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Q9H7L9 (SDS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sin3 histone deacetylase corepressor complex component SDS3
Alternative name(s):
45 kDa Sin3-associated polypeptide
Suppressor of defective silencing 3 protein homolog
Gene names
Name:SUDS3
Synonyms:SAP45, SDS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.11 UniProtKB Q8BR65

Subunit structure

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 By similarity. Interacts with HCFC1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with USP17L2; the interaction is direct. Ref.2 Ref.5 Ref.11 UniProtKB Q8BR65

Subcellular location

Nucleus Ref.11.

Tissue specificity

Expressed in various cancer cell ines. Ref.2

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the SDS3 family.

Sequence caution

The sequence BAB14685.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15750.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainCoiled coil
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

histone deacetylation

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 22783022. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity PubMed 11909966. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSin3 complex

Inferred from sequence or structural similarity PubMed 11909966. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.11. Source: UniProtKB

histone deacetylase binding

Inferred from sequence or structural similarity PubMed 11909966. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BRMS1Q9HCU92EBI-540496,EBI-714781
HCFC1P516102EBI-540496,EBI-396176

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 328327Sin3 histone deacetylase corepressor complex component SDS3
PRO_0000097652

Regions

Region2 – 170169Mediates interaction with USP17L2
Region188 – 22639Sin3 interaction domain (SID) By similarity UniProtKB Q8BR65
Coiled coil66 – 171106 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue321Phosphoserine Ref.12
Modified residue451Phosphoserine Ref.6 Ref.7 Ref.8 Ref.10 Ref.12
Modified residue491Phosphothreonine Ref.6 Ref.7 Ref.8 Ref.10
Modified residue531Phosphoserine Ref.7
Modified residue2281Phosphoserine Ref.12
Modified residue2341Phosphoserine Ref.7 Ref.9 Ref.10 Ref.12
Modified residue2371Phosphoserine By similarity
Modified residue2441Phosphothreonine Ref.7

Experimental info

Sequence conflict164 – 1718EKLTMELT → HASAHASA in AAH30252. Ref.2
Sequence conflict2861S → R in BAB14685. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9H7L9 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 10A7393B607117EB

FASTA32838,136
        10         20         30         40         50         60 
MSAAGLLAPA PAQAGAPPAP EYYPEEDEEL ESAEDDERSC RGRESDEDTE DASETDLAKH 

        70         80         90        100        110        120 
DEEDYVEMKE QMYQDKLASL KRQLQQLQEG TLQEYQKRMK KLDQQYKERI RNAELFLQLE 

       130        140        150        160        170        180 
TEQVERNYIK EKKAAVKEFE DKKVELKENL IAELEEKKKM IENEKLTMEL TGDSMEVKPI 

       190        200        210        220        230        240 
MTRKLRRRPN DPVPIPDKRR KPAPAQLNYL LTDEQIMEDL RTLNKLKSPK RPASPSSPEH 

       250        260        270        280        290        300 
LPATPAESPA QRFEARIEDG KLYYDKRWYH KSQAIYLESK DNQKLSCVIS SVGANEIWVR 

       310        320 
KTSDSTKMRI YLGQLQRGLF VIRRRSAA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of long cDNA clones from human adult spleen."
Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.
DNA Res. 7:357-366(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen.
[2]"Identification and characterization of three new components of the mSin3A corepressor complex."
Fleischer T.C., Yun U.J., Ayer D.E.
Mol. Cell. Biol. 23:3456-3467(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
[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].
Tissue: Lung and Placenta.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-328.
Tissue: Placenta and Spleen.
[5]"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCFC1.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49; SER-53; SER-234 AND THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND SER-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-63-specific deubiquitination of SDS3 by USP17 regulates HDAC activity."
Ramakrishna S., Suresh B., Lee E.J., Lee H.J., Ahn W.S., Baek K.H.
J. Biol. Chem. 286:10505-10514(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH USP17L2, SUBCELLULAR LOCATION, UBIQUITINATION, DEUBIQUITINATION BY USP17L2.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-45; SER-228 AND SER-234, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK024460 mRNA. Translation: BAB15750.1. Different initiation.
BC030252 mRNA. Translation: AAH30252.1.
BC098404 mRNA. Translation: AAH98404.1.
AK023801 mRNA. Translation: BAB14685.1. Different initiation.
RefSeqNP_071936.2. NM_022491.2.
UniGeneHs.416630.
Hs.602312.

3D structure databases

ProteinModelPortalQ9H7L9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122174. 14 interactions.
IntActQ9H7L9. 7 interactions.
STRING9606.ENSP00000380695.

PTM databases

PhosphoSiteQ9H7L9.

Polymorphism databases

DMDM68053233.

Proteomic databases

PaxDbQ9H7L9.
PRIDEQ9H7L9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000543473; ENSP00000443988; ENSG00000111707.
GeneID64426.
KEGGhsa:64426.
UCSCuc001twz.3. human.

Organism-specific databases

CTD64426.
GeneCardsGC12P118814.
HGNCHGNC:29545. SUDS3.
HPAHPA040402.
HPA041972.
MIM608250. gene.
neXtProtNX_Q9H7L9.
PharmGKBPA143485626.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311652.
HOGENOMHOG000007054.
HOVERGENHBG108465.
InParanoidQ9H7L9.
OrthoDBEOG7VQJFB.
PhylomeDBQ9H7L9.
TreeFamTF323740.

Gene expression databases

ArrayExpressQ9H7L9.
BgeeQ9H7L9.
CleanExHS_SUDS3.
GenevestigatorQ9H7L9.

Family and domain databases

InterProIPR013907. Sds3.
[Graphical view]
PfamPF08598. Sds3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUDS3. human.
GeneWikiSUDS3.
GenomeRNAi64426.
NextBio66429.
PROQ9H7L9.
SOURCESearch...

Entry information

Entry nameSDS3_HUMAN
AccessionPrimary (citable) accession number: Q9H7L9
Secondary accession number(s): Q4KMQ5, Q8N6H0, Q9H8D2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM