Q9P2I0 (CPSF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CPSF2
Synonyms:	CPSF100, KIAA1367

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	782 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.8
Subunit structure	Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF3, CSTF2 and SYMPK. Ref.6 Ref.8 Ref.11
Subcellular location	Nucleus Potential.
Sequence similarities	Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone mRNA 3'-end processing Inferred from direct assay Ref.8. Source: UniProtKB mRNA cleavage Inferred from electronic annotation. Source: InterPro mRNA export from nucleus Traceable author statement. Source: Reactome mRNA polyadenylation Inferred from electronic annotation. Source: InterPro mRNA splicing, via spliceosome Traceable author statement. Source: Reactome termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular_component	mRNA cleavage and polyadenylation specificity factor complex Inferred from direct assay PubMed 18305108Ref.11. Source: UniProtKB
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 782	782	Cleavage and polyadenylation specificity factor subunit 2		PRO_0000074393
Amino acid modifications
	Modified residue	412	1	Phosphoserine By similarity
	Modified residue	419	1	Phosphoserine Ref.9 Ref.10
	Modified residue	420	1	Phosphoserine Ref.9 Ref.10
	Modified residue	423	1	Phosphoserine Ref.7 Ref.9 Ref.10
	Modified residue	660	1	Phosphoserine Ref.9
Experimental info
	Mutagenesis	67	1	H → A: Inhibits histone 3'-end processing. Ref.8
	Mutagenesis	289	1	D → A: Does not inhibit histone 3'-end processing. Ref.8
	Mutagenesis	543	1	R → A: Inhibits histone 3'-end processing. Ref.8
	Sequence conflict	289	1	D → G in AAH70095. Ref.3
	Sequence conflict	654	1	K → R in AAH70095. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9P2I0 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: F67B4813B9883CE8	FASTA	782	88,487
	10 20 30 40 50 60 MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SMDIIDSLRK HVHQIDAVLL 70 80 90 100 110 120 SHPDPLHLGA LPYAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD 130 140 150 160 170 180 AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR 190 200 210 220 230 240 EIHLNGCSLE MLSRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA 250 260 270 280 290 300 GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN 310 320 330 340 350 360 NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK NSIILTYRTT 370 380 390 400 410 420 PGTLARFLID NPSEKITEIE LRKRVKLEGK ELEEYLEKEK LKKEAAKKLE QSKEADIDSS 430 440 450 460 470 480 DESDIEEDID QPSAHKTKHD LMMKGEGSRK GSFFKQAKKS YPMFPAPEER IKWDEYGEII 490 500 510 520 530 540 KPEDFLVPEL QATEEEKSKL ESGLTNGDEP MDQDLSDVPT KCISTTESIE IKARVTYIDY 550 560 570 580 590 600 EGRSDGDSIK KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT 610 620 630 640 650 660 SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE GELKDDGEDS 670 680 690 700 710 720 EMQVEAPSDS SVIAQQKAMK SLFGDDEKET GEESEIIPTL EPLPPHEVPG HQSVFMNEPR 730 740 750 760 770 780 LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV RRTETGRIGL EGCLCQDFYR IRDLLYEQYA IV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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]	"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-419; SER-420; SER-423 AND SER-660, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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.
[12]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00419531.
RefSeq	NP_059133.1. NM_017437.2.
UniGene	Hs.657632. Hs.736541.
3D structure databases
ProteinModelPortal	Q9P2I0.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42500N.
IntAct	Q9P2I0. 2 interactions.
MINT	MINT-1697677.
STRING	9606.ENSP00000298875.
PTM databases
PhosphoSite	Q9P2I0.
Polymorphism databases
DMDM	51338827.
Proteomic databases
PaxDb	Q9P2I0.
PeptideAtlas	Q9P2I0.
PRIDE	Q9P2I0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298875; ENSP00000298875; ENSG00000165934.
GeneID	53981.
KEGG	hsa:53981.
UCSC	uc001yah.2. human.
Organism-specific databases
CTD	53981.
GeneCards	GC14P092588.
HGNC	HGNC:2325. CPSF2.
HPA	HPA024238.
MIM	606028. gene.
neXtProt	NX_Q9P2I0.
PharmGKB	PA26842.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1236.
HOGENOM	HOG000264343.
HOVERGEN	HBG051106.
InParanoid	Q9P2I0.
KO	K14402.
OMA	NNPFQFK.
OrthoDB	EOG4MCWZQ.
PhylomeDB	Q9P2I0.
Enzyme and pathway databases
Reactome	REACT_1675. mRNA Processing. REACT_1788. Transcription. REACT_71. Gene Expression. REACT_78. Post-Elongation Processing of the Transcript.
Gene expression databases
ArrayExpress	Q9P2I0.
Bgee	Q9P2I0.
CleanEx	HS_CPSF2.
Genevestigator	Q9P2I0.
GermOnline	ENSG00000165934. Homo sapiens.
Family and domain databases
Gene3D	3.60.15.10. 3 hits.
InterPro	IPR001279. Beta-lactamas-like. IPR022712. Beta_Casp. IPR027075. CPSF2. IPR025069. Cpsf2_C. IPR011108. RMMBL. [Graphical view]
PANTHER	PTHR11203:SF5. PTHR11203:SF5. 1 hit.
Pfam	PF10996. Beta-Casp. 1 hit. PF13299. CPSF100_C. 1 hit. PF00753. Lactamase_B. 1 hit. PF07521. RMMBL. 1 hit. [Graphical view]
SMART	SM01027. Beta-Casp. 1 hit. SM00849. Lactamase_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CPSF2. human.
GenomeRNAi	53981.
NextBio	56268.
SOURCE	Search...

Entry information

Entry name

CPSF2_HUMAN

Accession

Primary (citable) accession number: Q9P2I0
Secondary accession number(s): B3KME1, Q6NSJ1, Q9H3W7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	August 16, 2004
Last modified:	May 29, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.