SGF29_MOUSE
ID SGF29_MOUSE Reviewed; 293 AA.
AC Q9DA08; Q8R0I6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=SAGA-associated factor 29 {ECO:0000305};
DE AltName: Full=Coiled-coil domain-containing protein 101;
DE AltName: Full=SAGA complex-associated factor 29 {ECO:0000312|MGI:MGI:1922815};
GN Name=Sgf29 {ECO:0000312|MGI:MGI:1922815}; Synonyms=Ccdc101;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
CC -!- FUNCTION: Chromatin reader component of some histone acetyltransferase
CC (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes.
CC SGF29 specifically recognizes and binds methylated 'Lys-4' of histone
CC H3 (H3K4me), with a preference for trimethylated form (H3K4me3). In the
CC SAGA-type complexes, SGF29 is required to recruit complexes to H3K4me.
CC Involved in the response to endoplasmic reticulum (ER) stress by
CC recruiting the SAGA complex to H3K4me, thereby promoting histone H3
CC acetylation and cell survival. {ECO:0000250|UniProtKB:Q96ES7}.
CC -!- SUBUNIT: Interacts with dimethylated and trimethylated 'Lys-4' of
CC histone H3 (H3K4me2 and H3K4me3), with a preference for the
CC trimethylated form (H3K4me3). Component of some SAGA-type complexes.
CC Component of the ADA2A-containing complex (ATAC), composed of KAT14,
CC KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By
CC similarity). Interacts with TADA3L, GCN5L2, SUPT3H and MYC (By
CC similarity). {ECO:0000250|UniProtKB:P0C606,
CC ECO:0000250|UniProtKB:Q96ES7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C606}.
CC -!- DOMAIN: The SGF29 C-terminal (also named tudor-like) domain mediates
CC binding to methylated 'Lys-4' of histone H3 (H3K4me).
CC {ECO:0000255|PROSITE-ProRule:PRU00851}.
CC -!- SIMILARITY: Belongs to the SGF29 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00851}.
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DR EMBL; AK006287; BAB24506.1; -; mRNA.
DR EMBL; AK139102; BAE23890.1; -; mRNA.
DR EMBL; AK169898; BAE41445.1; -; mRNA.
DR EMBL; BC026784; AAH26784.1; -; mRNA.
DR CCDS; CCDS21837.1; -.
DR RefSeq; NP_083615.3; NM_029339.3.
DR RefSeq; XP_017167854.1; XM_017312365.1.
DR AlphaFoldDB; Q9DA08; -.
DR SMR; Q9DA08; -.
DR BioGRID; 217581; 8.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR IntAct; Q9DA08; 3.
DR MINT; Q9DA08; -.
DR STRING; 10090.ENSMUSP00000032956; -.
DR iPTMnet; Q9DA08; -.
DR PhosphoSitePlus; Q9DA08; -.
DR EPD; Q9DA08; -.
DR MaxQB; Q9DA08; -.
DR PaxDb; Q9DA08; -.
DR PeptideAtlas; Q9DA08; -.
DR PRIDE; Q9DA08; -.
DR ProteomicsDB; 256979; -.
DR Antibodypedia; 56026; 121 antibodies from 21 providers.
DR DNASU; 75565; -.
DR Ensembl; ENSMUST00000032956; ENSMUSP00000032956; ENSMUSG00000030714.
DR GeneID; 75565; -.
DR KEGG; mmu:75565; -.
DR UCSC; uc009jse.2; mouse.
DR CTD; 112869; -.
DR MGI; MGI:1922815; Sgf29.
DR VEuPathDB; HostDB:ENSMUSG00000030714; -.
DR eggNOG; KOG3038; Eukaryota.
DR GeneTree; ENSGT00390000015229; -.
DR HOGENOM; CLU_056816_0_0_1; -.
DR InParanoid; Q9DA08; -.
DR OMA; TYIAKMG; -.
DR OrthoDB; 1040796at2759; -.
DR PhylomeDB; Q9DA08; -.
DR TreeFam; TF314958; -.
DR BioGRID-ORCS; 75565; 20 hits in 41 CRISPR screens.
DR ChiTaRS; Sgf29; mouse.
DR PRO; PR:Q9DA08; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DA08; protein.
DR Bgee; ENSMUSG00000030714; Expressed in primary oocyte and 256 other tissues.
DR ExpressionAtlas; Q9DA08; baseline and differential.
DR Genevisible; Q9DA08; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
DR GO; GO:0070461; C:SAGA-type complex; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:MGI.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
DR InterPro; IPR037802; SGF29.
DR InterPro; IPR010750; SGF29_tudor-like_dom.
DR PANTHER; PTHR21539; PTHR21539; 1.
DR Pfam; PF07039; DUF1325; 1.
DR PROSITE; PS51518; SGF29_C; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromatin regulator; Coiled coil; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..293
FT /note="SAGA-associated factor 29"
FT /id="PRO_0000274269"
FT DOMAIN 152..293
FT /note="SGF29 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT REGION 194..196
FT /note="Histone H3K4me3 N-terminus binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT REGION 240..243
FT /note="Histone H3K4me3 N-terminus binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT REGION 264..266
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT COILED 3..86
FT /evidence="ECO:0000255"
FT SITE 238
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT SITE 245
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00851"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96ES7"
FT CONFLICT 231
FT /note="E -> D (in Ref. 2; AAH26784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 33298 MW; B87D4D82670F5FFC CRC64;
MALVSADSRI AELLTELHQL IKQTQEERSR SEHNLVNIQK THERMQTENK ISPYYRTKLR
GLYTTAKTDA EAECNILRKA LDKIAEIKSL LEERRIAAKI AGLYNDSEPP RKTMRRGVLM
TLLQQSAMTL PLWIGKPGDK PPPLCGAIPA SGDYVAKPGD KVAARVKAVE GDEQWILAEV
VSYSHATNKY EVDDIDEEGK ERHTLSRRRI IPLPQWKANP ETDPEALFQK EQLVLALYPQ
TTCFYRALIH TPPQRPQDDY SVLFEDTSYA DGYSPPLNVA QRYVVACKEP KKK
