ID SGF29_HUMAN Reviewed; 293 AA. AC Q96ES7; Q96MF5; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 29-APR-2015, entry version 100. DE RecName: Full=SAGA-associated factor 29 homolog; DE AltName: Full=Coiled-coil domain-containing protein 101; GN Name=CCDC101; Synonyms=SGF29; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 MRNA]. RC TISSUE=Ovary; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX. RX PubMed=19103755; DOI=10.1128/MCB.01599-08; RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., RA Lill J.R., Zha J.; RT "The double-histone-acetyltransferase complex ATAC is essential for RT mammalian development."; RL Mol. Cell. Biol. 29:1176-1188(2009). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [5] RP METHYLATED HISTONE-BINDING, IDENTIFICATION IN A SAGA-TYPE COMPLEX, AND RP MUTAGENESIS OF TRP-175; GLU-179; PRO-214; GLN-232; TYR-238; TYR-245; RP PRO-256; PHE-264 AND ARG-282. RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020; RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., RA Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., RA Mann M.; RT "Quantitative interaction proteomics and genome-wide profiling of RT epigenetic histone marks and their readers."; RL Cell 142:967-980(2010). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 115-293 IN COMPLEX WITH RP H3K4ME2 PEPTIDE, INTERACTION WITH H3K4ME2 AND H3K4ME3, MUTAGENESIS OF RP ASP-194; ASP-196; TYR-238; GLN-240; THR-242; TYR-245; PHE-264 AND RP ASP-266, AND DOMAIN. RX PubMed=21685874; DOI=10.1038/emboj.2011.193; RA Bian C., Xu C., Ruan J., Lee K.K., Burke T.L., Tempel W., Barsyte D., RA Li J., Wu M., Zhou B.O., Fleharty B.E., Paulson A., Allali-Hassani A., RA Zhou J.Q., Mer G., Grant P.A., Workman J.L., Zang J., Min J.; RT "Sgf29 binds histone H3K4me2/3 and is required for SAGA complex RT recruitment and histone H3 acetylation."; RL EMBO J. 30:2829-2842(2011). CC -!- FUNCTION: Involved in transcriptional regulation, through CC association with histone acetyltransferase (HAT) SAGA-type CC complexes like the TFTC-HAT, ATAC or STAGA complexes. Specifically CC recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), CC with a preference for trimethylated form (H3K4me3). In the SAGA- CC type complexes, required to recruit complexes to H3K4me. May be CC involved in MYC-mediated oncogenic transformation. CC {ECO:0000269|PubMed:19103755}. CC -!- SUBUNIT: Interacts with TADA3L, GCN5L2, SUPT3H and MYC (By CC similarity). Component of some SAGA-type complexes. Interacts with CC dimethylated and trimethylated 'Lys-4' of histone H3 (H3K4me2 and CC H3K4me3), with a preference for the trimethylated form (H3K4me3). CC Component of the ADA2A-containing complex (ATAC), composed of CC CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 CC and DR1. {ECO:0000250, ECO:0000269|PubMed:19103755, CC ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:21685874}. CC -!- INTERACTION: CC A1A4H1:CCDC102B; NbExp=3; IntAct=EBI-743117, EBI-10171570; CC Q8NHS4:CLHC1; NbExp=3; IntAct=EBI-743117, EBI-10203156; CC P68431:HIST1H3D; NbExp=25; IntAct=EBI-743117, EBI-79722; CC A1A4E9:KRT13; NbExp=3; IntAct=EBI-743117, EBI-10171552; CC P19012:KRT15; NbExp=4; IntAct=EBI-743117, EBI-739566; CC Q8TBB1:LNX1; NbExp=3; IntAct=EBI-743117, EBI-739832; CC Q9NPJ6:MED4; NbExp=3; IntAct=EBI-743117, EBI-394607; CC O14777:NDC80; NbExp=4; IntAct=EBI-743117, EBI-715849; CC Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-743117, EBI-726876; CC O75528:TADA3; NbExp=4; IntAct=EBI-743117, EBI-473249; CC P15884:TCF4; NbExp=3; IntAct=EBI-743117, EBI-533224; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- DOMAIN: The SGF29 tudor-like domain mediates binding to methylated CC 'Lys-4' of histone H3 (H3K4me). {ECO:0000255|PROSITE- CC ProRule:PRU00851, ECO:0000269|PubMed:21685874}. CC -!- SIMILARITY: Belongs to the SGF29 family. {ECO:0000255|PROSITE- CC ProRule:PRU00851}. CC -!- SIMILARITY: Contains 1 SGF29 C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00851}. 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; AK057008; BAB71340.1; -; mRNA. DR EMBL; BC011981; AAH11981.1; -; mRNA. DR CCDS; CCDS10635.1; -. DR RefSeq; NP_612423.1; NM_138414.2. DR UniGene; Hs.655476; -. DR PDB; 3LX7; X-ray; 1.78 A; A=138-293. DR PDB; 3ME9; X-ray; 1.37 A; A/B=115-293. DR PDB; 3MEA; X-ray; 1.26 A; A=129-291. DR PDB; 3MET; X-ray; 2.00 A; A/B=115-293. DR PDB; 3MEU; X-ray; 1.28 A; A/B=115-293. DR PDB; 3MEV; X-ray; 1.83 A; A/B=115-293. DR PDB; 3MEW; X-ray; 1.92 A; A=129-287. DR PDBsum; 3LX7; -. DR PDBsum; 3ME9; -. DR PDBsum; 3MEA; -. DR PDBsum; 3MET; -. DR PDBsum; 3MEU; -. DR PDBsum; 3MEV; -. DR PDBsum; 3MEW; -. DR ProteinModelPortal; Q96ES7; -. DR SMR; Q96ES7; 116-291. DR BioGrid; 125213; 72. DR IntAct; Q96ES7; 19. DR MINT; MINT-3976256; -. DR STRING; 9606.ENSP00000316114; -. DR PhosphoSite; Q96ES7; -. DR BioMuta; CCDC101; -. DR DMDM; 74731608; -. DR MaxQB; Q96ES7; -. DR PaxDb; Q96ES7; -. DR PRIDE; Q96ES7; -. DR Ensembl; ENST00000317058; ENSP00000316114; ENSG00000176476. DR GeneID; 112869; -. DR KEGG; hsa:112869; -. DR UCSC; uc002dqf.3; human. DR CTD; 112869; -. DR GeneCards; GC16P028565; -. DR HGNC; HGNC:25156; CCDC101. DR HPA; HPA052590; -. DR HPA; HPA053608; -. DR MIM; 613374; gene. DR neXtProt; NX_Q96ES7; -. DR PharmGKB; PA144596468; -. DR eggNOG; NOG265941; -. DR GeneTree; ENSGT00390000015229; -. DR HOGENOM; HOG000006769; -. DR HOVERGEN; HBG059575; -. DR InParanoid; Q96ES7; -. DR KO; K11364; -. DR OMA; VPLPLMR; -. DR OrthoDB; EOG72RMZD; -. DR PhylomeDB; Q96ES7; -. DR TreeFam; TF314958; -. DR Reactome; REACT_264245; HATs acetylate histones. DR EvolutionaryTrace; Q96ES7; -. DR GenomeRNAi; 112869; -. DR NextBio; 78693; -. DR PRO; PR:Q96ES7; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; Q96ES7; -. DR CleanEx; HS_CCDC101; -. DR ExpressionAtlas; Q96ES7; baseline and differential. DR Genevestigator; Q96ES7; -. DR GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL. DR GO; GO:0070461; C:SAGA-type complex; IDA:UniProtKB. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0006325; P:chromatin organization; TAS:Reactome. DR GO; GO:0071169; P:establishment of protein localization to chromatin; TAS:UniProtKB. DR GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR010750; SGF29_tudor-like_dom. DR Pfam; PF07039; DUF1325; 1. DR PROSITE; PS51518; SGF29_C; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromatin regulator; Coiled coil; KW Complete proteome; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 293 SAGA-associated factor 29 homolog. FT /FTId=PRO_0000274268. FT DOMAIN 152 293 SGF29 C-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00851}. FT REGION 194 196 Histone H3K4me3 N-terminus binding. FT REGION 240 243 Histone H3K4me3 N-terminus binding. FT REGION 264 266 Histone H3K4me3 binding. FT COILED 3 88 {ECO:0000255}. FT BINDING 238 238 Histone H3K4me3. FT BINDING 245 245 Histone H3K4me3. FT MOD_RES 288 288 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MUTAGEN 175 175 W->A: Does not strongly affect binding to FT H3K4me. {ECO:0000269|PubMed:20850016}. FT MUTAGEN 179 179 E->A: Does not strongly affect binding to FT H3K4me. {ECO:0000269|PubMed:20850016}. FT MUTAGEN 194 194 D->A,R: Abolishes H3K4me3 binding. FT {ECO:0000269|PubMed:21685874}. FT MUTAGEN 196 196 D->R: Abolishes H3K4me3 binding. FT {ECO:0000269|PubMed:21685874}. FT MUTAGEN 214 214 P->A: Does not strongly affect binding to FT H3K4me. {ECO:0000269|PubMed:20850016}. FT MUTAGEN 232 232 Q->A: Does not strongly affect binding to FT H3K4me. {ECO:0000269|PubMed:20850016}. FT MUTAGEN 238 238 Y->A: Strongly reduced H3K4me3 binding. FT {ECO:0000269|PubMed:20850016, FT ECO:0000269|PubMed:21685874}. FT MUTAGEN 240 240 Q->A: Slightly reduced H3K4me3 binding. FT {ECO:0000269|PubMed:21685874}. FT MUTAGEN 242 242 T->A: Almost abolished H3K4me3 binding. FT {ECO:0000269|PubMed:21685874}. FT MUTAGEN 245 245 Y->A: Abolishes H3K4me3 binding. FT {ECO:0000269|PubMed:20850016, FT ECO:0000269|PubMed:21685874}. FT MUTAGEN 256 256 P->A: Does not strongly affect binding to FT H3K4me. {ECO:0000269|PubMed:20850016}. FT MUTAGEN 264 264 F->A: Strongly reduced binding to FT H3K4me3. {ECO:0000269|PubMed:20850016, FT ECO:0000269|PubMed:21685874}. FT MUTAGEN 266 266 D->A: Strongly reduced binding to FT H3K4me3. {ECO:0000269|PubMed:21685874}. FT MUTAGEN 282 282 R->A: Does not strongly affect binding to FT H3K4me. {ECO:0000269|PubMed:20850016}. FT CONFLICT 249 249 I -> N (in Ref. 1; BAB71340). FT {ECO:0000305}. FT HELIX 115 129 {ECO:0000244|PDB:3MEU}. FT STRAND 161 167 {ECO:0000244|PDB:3MEA}. FT STRAND 173 184 {ECO:0000244|PDB:3MEA}. FT TURN 185 188 {ECO:0000244|PDB:3MEA}. FT STRAND 189 194 {ECO:0000244|PDB:3MEA}. FT STRAND 201 206 {ECO:0000244|PDB:3MEA}. FT HELIX 207 209 {ECO:0000244|PDB:3MEA}. FT STRAND 210 212 {ECO:0000244|PDB:3MEA}. FT STRAND 215 217 {ECO:0000244|PDB:3MEA}. FT TURN 220 222 {ECO:0000244|PDB:3MEA}. FT HELIX 224 226 {ECO:0000244|PDB:3MEA}. FT STRAND 233 237 {ECO:0000244|PDB:3MEA}. FT STRAND 241 251 {ECO:0000244|PDB:3MEA}. FT STRAND 260 265 {ECO:0000244|PDB:3MEA}. FT STRAND 277 279 {ECO:0000244|PDB:3MEA}. FT HELIX 281 283 {ECO:0000244|PDB:3MEA}. FT STRAND 284 286 {ECO:0000244|PDB:3MEA}. SQ SEQUENCE 293 AA; 33238 MW; A1B4A8D9B0044CC7 CRC64; MALVSADSRI AELLTELHQL IKQTQEERSR SEHNLVNIQK THERMQTENK ISPYYRTKLR GLYTTAKADA EAECNILRKA LDKIAEIKSL LEERRIAAKI AGLYNDSEPP RKTMRRGVLM TLLQQSAMTL PLWIGKPGDK PPPLCGAIPA SGDYVARPGD KVAARVKAVD GDEQWILAEV VSYSHATNKY EVDDIDEEGK ERHTLSRRRV IPLPQWKANP ETDPEALFQK EQLVLALYPQ TTCFYRALIH APPQRPQDDY SVLFEDTSYA DGYSPPLNVA QRYVVACKEP KKK //