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Protein

Cleavage and polyadenylation specificity factor subunit 2

Gene

CPSF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Involved in the histone 3' end pre-mRNA processing.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165934-MONOMER.
ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-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, KIAA1367
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:2325. CPSF2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67H → A: Inhibits histone 3'-end processing. 1 Publication1
Mutagenesisi289D → A: Does not inhibit histone 3'-end processing. 1 Publication1
Mutagenesisi543R → A: Inhibits histone 3'-end processing. 1 Publication1

Organism-specific databases

DisGeNETi53981.
OpenTargetsiENSG00000165934.
PharmGKBiPA26842.

Polymorphism and mutation databases

BioMutaiCPSF2.
DMDMi51338827.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000743931 – 782Cleavage and polyadenylation specificity factor subunit 2Add BLAST782

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei419PhosphoserineCombined sources1
Modified residuei420PhosphoserineCombined sources1
Modified residuei423PhosphoserineCombined sources1
Modified residuei660PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P2I0.
MaxQBiQ9P2I0.
PaxDbiQ9P2I0.
PeptideAtlasiQ9P2I0.
PRIDEiQ9P2I0.

PTM databases

iPTMnetiQ9P2I0.
PhosphoSitePlusiQ9P2I0.

Expressioni

Gene expression databases

BgeeiENSG00000165934.
CleanExiHS_CPSF2.
ExpressionAtlasiQ9P2I0. baseline and differential.
GenevisibleiQ9P2I0. HS.

Organism-specific databases

HPAiHPA024238.

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).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSTF2P332402EBI-1043224,EBI-711360
SYMPKQ927973EBI-1043224,EBI-1051992

Protein-protein interaction databases

BioGridi119826. 50 interactors.
DIPiDIP-42500N.
IntActiQ9P2I0. 16 interactors.
MINTiMINT-1697677.
STRINGi9606.ENSP00000298875.

Structurei

3D structure databases

ProteinModelPortaliQ9P2I0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1135. Eukaryota.
COG1236. LUCA.
GeneTreeiENSGT00860000133746.
HOGENOMiHOG000264343.
HOVERGENiHBG051106.
InParanoidiQ9P2I0.
KOiK14402.
OMAiLMRNNIN.
OrthoDBiEOG091G03GG.
PhylomeDBiQ9P2I0.
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.

Q9P2I0-1 [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 NPSEKITEIE LRKRVKLEGK ELEEYLEKEK
410 420 430 440 450
LKKEAAKKLE QSKEADIDSS DESDIEEDID 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 EMQVEAPSDS SVIAQQKAMK SLFGDDEKET GEESEIIPTL
710 720 730 740 750
EPLPPHEVPG HQSVFMNEPR LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV
760 770 780
RRTETGRIGL EGCLCQDFYR IRDLLYEQYA IV
Length:782
Mass (Da):88,487
Last modified:August 16, 2004 - v2
Checksum:iF67B4813B9883CE8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti289D → G in AAH70095 (PubMed:15489334).Curated1
Sequence conflicti654K → R in AAH70095 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001627 mRNA. Translation: BAG50953.1.
CH471061 Genomic DNA. Translation: EAW81480.1.
BC070095 mRNA. Translation: AAH70095.1.
AB037788 mRNA. Translation: BAA92605.1.
AL442079 mRNA. Translation: CAC09445.1.
CCDSiCCDS9902.1.
RefSeqiNP_001309201.1. NM_001322272.1.
NP_059133.1. NM_017437.2.
UniGeneiHs.657632.
Hs.736541.

Genome annotation databases

EnsembliENST00000298875; ENSP00000298875; ENSG00000165934.
GeneIDi53981.
KEGGihsa:53981.
UCSCiuc001yah.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001627 mRNA. Translation: BAG50953.1.
CH471061 Genomic DNA. Translation: EAW81480.1.
BC070095 mRNA. Translation: AAH70095.1.
AB037788 mRNA. Translation: BAA92605.1.
AL442079 mRNA. Translation: CAC09445.1.
CCDSiCCDS9902.1.
RefSeqiNP_001309201.1. NM_001322272.1.
NP_059133.1. NM_017437.2.
UniGeneiHs.657632.
Hs.736541.

3D structure databases

ProteinModelPortaliQ9P2I0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119826. 50 interactors.
DIPiDIP-42500N.
IntActiQ9P2I0. 16 interactors.
MINTiMINT-1697677.
STRINGi9606.ENSP00000298875.

PTM databases

iPTMnetiQ9P2I0.
PhosphoSitePlusiQ9P2I0.

Polymorphism and mutation databases

BioMutaiCPSF2.
DMDMi51338827.

Proteomic databases

EPDiQ9P2I0.
MaxQBiQ9P2I0.
PaxDbiQ9P2I0.
PeptideAtlasiQ9P2I0.
PRIDEiQ9P2I0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298875; ENSP00000298875; ENSG00000165934.
GeneIDi53981.
KEGGihsa:53981.
UCSCiuc001yah.3. human.

Organism-specific databases

CTDi53981.
DisGeNETi53981.
GeneCardsiCPSF2.
HGNCiHGNC:2325. CPSF2.
HPAiHPA024238.
MIMi606028. gene.
neXtProtiNX_Q9P2I0.
OpenTargetsiENSG00000165934.
PharmGKBiPA26842.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1135. Eukaryota.
COG1236. LUCA.
GeneTreeiENSGT00860000133746.
HOGENOMiHOG000264343.
HOVERGENiHBG051106.
InParanoidiQ9P2I0.
KOiK14402.
OMAiLMRNNIN.
OrthoDBiEOG091G03GG.
PhylomeDBiQ9P2I0.
TreeFamiTF106131.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000165934-MONOMER.
ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-77595. Processing of Intronless Pre-mRNAs.

Miscellaneous databases

ChiTaRSiCPSF2. human.
GeneWikiiCPSF2.
GenomeRNAii53981.
PROiQ9P2I0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165934.
CleanExiHS_CPSF2.
ExpressionAtlasiQ9P2I0. baseline and differential.
GenevisibleiQ9P2I0. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q9P2I0
Secondary accession number(s): B3KME1, Q6NSJ1, Q9H3W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: August 16, 2004
Last modified: November 30, 2016
This is version 131 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. 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.