Skip Header

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

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. gene expression Source: Reactome
  2. histone mRNA 3'-end processing Source: UniProtKB
  3. mRNA 3'-end processing Source: Reactome
  4. mRNA cleavage Source: InterPro
  5. mRNA export from nucleus Source: Reactome
  6. mRNA polyadenylation Source: InterPro
  7. mRNA splicing, via spliceosome Source: Reactome
  8. RNA splicing Source: Reactome
  9. termination of RNA polymerase II transcription Source: Reactome
  10. 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_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:2325. CPSF2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671H → A: Inhibits histone 3'-end processing. 1 Publication
Mutagenesisi289 – 2891D → A: Does not inhibit histone 3'-end processing. 1 Publication
Mutagenesisi543 – 5431R → A: Inhibits histone 3'-end processing. 1 Publication

Organism-specific databases

PharmGKBiPA26842.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 782782Cleavage and polyadenylation specificity factor subunit 2PRO_0000074393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei419 – 4191Phosphoserine2 Publications
Modified residuei420 – 4201Phosphoserine2 Publications
Modified residuei423 – 4231Phosphoserine3 Publications
Modified residuei660 – 6601Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9P2I0.
PaxDbiQ9P2I0.
PeptideAtlasiQ9P2I0.
PRIDEiQ9P2I0.

PTM databases

PhosphoSiteiQ9P2I0.

Expressioni

Gene expression databases

BgeeiQ9P2I0.
CleanExiHS_CPSF2.
ExpressionAtlasiQ9P2I0. baseline and differential.
GenevestigatoriQ9P2I0.

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSTF2P332402EBI-1043224,EBI-711360
SYMPKQ927972EBI-1043224,EBI-1051992

Protein-protein interaction databases

BioGridi119826. 37 interactions.
DIPiDIP-42500N.
IntActiQ9P2I0. 10 interactions.
MINTiMINT-1697677.
STRINGi9606.ENSP00000298875.

Structurei

3D structure databases

ProteinModelPortaliQ9P2I0.
SMRiQ9P2I0. Positions 6-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1236.
GeneTreeiENSGT00780000122015.
HOGENOMiHOG000264343.
HOVERGENiHBG051106.
InParanoidiQ9P2I0.
KOiK14402.
OMAiHEERIKW.
OrthoDBiEOG741Z1H.
PhylomeDBiQ9P2I0.
TreeFamiTF106131.

Family and domain databases

Gene3Di3.60.15.10. 3 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR022712. Beta_Casp.
IPR027075. CPSF2.
IPR025069. Cpsf2_C.
IPR011108. RMMBL.
[Graphical view]
PANTHERiPTHR11203:SF5. PTHR11203:SF5. 1 hit.
PfamiPF10996. Beta-Casp. 1 hit.
PF13299. CPSF100_C. 1 hit.
PF00753. Lactamase_B. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2891D → G in AAH70095. (PubMed:15489334)Curated
Sequence conflicti654 – 6541K → R in AAH70095. (PubMed:15489334)Curated

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_059133.1. NM_017437.2.
XP_005267824.1. XM_005267767.1.
UniGeneiHs.657632.
Hs.736541.

Genome annotation databases

EnsembliENST00000298875; ENSP00000298875; ENSG00000165934.
GeneIDi53981.
KEGGihsa:53981.
UCSCiuc001yah.2. human.

Polymorphism databases

DMDMi51338827.

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_059133.1. NM_017437.2.
XP_005267824.1. XM_005267767.1.
UniGeneiHs.657632.
Hs.736541.

3D structure databases

ProteinModelPortaliQ9P2I0.
SMRiQ9P2I0. Positions 6-404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119826. 37 interactions.
DIPiDIP-42500N.
IntActiQ9P2I0. 10 interactions.
MINTiMINT-1697677.
STRINGi9606.ENSP00000298875.

PTM databases

PhosphoSiteiQ9P2I0.

Polymorphism databases

DMDMi51338827.

Proteomic databases

MaxQBiQ9P2I0.
PaxDbiQ9P2I0.
PeptideAtlasiQ9P2I0.
PRIDEiQ9P2I0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298875; ENSP00000298875; ENSG00000165934.
GeneIDi53981.
KEGGihsa:53981.
UCSCiuc001yah.2. human.

Organism-specific databases

CTDi53981.
GeneCardsiGC14P092588.
HGNCiHGNC:2325. CPSF2.
HPAiHPA024238.
MIMi606028. gene.
neXtProtiNX_Q9P2I0.
PharmGKBiPA26842.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1236.
GeneTreeiENSGT00780000122015.
HOGENOMiHOG000264343.
HOVERGENiHBG051106.
InParanoidiQ9P2I0.
KOiK14402.
OMAiHEERIKW.
OrthoDBiEOG741Z1H.
PhylomeDBiQ9P2I0.
TreeFamiTF106131.

Enzyme and pathway databases

ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiCPSF2. human.
GeneWikiiCPSF2.
GenomeRNAii53981.
NextBioi56268.
PROiQ9P2I0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2I0.
CleanExiHS_CPSF2.
ExpressionAtlasiQ9P2I0. baseline and differential.
GenevestigatoriQ9P2I0.

Family and domain databases

Gene3Di3.60.15.10. 3 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR022712. Beta_Casp.
IPR027075. CPSF2.
IPR025069. Cpsf2_C.
IPR011108. RMMBL.
[Graphical view]
PANTHERiPTHR11203:SF5. PTHR11203:SF5. 1 hit.
PfamiPF10996. Beta-Casp. 1 hit.
PF13299. CPSF100_C. 1 hit.
PF00753. Lactamase_B. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Testis.
  4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-782.
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-782.
    Tissue: Lymph node.
  6. "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.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: FUNCTION, INTERACTION WITH CPSF3; CSTF2 AND SYMPK, MUTAGENESIS OF HIS-67; ASP-289 AND ARG-543.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420; SER-423 AND SER-660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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-419; SER-420 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: February 4, 2015
This is version 112 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

External Data

Dasty 3

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 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.