Entry euk:CPSF2_MOUSE

ID   CPSF2_MOUSE             Reviewed;         782 AA.
AC   O35218;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   10-MAY-2017, entry version 124.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 2;
DE   AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
DE            Short=CPSF 100 kDa subunit;
GN   Name=Cpsf2; Synonyms=Cpsf100, Mcpsf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tevelev A., Schatz D.G.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH ZC3H3.
RX   PubMed=16115198; DOI=10.1111/j.1365-2443.2005.00887.x;
RA   Collart C., Remacle J.E., Barabino S., van Grunsven L.A., Nelles L.,
RA   Schellens A., Van de Putte T., Pype S., Huylebroeck D.,
RA   Verschueren K.;
RT   "Smicl is a novel Smad interacting protein and cleavage and
RT   polyadenylation specificity factor associated protein.";
RL   Genes Cells 10:897-906(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420 AND
RP   SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420 AND
RP   SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Component of the cleavage and polyadenylation
CC       specificity factor (CPSF) complex that play a key role in pre-mRNA
CC       3'-end formation, recognizing the AAUAAA signal sequence and
CC       interacting with poly(A) polymerase and other factors to bring
CC       about cleavage and poly(A) addition. Involved in the histone 3'
CC       end pre-mRNA processing (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC       factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC       FIP1L1. Interacts with CPSF3, CSTF2 and SYMPK (By similarity).
CC       Interacts with ZC3H3 (PubMed:16115198).
CC       {ECO:0000250|UniProtKB:Q9P2I0, ECO:0000269|PubMed:16115198}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF012822; AAB66830.1; -; mRNA.
DR   EMBL; BC013628; AAH13628.1; -; mRNA.
DR   EMBL; BC007163; AAH07163.1; -; mRNA.
DR   CCDS; CCDS26116.1; -.
DR   RefSeq; NP_058552.1; NM_016856.3.
DR   RefSeq; XP_006516134.1; XM_006516071.3.
DR   UniGene; Mm.716; -.
DR   ProteinModelPortal; O35218; -.
DR   BioGrid; 206172; 2.
DR   IntAct; O35218; 1.
DR   MINT; MINT-4091947; -.
DR   STRING; 10090.ENSMUSP00000047797; -.
DR   iPTMnet; O35218; -.
DR   PhosphoSitePlus; O35218; -.
DR   EPD; O35218; -.
DR   MaxQB; O35218; -.
DR   PaxDb; O35218; -.
DR   PeptideAtlas; O35218; -.
DR   PRIDE; O35218; -.
DR   Ensembl; ENSMUST00000047357; ENSMUSP00000047797; ENSMUSG00000041781.
DR   GeneID; 51786; -.
DR   KEGG; mmu:51786; -.
DR   UCSC; uc007otx.2; mouse.
DR   CTD; 53981; -.
DR   MGI; MGI:1861601; Cpsf2.
DR   eggNOG; KOG1135; Eukaryota.
DR   eggNOG; COG1236; LUCA.
DR   GeneTree; ENSGT00870000136523; -.
DR   HOGENOM; HOG000264343; -.
DR   HOVERGEN; HBG051106; -.
DR   InParanoid; O35218; -.
DR   KO; K14402; -.
DR   OMA; LMRNNIN; -.
DR   OrthoDB; EOG091G03GG; -.
DR   PhylomeDB; O35218; -.
DR   TreeFam; TF106131; -.
DR   Reactome; R-MMU-109688; Cleavage of Growing Transcript in the Termination Region.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-MMU-72187; mRNA 3'-end processing.
DR   Reactome; R-MMU-77595; Processing of Intronless Pre-mRNAs.
DR   PRO; PR:O35218; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000041781; -.
DR   CleanEx; MM_CPSF2; -.
DR   Genevisible; O35218; MM.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; ISS:UniProtKB.
DR   GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR   Gene3D; 3.60.15.10; -; 2.
DR   InterPro; IPR022712; Beta_Casp.
DR   InterPro; IPR027075; CPSF2.
DR   InterPro; IPR025069; Cpsf2_C.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR011108; RMMBL.
DR   PANTHER; PTHR11203:SF41; PTHR11203:SF41; 1.
DR   Pfam; PF10996; Beta-Casp; 1.
DR   Pfam; PF13299; CPSF100_C; 1.
DR   Pfam; PF16661; Lactamase_B_6; 1.
DR   Pfam; PF07521; RMMBL; 1.
DR   SMART; SM01027; Beta-Casp; 1.
DR   SUPFAM; SSF56281; SSF56281; 2.
PE   1: Evidence at protein level;
KW   Complete proteome; mRNA processing; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding.
FT   CHAIN         1    782       Cleavage and polyadenylation specificity
FT                                factor subunit 2.
FT                                /FTId=PRO_0000074394.
FT   MOD_RES     419    419       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     420    420       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     423    423       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:17622165,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     660    660       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P2I0}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       608    779       ipfam:CPSF100_C [T]
FT   MYHIT       243    368       ismart:Beta-Casp [T]
FT   MYHIT        22    197       ipfam:Lactamase_B_6 [T]
FT   MYHIT       529    591       ipfam:RMMBL [T]
FT   MYHIT       243    367       ipfam:Beta-Casp [T]
SQ   SEQUENCE   782 AA;  88383 MW;  5F60DBB9DEDEBB4B CRC64;
     MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SVDIIDSLRK HVHQIDAVLL
     SHPDPLHLGA LPFAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD
     AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR
     EIHLNGCSLE MLSRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA
     GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
     NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK NSIILTYRTT
     PGTLARFLID NPTEKVTEIE LRKRVKLEGK ELEEYVEKEK LKKEAAKKLE QSKEADIDSS
     DESDVEEDVD QPSAHKTKHD LMMKGEGSRK GSFFKQAKKS YPMFPAPEER IKWDEYGEII
     KPEDFLVPEL QATEEEKSKL ESGLTNGEEP MDQDLSDVPT KCVSATESIE IKARVTYIDY
     EGRSDGDSIK KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT
     SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE GELKDDGEDS
     EMQVDAPSDS SAMAQQKAMK SLFGEDEKEL GEETEIIPTL EPLPPHEVPG HQSVFMNEPR
     LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV RRTETGRIGL EGCLCQDFYR IRDLLYEQYA
     IV
//