081 Genomic DNA. Translation: ABN05292.1 .
CH236956 Genomic DNA. Translation: EAL23878.1 .
CH471091 Genomic DNA. Translation: EAW76667.1 .
CH471091 Genomic DNA. Translation: EAW76668.1 .
BC003101 mRNA. Translation: AAH03101.1 .
BC050738 mRNA. Translation: AAH50738.1 .
CCDSi CCDS47652.1. [O95639-2 ]
CCDS5664.1. [O95639-1 ]
RefSeqi NP_001075028.1. NM_001081559.1. [O95639-2 ]
NP_006684.1. NM_006693.2. [O95639-1 ]
UniGenei Hs.489287.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D9N NMR - A 61-126 [» ]
2RHK X-ray 1.95 C/D 61-121 [» ]
ProteinModelPortali O95639.
SMRi O95639. Positions 61-126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116104. 9 interactions.
DIPi DIP-48675N.
IntActi O95639. 7 interactions.
MINTi MINT-1429837.
STRINGi 9606.ENSP00000292476.

PTM databases

PhosphoSitei O95639.

Proteomic databases

MaxQBi O95639.
PaxDbi O95639.
PRIDEi O95639.

Protocols and materials databases

DNASUi 10898.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000292476 ; ENSP00000292476 ; ENSG00000160917 . [O95639-1 ]
ENST00000436336 ; ENSP00000395311 ; ENSG00000160917 . [O95639-2 ]
GeneIDi 10898.
KEGGi hsa:10898.
UCSCi uc003uqi.3. human. [O95639-2 ]
uc003uqj.3. human. [O95639-1 ]
uc003uqk.3. human. [O95639-3 ]

Organism-specific databases

CTDi 10898.
GeneCardsi GC07P099036.
HGNCi HGNC:2327. CPSF4.
HPAi HPA049094.
MIMi 603052. gene.
neXtProti NX_O95639.
PharmGKBi PA26844.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5084.
HOGENOMi HOG000212457.
HOVERGENi HBG051108.
InParanoidi O95639.
KOi K14404.
OMAi PLDQVTC.
OrthoDBi EOG7XH6QD.
PhylomeDBi O95639.
TreeFami TF314871.

Enzyme and pathway databases

Reactomei REACT_6173. Inhibition of Host mRNA Processing and RNA Silencing.

Miscellaneous databases

EvolutionaryTracei O95639.
GeneWikii CPSF4.
GenomeRNAii 10898.
NextBioi 41385.
PROi O95639.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95639.
Bgeei O95639.
CleanExi HS_CPSF4.
Genevestigatori O95639.

Family and domain databases

Gene3Di 4.10.1000.10. 2 hits.
4.10.60.10. 1 hit.
InterProi IPR000571. Znf_CCCH.
IPR001878. Znf_CCHC.
[Graphical view ]
Pfami PF00642. zf-CCCH. 2 hits.
PF00098. zf-CCHC. 1 hit.
[Graphical view ]
SMARTi SM00343. ZnF_C2HC. 1 hit.
SM00356. ZnF_C3H1. 5 hits.
[Graphical view ]
SUPFAMi SSF57756. SSF57756. 1 hit.
PROSITEi PS50103. ZF_C3H1. 5 hits.
PS50158. ZF_CCHC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Assignment of the human homolog of the zebrafish essential gene no arches to 7q22.1."
    Kawakami K., Gaiano N., Grosshans D., Scherer S., Tsui L.-C., Hopkins N.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. SeattleSNPs variation discovery resource
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 2 AND 3).
    Tissue: Eye and PNS.
  7. "The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins."
    Barabino S.M.L., Huebner W., Jenny A., Minvielle-Sebastia L., Keller W.
    Genes Dev. 11:1703-1716(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs."
    Nemeroff M.E., Barabino S.M.L., Li Y., Keller W., Krug R.M.
    Mol. Cell 1:991-1000(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INFLUENZA A VIRUS NS1 PROTEIN.
  9. "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, INTERACTION WITH FIP1L1.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Solution structure of CCCH-type zinc-finger domain 2 in cleavage and polyadenylation specificity factor."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 61-126.

Entry informationi

Entry nameiCPSF4_HUMAN
AccessioniPrimary (citable) accession number: O95639
Secondary accession number(s): D6W5S8
, Q6FGE6, Q86TF8, Q9BTW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 123 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 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi