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Protein

SAGA-associated factor 29

Gene

Sgf29

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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:17334388). SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3) (By similarity). In the SAGA-type complexes, SGF29 is required to recruit complexes to H3K4me (By similarity). Involved in the response to endoplasmic reticulum (ER) stress by recruiting the SAGA complex to H3K4me, thereby promoting histone H3 acetylation and cell survival (By similarity). May be involved in MYC-mediated oncogenic transformation (PubMed:17334388).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei238Histone H3K4me3PROSITE-ProRule annotation1
Binding sitei245Histone H3K4me3PROSITE-ProRule annotation1

GO - Molecular functioni

  • enzyme binding Source: RGD
  • methylated histone binding Source: UniProtKB
  • protein N-terminus binding Source: RGD

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
SAGA-associated factor 29Curated
Short name:
rSGF29
Alternative name(s):
Coiled-coil domain-containing protein 101
SAGA complex-associated factor 29Imported
Gene namesi
Name:Sgf29Imported
Synonyms:Ccdc101
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1310609. Sgf29.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003140271 – 293SAGA-associated factor 29Add BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei288N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0C606.
PRIDEiP0C606.

PTM databases

iPTMnetiP0C606.
PhosphoSitePlusiP0C606.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis. Highly expressed in hepatoma and other tumor cell lines.1 Publication

Gene expression databases

BgeeiENSRNOG00000019245.
ExpressionAtlasiP0C606. baseline and differential.
GenevisibleiP0C606. RN.

Interactioni

Subunit structurei

Interacts with dimethylated and trimethylated 'Lys-4' of histone H3 (H3K4me2 and H3K4me3), with a preference for the trimethylated form (H3K4me3). Component of some SAGA-type complexes. Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity). Interacts with TADA3L, GCN5L2, SUPT3H and MYC (PubMed:17334388).By similarity1 Publication

GO - Molecular functioni

  • enzyme binding Source: RGD
  • methylated histone binding Source: UniProtKB
  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026146.

Structurei

3D structure databases

SMRiP0C606.
ModBaseiSearch...
MobiDBiSearch...

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 bindingPROSITE-ProRule annotation3
Regioni240 – 243Histone H3K4me3 N-terminus bindingPROSITE-ProRule annotation4
Regioni264 – 266Histone H3K4me3 bindingPROSITE-ProRule annotation3

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).PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the SGF29 family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3038. Eukaryota.
ENOG410XPFD. LUCA.
GeneTreeiENSGT00390000015229.
HOGENOMiHOG000006769.
HOVERGENiHBG059575.
InParanoidiP0C606.
OMAiTCFYKAV.
OrthoDBiEOG091G0G88.
PhylomeDBiP0C606.
TreeFamiTF314958.

Family and domain databases

InterProiView protein in InterPro
IPR010750. SGF29_tudor-like_dom.
PfamiView protein in Pfam
PF07039. DUF1325. 1 hit.
PROSITEiView protein in PROSITE
PS51518. SGF29_C. 1 hit.

Sequencei

Sequence statusi: Complete.

P0C606-1 [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
SGDYVAKPGD KVAARVKAVE GDEQWILAEV VSYSHATNKY EVDDIDEEGK
210 220 230 240 250
ERHTLSRRRI IPLPQWKANP ETDPEALFQK EQLVLALYPQ TTCFYRALIH
260 270 280 290
TPPQRPQDDY SVLFEDTSYA DGYSPPLNVA QRYVVACKEP KKK
Length:293
Mass (Da):33,268
Last modified:January 15, 2008 - v1
Checksum:i52D0E6F27AA89580
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03005493 Genomic DNA. No translation available.
AABR03001099 Genomic DNA. No translation available.
RefSeqiXP_006230293.1. XM_006230231.3.
XP_006230294.1. XM_006230232.3.
UniGeneiRn.34983.

Genome annotation databases

EnsembliENSRNOT00000026146; ENSRNOP00000026146; ENSRNOG00000019245.
GeneIDi293488.
UCSCiRGD:1310609. rat.

Similar proteinsi

Entry informationi

Entry nameiSGF29_RAT
AccessioniPrimary (citable) accession number: P0C606
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: September 27, 2017
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families