SIN3A_MOUSE - dbPTM
SIN3A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIN3A_MOUSE
UniProt AC Q60520
Protein Name Paired amphipathic helix protein Sin3a
Gene Name Sin3a
Organism Mus musculus (Mouse).
Sequence Length 1274
Subcellular Localization Nucleus . Nucleus, nucleolus . Recruited to the nucleolus by SAP30L.
Protein Description 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 the 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. Cooperates with FOXK1 to regulate cell cycle progression probably by repressing cell cycle inhibitor genes expression. [PubMed: 22476904]
Protein Sequence MKRRLDDQESPVYAAQQRRIPGSTEAFSHQHRVLAPAPPVYEAVSETMQSATGIQYSVAPNYQVSAVPQSSGSHGPAIAAVHSSHHHPTAVQPHGGQVVQSHAHPAPPVAPVQGQQQFQRLKVEDALSYLDQVKLQFGSQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPDLIMGFNTFLPPGYKIEVQTNDMVNVTTPGQVHQIPTHGIQPQPQPPPQHPSQPSSQSAPTPAQPAPQPTAAKVSKPSQLQAHTPASQQTPPLPPYASPRSPPVQPHTPVTISLGTAPSLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALTEQEVYAQVARLFKNQEDLLSEFGQFLPDANSSVLLSKTTAEKVDSVRNDHGGTVKKPQLNNKPQRPSQNGCQIRRHSGTGATPPVKKKPKLMSLKESSMADASKHGVGTESLFFDKVRKALRSAEAYENFLRCLVIFNQEVISRAELVQLVSPFLGKFPELFNWFKNFLGYKESVHLESFPKERATEGIAMEIDYASCKRLGSSYRALPKSYQQPKCTGRTPLCKEVLNDTWVSFPSWSEDSTFVSSKKTQYEEHIYRCEDERFELDVVLETNLATIRVLEAIQKKLSRLSAEEQAKFRLDNTLGGTSEVIHRKALQRIYADKAADIIDGLRKNPSIAVPIVLKRLKMKEEEWREAQRGFNKVWREQNEKYYLKSLDHQGINFKQNDTKVLRSKSLLNEIESIYDERQEQATEENAGVPVGPHLSLAYEDKQILEDAAALIIHHVKRQTGIQKEDKYKIKQIMHHFIPDLLFAQRGDLSDVEEEEEEEMDVDEATGAPKKHNGVGGSPPKSKLLFSNTAAQKLRGMDEVYNLFYVNNNWYIFMRLHQILCLRLLRICSQAERQIEEENREREWEREVLGIKRDKSDSPAIQLRLKEPMDVDVEDYYPAFLDMVRSLLDGNIDSSQYEDSLREMFTIHAYIAFTMDKLIQSIVRQLQHIVSDEVCVQVTDLYLAENNNGATGGQLNSQTSRSLLESAYQRKAEQLMSDENCFKLMFIQSQGQVQLTVELLDTEEENSDDPVEAERWSDYVERYMSSDTTSPELREHLAQKPVFLPRNLRRIRKCQRGREQQEKEGKEGNSKKTMENVESLDKLECRFKLNSYKMVYVIKSEDYMYRRTALLRAHQSHERVSKRLHQRFQAWVDKWTKEHVPREMAAETSKWLMGEGLEGLVPCTTTCDTETLHFVSINKYRVKYGTVFKAP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationRRLDDQESPVYAAQQ
CCCCCCCCHHHHHHH		17.6521082442
155UbiquitinationLDIMKEFKSQSIDTP
HHHHHHHHHCCCCCC		48.9927667366
251PhosphorylationQPTAAKVSKPSQLQA
CCCCCCCCCHHHCCC		37.8426643407
251O-linked_GlycosylationQPTAAKVSKPSQLQA
CCCCCCCCCHHHCCC		37.8422517741
254PhosphorylationAAKVSKPSQLQAHTP
CCCCCCHHHCCCCCC		47.4626643407
260PhosphorylationPSQLQAHTPASQQTP
HHHCCCCCCHHHCCC		24.4626643407
263PhosphorylationLQAHTPASQQTPPLP
CCCCCCHHHCCCCCC		24.8326643407
266PhosphorylationHTPASQQTPPLPPYA
CCCHHHCCCCCCCCC		21.1626643407
272PhosphorylationQTPPLPPYASPRSPP
CCCCCCCCCCCCCCC		20.1226643407
274PhosphorylationPPLPPYASPRSPPVQ
CCCCCCCCCCCCCCC		18.2725266776
277PhosphorylationPPYASPRSPPVQPHT
CCCCCCCCCCCCCCC		36.6226824392
284PhosphorylationSPPVQPHTPVTISLG
CCCCCCCCCEEEEEC		26.5721082442
287PhosphorylationVQPHTPVTISLGTAP
CCCCCCEEEEECCCC		13.1725159016
289PhosphorylationPHTPVTISLGTAPSL
CCCCEEEEECCCCCC		16.0425159016
292PhosphorylationPVTISLGTAPSLQNN
CEEEEECCCCCCCCC		40.4626160508
295PhosphorylationISLGTAPSLQNNQPV
EEECCCCCCCCCCCC		39.8725293948
310PhosphorylationEFNHAINYVNKIKNR
CHHHHHHHHHHHHHH		10.1725293948
349PhosphorylationAKEAGGNYTPALTEQ
HHHCCCCCCCCCCHH		19.8530635358
350PhosphorylationKEAGGNYTPALTEQE
HHCCCCCCCCCCHHH		13.1930635358
354PhosphorylationGNYTPALTEQEVYAQ
CCCCCCCCHHHHHHH		37.4230635358
431PhosphorylationGCQIRRHSGTGATPP
CCCEECCCCCCCCCC		35.9226824392
433PhosphorylationQIRRHSGTGATPPVK
CEECCCCCCCCCCCC		27.0223984901
436PhosphorylationRHSGTGATPPVKKKP
CCCCCCCCCCCCCCC		29.4827149854
470AcetylationTESLFFDKVRKALRS
HHHHHHHHHHHHHHH		38.49-
559PhosphorylationCKRLGSSYRALPKSY
HHHCCCCCCCCCHHH		11.12-
566PhosphorylationYRALPKSYQQPKCTG
CCCCCHHHCCCCCCC		19.79-
572PhosphorylationSYQQPKCTGRTPLCK
HHCCCCCCCCCCCHH		35.5127149854
639AcetylationRVLEAIQKKLSRLSA
HHHHHHHHHHHCCCH		49.9522733758
729PhosphorylationNEKYYLKSLDHQGIN
HHHHCCCCCCCCCCC		36.11-
742PhosphorylationINFKQNDTKVLRSKS
CCCCCCCHHHHHCHH		30.5125159016
833PhosphorylationFAQRGDLSDVEEEEE
HHCCCCCHHCCHHHH		44.3324925903
843OxidationEEEEEEEMDVDEATG
CHHHHHCCCHHHHCC		7.4217242355
849PhosphorylationEMDVDEATGAPKKHN
CCCHHHHCCCCCCCC		31.6525619855
861PhosphorylationKHNGVGGSPPKSKLL
CCCCCCCCCCCHHHC		31.9127087446
865PhosphorylationVGGSPPKSKLLFSNT
CCCCCCCHHHCCCHH		34.0225266776
866AcetylationGGSPPKSKLLFSNTA
CCCCCCHHHCCCHHH		56.1723806337
876UbiquitinationFSNTAAQKLRGMDEV
CCHHHHHHHCCCCHH		35.1127667366
876AcetylationFSNTAAQKLRGMDEV
CCHHHHHHHCCCCHH		35.1123806337
938UbiquitinationVLGIKRDKSDSPAIQ
HHCCCCCCCCCCCEE		61.26-
939PhosphorylationLGIKRDKSDSPAIQL
HCCCCCCCCCCCEEC		47.8425619855
941PhosphorylationIKRDKSDSPAIQLRL
CCCCCCCCCCEECCC		24.2725521595
1090PhosphorylationLDTEEENSDDPVEAE
CCCCCCCCCCCCHHH		46.82-
1106PhosphorylationWSDYVERYMSSDTTS
HHHHHHHHHCCCCCC		6.4528833060
1108PhosphorylationDYVERYMSSDTTSPE
HHHHHHHCCCCCCHH		19.0026239621
1109PhosphorylationYVERYMSSDTTSPEL
HHHHHHCCCCCCHHH		23.5826239621
1111PhosphorylationERYMSSDTTSPELRE
HHHHCCCCCCHHHHH		30.9921082442
1111 (in isoform 1)Phosphorylation-30.9925266776
1112PhosphorylationRYMSSDTTSPELREH
HHHCCCCCCHHHHHH		47.4722942356
1113PhosphorylationYMSSDTTSPELREHL
HHCCCCCCHHHHHHH		20.6125521595
1114 (in isoform 1)Phosphorylation-42.4225266776
1115 (in isoform 1)Phosphorylation-61.2925266776
1116PhosphorylationSDTTSPELREHLAQK
CCCCCHHHHHHHHCC		9.8824719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SIN3A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIN3A_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SIN3A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN2_HUMANCOPS2physical
10207062
HDAC1_MOUSEHdac1physical
10688671
SUFU_MOUSESufugenetic
11960000
SMAD4_MOUSESmad4physical
17226765
P53_MOUSETrp53physical
20211142
NANOG_MOUSENanogphysical
18454139
SNAI1_HUMANSNAI1physical
14673164
SNAI2_HUMANSNAI2physical
14673164
SNAI3_HUMANSNAI3physical
14673164
HDAC2_MOUSEHdac2physical
16109738
SP3_MOUSESp3physical
16109738
MNT_MOUSEMntphysical
16103876
SIN3B_MOUSESin3bphysical
16103876
HDAC1_MOUSEHdac1physical
16103876
SDS3_MOUSESuds3physical
15489224
P53_HUMANTP53physical
11313951
TBP_HUMANTBPphysical
11313951
KLF1_HUMANKLF1physical
11287616
SFPQ_HUMANSFPQphysical
11259580
MAD1_HUMANMXD1physical
10551834
HDAC1_MOUSEHdac1physical
10409740
CEBPB_MOUSECebpbphysical
21521687
HDAC1_MOUSEHdac1physical
21454521
GON4L_MOUSEGon4lphysical
21454521
TYY1_MOUSEYy1physical
21454521
HDAC1_MOUSEHdac1physical
21448134
KDM5B_MOUSEKdm5bphysical
21448134
PER2_MOUSEPer2physical
21680841
SFPQ_MOUSESfpqphysical
21680841
ETV6_MOUSEEtv6physical
12527908
TET1_MOUSETet1physical
21490601
GOGA1_HUMANGOLGA1physical
26496610
HDAC1_HUMANHDAC1physical
26496610
ING1_HUMANING1physical
26496610
ARI4A_HUMANARID4Aphysical
26496610
RBBP7_HUMANRBBP7physical
26496610
SAP30_HUMANSAP30physical
26496610
NCOR1_HUMANNCOR1physical
26496610
VINEX_HUMANSORBS3physical
26496610
BRMS1_HUMANBRMS1physical
26496610
FA60A_HUMANFAM60Aphysical
26496610
SDS3_HUMANSUDS3physical
26496610
SP130_HUMANSAP130physical
26496610
BRM1L_HUMANBRMS1Lphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIN3A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861, AND MASSSPECTROMETRY.

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