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Protein

SAGA-associated factor 29

Gene

SGF29

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

Functioni

Chromatin reader component of some histone acetyltransferase (HAT) SAGA-type complexes like the TFTC-HAT, ATAC or STAGA complexes (PubMed:19103755, PubMed:20850016, PubMed:26421618, PubMed:21685874, PubMed:26578293). SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3) (PubMed:20850016, PubMed:26421618, PubMed:21685874, PubMed:26578293). In the SAGA-type complexes, SGF29 is required to recruit complexes to H3K4me (PubMed:20850016). Involved in the response to endoplasmic reticulum (ER) stress by recruiting the SAGA complex to H3K4me, thereby promoting histone H3 acetylation and cell survival (PubMed:23894581).6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei238Histone H3K4me31 Publication1
Binding sitei245Histone H3K4me32 Publications1

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

GO - Biological processi

  • establishment of protein localization to chromatin Source: UniProtKB
  • histone acetylation Source: UniProtKB
  • histone H3 acetylation Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionChromatin regulator
Biological processTranscription, 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:CCDC101Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000176476.8
HGNCiHGNC:25156 SGF29
MIMi613374 gene
neXtProtiNX_Q96ES7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
Mutagenesisi238Y → F: Does not affect binding to H3K4me3. 1 Publication1
Mutagenesisi240Q → A: Slightly reduced H3K4me3 binding. 1 Publication1
Mutagenesisi242T → A: Almost abolished H3K4me3 binding. 1 Publication1
Mutagenesisi245Y → A: Abolishes H3K4me3 binding. 2 Publications1
Mutagenesisi245Y → F: Reduced H3K4me3 binding. 1 Publication1
Mutagenesisi256P → A: Does not strongly affect binding to H3K4me. 1 Publication1
Mutagenesisi264F → A: Strongly reduced binding to H3K4me3. 2 Publications1
Mutagenesisi266D → A, F, Y or W: Strongly reduced binding to H3K4me3. 2 Publications1
Mutagenesisi266D → E: Does not affect binding to H3K4me3. 1 Publication1
Mutagenesisi266D → N: Slightly 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
ProteomicsDBi76446

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 dimethylated and trimethylated 'Lys-4' of histone H3 (H3K4me2 and H3K4me3), with a preference for the trimethylated form (H3K4me3) (PubMed:21685874, PubMed:26578293). Component of some SAGA-type complexes (PubMed:20850016). Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (PubMed:19103755). Interacts with TADA3L, GCN5L2, SUPT3H and MYC (By similarity).By similarity4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi125213, 92 interactors
ComplexPortaliCPX-1004 PCAF-containing ATAC complex
CPX-900 SAGA complex
CPX-997 GCN5-containing ATAC complex
CORUMiQ96ES7
IntActiQ96ES7, 50 interactors
MINTiQ96ES7
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 binding2 Publications3
Regioni240 – 243Histone H3K4me3 N-terminus binding2 Publications4
Regioni264 – 266Histone H3K4me3 binding1 Publication3

Coiled coil

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

Domaini

The SGF29 C-terminal (also named tudor-like) domain mediates binding to methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3).PROSITE-ProRule annotation3 Publications

Sequence similaritiesi

Belongs to the SGF29 family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR037802 SGF29
IPR010750 SGF29_tudor-like_dom
PANTHERiPTHR21539 PTHR21539, 1 hit
PfamiView protein in Pfam
PF07039 DUF1325, 1 hit
PROSITEiView protein in PROSITE
PS51518 SGF29_C, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiSGF29_HUMAN
AccessioniPrimary (citable) accession number: Q96ES7
Secondary accession number(s): Q96MF5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: December 1, 2001
Last modified: June 20, 2018
This is version 126 of the entry and version 1 of the sequence. See 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

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