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Q96ST3 (SIN3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Paired amphipathic helix protein Sin3a
Alternative name(s):
Histone deacetylase complex subunit Sin3a
Transcriptional corepressor Sin3a
Gene names
Name:SIN3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1273 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.22

Subcellular location

Nucleus. Nucleusnucleolus. Note: Recruited to the nucleolus by SAP30L. Ref.14

Post-translational modification

SUMO1 sumoylated by TOPORS. Probably desumoylated by SENP2. Ref.15

Sequence similarities

Contains 3 PAH (paired amphipathic helix) domains.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: Ensembl

activation of innate immune response

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

aging

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular protein localization

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of histone H3-K27 acetylation

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

negative regulation of protein localization to nucleus

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

negative regulation of transcription from RNA polymerase II promoter

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

negative regulation of transcription regulatory region DNA binding

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

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of G2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of chromatin silencing

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

positive regulation of defense response to virus by host

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

positive regulation of transcription from RNA polymerase II promoter

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

protein deacetylation

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

regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to methylglyoxal

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentSin3 complex

Inferred from direct assay PubMed 14966270. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

intercellular bridge

Inferred from direct assay. Source: HPA

kinetochore

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

transcriptional repressor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 22783022. Source: BHF-UCL

RNA polymerase II transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 11238380Ref.7Ref.10Ref.15. Source: UniProtKB

protein deacetylase activity

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

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12731273Paired amphipathic helix protein Sin3a
PRO_0000121537

Regions

Domain119 – 18971PAH 1
Domain300 – 38384PAH 2
Domain456 – 52570PAH 3
Region119 – 19678Interaction with HCFC1 Ref.10
Region205 – 480276Interaction with REST By similarity
Region458 – 52568Interaction with SAP30 By similarity UniProtKB Q60520
Region523 – 850328Interaction with NCOR1 By similarity UniProtKB Q60520
Region524 – 659136Interaction with SUDS3 and SAP130
Region687 – 829143Interaction with HDAC1 and ARID4B
Region888 – 96780Interaction with OGT
Coiled coil903 – 93230 Potential
Compositional bias218 – 28568Pro-rich
Compositional bias835 – 8417Poly-Glu

Amino acid modifications

Modified residue101Phosphoserine Ref.16 Ref.17
Modified residue2771Phosphoserine Ref.17
Modified residue4691N6-acetyllysine Ref.19
Modified residue8321Phosphoserine Ref.17 Ref.18 Ref.20 Ref.23 PubMed 15302935
Modified residue8601Phosphoserine Ref.13 Ref.20 Ref.23 PubMed 15302935
Modified residue8651N6-acetyllysine By similarity
Modified residue8751N6-acetyllysine By similarity
Modified residue9401Phosphoserine Ref.17 Ref.20
Modified residue11121Phosphoserine Ref.17 Ref.18 Ref.20 PubMed 15302935

Natural variations

Natural variant11561M → L.
Corresponds to variant rs60213317 [ dbSNP | Ensembl ].
VAR_062129

Experimental info

Sequence conflict1631G → R in AAK95854. Ref.4
Sequence conflict170 – 1778QLFKGHPD → HYSKGPPI in AAK95854. Ref.4
Sequence conflict182 – 19211FNTFLPPGYKI → IQHLFAPWATKM in AAK95854. Ref.4
Sequence conflict2161I → T in BAC04801. Ref.3
Sequence conflict3861S → F in AAK95854. Ref.4
Sequence conflict5361E → D in AAK95854. Ref.4
Sequence conflict5621P → G in AAK95854. Ref.4
Sequence conflict575 – 5762PL → GV in AAK95854. Ref.4
Sequence conflict5951S → C in AAK95854. Ref.4
Sequence conflict618 – 6203ELD → DLM in AAK95854. Ref.4
Sequence conflict10091Q → R in BAC11280. Ref.3
Sequence conflict1247 – 12482TT → NN in AAP97288. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q96ST3 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: E6A329BE0EAD84CD

FASTA1,273145,175
        10         20         30         40         50         60 
MKRRLDDQES PVYAAQQRRI PGSTEAFPHQ HRVLAPAPPV YEAVSETMQS ATGIQYSVTP 

        70         80         90        100        110        120 
SYQVSAMPQS SGSHGPAIAA VHSSHHHPTA VQPHGGQVVQ SHAHPAPPVA PVQGQQQFQR 

       130        140        150        160        170        180 
LKVEDALSYL DQVKLQFGSQ PQVYNDFLDI MKEFKSQSID TPGVISRVSQ LFKGHPDLIM 

       190        200        210        220        230        240 
GFNTFLPPGY KIEVQTNDMV NVTTPGQVHQ IPTHGIQPQP QPPPQHPSQP SAQSAPAPAQ 

       250        260        270        280        290        300 
PAPQPPPAKV SKPSQLQAHT PASQQTPPLP PYASPRSPPV QPHTPVTISL GTAPSLQNNQ 

       310        320        330        340        350        360 
PVEFNHAINY VNKIKNRFQG QPDIYKAFLE ILHTYQKEQR NAKEAGGNYT PALTEQEVYA 

       370        380        390        400        410        420 
QVARLFKNQE DLLSEFGQFL PDANSSVLLS KTTAEKVDSV RNDHGGTVKK PQLNNKPQRP 

       430        440        450        460        470        480 
SQNGCQIRRH PTGTTPPVKK KPKLLNLKDS SMADASKHGG GTESLFFDKV RKALRSAEAY 

