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Q96ST3

- SIN3A_HUMAN

UniProt

Q96ST3 - SIN3A_HUMAN

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Protein

Paired amphipathic helix protein Sin3a

Gene

SIN3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Involved in he control of the circadian rhythms. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation.1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. protein deacetylase activity Source: BHF-UCL
  3. RNA polymerase II activating transcription factor binding Source: BHF-UCL
  4. RNA polymerase II transcription corepressor activity Source: Ensembl
  5. sequence-specific DNA binding transcription factor activity Source: Ensembl
  6. transcription regulatory region sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  1. activation of innate immune response Source: BHF-UCL
  2. aging Source: Ensembl
  3. blood coagulation Source: Reactome
  4. cellular lipid metabolic process Source: Reactome
  5. cellular protein localization Source: Ensembl
  6. cellular response to glucose stimulus Source: Ensembl
  7. DNA replication Source: Ensembl
  8. hematopoietic progenitor cell differentiation Source: Ensembl
  9. in utero embryonic development Source: Ensembl
  10. negative regulation of apoptotic process Source: Ensembl
  11. negative regulation of circadian rhythm Source: UniProtKB
  12. negative regulation of histone H3-K27 acetylation Source: BHF-UCL
  13. negative regulation of protein localization to nucleus Source: BHF-UCL
  14. negative regulation of transcription, DNA-templated Source: UniProtKB
  15. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  16. negative regulation of transcription regulatory region DNA binding Source: BHF-UCL
  17. positive regulation of chromatin silencing Source: BHF-UCL
  18. positive regulation of defense response to virus by host Source: BHF-UCL
  19. positive regulation of G2/M transition of mitotic cell cycle Source: Ensembl
  20. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  21. protein deacetylation Source: BHF-UCL
  22. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: Ensembl
  23. response to methylglyoxal Source: Ensembl
  24. response to organonitrogen compound Source: Ensembl
  25. rhythmic process Source: UniProtKB-KW
  26. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Paired amphipathic helix protein Sin3a
Alternative name(s):
Histone deacetylase complex subunit Sin3a
Transcriptional corepressor Sin3a
Gene namesi
Name:SIN3AImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:19353. SIN3A.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation. Nucleusnucleolus 1 Publication
Note: Recruited to the nucleolus by SAP30L.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. intercellular bridge Source: HPA
  3. kinetochore Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. Sin3 complex Source: UniProtKB
  7. transcriptional repressor complex Source: Ensembl
  8. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134993567.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12731273Paired amphipathic helix protein Sin3aPRO_0000121537Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine2 Publications
Modified residuei277 – 2771Phosphoserine1 Publication
Modified residuei469 – 4691N6-acetyllysine1 Publication
Modified residuei832 – 8321Phosphoserine4 Publications
Modified residuei860 – 8601Phosphoserine3 Publications
Modified residuei865 – 8651N6-acetyllysineBy similarity
Modified residuei875 – 8751N6-acetyllysineBy similarity
Modified residuei940 – 9401Phosphoserine2 Publications
Modified residuei1112 – 11121Phosphoserine3 Publications

Post-translational modificationi

SUMO1 sumoylated by TOPORS. Probably desumoylated by SENP2.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96ST3.
PaxDbiQ96ST3.
PeptideAtlasiQ96ST3.
PRIDEiQ96ST3.

PTM databases

PhosphoSiteiQ96ST3.

Expressioni

Gene expression databases

BgeeiQ96ST3.
CleanExiHS_SIN3A.
ExpressionAtlasiQ96ST3. baseline and differential.
GenevestigatoriQ96ST3.

Organism-specific databases

HPAiCAB004506.
HPA047213.

Interactioni

Subunit structurei

Interacts with ARID4B, BRMS1L, HCFC1, HDAC1, HDAC2, MXI1, SAP30L, SAP130, SFPQ and TOPORS. Interacts with OGT (via TPRs 1-6); the interaction mediates transcriptional repression in parallel with histone deacetylase (By similarity). Interacts with BAZ2A, MXD3, MXD4, MBD2, DACH1, NCOR1, NR4A2, REST, RLIM, SAP30, SETDB1, SMYD2, and SUDS3. Interacts with PHF12 in a complex composed of HDAC1, PHF12 and SAP30. Interacts with TET1; the interaction recruits SIN3A to gene promoters. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Interacts with KLF11 (By similarity).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX30Q7L2E33EBI-347218,EBI-1211456
HCFC1P516106EBI-347218,EBI-396176
HDAC2Q927694EBI-347218,EBI-301821
NR2E3Q9Y5X42EBI-347218,EBI-7216962
PA2G4Q9UQ804EBI-347218,EBI-924893
SFPQP232462EBI-347218,EBI-355453
SKIP127553EBI-347218,EBI-347281
TP53P046372EBI-347218,EBI-366083

