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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)DescriptionActionsGraphical viewLength
Binding sitei238Histone H3K4me31
Binding sitei245Histone H3K4me31

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

GO - Biological processi

  • 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

BioCyciZFISH:ENSG00000176476-MONOMER.
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)DescriptionActionsGraphical viewLength
Mutagenesisi175W → A: Does not strongly affect binding to H3K4me. 1 Publication1
Mutagenesisi179E → A: Does not strongly affect binding to H3K4me. 1 Publication1
Mutagenesisi194D → A or R: Abolishes H3K4me3 binding. 1 Publication1
Mutagenesisi196D → R: Abolishes H3K4me3 binding. 1 Publication1
Mutagenesisi214P → A: Does not strongly affect binding to H3K4me. 1 Publication1
Mutagenesisi232Q → A: Does not strongly affect binding to H3K4me. 1 Publication1
Mutagenesisi238Y → A: Strongly reduced H3K4me3 binding. 2 Publications1
Mutagenesisi240Q → A: Slightly reduced H3K4me3 binding. 1 Publication1
Mutagenesisi242T → A: Almost abolished H3K4me3 binding. 1 Publication1
Mutagenesisi245Y → A: Abolishes H3K4me3 binding. 2 Publications1
Mutagenesisi256P → A: Does not strongly affect binding to H3K4me. 1 Publication1
Mutagenesisi264F → A: Strongly reduced binding to H3K4me3. 2 Publications1
Mutagenesisi266D → A: Strongly reduced binding to H3K4me3. 1 Publication1
Mutagenesisi282R → A: Does not strongly affect binding to H3K4me. 1 Publication1

Organism-specific databases

DisGeNETi112869.
OpenTargetsiENSG00000176476.
PharmGKBiPA144596468.

Polymorphism and mutation databases

BioMutaiCCDC101.
DMDMi74731608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002742681 – 293SAGA-associated factor 29Add BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei288N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ96ES7.
MaxQBiQ96ES7.
PaxDbiQ96ES7.
PeptideAtlasiQ96ES7.
PRIDEiQ96ES7.

PTM databases

iPTMnetiQ96ES7.
PhosphoSitePlusiQ96ES7.

Expressioni

Gene expression databases

BgeeiENSG00000176476.
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 KAT14, 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
HIST1H3DP6843125EBI-743117,EBI-79722
KRT13A1A4E93EBI-743117,EBI-10171552
KRT15P190124EBI-743117,EBI-739566
LNX1Q8TBB13EBI-743117,EBI-739832
MED4Q9NPJ63EBI-743117,EBI-394607
NDC80O147776EBI-743117,EBI-715849
RINT1Q6NUQ15EBI-743117,EBI-726876
TADA3O755289EBI-743117,EBI-473249
TCF4P158844EBI-743117,EBI-533224

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi125213. 87 interactors.
IntActiQ96ES7. 46 interactors.
MINTiMINT-3976256.
STRINGi9606.ENSP00000316114.

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi115 – 129Combined sources15
Beta strandi161 – 167Combined sources7
Beta strandi173 – 184Combined sources12
Turni185 – 188Combined sources4
Beta strandi189 – 194Combined sources6
Beta strandi201 – 206Combined sources6
Helixi207 – 209Combined sources3
Beta strandi210 – 212Combined sources3
Beta strandi215 – 217Combined sources3
Turni220 – 222Combined sources3
Helixi224 – 226Combined sources3
Beta strandi233 – 237Combined sources5
Beta strandi241 – 251Combined sources11
Beta strandi260 – 265Combined sources6
Beta strandi277 – 279Combined sources3
Helixi281 – 283Combined sources3
Beta strandi284 – 286Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96ES7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini152 – 293SGF29 C-terminalPROSITE-ProRule annotationAdd BLAST142

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 196Histone H3K4me3 N-terminus binding3
Regioni240 – 243Histone H3K4me3 N-terminus binding4
Regioni264 – 266Histone H3K4me3 binding3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili3 – 88Sequence analysisAdd BLAST86

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.
OrthoDBiEOG091G0G88.
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)DescriptionActionsGraphical viewLength
Sequence conflicti249I → N in BAB71340 (PubMed:14702039).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125213. 87 interactors.
IntActiQ96ES7. 46 interactors.
MINTiMINT-3976256.
STRINGi9606.ENSP00000316114.

PTM databases

iPTMnetiQ96ES7.
PhosphoSitePlusiQ96ES7.

Polymorphism and mutation databases

BioMutaiCCDC101.
DMDMi74731608.

Proteomic databases

EPDiQ96ES7.
MaxQBiQ96ES7.
PaxDbiQ96ES7.
PeptideAtlasiQ96ES7.
PRIDEiQ96ES7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi112869.
DisGeNETi112869.
GeneCardsiCCDC101.
HGNCiHGNC:25156. SGF29.
HPAiHPA052590.
HPA053608.
MIMi613374. gene.
neXtProtiNX_Q96ES7.
OpenTargetsiENSG00000176476.
PharmGKBiPA144596468.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3038. Eukaryota.
ENOG410XPFD. LUCA.
GeneTreeiENSGT00390000015229.
HOGENOMiHOG000006769.
HOVERGENiHBG059575.
InParanoidiQ96ES7.
KOiK11364.
OMAiTCFYKAV.
OrthoDBiEOG091G0G88.
PhylomeDBiQ96ES7.
TreeFamiTF314958.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000176476-MONOMER.
ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTraceiQ96ES7.
GenomeRNAii112869.
PROiQ96ES7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000176476.
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...

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: November 30, 2016
This is version 116 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.