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P33240

- CSTF2_HUMAN

UniProt

P33240 - CSTF2_HUMAN

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Protein

Cleavage stimulation factor subunit 2

Gene

CSTF2

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

Functioni

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).By similarity

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: ProtInc

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA 3'-end processing Source: Reactome
  3. mRNA cleavage Source: ProtInc
  4. mRNA polyadenylation Source: ProtInc
  5. mRNA splicing, via spliceosome Source: Reactome
  6. RNA splicing Source: Reactome
  7. termination of RNA polymerase II transcription Source: Reactome
  8. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CSTF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:2484. CSTF2.

Subcellular locationi

Nucleus 1 Publication
Note: Localized with DDX1 in cleavage bodies.

GO - Cellular componenti

  1. cleavage body Source: UniProtKB
  2. mRNA cleavage and polyadenylation specificity factor complex Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26986.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577Cleavage stimulation factor subunit 2PRO_0000081531Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei518 – 5181Phosphoserine1 Publication
Modified residuei524 – 5241Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP33240.
PaxDbiP33240.
PRIDEiP33240.

PTM databases

PhosphoSiteiP33240.

Expressioni

Inductioni

Up-regulated during the G0 to S phase transition.1 Publication

Gene expression databases

BgeeiP33240.
CleanExiHS_CSTF2.
ExpressionAtlasiP33240. baseline and differential.
GenevestigatoriP33240.

Organism-specific databases

HPAiCAB004680.
HPA000427.

Interactioni

Subunit structurei

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 DDX1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BARD1Q997288EBI-711360,EBI-473181
CPSF2Q9P2I02EBI-711360,EBI-1043224
PARNO954535EBI-711360,EBI-372832
SUB1P539993EBI-711374,EBI-998260

Protein-protein interaction databases

BioGridi107860. 48 interactions.
DIPiDIP-36129N.
IntActiP33240. 19 interactions.
MINTiMINT-1375144.
STRINGi9606.ENSP00000362063.

Structurei

Secondary structure

1
577
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 154Combined sources
Beta strandi18 – 225Combined sources
Helixi29 – 379Combined sources
Beta strandi43 – 508Combined sources
Turni51 – 544Combined sources
Beta strandi55 – 639Combined sources
Helixi67 – 7610Combined sources
Beta strandi77 – 815Combined sources
Beta strandi83 – 853Combined sources
Beta strandi87 – 915Combined sources
Helixi97 – 1048Combined sources
Helixi532 – 5354Combined sources
Helixi537 – 5459Combined sources
Helixi549 – 5535Combined sources
Helixi557 – 5604Combined sources
Helixi562 – 57110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P1TNMR-A8-111[»]
2J8PNMR-A531-577[»]
ProteinModelPortaliP33240.
SMRiP33240. Positions 8-111, 529-577.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33240.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9479RRMPROSITE-ProRule annotationAdd
BLAST
Repeati410 – 41451; approximate
Repeati415 – 41952
Repeati420 – 42453
Repeati425 – 42954; approximate
Repeati430 – 43455; approximate
Repeati435 – 43956
Repeati440 – 44457
Repeati445 – 44958
Repeati450 – 45459
Repeati455 – 459510; approximate
Repeati460 – 464511
Repeati465 – 469512; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 248141Interactions with CSTF3 and SYMPKAdd
BLAST
Regioni410 – 4696012 X 5 AA tandem repeats of M-E-A-R-[AG]Add
BLAST
Regioni514 – 57764Interaction with RPO2TC1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi198 – 409212Gly/Pro-richAdd
BLAST
Compositional biasi470 – 52657Gly/Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000119351.
HOGENOMiHOG000214373.
HOVERGENiHBG051145.
InParanoidiP33240.
KOiK14407.
OrthoDBiEOG7N63NZ.
PhylomeDBiP33240.
TreeFamiTF314948.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR025742. CSTF2_hinge.
IPR026896. CSTF_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF14327. CSTF2_hinge. 1 hit.
PF14304. CSTF_C. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P33240-1) [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
MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD
60 70 80 90 100
RETGKPKGYG FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE
110 120 130 140 150
LKSLGTGAPV IESPYGETIS PEDAPESISK AVASLPPEQM FELMKQMKLC
160 170 180 190 200
VQNSPQEARN MLLQNPQLAY ALLQAQVVMR IVDPEIALKI LHRQTNIPTL
210 220 230 240 250
IAGNPQPVHG AGPGSGSNVS MNQQNPQAPQ AQSLGGMHVN GAPPLMQASM
260 270 280 290 300
QGGVPAPGQM PAAVTGPGPG SLAPGGGMQA QVGMPGSGPV SMERGQVPMQ
310 320 330 340 350
DPRAAMQRGS LPANVPTPRG LLGDAPNDPR GGTLLSVTGE VEPRGYLGPP
360 370 380 390 400
HQGPPMHHVP GHESRGPPPH ELRGGPLPEP RPLMAEPRGP MLDQRGPPLD
410 420 430 440 450
GRGGRDPRGI DARGMEARAM EARGLDARGL EARAMEARAM EARAMEARAM
460 470 480 490 500
EARAMEVRGM EARGMDTRGP VPGPRGPIPS GMQGPSPINM GAVVPQGSRQ
510 520 530 540 550
VPVMQGTGMQ GASIQGGSQP GGFSPGQNQV TPQDHEKAAL IMQVLQLTAD
560 570
QIAMLPPEQR QSILILKEQI QKSTGAP
Length:577
Mass (Da):60,959
Last modified:February 1, 1994 - v1
Checksum:iB76595E9BF8FABBD
GO
Isoform 2 (identifier: P33240-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     235-251: Missing.

