ID A0A7P0T9U7_HUMAN Unreviewed; 764 AA. AC A0A7P0T9U7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 03-AUG-2022, entry version 5. DE RecName: Full=Splicing factor 1 {ECO:0000256|RuleBase:RU367126}; GN Name=SF1 {ECO:0000313|Ensembl:ENSP00000505779}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000505779, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000505779, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000505779} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2021) to UniProtKB. CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. Has a role in the CC recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract CC and the 3'-splice site at the 3'-end of introns. CC {ECO:0000256|RuleBase:RU367126}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|RuleBase:RU367126}. CC -!- SIMILARITY: Belongs to the BBP/SF1 family. CC {ECO:0000256|ARBA:ARBA00010382, ECO:0000256|RuleBase:RU367126}. 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; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A7P0T9U7; -. DR PeptideAtlas; A0A7P0T9U7; -. DR Ensembl; ENST00000681407.1; ENSP00000505779.1; ENSG00000168066.21. DR HGNC; HGNC:12950; SF1. DR GeneTree; ENSGT00940000157258; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000168066; Expressed in right uterine tube and 210 other tissues. DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW. DR GO; GO:0045131; F:pre-mRNA branch point binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1370.10; -; 1. DR InterPro; IPR045071; BBP-like. DR InterPro; IPR031150; BBP/SF1. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR InterPro; IPR032570; SF1-HH. DR InterPro; IPR001878; Znf_CCHC. DR PANTHER; PTHR11208; PTHR11208; 1. DR PANTHER; PTHR11208:SF45; PTHR11208:SF45; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF16275; SF1-HH; 1. DR Pfam; PF00098; zf-CCHC; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00343; ZnF_C2HC; 1. DR SUPFAM; SSF54791; SSF54791; 1. DR PROSITE; PS50158; ZF_CCHC; 1. PE 1: Evidence at protein level; KW Metal-binding {ECO:0000256|RuleBase:RU367126}; KW mRNA processing {ECO:0000256|RuleBase:RU367126}; KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187, KW ECO:0000256|RuleBase:RU367126}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367126}; KW Proteomics identification {ECO:0007829|EPD:A0A7P0T9U7, KW ECO:0007829|MaxQB:A0A7P0T9U7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Spliceosome {ECO:0000256|RuleBase:RU367126}; KW Zinc {ECO:0000256|RuleBase:RU367126}; KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047, KW ECO:0000256|RuleBase:RU367126}. FT DOMAIN 404..418 FT /note="CCHC-type" FT /evidence="ECO:0000259|PROSITE:PS50158" FT REGION 1..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 190..219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 450..764 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 13..55 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 65..126 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 471..486 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 540..570 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 597..643 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 644..686 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 689..735 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 750..764 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 764 AA; 80370 MW; A4B3A1A996AB9FD8 CRC64; MATGANATPL GKLGPPGLPP LPGPKGGFEP GPPPAPGPGA GLLAPGPPPP PPVGSMGALT AAFPFAALPP PPPPPPPPPP QQPPPPPPPP SPGASYPPPQ PPPPPPLYQR VSPPQPPPPQ PPRKDQQPGP AGGGGDFPSK KRKRSRWNQD TMEQKTVIPG MPTVIPPGLT REQERAYIVQ LQIEDLTRKL RTGDLGIPPN PEDRSPSPEP IYNSEGKRLN TREFRTRKKL EEERHNLITE MVALNPDFKP PADYKPPATR VSDKVMIPQD EYPEINFVGL LIGPRGNTLK NIEKECNAKI MIRGKGSVKE GKVGRKDGQM LPGEDEPLHA LVTANTMENV KKAVEQIRNI LKQGIETPED QNDLRKMQLR ELARLNGTLR EDDNRILRPW QSSETRSITN TTVCTKCGGA GHIASDCKFQ RPGDPQSAQD KARMDKEYLS LMAELGEAPV PASVGSTSGP ATTPLASAPR PAAPANNPPP PSLMSTTQSR PPWMNSGPSE SRPYHGMHGG GPGGPGGGPH SFPHPLPSLT GGHGGHPMQH NPNGPPPPWM QPPPPPMNQG PHPPGHHGPP PMDQYLGSTP VGSGVYRLHQ GKGMMPPPPM GMMPPPPPPP SGQPPPPPSG PLPPWQQQQQ QPPPPPPPSS SMASSTPLPW QQNTTTTTTS AGTGSIPPWQ QQQAAAAASP GAPQMQGNPT MVPLPPGVQP PLPPGAPPPP PPPPPGSAGM MYAPPPPPPP PMDPSNFVTM MGMGVAGMPP FGMPPAPPPP PPQN //