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P33240 (CSTF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cleavage stimulation factor subunit 2
Alternative name(s):
CF-1 64 kDa subunit
Cleavage stimulation factor 64 kDa subunit
Short name=CSTF 64 kDa subunit
Short name=CstF-64
Gene names
Name:CSTF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs By similarity. Ref.5

Subunit structure

The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF2 directly interacts with CSTF3, SYMPK and RPO2TC1. Interacts with HSF1 in heat-stressed cells. Interacts with CPSF2, CPSF3 and FIP1L1. Interacts with DDX1. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16

Subcellular location

Nucleus. Note: Localized with DDX1 in cleavage bodies. Ref.9

Induction

Up-regulated during the G0 to S phase transition. Ref.6

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence CAI42681.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P33240-1)

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.
Isoform 2 (identifier: P33240-2)

The sequence of this isoform differs from the canonical sequence as follows:
     235-251: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Cleavage stimulation factor subunit 2
PRO_0000081531

Regions

Domain16 – 9479RRM
Repeat410 – 41451; approximate
Repeat415 – 41952
Repeat420 – 42453
Repeat425 – 42954; approximate
Repeat430 – 43455; approximate
Repeat435 – 43956
Repeat440 – 44457
Repeat445 – 44958
Repeat450 – 45459
Repeat455 – 459510; approximate
Repeat460 – 464511
Repeat465 – 469512; approximate
Region108 – 248141Interactions with CSTF3 and SYMPK
Region410 – 4696012 X 5 AA tandem repeats of M-E-A-R-[AG]
Region514 – 57764Interaction with RPO2TC1
Compositional bias198 – 409212Gly/Pro-rich
Compositional bias470 – 52657Gly/Pro-rich

Amino acid modifications

Modified residue5181Phosphoserine Ref.12
Modified residue5241Phosphoserine Ref.14 Ref.15

Natural variations

Alternative sequence235 – 25117Missing in isoform 2.
VSP_014841

Secondary structure

.............................. 577
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: B76595E9BF8FABBD

FASTA57760,959
        10         20         30         40         50         60 
MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG 

        70         80         90        100        110        120 
FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGETIS 

       130        140        150        160        170        180 
PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR 

       190        200        210        220        230        240 
IVDPEIALKI LHRQTNIPTL IAGNPQPVHG AGPGSGSNVS MNQQNPQAPQ AQSLGGMHVN 

       250        260        270        280        290        300 
GAPPLMQASM QGGVPAPGQM PAAVTGPGPG SLAPGGGMQA QVGMPGSGPV SMERGQVPMQ 

       310        320        330        340        350        360 
DPRAAMQRGS LPANVPTPRG LLGDAPNDPR GGTLLSVTGE VEPRGYLGPP HQGPPMHHVP 

       370        380        390        400        410        420 
GHESRGPPPH ELRGGPLPEP RPLMAEPRGP MLDQRGPPLD GRGGRDPRGI DARGMEARAM 

       430        440        450        460        470        480 
EARGLDARGL EARAMEARAM EARAMEARAM EARAMEVRGM EARGMDTRGP VPGPRGPIPS 

       490        500        510        520        530        540 
GMQGPSPINM GAVVPQGSRQ VPVMQGTGMQ GASIQGGSQP GGFSPGQNQV TPQDHEKAAL 

       550        560        570 
IMQVLQLTAD QIAMLPPEQR QSILILKEQI QKSTGAP 

« Hide

Isoform 2 [UniParc].

Checksum: D76823A0FF6363B8
Show »

FASTA56059,251

References

« Hide 'large scale' references
[1]"The human 64-kDa polyadenylylation factor contains a ribonucleoprotein-type RNA binding domain and unusual auxiliary motifs."
Takagaki Y., Macdonald C.C., Shenk T., Manley J.L.
Proc. Natl. Acad. Sci. U.S.A. 89:1403-1407(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, RNA-BINDING.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 1 AND 2).
Tissue: Kidney and Ovary.
[5]"RNA recognition by the human polyadenylation factor CstF."
Takagaki Y., Manley J.L.
Mol. Cell. Biol. 17:3907-3914(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, FUNCTION.
[6]"Increase in the 64-kDa subunit of the polyadenylation/cleavage stimulatory factor during the G0 to S phase transition."
Martincic K., Campbell R., Edwalds-Gilbert G., Souan L., Lotze M.T., Milcarek C.
Proc. Natl. Acad. Sci. U.S.A. 95:11095-11100(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Complex protein interactions within the human polyadenylation machinery identify a novel component."
Takagaki Y., Manley J.L.
Mol. Cell. Biol. 20:1515-1525(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSTF3 AND SYMPK.
[8]"Evolutionarily conserved interaction between CstF-64 and PC4 links transcription, polyadenylation, and termination."
Calvo O., Manley J.L.
Mol. Cell 7:1013-1023(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPO2TC1.
[9]"Association of human DEAD box protein DDX1 with a cleavage stimulation factor involved in 3'-end processing of pre-MRNA."
Bleoo S., Sun X., Hendzel M.J., Rowe J.M., Packer M., Godbout R.
Mol. Biol. Cell 12:3046-3059(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX1, SUBCELLULAR LOCATION.
[10]"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: INTERACTION WITH FIP1L1.
[11]"HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin."
Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D.
J. Biol. Chem. 279:10551-10555(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSF1.
[12]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[13]"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: INTERACTION WITH CPSF2 AND CPSF3.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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.
[17]"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.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein."
Perez Canadillas J.M., Varani G.
EMBO J. 22:2821-2830(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 8-111.
[21]"The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3'-end processing."
Qu X., Perez-Canadillas J.M., Agrawal S., De Baecke J., Cheng H., Varani G., Moore C.
J. Biol. Chem. 282:2101-2115(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 531-577.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85085 mRNA. Translation: AAA35724.1.
BT009778 mRNA. Translation: AAP88780.1.
Z83819, Z95327 Genomic DNA. Translation: CAB06072.2.
Z95327, Z83819 Genomic DNA. Translation: CAI42680.1.
Z95327 Genomic DNA. Translation: CAI42681.1. Sequence problems.
BC017712 mRNA. Translation: AAH17712.1.
BC033135 mRNA. Translation: AAH33135.1.
PIRA40220.
RefSeqNP_001316.1. NM_001325.2.
UniGeneHs.132370.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P1TNMR-A8-111[»]
2J8PNMR-A531-577[»]
ProteinModelPortalP33240.
SMRP33240. Positions 8-164, 529-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107860. 41 interactions.
DIPDIP-36129N.
IntActP33240. 19 interactions.
MINTMINT-1375144.
STRING9606.ENSP00000362063.

PTM databases

PhosphoSiteP33240.

Polymorphism databases

DMDM461847.

Proteomic databases

PaxDbP33240.
PRIDEP33240.

Protocols and materials databases

DNASU1478.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372972; ENSP00000362063; ENSG00000101811. [P33240-1]
GeneID1478.
KEGGhsa:1478.
UCSCuc004egh.3. human. [P33240-1]
uc004egi.3. human. [P33240-2]

Organism-specific databases

CTD1478.
GeneCardsGC0XP100075.
HGNCHGNC:2484. CSTF2.
HPACAB004680.
HPA000427.
MIM300907. gene.
neXtProtNX_P33240.
PharmGKBPA26986.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000214373.
HOVERGENHBG051145.
InParanoidP33240.
KOK14407.
OrthoDBEOG7N63NZ.
PhylomeDBP33240.
TreeFamTF314948.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressP33240.
BgeeP33240.
CleanExHS_CSTF2.
GenevestigatorP33240.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR025742. CSTF2_hinge.
IPR026896. CSTF_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF14327. CSTF2_hinge. 1 hit.
PF14304. CSTF_C. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33240.
GeneWikiCSTF2.
GenomeRNAi1478.
NextBio6073.
PROP33240.
SOURCESearch...

Entry information

Entry nameCSTF2_HUMAN
AccessionPrimary (citable) accession number: P33240
Secondary accession number(s): Q5H951, Q6LA74, Q8N502
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM