SFR1_HUMAN
ID SFR1_HUMAN Reviewed; 245 AA.
AC Q86XK3; A8K569; B2RTV8; Q5JT39; Q5JT40; Q8WW47;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Swi5-dependent recombination DNA repair protein 1 homolog;
DE AltName: Full=Meiosis protein 5 homolog;
GN Name=SFR1; Synonyms=C10orf78, MEI5, MEIR5;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-19.
RC TISSUE=Brain, and Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE SWI5-SFR1 COMPLEX, INTERACTION WITH RAD51,
RP AND TISSUE SPECIFICITY.
RX PubMed=21252223; DOI=10.1074/jbc.m110.207290;
RA Yuan J., Chen J.;
RT "The role of human SWI5-MEI5 complex in homologous recombination repair.";
RL J. Biol. Chem. 286:9888-9893(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 3), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP INTERACTION WITH ESR1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=23874500; DOI=10.1371/journal.pone.0068075;
RA Feng Y., Singleton D., Guo C., Gardner A., Pakala S., Kumar R., Jensen E.,
RA Zhang J., Khan S.;
RT "DNA homologous recombination factor SFR1 physically and functionally
RT interacts with estrogen receptor alpha.";
RL PLoS ONE 8:E68075-E68075(2013).
CC -!- FUNCTION: Component of the SWI5-SFR1 complex, a complex required for
CC double-strand break repair via homologous recombination
CC (PubMed:21252223). Acts as a transcriptional modulator for ESR1
CC (PubMed:23874500). {ECO:0000269|PubMed:21252223,
CC ECO:0000269|PubMed:23874500}.
CC -!- SUBUNIT: Component of the SWI5-SFR1 complex. Interacts with RAD51; the
CC interaction is weak (PubMed:21252223). Interacts with ESR1 in the
CC ligand-independent and ligand-dependent manner (PubMed:23874500).
CC {ECO:0000269|PubMed:21252223, ECO:0000269|PubMed:23874500}.
CC -!- INTERACTION:
CC Q86XK3; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-1104535, EBI-739624;
CC Q86XK3; Q6NT76-2: HMBOX1; NbExp=3; IntAct=EBI-1104535, EBI-10212206;
CC Q86XK3; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-1104535, EBI-748896;
CC Q86XK3; O14777: NDC80; NbExp=3; IntAct=EBI-1104535, EBI-715849;
CC Q86XK3; Q13287: NMI; NbExp=6; IntAct=EBI-1104535, EBI-372942;
CC Q86XK3; Q6NUQ1: RINT1; NbExp=4; IntAct=EBI-1104535, EBI-726876;
CC Q86XK3; O75150: RNF40; NbExp=3; IntAct=EBI-1104535, EBI-744408;
CC Q86XK3; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-1104535, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23874500}.
CC Note=Colocalizes with ESR1 in the nucleus.
CC {ECO:0000269|PubMed:23874500}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86XK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86XK3-2; Sequence=VSP_040038;
CC Name=3;
CC IsoId=Q86XK3-3; Sequence=VSP_040037;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21252223}.
CC -!- SIMILARITY: Belongs to the SFR1/MEI5 family. {ECO:0000305}.
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DR EMBL; AK291184; BAF83873.1; -; mRNA.
DR EMBL; AL357336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49610.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49611.1; -; Genomic_DNA.
DR EMBL; BC020892; AAH20892.2; -; mRNA.
DR EMBL; BC140835; AAI40836.1; -; mRNA.
DR CCDS; CCDS31279.1; -. [Q86XK3-1]
DR CCDS; CCDS31280.1; -. [Q86XK3-3]
DR RefSeq; NP_001002759.1; NM_001002759.1. [Q86XK3-1]
DR RefSeq; NP_660290.3; NM_145247.4. [Q86XK3-3]
DR RefSeq; XP_005269578.1; XM_005269521.3. [Q86XK3-2]
DR RefSeq; XP_016871161.1; XM_017015672.1.
DR AlphaFoldDB; Q86XK3; -.
DR SMR; Q86XK3; -.
DR BioGRID; 125639; 33.
DR IntAct; Q86XK3; 12.
DR STRING; 9606.ENSP00000358742; -.
DR iPTMnet; Q86XK3; -.
DR PhosphoSitePlus; Q86XK3; -.
DR BioMuta; SFR1; -.
DR DMDM; 311033362; -.
DR EPD; Q86XK3; -.
DR jPOST; Q86XK3; -.
DR MassIVE; Q86XK3; -.
DR MaxQB; Q86XK3; -.
DR PaxDb; Q86XK3; -.
DR PeptideAtlas; Q86XK3; -.
DR PRIDE; Q86XK3; -.
DR ProteomicsDB; 70291; -. [Q86XK3-1]
DR ProteomicsDB; 70292; -. [Q86XK3-2]
DR ProteomicsDB; 70293; -. [Q86XK3-3]
DR Antibodypedia; 48828; 90 antibodies from 13 providers.
DR DNASU; 119392; -.
DR Ensembl; ENST00000369727.4; ENSP00000358742.3; ENSG00000156384.15. [Q86XK3-1]
DR Ensembl; ENST00000369729.7; ENSP00000358744.3; ENSG00000156384.15. [Q86XK3-3]
DR GeneID; 119392; -.
DR KEGG; hsa:119392; -.
DR MANE-Select; ENST00000369727.4; ENSP00000358742.3; NM_001002759.2; NP_001002759.1.
DR UCSC; uc001kxs.3; human. [Q86XK3-1]
DR CTD; 119392; -.
DR DisGeNET; 119392; -.
DR GeneCards; SFR1; -.
DR HGNC; HGNC:29574; SFR1.
DR HPA; ENSG00000156384; Low tissue specificity.
DR MIM; 616527; gene.
DR neXtProt; NX_Q86XK3; -.
DR OpenTargets; ENSG00000156384; -.
DR PharmGKB; PA134989928; -.
DR VEuPathDB; HostDB:ENSG00000156384; -.
DR eggNOG; ENOG502S1QX; Eukaryota.
DR GeneTree; ENSGT00390000018550; -.
DR HOGENOM; CLU_075586_1_0_1; -.
DR InParanoid; Q86XK3; -.
DR OMA; RNEEEFM; -.
DR OrthoDB; 1628702at2759; -.
DR PhylomeDB; Q86XK3; -.
DR TreeFam; TF332725; -.
DR PathwayCommons; Q86XK3; -.
DR SignaLink; Q86XK3; -.
DR BioGRID-ORCS; 119392; 67 hits in 1079 CRISPR screens.
DR ChiTaRS; SFR1; human.
DR GenomeRNAi; 119392; -.
DR Pharos; Q86XK3; Tbio.
DR PRO; PR:Q86XK3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86XK3; protein.
DR Bgee; ENSG00000156384; Expressed in epithelial cell of pancreas and 180 other tissues.
DR Genevisible; Q86XK3; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032798; C:Swi5-Sfr1 complex; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR042429; SFR1.
DR InterPro; IPR018468; SFR1/Mei5.
DR PANTHER; PTHR28643; PTHR28643; 1.
DR Pfam; PF10376; Mei5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; DNA damage; DNA repair;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..245
FT /note="Swi5-dependent recombination DNA repair protein 1
FT homolog"
FT /id="PRO_0000089805"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..177
FT /evidence="ECO:0000255"
FT COMPBIAS 13..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP27"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040037"
FT VAR_SEQ 1..4
FT /note="MAEG -> MKNLVVPMWEGKWKTAKRARMNYKVKLEEISGLLVDALYTNTIY
FT YLIKVDYREVWLIRLFYNFSFL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040038"
FT VARIANT 19
FT /note="D -> G (in dbSNP:rs10786783)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_023098"
FT MOD_RES Q86XK3-3:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 245 AA; 28262 MW; 65CCD48BAD5C45AD CRC64;
MAEGEKNQDF TFKMESPSDS AVVLPSTPQA SANPSSPYTN SSRKQPMSAT LRERLRKTRF
SFNSSYNVVK RLKVESEEND QTFSEKPASS TEENCLEFQE SFKHIDSEFE ENTNLKNTLK
NLNVCESQSL DSGSCSALQN EFVSEKLPKQ RLNAEKAKLV KQVQEKEDLL RRLKLVKMYR
SKNDLSQLQL LIKKWRSCSQ LLLYELQSAV SEENKKLSLT QLIDHYGLDD KLLHYNRSEE
EFIDV
