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Protein

Cleavage and polyadenylation specificity factor subunit 2

Gene

CPSF2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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. Involved in the histone 3' end pre-mRNA processing (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-BTA-109688. Cleavage of Growing Transcript in the Termination Region.
R-BTA-72163. mRNA Splicing - Major Pathway.
R-BTA-72187. mRNA 3'-end processing.
R-BTA-77595. Processing of Intronless Pre-mRNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Cleavage and polyadenylation specificity factor subunit 2
Alternative name(s):
Cleavage and polyadenylation specificity factor 100 kDa subunit
Short name:
CPSF 100 kDa subunit
Gene namesi
Name:CPSF2
Synonyms:CPSF100
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 21

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000743921 – 782Cleavage and polyadenylation specificity factor subunit 2Add BLAST782

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei419PhosphoserineBy similarity1
Modified residuei420PhosphoserineBy similarity1
Modified residuei423PhosphoserineBy similarity1
Modified residuei660PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ10568.
PRIDEiQ10568.

Expressioni

Gene expression databases

BgeeiENSBTAG00000010227.

Interactioni

Subunit structurei

Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF3, CSTF2 and SYMPK. Interacts with ZC3H3.By similarity

Protein-protein interaction databases

IntActiQ10568. 1 interactor.
STRINGi9913.ENSBTAP00000013500.

Structurei

3D structure databases

ProteinModelPortaliQ10568.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1135. Eukaryota.
COG1236. LUCA.
GeneTreeiENSGT00860000133746.
HOGENOMiHOG000264343.
HOVERGENiHBG051106.
InParanoidiQ10568.
KOiK14402.
OMAiLMRNNIN.
OrthoDBiEOG091G03GG.
TreeFamiTF106131.

Family and domain databases

Gene3Di3.60.15.10. 3 hits.
InterProiIPR022712. Beta_Casp.
IPR027075. CPSF2.
IPR025069. Cpsf2_C.
IPR001279. Metallo-B-lactamas.
IPR011108. RMMBL.
[Graphical view]
PANTHERiPTHR11203:SF5. PTHR11203:SF5. 2 hits.
PfamiPF10996. Beta-Casp. 1 hit.
PF13299. CPSF100_C. 1 hit.
PF16661. Lactamase_B_6. 1 hit.
PF07521. RMMBL. 1 hit.
[Graphical view]
SMARTiSM01027. Beta-Casp. 1 hit.
SM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 2 hits.

Sequencei

Sequence statusi: Complete.

Q10568-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SMDIIDSLRK
60 70 80 90 100
HVHQIDAVLL SHPDPLHLGA LPYAVGKLGL NCAIYATIPV YKMGQMFMYD
110 120 130 140 150
LYQSRHNTED FTLFTLDDVD AAFDKIQQLK FSQIVNLKGK GHGLSITPLP
160 170 180 190 200
AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR EIHLNGCSLE MLSRPSLLIT
210 220 230 240 250
DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA GRVLELAQLL
260 270 280 290 300
DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
310 320 330 340 350
NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK
360 370 380 390 400
NSIILTYRTT PGTLARFLID NPSEKVTEIE LRKRVKLEGK ELEEYLEKEK
410 420 430 440 450
LKKEAAKKLE QSKEADIDSS DESDAEEDID QPSAHKTKHD LMMKGEGSRK
460 470 480 490 500
GSFFKQAKKS YPMFPAPEER IKWDEYGEII KPEDFLVPEL QATEEEKSKL
510 520 530 540 550
ESGLTNGDEP MDQDLSDVPT KCISTTESIE IKARVTYIDY EGRSDGDSIK
560 570 580 590 600
KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT
610 620 630 640 650
SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE
660 670 680 690 700
GELKDDGEDS EMQVDAPSDS SVIAQQKAMK SLFGDDEKET GEESEIIPTL
710 720 730 740 750
EPLPPHEVPG HQSVFMNEPR LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV
760 770 780
RRTETGRIGL EGCLCQDFYR IRDLLYEQYA IV
Length:782
Mass (Da):88,417
Last modified:October 1, 1996 - v1
Checksum:i0934519C6A73C2A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75931 mRNA. Translation: CAA53535.1.
PIRiA56351.
RefSeqiNP_787002.1. NM_175808.2.
XP_005222184.1. XM_005222127.3.
UniGeneiBt.4077.

Genome annotation databases

EnsembliENSBTAT00000013500; ENSBTAP00000013500; ENSBTAG00000010227.
GeneIDi327689.
KEGGibta:327689.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75931 mRNA. Translation: CAA53535.1.
PIRiA56351.
RefSeqiNP_787002.1. NM_175808.2.
XP_005222184.1. XM_005222127.3.
UniGeneiBt.4077.

3D structure databases

ProteinModelPortaliQ10568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ10568. 1 interactor.
STRINGi9913.ENSBTAP00000013500.

Proteomic databases

PaxDbiQ10568.
PRIDEiQ10568.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000013500; ENSBTAP00000013500; ENSBTAG00000010227.
GeneIDi327689.
KEGGibta:327689.

Organism-specific databases

CTDi53981.

Phylogenomic databases

eggNOGiKOG1135. Eukaryota.
COG1236. LUCA.
GeneTreeiENSGT00860000133746.
HOGENOMiHOG000264343.
HOVERGENiHBG051106.
InParanoidiQ10568.
KOiK14402.
OMAiLMRNNIN.
OrthoDBiEOG091G03GG.
TreeFamiTF106131.

Enzyme and pathway databases

ReactomeiR-BTA-109688. Cleavage of Growing Transcript in the Termination Region.
R-BTA-72163. mRNA Splicing - Major Pathway.
R-BTA-72187. mRNA 3'-end processing.
R-BTA-77595. Processing of Intronless Pre-mRNAs.

Gene expression databases

BgeeiENSBTAG00000010227.

Family and domain databases

Gene3Di3.60.15.10. 3 hits.
InterProiIPR022712. Beta_Casp.
IPR027075. CPSF2.
IPR025069. Cpsf2_C.
IPR001279. Metallo-B-lactamas.
IPR011108. RMMBL.
[Graphical view]
PANTHERiPTHR11203:SF5. PTHR11203:SF5. 2 hits.
PfamiPF10996. Beta-Casp. 1 hit.
PF13299. CPSF100_C. 1 hit.
PF16661. Lactamase_B_6. 1 hit.
PF07521. RMMBL. 1 hit.
[Graphical view]
SMARTiSM01027. Beta-Casp. 1 hit.
SM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCPSF2_BOVIN
AccessioniPrimary (citable) accession number: Q10568
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.