Protein-protein interaction databases

BioGridi117439. 186 interactions.
DIPiDIP-31515N.
IntActiQ96ST3. 42 interactions.
MINTiMINT-2815493.
STRINGi9606.ENSP00000353622.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PO4model-B295-383[»]
ProteinModelPortaliQ96ST3.
SMRiQ96ST3. Positions 119-189, 295-385, 453-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 18971PAH 1PROSITE-ProRule annotationAdd
BLAST
Domaini300 – 38384PAH 2PROSITE-ProRule annotationAdd
BLAST
Domaini456 – 52570PAH 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni119 – 19678Interaction with HCFC11 PublicationAdd
BLAST
Regioni205 – 480276Interaction with RESTBy similarityAdd
BLAST
Regioni458 – 52568Interaction with SAP30By similarityAdd
BLAST
Regioni523 – 850328Interaction with NCOR1By similarityAdd
BLAST
Regioni524 – 659136Interaction with SUDS3 and SAP130Add
BLAST
Regioni687 – 829143Interaction with HDAC1 and ARID4BAdd
BLAST
Regioni888 – 96780Interaction with OGTAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili903 – 93230Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi218 – 28568Pro-richAdd
BLAST
Compositional biasi835 – 8417Poly-Glu

Sequence similaritiesi

Contains 3 PAH (paired amphipathic helix) domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5602.
GeneTreeiENSGT00390000007239.
HOVERGENiHBG060425.
InParanoidiQ96ST3.
KOiK11644.
OMAiNDHGGTA.
OrthoDBiEOG7SV0TV.
PhylomeDBiQ96ST3.
TreeFamiTF106187.

Family and domain databases

Gene3Di1.20.1160.11. 3 hits.
InterProiIPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view]
PfamiPF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
[Graphical view]
SMARTiSM00761. HDAC_interact. 1 hit.
[Graphical view]
SUPFAMiSSF47762. SSF47762. 3 hits.
PROSITEiPS51477. PAH. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96ST3 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKRRLDDQES PVYAAQQRRI PGSTEAFPHQ HRVLAPAPPV YEAVSETMQS
60 70 80 90 100
ATGIQYSVTP SYQVSAMPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ
110 120 130 140 150
SHAHPAPPVA PVQGQQQFQR LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI
160 170 180 190 200
MKEFKSQSID TPGVISRVSQ LFKGHPDLIM GFNTFLPPGY KIEVQTNDMV
210 220 230 240 250
NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SAQSAPAPAQ PAPQPPPAKV
260 270 280 290 300
SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ
310 320 330 340 350
PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT
360 370 380 390 400
PALTEQEVYA QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV
410 420 430 440 450
RNDHGGTVKK PQLNNKPQRP SQNGCQIRRH PTGTTPPVKK KPKLLNLKDS
460 470 480 490 500
SMADASKHGG GTESLFFDKV RKALRSAEAY ENFLRCLVIF NQEVISRAEL
510 520 530 540 550
VQLVSPFLGK FPELFNWFKN FLGYKESVHL ETYPKERATE GIAMEIDYAS
560 570 580 590 600
CKRLGSSYRA LPKSYQQPKC TGRTPLCKEV LNDTWVSFPS WSEDSTFVSS
610 620 630 640 650
KKTQYEEHIY RCEDERFELD VVLETNLATI RVLEAIQKKL SRLSAEEQAK
660 670 680 690 700
FRLDNTLGGT SEVIHRKALQ RIYADKAADI IDGLRKNPSI AVPIVLKRLK
710 720 730 740 750
MKEEEWREAQ RGFNKVWREQ NEKYYLKSLD HQGINFKQND TKVLRSKSLL
760 770 780 790 800
NEIESIYDER QEQATEENAG VPVGPHLSLA YEDKQILEDA AALIIHHVKR
810 820 830 840 850
QTGIQKEDKY KIKQIMHHFI PDLLFAQRGD LSDVEEEEEE EMDVDEATGA
860 870 880 890 900
VKKHNGVGGS PPKSKLLFSN TAAQKLRGMD EVYNLFYVNN NWYIFMRLHQ
910 920 930 940 950
ILCLRLLRIC SQAERQIEEE NREREWEREV LGIKRDKSDS PAIQLRLKEP
960 970 980 990 1000
MDVDVEDYYP AFLDMVRSLL DGNIDSSQYE DSLREMFTIH AYIAFTMDKL
1010 1020 1030 1040 1050
IQSIVRQLQH IVSDEICVQV TDLYLAENNN GATGGQLNTQ NSRSLLESTY
1060 1070 1080 1090 1100
QRKAEQLMSD ENCFKLMFIQ SQGQVQLTIE LLDTEEENSD DPVEAERWSD
1110 1120 1130 1140 1150
YVERYMNSDT TSPELREHLA QKPVFLPRNL RRIRKCQRGR EQQEKEGKEG
1160 1170 1180 1190 1200
NSKKTMENVD SLDKLECRFK LNSYKMVYVI KSEDYMYRRT ALLRAHQSHE
1210 1220 1230 1240 1250
RVSKRLHQRF QAWVDKWTKE HVPREMAAET SKWLMGEGLE GLVPCTTTCD
1260 1270
TETLHFVSIN KYRVKYGTVF KAP
Length:1,273
Mass (Da):145,175
Last modified:October 24, 2003 - v2
Checksum:iE6A329BE0EAD84CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631G → R in AAK95854. 1 PublicationCurated
Sequence conflicti170 – 1778QLFKGHPD → HYSKGPPI in AAK95854. 1 PublicationCurated
Sequence conflicti182 – 19211FNTFLPPGYKI → IQHLFAPWATKM in AAK95854. 1 PublicationCuratedAdd
BLAST
Sequence conflicti216 – 2161I → T in BAC04801. (PubMed:14702039)Curated
Sequence conflicti386 – 3861S → F in AAK95854. 1 PublicationCurated
Sequence conflicti536 – 5361E → D in AAK95854. 1 PublicationCurated
Sequence conflicti562 – 5621P → G in AAK95854. 1 PublicationCurated
Sequence conflicti575 – 5762PL → GV in AAK95854. 1 PublicationCurated
Sequence conflicti595 – 5951S → C in AAK95854. 1 PublicationCurated
Sequence conflicti618 – 6203ELD → DLM in AAK95854. 1 PublicationCurated
Sequence conflicti1009 – 10091Q → R in BAC11280. (PubMed:14702039)Curated
Sequence conflicti1247 – 12482TT → NN in AAP97288. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1156 – 11561M → L.
Corresponds to variant rs60213317 [ dbSNP | Ensembl ].
VAR_062129

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF418569 mRNA. Translation: AAP97288.1.
BC018973 mRNA. Translation: AAH18973.1.
BC137098 mRNA. Translation: AAI37099.1.
BC137099 mRNA. Translation: AAI37100.1.
AK027559 mRNA. Translation: BAB55197.1.
AK074903 mRNA. Translation: BAC11280.1.
AK096477 mRNA. Translation: BAC04801.1.
AY044430 mRNA. Translation: AAK95854.1.
AL117513 mRNA. Translation: CAB55972.1.
CCDSiCCDS10279.1.
PIRiT17282.
RefSeqiNP_001138829.1. NM_001145357.1.
NP_001138830.1. NM_001145358.1.
NP_056292.1. NM_015477.2.
XP_006720528.1. XM_006720465.1.
XP_006720529.1. XM_006720466.1.
XP_006720530.1. XM_006720467.1.
UniGeneiHs.513039.

Genome annotation databases

EnsembliENST00000360439; ENSP00000353622; ENSG00000169375.
ENST00000394947; ENSP00000378402; ENSG00000169375.
ENST00000394949; ENSP00000378403; ENSG00000169375.
GeneIDi25942.
KEGGihsa:25942.
UCSCiuc002bai.3. human.

Polymorphism databases

DMDMi37999759.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF418569 mRNA. Translation: AAP97288.1 .
BC018973 mRNA. Translation: AAH18973.1 .
BC137098 mRNA. Translation: AAI37099.1 .
BC137099 mRNA. Translation: AAI37100.1 .
AK027559 mRNA. Translation: BAB55197.1 .
AK074903 mRNA. Translation: BAC11280.1 .
AK096477 mRNA. Translation: BAC04801.1 .
AY044430 mRNA. Translation: AAK95854.1 .
AL117513 mRNA. Translation: CAB55972.1 .
CCDSi CCDS10279.1.
PIRi T17282.
RefSeqi NP_001138829.1. NM_001145357.1.
NP_001138830.1. NM_001145358.1.
NP_056292.1. NM_015477.2.
XP_006720528.1. XM_006720465.1.
XP_006720529.1. XM_006720466.1.
XP_006720530.1. XM_006720467.1.
UniGenei Hs.513039.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PO4 model - B 295-383 [» ]
ProteinModelPortali Q96ST3.
SMRi Q96ST3. Positions 119-189, 295-385, 453-527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117439. 186 interactions.
DIPi DIP-31515N.
IntActi Q96ST3. 42 interactions.
MINTi MINT-2815493.
STRINGi 9606.ENSP00000353622.

PTM databases

PhosphoSitei Q96ST3.

Polymorphism databases

DMDMi 37999759.

Proteomic databases

MaxQBi Q96ST3.
PaxDbi Q96ST3.
PeptideAtlasi Q96ST3.
PRIDEi Q96ST3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360439 ; ENSP00000353622 ; ENSG00000169375 .
ENST00000394947 ; ENSP00000378402 ; ENSG00000169375 .
ENST00000394949 ; ENSP00000378403 ; ENSG00000169375 .
GeneIDi 25942.
KEGGi hsa:25942.
UCSCi uc002bai.3. human.

Organism-specific databases

CTDi 25942.
GeneCardsi GC15M075661.
H-InvDB HIX0012443.
HIX0019634.
HIX0172841.
HGNCi HGNC:19353. SIN3A.
HPAi CAB004506.
HPA047213.
MIMi 607776. gene.
neXtProti NX_Q96ST3.
PharmGKBi PA134993567.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5602.
GeneTreei ENSGT00390000007239.
HOVERGENi HBG060425.
InParanoidi Q96ST3.
KOi K11644.
OMAi NDHGGTA.
OrthoDBi EOG7SV0TV.
PhylomeDBi Q96ST3.
TreeFami TF106187.

Enzyme and pathway databases

Reactomei REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi SIN3A. human.
GeneWikii SIN3A.
GenomeRNAii 25942.
NextBioi 47516.
PROi Q96ST3.
SOURCEi Search...

Gene expression databases

Bgeei Q96ST3.
CleanExi HS_SIN3A.
ExpressionAtlasi Q96ST3. baseline and differential.
Genevestigatori Q96ST3.

Family and domain databases

Gene3Di 1.20.1160.11. 3 hits.
InterProi IPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view ]
Pfami PF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
[Graphical view ]
SMARTi SM00761. HDAC_interact. 1 hit.
[Graphical view ]
SUPFAMi SSF47762. SSF47762. 3 hits.
PROSITEi PS51477. PAH. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Guo J.H., Yu L.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "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 UterusImported.
  3. "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.
    , 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 1-1026.
    Tissue: Brain and Teratocarcinoma.
  4. Bu X., Fu Y., Jiang S., Avraham S., Avraham H.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-620.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 913-1273.
    Tissue: Testis.
  6. "PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors."
    Mathur M., Tucker P.W., Samuels H.H.
    Mol. Cell. Biol. 21:2298-2311(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFPQ.
  7. "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression."
    Yang X., Zhang F., Kudlow J.E.
    Cell 110:69-80(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OGT, FUNCTION.
  8. "Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription."
    Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R.
    Endocrinology 143:1280-1290(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFPQ.
  9. Cited for: INTERACTION WITH DACH1.
  10. "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.
  11. "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: INTERACTION WITH SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
  12. "Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex."
    Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.
    Biochem. Biophys. Res. Commun. 323:1216-1222(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRMS1L.
  13. "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-860, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus."
    Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O.
    Nucleic Acids Res. 34:3288-3298(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SAP30L.
  15. "TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins."
    Pungaliya P., Kulkarni D., Park H.J., Marshall H., Zheng H., Lackland H., Saleem A., Rubin E.H.
    J. Proteome Res. 6:3918-3923(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOPORS, SUMOYLATION BY TOPORS, DESUMOYLATION BY SENP2.
  16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-277; SER-832; SER-940 AND SER-1112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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-832 AND SER-1112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-832; SER-860; SER-940 AND SER-1112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity."
    Williams K., Christensen J., Pedersen M.T., Johansen J.V., Cloos P.A., Rappsilber J., Helin K.
    Nature 473:343-348(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TET1.
  23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 AND SER-860, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSIN3A_HUMAN
AccessioniPrimary (citable) accession number: Q96ST3
Secondary accession number(s): B2RNS5
, Q8N8N4, Q8NC83, Q8WV18, Q96L98, Q9UFQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: October 29, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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