PUF60_BOVIN
ID PUF60_BOVIN Reviewed; 530 AA.
AC Q2HJG2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Poly(U)-binding-splicing factor PUF60 {ECO:0000250|UniProtKB:Q9UHX1};
DE AltName: Full=60 kDa poly(U)-binding-splicing factor {ECO:0000250|UniProtKB:Q9UHX1};
GN Name=PUF60 {ECO:0000250|UniProtKB:Q9UHX1};
GN Synonyms=Siahbp1 {ECO:0000250|UniProtKB:Q9UHX1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA- and RNA-binding protein, involved in several nuclear
CC processes such as pre-mRNA splicing, apoptosis and transcription
CC regulation. In association with FUBP1 regulates MYC transcription at
CC the P2 promoter through the core-TFIIH basal transcription factor. Acts
CC as a transcriptional repressor through the core-TFIIH basal
CC transcription factor. Represses FUBP1-induced transcriptional
CC activation but not basal transcription. Decreases ERCC3 helicase
CC activity. Is also involved in pre-mRNA splicing. Promotes splicing of
CC an intron with weak 3'-splice site and pyrimidine tract in a
CC cooperative manner with U2AF2. Involved in apoptosis induction when
CC overexpressed in HeLa cells. Modulates alternative splicing of several
CC mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the
CC pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is
CC enhanced in presence of U2AF2. Binds to Y5 RNA in association with
CC RO60. Binds to poly(U) RNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Associates with the spliceosome (By
CC similarity). Found in a complex with RO60 and Y5 RNA (By similarity).
CC Found in a complex with FUBP1 and far upstream element (FUSE) DNA
CC segment (By similarity). Interacts directly with ERCC3 (By similarity).
CC Interacts with CDK7 and GTF2H1 (By similarity). Interacts with
CC SRSF11/P54 (By similarity). {ECO:0000250|UniProtKB:Q9UHX1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UHX1}.
CC Note=Colocalizes partially with RO60. {ECO:0000250|UniProtKB:Q9UHX1}.
CC -!- DOMAIN: The third RNA recognition motif, called PUMP domain, is
CC atypical and may rather mediate homodimerization and/or protein-protein
CC interactions.
CC -!- SIMILARITY: Belongs to the RRM half pint family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC105447; AAI05448.1; -; mRNA.
DR RefSeq; NP_001039598.1; NM_001046133.2.
DR AlphaFoldDB; Q2HJG2; -.
DR BMRB; Q2HJG2; -.
DR SMR; Q2HJG2; -.
DR STRING; 9913.ENSBTAP00000002882; -.
DR PaxDb; Q2HJG2; -.
DR PeptideAtlas; Q2HJG2; -.
DR PRIDE; Q2HJG2; -.
DR GeneID; 512824; -.
DR KEGG; bta:512824; -.
DR CTD; 22827; -.
DR eggNOG; KOG0124; Eukaryota.
DR InParanoid; Q2HJG2; -.
DR OrthoDB; 861359at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12370; RRM1_PUF60; 1.
DR CDD; cd12371; RRM2_PUF60; 1.
DR CDD; cd12648; RRM3_UHM_PUF60; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR006532; PUF60-like.
DR InterPro; IPR034209; PUF60_RRM1.
DR InterPro; IPR034211; PUF60_RRM2.
DR InterPro; IPR034212; PUF60_RRM3.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01645; half-pint; 1.
DR PROSITE; PS50102; RRM; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; DNA-binding; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Ribonucleoprotein; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..530
FT /note="Poly(U)-binding-splicing factor PUF60"
FT /id="PRO_0000299518"
FT DOMAIN 100..178
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 197..275
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 433..520
FT /note="RRM 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..487
FT /note="Inhibits homodimerization"
FT /evidence="ECO:0000250"
FT REGION 48..530
FT /note="Inhibits transcriptional repression, interaction
FT with ERCC3 and apoptosis induction"
FT /evidence="ECO:0000250"
FT REGION 387..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEB3"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT MOD_RES 285
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT MOD_RES 425
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
SQ SEQUENCE 530 AA; 57087 MW; BB9C5E066B2CDA46 CRC64;
MATATIALGT DSIKMENGQG TAAKLGLPPL TPEQQEALQK AKKYAMEQSI KSVLVKQTIA
HQQQQLTNLQ MAAVTMGFGD PLSPLQSMAA QRQRALAIMC RVYVGSIYYE LGEDTIRQAF
APFGPIKSID MSWDSVTMKH KGFAFVEYEV PEAAQLALEQ MNSVMLGGRN IKVGRPSNIG
QAQPIIDQLA EEARAFNRIY VASVHQDLSD DDIKSVFEAF GKIKSCTLAR DPTTGKHKGY
GFIEYEKAQS SQDAVSSMNL FDLGGQYLRV GKAVTPPMPL LTPATPGGLP PAAAVAAAAA
TAKITAQEAV AGAAVLGTLA TPGLVSPALT LAQPLGALPQ AVMAAQAPGV ITGVTPARPP
IPVTIPSVGV VNPILASPPT LGLLEPKKEK EEEELFPESE RPEMLSEQEH MSISGSSARH
MVMQKLLRKQ ESTVMVLRNM VDPKDIDDDL EGEVTEECGK FGAVNRVIIY QEKQGEEEDA
EIIVKIFVEF SVASETHKAI QDLNGRWFAG RKVVAEVYDQ ERFDNSDLSA
