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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

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 (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei238 – 2381Histone H3K4me3PROSITE-ProRule annotation
Binding sitei245 – 2451Histone H3K4me3PROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1310609. Sgf29.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293SAGA-associated factor 29PRO_0000314027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei288 – 2881N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0C606.
PRIDEiP0C606.

PTM databases

iPTMnetiP0C606.

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiP0C606. baseline and differential.
GenevisibleiP0C606. RN.

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) (By similarity). Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.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.

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 bindingPROSITE-ProRule annotation
Regioni240 – 2434Histone H3K4me3 N-terminus bindingPROSITE-ProRule annotation
Regioni264 – 2663Histone H3K4me3 bindingPROSITE-ProRule annotation

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 annotation

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.
InParanoidiP0C606.
OMAiTCFYKAV.
OrthoDBiEOG72RMZD.
PhylomeDBiP0C606.
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.

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_006230231.2.
XP_006230294.1. XM_006230232.2.
UniGeneiRn.34983.

Genome annotation databases

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

Cross-referencesi

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_006230231.2.
XP_006230294.1. XM_006230232.2.
UniGeneiRn.34983.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026146.

PTM databases

iPTMnetiP0C606.

Proteomic databases

PaxDbiP0C606.
PRIDEiP0C606.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi112869.
RGDi1310609. Sgf29.

Phylogenomic databases

eggNOGiKOG3038. Eukaryota.
ENOG410XPFD. LUCA.
GeneTreeiENSGT00390000015229.
HOGENOMiHOG000006769.
HOVERGENiHBG059575.
InParanoidiP0C606.
OMAiTCFYKAV.
OrthoDBiEOG72RMZD.
PhylomeDBiP0C606.
TreeFamiTF314958.

Miscellaneous databases

PROiP0C606.

Gene expression databases

ExpressionAtlasiP0C606. baseline and differential.
GenevisibleiP0C606. RN.

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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc."
    Kurabe N., Katagiri K., Komiya Y., Ito R., Sugiyama A., Kawasaki Y., Tashiro F.
    Oncogene 26:5626-5634(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH TADA3L; GCN5L2; SUPT3H AND MYC.

Entry informationi

Entry nameiSGF29_RAT
AccessioniPrimary (citable) accession number: P0C606
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: May 11, 2016
This is version 67 of the entry and version 1 of the sequence. [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

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.