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Protein

Sin3 histone deacetylase corepressor complex component SDS3

Gene

Suds3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory protein which represses transcription and augments histone deacetylase activity of HDAC1. May have a potential role in tumor suppressor pathways through regulation of apoptosis. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity).By similarity1 Publication

GO - Molecular functioni

  • enzyme binding Source: MGI
  • histone deacetylase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Sin3 histone deacetylase corepressor complex component SDS3
Alternative name(s):
Suppressor of defective silencing 3 protein homolog
Gene namesi
Name:Suds3
Synonyms:Sds3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1919204. Suds3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleus Source: UniProtKB
  • Sin3 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 328327Sin3 histone deacetylase corepressor complex component SDS3PRO_0000097653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei45 – 451PhosphoserineCombined sources
Modified residuei49 – 491PhosphothreonineCombined sources
Modified residuei53 – 531PhosphoserineBy similarity
Cross-linki69 – 69Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki178 – 178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei228 – 2281PhosphoserineBy similarity
Modified residuei234 – 2341PhosphoserineCombined sources
Modified residuei237 – 2371PhosphoserineCombined sources
Modified residuei244 – 2441PhosphothreonineBy similarity

Post-translational modificationi

Polyubiquitinated. 'Lys-63'-polyubiquitinated SUDS3 positively regulates histone deacetylation. Regulated through deubiquitination by USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8BR65.
MaxQBiQ8BR65.
PaxDbiQ8BR65.
PRIDEiQ8BR65.

PTM databases

iPTMnetiQ8BR65.
PhosphoSiteiQ8BR65.

Expressioni

Tissue specificityi

Expressed in all newborn tissues tested, including brain, kidney and liver.1 Publication

Gene expression databases

BgeeiQ8BR65.
GenevisibleiQ8BR65. MM.

Interactioni

Subunit structurei

Interacts with HCFC1 (By similarity). Homodimer. Component of the SIN3 histone deacetylase (HDAC) corepressor complex. Interacts with SIN3A. Interaction with SIN3B enhances the interaction between SIN3B and HDAC1 to form a complex. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with USP17L2; the interaction is direct (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-591431,EBI-591431
Sin3aQ605204EBI-591431,EBI-349034
Sin3bQ621415EBI-591431,EBI-591450

GO - Molecular functioni

  • enzyme binding Source: MGI
  • histone deacetylase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi215053. 9 interactions.
IntActiQ8BR65. 3 interactions.
MINTiMINT-4112013.
STRINGi10090.ENSMUSP00000130535.

Structurei

Secondary structure

1
328
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi90 – 17081Combined sources
Helixi213 – 22311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2N2HNMR-A205-228[»]
4ZQAX-ray1.65A90-172[»]
ProteinModelPortaliQ8BR65.
SMRiQ8BR65. Positions 90-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 170169Mediates interaction with USP17L2By similarityAdd
BLAST
Regioni188 – 22639Sin3 interaction domain (SID)Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili66 – 171106Sequence analysisAdd
BLAST

Domaini

The C-terminus is involved in transcriptional repression by HDAC-independent mechanisms.By similarity

Sequence similaritiesi

Belongs to the SDS3 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4466. Eukaryota.
ENOG410Y9N9. LUCA.
GeneTreeiENSGT00530000063177.
HOGENOMiHOG000007054.
HOVERGENiHBG108465.
InParanoidiQ8BR65.
KOiK19201.
OrthoDBiEOG7VQJFB.
PhylomeDBiQ8BR65.
TreeFamiTF323740.