Note: No experimental confirmation available.

Show »
Length:560
Mass (Da):59,251
Checksum:iD76823A0FF6363B8
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei235 – 25117Missing in isoform 2. 1 PublicationVSP_014841Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14473.1. [P33240-1]
PIRiA40220.
RefSeqiNP_001316.1. NM_001325.2. [P33240-1]
UniGeneiHs.132370.

Genome annotation databases

EnsembliENST00000372972; ENSP00000362063; ENSG00000101811. [P33240-1]
GeneIDi1478.
KEGGihsa:1478.
UCSCiuc004egh.3. human. [P33240-1]
uc004egi.3. human. [P33240-2]

Polymorphism databases

DMDMi461847.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS14473.1. [P33240-1 ]
PIRi A40220.
RefSeqi NP_001316.1. NM_001325.2. [P33240-1 ]
UniGenei Hs.132370.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P1T NMR - A 8-111 [» ]
2J8P NMR - A 531-577 [» ]
ProteinModelPortali P33240.
SMRi P33240. Positions 8-111, 529-577.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107860. 48 interactions.
DIPi DIP-36129N.
IntActi P33240. 19 interactions.
MINTi MINT-1375144.
STRINGi 9606.ENSP00000362063.

PTM databases

PhosphoSitei P33240.

Polymorphism databases

DMDMi 461847.

Proteomic databases

MaxQBi P33240.
PaxDbi P33240.
PRIDEi P33240.

Protocols and materials databases

DNASUi 1478.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372972 ; ENSP00000362063 ; ENSG00000101811 . [P33240-1 ]
GeneIDi 1478.
KEGGi hsa:1478.
UCSCi uc004egh.3. human. [P33240-1 ]
uc004egi.3. human. [P33240-2 ]

Organism-specific databases

CTDi 1478.
GeneCardsi GC0XP100075.
HGNCi HGNC:2484. CSTF2.
HPAi CAB004680.
HPA000427.
MIMi 300907. gene.
neXtProti NX_P33240.
PharmGKBi PA26986.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00760000119351.
HOGENOMi HOG000214373.
HOVERGENi HBG051145.
InParanoidi P33240.
KOi K14407.
OrthoDBi EOG7N63NZ.
PhylomeDBi P33240.
TreeFami TF314948.

Enzyme and pathway databases

Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi CSTF2. human.
EvolutionaryTracei P33240.
GeneWikii CSTF2.
GenomeRNAii 1478.
NextBioi 6073.
PROi P33240.
SOURCEi Search...

Gene expression databases

Bgeei P33240.
CleanExi HS_CSTF2.
ExpressionAtlasi P33240. baseline and differential.
Genevestigatori P33240.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR025742. CSTF2_hinge.
IPR026896. CSTF_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF14327. CSTF2_hinge. 1 hit.
PF14304. CSTF_C. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiCSTF2_HUMAN
AccessioniPrimary (citable) accession number: P33240
Secondary accession number(s): Q5H951, Q6LA74, Q8N502
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 26, 2014
This is version 145 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 X
    Human chromosome X: 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