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Q9H7L9 (SDS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. 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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
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 By similarity. 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 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. Ref.5 UniProtKB Q8BR65

Tissue specificity

Expressed in various cancer cell ines. Ref.2

Domain

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

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.

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

Chain1 – 328328Sin3 histone deacetylase corepressor complex component SDS3
PRO_0000097652

Regions

Region188 – 22639Sin3 interaction domain (SID) By similarity UniProtKB Q8BR65
Coiled coil66 – 171106 Potential

Amino acid modifications

Modified residue451Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue491Phosphothreonine Ref.6 Ref.8 Ref.9
Modified residue531Phosphoserine Ref.8 Ref.9
Modified residue551Phosphothreonine Ref.6
Modified residue2341Phosphoserine Ref.6 Ref.8 Ref.10
Modified residue2361Phosphoserine Ref.7
Modified residue2371Phosphoserine Ref.8
Modified residue2441Phosphothreonine Ref.7 Ref.8

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: 11214971] [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: 12724404] [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: 15489334] [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: 14702039] [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: 12670868] [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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49; THR-55 AND SER-234, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236 AND THR-244, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49; SER-53; SER-234; SER-237 AND THR-244, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"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: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND SER-53, MASS SPECTROMETRY.
Tissue: Liver.
[10]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
+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.
IPIIPI00607645.
RefSeqNP_071936.2. NM_022491.2.
UniGeneHs.416630.
Hs.602312.

3D structure databases

ProteinModelPortalQ9H7L9.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9H7L9. 3 interactions.
STRINGQ9H7L9.

PTM databases

PhosphoSiteQ9H7L9.

Polymorphism databases

DMDM68053233.

Proteomic databases

PRIDEQ9H7L9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397564; ENSP00000380695; ENSG00000111707.
GeneID64426.
KEGGhsa:64426.
UCSCuc001twz.1. human.

Organism-specific databases

CTD64426.
GeneCardsGC12P118814.
H-InvDBHIX0011049.
HGNCHGNC:29545. SUDS3.
MIM608250. gene.
neXtProtNX_Q9H7L9.
PharmGKBPA143485626.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07799.
GeneTreeENSGT00530000063177.
HOGENOMHBG446382.
HOVERGENHBG108465.
InParanoidQ9H7L9.
OMAVEMKEQM.
OrthoDBEOG4N8R5F.
PhylomeDBQ9H7L9.

Gene expression databases

ArrayExpressQ9H7L9.
BgeeQ9H7L9.
CleanExHS_SUDS3.
GenevestigatorQ9H7L9.
GermOnlineENSG00000111707. Homo sapiens.

Family and domain databases

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

Other

NextBio66429.
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: January 25, 2012
This is version 75 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

Human chromosome 12

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families