Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

SAGA-associated factor 29

Gene

SGF29

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in transcriptional regulation, through association with histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes. Specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). In the SAGA-type complexes, required to recruit complexes to H3K4me. May be involved in MYC-mediated oncogenic transformation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei238 – 2381Histone H3K4me3
Binding sitei245 – 2451Histone H3K4me3

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

GO - Biological processi

  • chromatin organization Source: Reactome
  • establishment of protein localization to chromatin Source: UniProtKB
  • histone H3 acetylation Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
SAGA-associated factor 29Curated
Alternative name(s):
Coiled-coil domain-containing protein 101
SAGA complex-associated factor 29Imported
Gene namesi
Name:SGF29Imported
Synonyms:CCDC101
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25156. SGF29.

Subcellular locationi

GO - Cellular componenti

  • Ada2/Gcn5/Ada3 transcription activator complex Source: BHF-UCL
  • SAGA-type complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi175 – 1751W → A: Does not strongly affect binding to H3K4me. 1 Publication
Mutagenesisi179 – 1791E → A: Does not strongly affect binding to H3K4me. 1 Publication
Mutagenesisi194 – 1941D → A or R: Abolishes H3K4me3 binding. 1 Publication
Mutagenesisi196 – 1961D → R: Abolishes H3K4me3 binding. 1 Publication
Mutagenesisi214 – 2141P → A: Does not strongly affect binding to H3K4me. 1 Publication
Mutagenesisi232 – 2321Q → A: Does not strongly affect binding to H3K4me. 1 Publication
Mutagenesisi238 – 2381Y → A: Strongly reduced H3K4me3 binding. 2 Publications
Mutagenesisi240 – 2401Q → A: Slightly reduced H3K4me3 binding. 1 Publication
Mutagenesisi242 – 2421T → A: Almost abolished H3K4me3 binding. 1 Publication
Mutagenesisi245 – 2451Y → A: Abolishes H3K4me3 binding. 2 Publications
Mutagenesisi256 – 2561P → A: Does not strongly affect binding to H3K4me. 1 Publication
Mutagenesisi264 – 2641F → A: Strongly reduced binding to H3K4me3. 2 Publications
Mutagenesisi266 – 2661D → A: Strongly reduced binding to H3K4me3. 1 Publication
Mutagenesisi282 – 2821R → A: Does not strongly affect binding to H3K4me. 1 Publication

Organism-specific databases

PharmGKBiPA144596468.

Polymorphism and mutation databases

BioMutaiCCDC101.
DMDMi74731608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293SAGA-associated factor 29PRO_0000274268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei288 – 2881N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ96ES7.
MaxQBiQ96ES7.
PaxDbiQ96ES7.
PRIDEiQ96ES7.

PTM databases

iPTMnetiQ96ES7.
PhosphoSiteiQ96ES7.

Expressioni

Gene expression databases

BgeeiQ96ES7.
CleanExiHS_CCDC101.
ExpressionAtlasiQ96ES7. baseline and differential.
GenevisibleiQ96ES7. HS.

Organism-specific databases

HPAiHPA052590.
HPA053608.

Interactioni

Subunit structurei

Interacts with TADA3L, GCN5L2, SUPT3H and MYC (By similarity). Component of some SAGA-type complexes. Interacts with dimethylated and trimethylated 'Lys-4' of histone H3 (H3K4me2 and H3K4me3), with a preference for the trimethylated form (H3K4me3). Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC102BA1A4H13EBI-743117,EBI-10171570
CLHC1Q8NHS43EBI-743117,EBI-10203156
HIST1H3FP6843125EBI-743117,EBI-79722
KRT13A1A4E93EBI-743117,EBI-10171552
KRT15P190124EBI-743117,EBI-739566
LNX1Q8TBB13EBI-743117,EBI-739832
MED4Q9NPJ63EBI-743117,EBI-394607
NDC80O147774EBI-743117,EBI-715849
RINT1Q6NUQ13EBI-743117,EBI-726876
TADA3O755285EBI-743117,EBI-473249
TCF4P158844EBI-743117,EBI-533224

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi125213. 86 interactions.
IntActiQ96ES7. 37 interactions.
MINTiMINT-3976256.
STRINGi9606.ENSP00000316114.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi115 – 12915Combined sources
Beta strandi161 – 1677Combined sources
Beta strandi173 – 18412Combined sources
Turni185 – 1884Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi201 – 2066Combined sources
Helixi207 – 2093Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi215 – 2173Combined sources
Turni220 – 2223Combined sources
Helixi224 – 2263Combined sources
Beta strandi233 – 2375Combined sources
Beta strandi241 – 25111Combined sources
Beta strandi260 – 2656Combined sources
Beta strandi277 – 2793Combined sources
Helixi281 – 2833Combined sources
Beta strandi284 – 2863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LX7X-ray1.78A138-293[»]
3ME9X-ray1.37A/B115-293[»]
3MEAX-ray1.26A129-291[»]
3METX-ray2.00A/B115-293[»]
3MEUX-ray1.28A/B115-293[»]
3MEVX-ray1.83A/B115-293[»]
3MEWX-ray1.92A129-287[»]
5C0MX-ray1.60A/B115-293[»]
ProteinModelPortaliQ96ES7.
SMRiQ96ES7. Positions 116-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96ES7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 293142SGF29 C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 1963Histone H3K4me3 N-terminus binding
Regioni240 – 2434Histone H3K4me3 N-terminus binding
Regioni264 – 2663Histone H3K4me3 binding

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili3 – 8886Sequence analysisAdd
BLAST

Domaini

The SGF29 tudor-like domain mediates binding to methylated 'Lys-4' of histone H3 (H3K4me).PROSITE-ProRule annotation1 Publication

Sequence similaritiesi

Belongs to the SGF29 family.PROSITE-ProRule annotation
Contains 1 SGF29 C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3038. Eukaryota.
ENOG410XPFD. LUCA.
GeneTreeiENSGT00390000015229.
HOGENOMiHOG000006769.
HOVERGENiHBG059575.
InParanoidiQ96ES7.
KOiK11364.
OMAiTCFYKAV.
OrthoDBiEOG72RMZD.
PhylomeDBiQ96ES7.
TreeFamiTF314958.

Family and domain databases

InterProiIPR010750. SGF29_tudor-like_dom.
[Graphical view]
PfamiPF07039. DUF1325. 1 hit.
[Graphical view]
PROSITEiPS51518. SGF29_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96ES7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALVSADSRI AELLTELHQL IKQTQEERSR SEHNLVNIQK THERMQTENK
60 70 80 90 100
ISPYYRTKLR GLYTTAKADA EAECNILRKA LDKIAEIKSL LEERRIAAKI
110 120 130 140 150
AGLYNDSEPP RKTMRRGVLM TLLQQSAMTL PLWIGKPGDK PPPLCGAIPA
160 170 180 190 200
SGDYVARPGD KVAARVKAVD GDEQWILAEV VSYSHATNKY EVDDIDEEGK
210 220 230 240 250
ERHTLSRRRV IPLPQWKANP ETDPEALFQK EQLVLALYPQ TTCFYRALIH
260 270 280 290
APPQRPQDDY SVLFEDTSYA DGYSPPLNVA QRYVVACKEP KKK
Length:293
Mass (Da):33,238
Last modified:December 1, 2001 - v1
Checksum:iA1B4A8D9B0044CC7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti249 – 2491I → N in BAB71340 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK057008 mRNA. Translation: BAB71340.1.
BC011981 mRNA. Translation: AAH11981.1.
CCDSiCCDS10635.1.
RefSeqiNP_612423.1. NM_138414.2.
UniGeneiHs.655476.

Genome annotation databases

EnsembliENST00000317058; ENSP00000316114; ENSG00000176476.
GeneIDi112869.
KEGGihsa:112869.
UCSCiuc002dqf.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK057008 mRNA. Translation: BAB71340.1.
BC011981 mRNA. Translation: AAH11981.1.
CCDSiCCDS10635.1.
RefSeqiNP_612423.1. NM_138414.2.
UniGeneiHs.655476.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LX7X-ray1.78A138-293[»]
3ME9X-ray1.37A/B115-293[»]
3MEAX-ray1.26A129-291[»]
3METX-ray2.00A/B115-293[»]
3MEUX-ray1.28A/B115-293[»]
3MEVX-ray1.83A/B115-293[»]
3MEWX-ray1.92A129-287[»]
5C0MX-ray1.60A/B115-293[»]
ProteinModelPortaliQ96ES7.
SMRiQ96ES7. Positions 116-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125213. 86 interactions.
IntActiQ96ES7. 37 interactions.
MINTiMINT-3976256.
STRINGi9606.ENSP00000316114.

PTM databases

iPTMnetiQ96ES7.
PhosphoSiteiQ96ES7.

Polymorphism and mutation databases

BioMutaiCCDC101.
DMDMi74731608.

Proteomic databases

EPDiQ96ES7.
MaxQBiQ96ES7.
PaxDbiQ96ES7.
PRIDEiQ96ES7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317058; ENSP00000316114; ENSG00000176476.
GeneIDi112869.
KEGGihsa:112869.
UCSCiuc002dqf.4. human.

Organism-specific databases

CTDi112869.
GeneCardsiCCDC101.
HGNCiHGNC:25156. SGF29.
HPAiHPA052590.
HPA053608.
MIMi613374. gene.
neXtProtiNX_Q96ES7.
PharmGKBiPA144596468.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3038. Eukaryota.
ENOG410XPFD. LUCA.
GeneTreeiENSGT00390000015229.
HOGENOMiHOG000006769.
HOVERGENiHBG059575.
InParanoidiQ96ES7.
KOiK11364.
OMAiTCFYKAV.
OrthoDBiEOG72RMZD.
PhylomeDBiQ96ES7.
TreeFamiTF314958.

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTraceiQ96ES7.
GenomeRNAii112869.
NextBioi78693.
PROiQ96ES7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96ES7.
CleanExiHS_CCDC101.
ExpressionAtlasiQ96ES7. baseline and differential.
GenevisibleiQ96ES7. HS.

Family and domain databases

InterProiIPR010750. SGF29_tudor-like_dom.
[Graphical view]
PfamiPF07039. DUF1325. 1 hit.
[Graphical view]
PROSITEiPS51518. SGF29_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. "The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
    Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
    Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
  4. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
    Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
    Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATED HISTONE-BINDING, IDENTIFICATION IN A SAGA-TYPE COMPLEX, MUTAGENESIS OF TRP-175; GLU-179; PRO-214; GLN-232; TYR-238; TYR-245; PRO-256; PHE-264 AND ARG-282.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation."
    Bian C., Xu C., Ruan J., Lee K.K., Burke T.L., Tempel W., Barsyte D., Li J., Wu M., Zhou B.O., Fleharty B.E., Paulson A., Allali-Hassani A., Zhou J.Q., Mer G., Grant P.A., Workman J.L., Zang J., Min J.
    EMBO J. 30:2829-2842(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 115-293 IN COMPLEX WITH H3K4ME2 PEPTIDE, INTERACTION WITH H3K4ME2 AND H3K4ME3, MUTAGENESIS OF ASP-194; ASP-196; TYR-238; GLN-240; THR-242; TYR-245; PHE-264 AND ASP-266, DOMAIN.

Entry informationi

Entry nameiSGF29_HUMAN
AccessioniPrimary (citable) accession number: Q96ES7
Secondary accession number(s): Q96MF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.