       490        500        510        520        530        540 
ENFLRCLVIF NQEVISRAEL VQLVSPFLGK FPELFNWFKN FLGYKESVHL ETYPKERATE 

       550        560        570        580        590        600 
GIAMEIDYAS CKRLGSSYRA LPKSYQQPKC TGRTPLCKEV LNDTWVSFPS WSEDSTFVSS 

       610        620        630        640        650        660 
KKTQYEEHIY RCEDERFELD VVLETNLATI RVLEAIQKKL SRLSAEEQAK FRLDNTLGGT 

       670        680        690        700        710        720 
SEVIHRKALQ RIYADKAADI IDGLRKNPSI AVPIVLKRLK MKEEEWREAQ RGFNKVWREQ 

       730        740        750        760        770        780 
NEKYYLKSLD HQGINFKQND TKVLRSKSLL NEIESIYDER QEQATEENAG VPVGPHLSLA 

       790        800        810        820        830        840 
YEDKQILEDA AALIIHHVKR QTGIQKEDKY KIKQIMHHFI PDLLFAQRGD LSDVEEEEEE 

       850        860        870        880        890        900 
EMDVDEATGA VKKHNGVGGS PPKSKLLFSN TAAQKLRGMD EVYNLFYVNN NWYIFMRLHQ 

       910        920        930        940        950        960 
ILCLRLLRIC SQAERQIEEE NREREWEREV LGIKRDKSDS PAIQLRLKEP MDVDVEDYYP 

       970        980        990       1000       1010       1020 
AFLDMVRSLL DGNIDSSQYE DSLREMFTIH AYIAFTMDKL IQSIVRQLQH IVSDEICVQV 

      1030       1040       1050       1060       1070       1080 
TDLYLAENNN GATGGQLNTQ NSRSLLESTY QRKAEQLMSD ENCFKLMFIQ SQGQVQLTIE 

      1090       1100       1110       1120       1130       1140 
LLDTEEENSD DPVEAERWSD YVERYMNSDT TSPELREHLA QKPVFLPRNL RRIRKCQRGR 

      1150       1160       1170       1180       1190       1200 
EQQEKEGKEG NSKKTMENVD SLDKLECRFK LNSYKMVYVI KSEDYMYRRT ALLRAHQSHE 

      1210       1220       1230       1240       1250       1260 
RVSKRLHQRF QAWVDKWTKE HVPREMAAET SKWLMGEGLE GLVPCTTTCD TETLHFVSIN 

      1270 
KYRVKYGTVF KAP 

« Hide

References

« Hide 'large scale' references
[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 Uterus.
[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. 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 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"DACH1 inhibits transforming growth factor-beta signaling through binding Smad4."
Wu K., Yang Y., Wang C., Davoli M.A., D'Amico M., Li A., Cveklova K., Kozmik Z., Lisanti M.P., Russell R.G., Cvekl A., Pestell R.G.
J. Biol. Chem. 278:51673-51684(2003) [PubMed] [Europe PMC] [Abstract]
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]"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-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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10279.1.
PIRT17282.
RefSeqNP_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.
UniGeneHs.513039.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PO4model-B295-383[»]
ProteinModelPortalQ96ST3.
SMRQ96ST3. Positions 119-189, 295-385, 453-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117439. 181 interactions.
IntActQ96ST3. 39 interactions.
MINTMINT-2815493.
STRING9606.ENSP00000353622.

PTM databases

PhosphoSiteQ96ST3.

Polymorphism databases

DMDM37999759.

Proteomic databases

MaxQBQ96ST3.
PaxDbQ96ST3.
PeptideAtlasQ96ST3.
PRIDEQ96ST3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360439; ENSP00000353622; ENSG00000169375.
ENST00000394947; ENSP00000378402; ENSG00000169375.
ENST00000394949; ENSP00000378403; ENSG00000169375.
GeneID25942.
KEGGhsa:25942.
UCSCuc002bai.3. human.

Organism-specific databases

CTD25942.
GeneCardsGC15M075661.
H-InvDBHIX0012443.
HIX0019634.
HIX0172841.
HGNCHGNC:19353. SIN3A.
HPACAB004506.
HPA047213.
MIM607776. gene.
neXtProtNX_Q96ST3.
PharmGKBPA134993567.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5602.
HOVERGENHBG060425.
InParanoidQ96ST3.
KOK11644.
OMANDHGGTA.
OrthoDBEOG7SV0TV.
PhylomeDBQ96ST3.
TreeFamTF106187.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_604. Hemostasis.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ96ST3.
BgeeQ96ST3.
CleanExHS_SIN3A.
GenevestigatorQ96ST3.

Family and domain databases

Gene3D1.20.1160.11. 3 hits.
InterProIPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view]
PfamPF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
[Graphical view]
SMARTSM00761. HDAC_interact. 1 hit.
[Graphical view]
SUPFAMSSF47762. SSF47762. 3 hits.
PROSITEPS51477. PAH. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSIN3A. human.
GeneWikiSIN3A.
GenomeRNAi25942.
NextBio47516.
PROQ96ST3.
SOURCESearch...

Entry information

Entry nameSIN3A_HUMAN
AccessionPrimary (citable) accession number: Q96ST3
Secondary accession number(s): B2RNS5 expand/collapse secondary AC list , Q8N8N4, Q8NC83, Q8WV18, Q96L98, Q9UFQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: July 9, 2014
This is version 129 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM