SGF29_RAT
ID SGF29_RAT Reviewed; 293 AA.
AC P0C606;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=SAGA-associated factor 29 {ECO:0000305};
DE Short=rSGF29;
DE AltName: Full=Coiled-coil domain-containing protein 101;
DE AltName: Full=SAGA complex-associated factor 29 {ECO:0000312|RGD:1310609};
GN Name=Sgf29 {ECO:0000312|RGD:1310609}; Synonyms=Ccdc101;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP TADA3L; GCN5L2; SUPT3H AND MYC.
RX PubMed=17334388; DOI=10.1038/sj.onc.1210349;
RA Kurabe N., Katagiri K., Komiya Y., Ito R., Sugiyama A., Kawasaki Y.,
RA Tashiro F.;
RT "Deregulated expression of a novel component of TFTC/STAGA histone
RT acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma:
RT possible implication for the oncogenic potential of c-Myc.";
RL Oncogene 26:5626-5634(2007).
CC -!- FUNCTION: Chromatin reader component of some histone acetyltransferase
CC (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes
CC (PubMed:17334388). SGF29 specifically recognizes and binds methylated
CC 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated
CC form (H3K4me3) (By similarity). In the SAGA-type complexes, SGF29 is
CC required to recruit complexes to H3K4me (By similarity). Involved in
CC the response to endoplasmic reticulum (ER) stress by recruiting the
CC SAGA complex to H3K4me, thereby promoting histone H3 acetylation and
CC cell survival (By similarity). May be involved in MYC-mediated
CC oncogenic transformation (PubMed:17334388).
CC {ECO:0000250|UniProtKB:Q96ES7, ECO:0000269|PubMed:17334388}.
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
CC (PubMed:17334388). {ECO:0000250|UniProtKB:Q96ES7,
CC ECO:0000269|PubMed:17334388}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17334388}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis.
CC Highly expressed in hepatoma and other tumor cell lines.
CC {ECO:0000269|PubMed:17334388}.
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; AABR03005493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03001099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006230293.1; XM_006230231.3.
DR RefSeq; XP_006230294.1; XM_006230232.3.
DR AlphaFoldDB; P0C606; -.
DR SMR; P0C606; -.
DR STRING; 10116.ENSRNOP00000026146; -.
DR iPTMnet; P0C606; -.
DR PhosphoSitePlus; P0C606; -.
DR PaxDb; P0C606; -.
DR GeneID; 293488; -.
DR UCSC; RGD:1310609; rat.
DR CTD; 112869; -.
DR RGD; 1310609; Sgf29.
DR VEuPathDB; HostDB:ENSRNOG00000019245; -.
DR eggNOG; KOG3038; Eukaryota.
DR HOGENOM; CLU_056816_0_0_1; -.
DR InParanoid; P0C606; -.
DR OMA; TYIAKMG; -.
DR OrthoDB; 1040796at2759; -.
DR PhylomeDB; P0C606; -.
DR TreeFam; TF314958; -.
DR PRO; PR:P0C606; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019245; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; P0C606; baseline and differential.
DR Genevisible; P0C606; RN.
DR GO; GO:0140672; C:ATAC complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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; IPI:RGD.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
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:RGD.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:RGD.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:RGD.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0051302; P:regulation of cell division; ISO:RGD.
DR GO; GO:0045995; P:regulation of embryonic development; ISO:RGD.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:RGD.
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 1: Evidence at protein 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_0000314027"
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..88
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"
SQ SEQUENCE 293 AA; 33268 MW; 52D0E6F27AA89580 CRC64;
MALVSADSRI AELLTELHQL IKQTQEERSR SEHNLVNIQK THERMQTENK ISPYYRTKLR
GLYTTAKADA EAECNILRKA LDKIAEIKSL LEERRIAAKI AGLYNDSEPP RKTMRRGVLM
TLLQQSAMTL PLWIGKPGDK PPPLCGAIPA SGDYVAKPGD KVAARVKAVE GDEQWILAEV
VSYSHATNKY EVDDIDEEGK ERHTLSRRRI IPLPQWKANP ETDPEALFQK EQLVLALYPQ
TTCFYRALIH TPPQRPQDDY SVLFEDTSYA DGYSPPLNVA QRYVVACKEP KKK