Family and domain databases

InterProiIPR013907. Sds3.
[Graphical view]
PfamiPF08598. Sds3. 1 hit.
[Graphical view]
SMARTiSM01401. Sds3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BR65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAAGLLAPA PAPAAAPAAP EYYPEDEEEL ESAEDDERSC RGRESDEDTE
60 70 80 90 100
DASETDLAKH DEEDYVEMKE QMYQDKLASL KRQLQQLQEG TLQEYQKRMK
110 120 130 140 150
KLDQQYRERI RNAELFLQLE TEQVERNYIK EKKAAVKEFE DKKVELKENL
160 170 180 190 200
IAELEEKKKM IENEKLTMEL TGDSMEVKPI MTRKLRRRPN DPVPIPDKRR
210 220 230 240 250
KPAPAQLNYL LTDEQIMEDL RTLNKLKSPK RPASPSSPEH LPATPAESPA
260 270 280 290 300
QRFEARIEDG KLYYDKRWYH KSQAIYLESK DNQKLSCVIS SVGANEIWVR
310 320
KTSDSTKMRI YVGQLQRGLF VIRRRSAA
Length:328
Mass (Da):38,107
Last modified:March 1, 2003 - v1
Checksum:i05C22EA578C318E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421K → N in BAC31608 (PubMed:16141072).Curated
Sequence conflicti186 – 1861R → W in AAM22676 (PubMed:11909966).Curated
Sequence conflicti326 – 3283SAA → KFLTYRD in AAH62176 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF469109 mRNA. Translation: AAM22676.1.
AK043652 mRNA. Translation: BAC31608.1.
AK045475 mRNA. Translation: BAC32387.1.
AK138947 mRNA. Translation: BAE23831.1.
AK150633 mRNA. Translation: BAE29722.1.
BC055764 mRNA. Translation: AAH55764.2.
BC062176 mRNA. Translation: AAH62176.1.
CCDSiCCDS39232.1.
RefSeqiNP_001116138.1. NM_001122666.2.
NP_848737.3. NM_178622.5.
UniGeneiMm.34456.

Genome annotation databases

EnsembliENSMUST00000086471; ENSMUSP00000083662; ENSMUSG00000066900.
GeneIDi71954.
KEGGimmu:71954.
UCSCiuc008zff.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF469109 mRNA. Translation: AAM22676.1.
AK043652 mRNA. Translation: BAC31608.1.
AK045475 mRNA. Translation: BAC32387.1.
AK138947 mRNA. Translation: BAE23831.1.
AK150633 mRNA. Translation: BAE29722.1.
BC055764 mRNA. Translation: AAH55764.2.
BC062176 mRNA. Translation: AAH62176.1.
CCDSiCCDS39232.1.
RefSeqiNP_001116138.1. NM_001122666.2.
NP_848737.3. NM_178622.5.
UniGeneiMm.34456.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2N2HNMR-A205-228[»]
4ZQAX-ray1.65A90-172[»]
ProteinModelPortaliQ8BR65.
SMRiQ8BR65. Positions 90-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215053. 9 interactions.
IntActiQ8BR65. 3 interactions.
MINTiMINT-4112013.
STRINGi10090.ENSMUSP00000130535.

PTM databases

iPTMnetiQ8BR65.
PhosphoSiteiQ8BR65.

Proteomic databases

EPDiQ8BR65.
MaxQBiQ8BR65.
PaxDbiQ8BR65.
PRIDEiQ8BR65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000086471; ENSMUSP00000083662; ENSMUSG00000066900.
GeneIDi71954.
KEGGimmu:71954.
UCSCiuc008zff.3. mouse.

Organism-specific databases

CTDi64426.
MGIiMGI:1919204. Suds3.

Phylogenomic databases

eggNOGiKOG4466. Eukaryota.
ENOG410Y9N9. LUCA.
GeneTreeiENSGT00530000063177.
HOGENOMiHOG000007054.
HOVERGENiHBG108465.
InParanoidiQ8BR65.
KOiK19201.
OrthoDBiEOG7VQJFB.
PhylomeDBiQ8BR65.
TreeFamiTF323740.

Miscellaneous databases

PROiQ8BR65.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BR65.
GenevisibleiQ8BR65. MM.

Family and domain databases

InterProiIPR013907. Sds3.
[Graphical view]
PfamiPF08598. Sds3. 1 hit.
[Graphical view]
SMARTiSM01401. Sds3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex."
    Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr., Chen K., DePinho R.A.
    Mol. Cell. Biol. 22:2743-2750(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH SIN3A AND SIN3B, TISSUE SPECIFICITY.
    Strain: C57BL/6JImported.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Aorta, Bone marrow macrophage, Brain cortex, Corpora quadrigemina and Vein.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain and LimbImported.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND SER-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiSDS3_MOUSE
AccessioniPrimary (citable) accession number: Q8BR65
Secondary accession number(s): Q3UC92
, Q6P6K1, Q7TNT0, Q8BRR7, Q8K5B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 120 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.