PUF60_PONAB
ID PUF60_PONAB Reviewed; 558 AA.
AC Q5R469; Q5RFS8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Heart;
RG The German cDNA consortium;
RL Submitted (APR-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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R469-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R469-2; Sequence=VSP_027722, VSP_027723;
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}.
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DR EMBL; CR857074; CAH89379.1; -; mRNA.
DR EMBL; CR861389; CAH93447.1; -; mRNA.
DR RefSeq; NP_001127017.1; NM_001133545.1. [Q5R469-1]
DR RefSeq; NP_001128734.1; NM_001135262.1.
DR AlphaFoldDB; Q5R469; -.
DR BMRB; Q5R469; -.
DR SMR; Q5R469; -.
DR STRING; 9601.ENSPPYP00000021256; -.
DR PRIDE; Q5R469; -.
DR GeneID; 100174042; -.
DR GeneID; 100189623; -.
DR KEGG; pon:100174042; -.
DR CTD; 22827; -.
DR eggNOG; KOG0124; Eukaryota.
DR InParanoid; Q5R469; -.
DR OrthoDB; 861359at2759; -.
DR Proteomes; UP000001595; 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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; Alternative splicing; Apoptosis; DNA-binding; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..558
FT /note="Poly(U)-binding-splicing factor PUF60"
FT /id="PRO_0000299521"
FT DOMAIN 128..206
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 225..303
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 461..548
FT /note="RRM 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..515
FT /note="Inhibits homodimerization"
FT /evidence="ECO:0000250"
FT REGION 76..558
FT /note="Inhibits transcriptional repression, interaction
FT with ERCC3 and apoptosis induction"
FT /evidence="ECO:0000250"
FT REGION 415..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEB3"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT MOD_RES 453
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT CROSSLNK 79
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX1"
FT VAR_SEQ 9..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_027722"
FT VAR_SEQ 100..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_027723"
FT CONFLICT 418
FT /note="R -> K (in Ref. 1; CAH89379)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 59832 MW; 39F821147BA5030B CRC64;
MATATIALQV NGQQGGGSEP AAAAVVAAGD KWKPPQGTDS IKMENGQSTA AKLGLPPLTP
EQQEALQKAK KYAMEQSIKS VLVKQTIAHQ QQQLTNLQMA AVTMGFGDPL SPLQSMAAQR
QRALAIMCRV YVGSIYYELG EDTIRQAFAP FGPIKSIDMS WDSVTMKHKG FAFVEYEVPE
AAQLALEQMN SVMLGGRNIK VGRPSNIGQA QPIIDQLAEE ARAFNRIYVA SVHQDLSDDD
IKSVFEAFGK IKSCTLARDP TTGKHKGYGF IEYEKAQSSQ DAVSSMNLFD LGGQYLRVGK
AVTPPMPLLT PATPGGLPPA AAVAAAAATA KITAQEAVAG AAVLGTLGTP GLVSPALTLA
QPLGTLPQAV MAAQAPGVIT GVTPARPPIP VTIPSVGVVN PILASPPTLG LLEPKKEREE
EELFPESERP EMLSEQEHMS ISGSSARHMV MQKLLRKQES TVMVLRNMVD PKDIDDDLEG
EVTEECGKFG AVNRVIIYQE KQGEEEDAEI IVKIFVEFSI ASETHKAIQA LNGRWFAGRK
VVAEVYDQER FDNSDLSA
