Q96ST3 (SIN3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Paired amphipathic helix protein Sin3a

Alternative name(s):
Histone deacetylase complex subunit Sin3a
Transcriptional corepressor Sin3a

Gene names

Name:

SIN3A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1273 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation. Ref.7
Subunit structure	Interacts with BAZ2A, MXD3, MXD4, MBD2, NCOR1, NR4A2, REST, RLIM, SAP30, SETDB1 and SMYD2. Interacts with PHF12 in a complex composed of HDAC1, PHF12 and SAP30 By similarity. Interacts with ARID4B, BRMS1L, DACH1, HCFC1, HDAC1, HDAC2, MXI1, SAP30L, SAP130, SFPQ, SUDS3 and TOPORS. Interacts with TET1; the interaction recruits SIN3A to gene promoters. Interacts with OGT (via TPRs 1-6); the interaction mediates transcriptional repression in parallel with histone deacetylase. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.22
Subcellular location	Nucleus. Nucleus › nucleolus. 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
Molecular function	Repressor
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: Compara activation of innate immune response Inferred from mutant phenotype PubMed 22783022. Source: BHF-UCL aging Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome cellular lipid metabolic process Traceable author statement. Source: Reactome cellular protein localization Inferred from electronic annotation. Source: Compara cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara interphase of mitotic cell cycle Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara 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 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 regulation of transcription from RNA polymerase II promoter in response to oxidative stress Inferred from electronic annotation. Source: Compara response to methylglyoxal Inferred from electronic annotation. Source: Compara response to organic nitrogen Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Sin3 complex Inferred from direct assay PubMed 14966270. Source: UniProtKB kinetochore Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell transcription factor complex Inferred from electronic annotation. Source: Compara transcriptional repressor complex Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: Compara RNA polymerase II transcription corepressor activity Inferred from electronic annotation. Source: Compara chromatin binding Inferred from electronic annotation. Source: Compara protein deacetylase activity Inferred from mutant phenotype PubMed 22783022. Source: BHF-UCL sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HCFC1	P51610	6	EBI-347218,EBI-396176
HDAC2	Q92769	3	EBI-347218,EBI-301821
PA2G4	Q9UQ80	4	EBI-347218,EBI-924893
SFPQ	P23246	2	EBI-347218,EBI-355453
SKI	P12755	3	EBI-347218,EBI-347281
TP53	P04637	2	EBI-347218,EBI-366083

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1273	1273	Paired amphipathic helix protein Sin3a		PRO_0000121537
Regions
	Domain	119 – 189	71	PAH 1
	Domain	300 – 383	84	PAH 2
	Domain	456 – 525	70	PAH 3
	Region	119 – 196	78	Interaction with HCFC1 Ref.10
	Region	205 – 480	276	Interaction with REST By similarity
	Region	458 – 525	68	Interaction with SAP30 By similarity UniProtKB Q60520
	Region	523 – 850	328	Interaction with NCOR1 By similarity UniProtKB Q60520
	Region	524 – 659	136	Interaction with SUDS3 and SAP130
	Region	687 – 829	143	Interaction with HDAC1 and ARID4B
	Region	888 – 967	80	Interaction with OGT
	Coiled coil	903 – 932	30	Potential
	Compositional bias	218 – 285	68	Pro-rich
	Compositional bias	835 – 841	7	Poly-Glu
Amino acid modifications
	Modified residue	10	1	Phosphoserine Ref.16 Ref.17
	Modified residue	277	1	Phosphoserine Ref.17
	Modified residue	469	1	N6-acetyllysine Ref.19
	Modified residue	832	1	Phosphoserine Ref.17 Ref.18 Ref.20 Ref.23 PubMed 15302935
	Modified residue	860	1	Phosphoserine Ref.13 Ref.20 Ref.23 PubMed 15302935
	Modified residue	940	1	Phosphoserine Ref.17 Ref.20
	Modified residue	1112	1	Phosphoserine Ref.17 Ref.18 Ref.20 PubMed 15302935
Natural variations
	Natural variant	1156	1	M → L. Corresponds to variant rs60213317 [ dbSNP | Ensembl ].		VAR_062129
Experimental info
	Sequence conflict	163	1	G → R in AAK95854. Ref.4
	Sequence conflict	170 – 177	8	QLFKGHPD → HYSKGPPI in AAK95854. Ref.4
	Sequence conflict	182 – 192	11	FNTFLPPGYKI → IQHLFAPWATKM in AAK95854. Ref.4
	Sequence conflict	216	1	I → T in BAC04801. Ref.3
	Sequence conflict	386	1	S → F in AAK95854. Ref.4
	Sequence conflict	536	1	E → D in AAK95854. Ref.4
	Sequence conflict	562	1	P → G in AAK95854. Ref.4
	Sequence conflict	575 – 576	2	PL → GV in AAK95854. Ref.4
	Sequence conflict	595	1	S → C in AAK95854. Ref.4
	Sequence conflict	618 – 620	3	ELD → DLM in AAK95854. Ref.4
	Sequence conflict	1009	1	Q → R in BAC11280. Ref.3
	Sequence conflict	1247 – 1248	2	TT → NN in AAP97288. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q96ST3 [UniParc]. Last modified October 24, 2003. Version 2. Checksum: E6A329BE0EAD84CD	FASTA	1,273	145,175
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.

IPI

IPI00170596.

PIR

T17282.

RefSeq

NP_001138829.1. NM_001145357.1.
NP_001138830.1. NM_001145358.1.
NP_056292.1. NM_015477.2.

UniGene

Hs.513039.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PO4	model	-	B	295-383	[»]

ProteinModelPortal

Q96ST3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96ST3. 27 interactions.

MINT

MINT-2815493.

STRING

9606.ENSP00000353622.

PTM databases

PhosphoSite

Q96ST3.

Polymorphism databases

DMDM

37999759.

Proteomic databases

PaxDb

Q96ST3.

PeptideAtlas

Q96ST3.

PRIDE

Q96ST3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360439; ENSP00000353622; ENSG00000169375.
ENST00000394947; ENSP00000378402; ENSG00000169375.
ENST00000394949; ENSP00000378403; ENSG00000169375.

GeneID

25942.

KEGG

hsa:25942.

UCSC

uc002bai.3. human.

Organism-specific databases

CTD

25942.

GeneCards

GC15M075661.

H-InvDB

HIX0012443.
HIX0019634.
HIX0172841.

HGNC

HGNC:19353. SIN3A.

HPA

CAB004506.

MIM

607776. gene.

neXtProt

NX_Q96ST3.

PharmGKB

PA134993567.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5602.

HOVERGEN

HBG060425.

InParanoid

Q96ST3.

KO

K11644.

OMA

PNQNGCQ.

OrthoDB

EOG48KR9G.

PhylomeDB

Q96ST3.

Enzyme and pathway databases

Pathway_Interaction_DB

hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Reactome

REACT_111217. Metabolism.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q96ST3.

Bgee

Q96ST3.

CleanEx

HS_SIN3A.

Genevestigator

Q96ST3.

GermOnline

ENSG00000169375. Homo sapiens.

Family and domain databases

Gene3D

1.20.1160.11. 3 hits.

InterPro

IPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view]

Pfam

PF02671. PAH. 3 hits.
PF08295. Sin3_corepress. 1 hit.
[Graphical view]

SMART

SM00761. HDAC_interact. 1 hit.
[Graphical view]

SUPFAM

SSF47762. PAH. 3 hits.

PROSITE

PS51477. PAH. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SIN3A. human.

GenomeRNAi

25942.

NextBio

47516.

SOURCE

Search...

Entry information

Entry name

SIN3A_HUMAN

Accession

Primary (citable) accession number: Q96ST3
Secondary accession number(s): B2RNS5 , Q8N8N4, Q8NC83, Q8WV18, Q96L98, Q9UFQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2003
Last sequence update:	October 24, 2003
Last modified:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.