SIN3B_HUMAN - dbPTM
SIN3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIN3B_HUMAN
UniProt AC O75182
Protein Name Paired amphipathic helix protein Sin3b
Gene Name SIN3B {ECO:0000312|HGNC:HGNC:19354}
Organism Homo sapiens (Human).
Sequence Length 1162
Subcellular Localization Nucleus .
Protein Description Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. With FOXK1, regulates cell cycle progression probably by repressing cell cycle inhibitor genes expression..
Protein Sequence MAHAGGGSGGSGAGGPAGRGLSGARWGRSGSAGHEKLPVHVEDALTYLDQVKIRFGSDPATYNGFLEIMKEFKSQSIDTPGVIRRVSQLFHEHPDLIVGFNAFLPLGYRIDIPKNGKLNIQSPLTSQENSHNHGDGAEDFKQQVPYKEDKPQVPLESDSVEFNNAISYVNKIKTRFLDHPEIYRSFLEILHTYQKEQLNTRGRPFRGMSEEEVFTEVANLFRGQEDLLSEFGQFLPEAKRSLFTGNGPCEMHSVQKNEHDKTPEHSRKRSRPSLLRPVSAPAKKKMKLRGTKDLSIAAVGKYGTLQEFSFFDKVRRVLKSQEVYENFLRCIALFNQELVSGSELLQLVSPFLGKFPELFAQFKSFLGVKELSFAPPMSDRSGDGISREIDYASCKRIGSSYRALPKTYQQPKCSGRTAICKELDHWTLLQGSWTDDYCMSKFKNTCWIPGYSAGVLNDTWVSFPSWSEDSTFVSSKKTPYEEQLHRCEDERFELDVVLETNLATIRVLESVQKKLSRMAPEDQEKFRLDDSLGGTSEVIQRRAIYRIYGDKAPEIIESLKKNPVTAVPVVLKRLKAKEEEWREAQQGFNKIWREQYEKAYLKSLDHQAVNFKQNDTKALRSKSLLNEIESVYDEHQEQHSEGRSAPSSEPHLIFVYEDRQILEDAAALISYYVKRQPAIQKEDQGTIHQLLHQFVPSLFFSQQLDLGASEESADEDRDSPQGQTTDPSERKKPAPGPHSSPPEEKGAFGDAPATEQPPLPPPAPHKPLDDVYSLFFANNNWYFFLRLHQTLCSRLLKIYRQAQKQLLEYRTEKEREKLLCEGRREKGSDPAMELRLKQPSEVELEEYYPAFLDMVRSLLEGSIDPTQYEDTLREMFTIHAYVGFTMDKLVQNIARQLHHLVSDDVCLKVVELYLNEKKRGAAGGNLSSRCVRAARETSYQWKAERCMADENCFKVMFLQRKGQVIMTIELLDTEEAQTEDPVEVQHLARYVEQYVGTEGASSSPTEGFLLKPVFLQRNLKKFRRRWQSEQARALRGEARSSWKRLVGVESACDVDCRFKLSTHKMVFIVNSEDYMYRRGTLCRAKQVQPLVLLRHHQHFEEWHSRWLEDNVTVEAASLVQDWLMGEEDEDMVPCKTLCETVHVHGLPVTRYRVQYSRRPASP
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
8PhosphorylationMAHAGGGSGGSGAGG
CCCCCCCCCCCCCCC		43.1629255136
11PhosphorylationAGGGSGGSGAGGPAG
CCCCCCCCCCCCCCC		29.0629255136
19MethylationGAGGPAGRGLSGARW
CCCCCCCCCCCCCCC		45.0158859561
29PhosphorylationSGARWGRSGSAGHEK
CCCCCCCCCCCCCCC		32.9124719451
31PhosphorylationARWGRSGSAGHEKLP
CCCCCCCCCCCCCCC		32.1223312004
36UbiquitinationSGSAGHEKLPVHVED
CCCCCCCCCCCCHHH		53.03-
46PhosphorylationVHVEDALTYLDQVKI
CCHHHHHHHHHHHEE		24.6128509920
47PhosphorylationHVEDALTYLDQVKIR
CHHHHHHHHHHHEEE		14.7728509920
74PhosphorylationEIMKEFKSQSIDTPG
HHHHHHHHCCCCCHH		34.1921406692
76PhosphorylationMKEFKSQSIDTPGVI
HHHHHHCCCCCHHHH		29.5324719451
79PhosphorylationFKSQSIDTPGVIRRV
HHHCCCCCHHHHHHH		21.9224719451
122PhosphorylationNGKLNIQSPLTSQEN
CCEECCCCCCCCCCC		20.3423401153
125PhosphorylationLNIQSPLTSQENSHN
ECCCCCCCCCCCCCC		31.5723663014
126PhosphorylationNIQSPLTSQENSHNH
CCCCCCCCCCCCCCC		43.0823663014
130PhosphorylationPLTSQENSHNHGDGA
CCCCCCCCCCCCCCH		25.5523663014
146PhosphorylationDFKQQVPYKEDKPQV
HHHHHCCCCCCCCCC		28.31-
239 (in isoform 1)Ubiquitination-40.6421906983
239UbiquitinationGQFLPEAKRSLFTGN
HHHCHHHHHHHHCCC		40.642190698
239 (in isoform 3)Ubiquitination-40.6421906983
239 (in isoform 2)Ubiquitination-40.6421906983
241PhosphorylationFLPEAKRSLFTGNGP
HCHHHHHHHHCCCCC		27.42-
253PhosphorylationNGPCEMHSVQKNEHD
CCCCEEECCCCCCCC		25.5728555341
262PhosphorylationQKNEHDKTPEHSRKR
CCCCCCCCHHHHCCC		39.7130576142
266PhosphorylationHDKTPEHSRKRSRPS
CCCCHHHHCCCCCCH		37.5228985074
270PhosphorylationPEHSRKRSRPSLLRP
HHHHCCCCCCHHHCC		52.1323312004
273PhosphorylationSRKRSRPSLLRPVSA
HCCCCCCHHHCCCCC		38.6425159151
279PhosphorylationPSLLRPVSAPAKKKM
CHHHCCCCCCCHHHC		31.0825159151
284AcetylationPVSAPAKKKMKLRGT
CCCCCCHHHCCCCCC		61.277851831
304PhosphorylationAAVGKYGTLQEFSFF
EEECCCCCCHHCCHH		23.37-
381PhosphorylationAPPMSDRSGDGISRE
CCCCCCCCCCCCCCC		46.3429083192
386PhosphorylationDRSGDGISREIDYAS
CCCCCCCCCCCHHHH		29.4129083192
393PhosphorylationSREIDYASCKRIGSS
CCCCHHHHHHCCCCC		17.5929083192
406UbiquitinationSSYRALPKTYQQPKC
CCCCCCCCCCCCCCC		61.79-
531PhosphorylationEKFRLDDSLGGTSEV
HHHCCCCCCCCCHHH		28.6923403867
535PhosphorylationLDDSLGGTSEVIQRR
CCCCCCCCHHHHHHH		21.6623403867
536PhosphorylationDDSLGGTSEVIQRRA
CCCCCCCHHHHHHHH		32.8923403867
548PhosphorylationRRAIYRIYGDKAPEI
HHHHHHHHCCCHHHH		15.4129523821
551UbiquitinationIYRIYGDKAPEIIES
HHHHHCCCHHHHHHH		62.57-
558PhosphorylationKAPEIIESLKKNPVT
CHHHHHHHHHHCCCC		34.7729523821
590UbiquitinationEAQQGFNKIWREQYE
HHHHHHHHHHHHHHH		41.19-
600PhosphorylationREQYEKAYLKSLDHQ
HHHHHHHHHHHCCHH		26.2320068231
602UbiquitinationQYEKAYLKSLDHQAV
HHHHHHHHHCCHHCC		35.97-
603PhosphorylationYEKAYLKSLDHQAVN
HHHHHHHHCCHHCCC		36.1120068231
616PhosphorylationVNFKQNDTKALRSKS
CCCCCCCHHHHHCHH		26.2620068231
630PhosphorylationSLLNEIESVYDEHQE
HHHHHHHHHHHHHHH		31.4727732954
632PhosphorylationLNEIESVYDEHQEQH
HHHHHHHHHHHHHHH		25.5427732954
640PhosphorylationDEHQEQHSEGRSAPS
HHHHHHHCCCCCCCC		41.2527732954
709PhosphorylationQQLDLGASEESADED
HCCCCCCCCCCCCCC		39.85-
712PhosphorylationDLGASEESADEDRDS
CCCCCCCCCCCCCCC		36.65-
719PhosphorylationSADEDRDSPQGQTTD
CCCCCCCCCCCCCCC		21.73-
728PhosphorylationQGQTTDPSERKKPAP
CCCCCCHHHCCCCCC		53.49-
739PhosphorylationKPAPGPHSSPPEEKG
CCCCCCCCCCHHHCC		47.9023401153
740PhosphorylationPAPGPHSSPPEEKGA
CCCCCCCCCHHHCCC		41.2530266825
817UbiquitinationRTEKEREKLLCEGRR
HCHHHHHHHHHHCCH		53.64-
877PhosphorylationDTLREMFTIHAYVGF
HHHHHHHHHHHHHCC		15.56-
881PhosphorylationEMFTIHAYVGFTMDK
HHHHHHHHHCCCHHH		6.22-
990PhosphorylationEVQHLARYVEQYVGT
HHHHHHHHHHHHHCC		11.6125022875
994PhosphorylationLARYVEQYVGTEGAS
HHHHHHHHHCCCCCC		6.3229978859
997PhosphorylationYVEQYVGTEGASSSP
HHHHHHCCCCCCCCC		22.6225022875
1001PhosphorylationYVGTEGASSSPTEGF
HHCCCCCCCCCCCCC		42.0519276368
1002PhosphorylationVGTEGASSSPTEGFL
HCCCCCCCCCCCCCC		39.5425159151
1003PhosphorylationGTEGASSSPTEGFLL
CCCCCCCCCCCCCCC		33.0925159151
1005PhosphorylationEGASSSPTEGFLLKP
CCCCCCCCCCCCCCH		51.1725022875
1071PhosphorylationKMVFIVNSEDYMYRR
CEEEEECCHHHCHHC		22.43-
1074PhosphorylationFIVNSEDYMYRRGTL
EEECCHHHCHHCCCC		7.6229759185
1076PhosphorylationVNSEDYMYRRGTLCR
ECCHHHCHHCCCCCC		7.3129759185
1140PhosphorylationPCKTLCETVHVHGLP
CCHHHEEEEEECCEE		18.2126074081
1149PhosphorylationHVHGLPVTRYRVQYS
EECCEECEEEEEEEC		21.7526074081
1151PhosphorylationHGLPVTRYRVQYSRR
CCEECEEEEEEECCC		13.0326074081
1155PhosphorylationVTRYRVQYSRRPASP
CEEEEEEECCCCCCC		10.9926074081
1156PhosphorylationTRYRVQYSRRPASP-
EEEEEEECCCCCCC-		12.5326074081
1161PhosphorylationQYSRRPASP------
EECCCCCCC------		33.5526074081
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
-KUbiquitinationE3 ubiquitin ligaseRNF220Q5VTB9
PMID:20170641
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIN3B_HUMAN !!
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 SIN3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SETB1_HUMANSETDB1physical
12398767
HDAC1_HUMANHDAC1physical
10357820
IKZF1_HUMANIKZF1physical
10357820
ZBT16_HUMANZBTB16physical
9627120
IKZF1_HUMANIKZF1physical
12015313
NSD2_HUMANWHSC1physical
16197452
RN220_HUMANRNF220physical
20170641
SMCA4_HUMANSMARCA4physical
14559996
SMCA2_HUMANSMARCA2physical
14559996
SMCE1_HUMANSMARCE1physical
14559996
SNF5_HUMANSMARCB1physical
14559996
MYT1_HUMANMYT1physical
15935060
HDAC2_HUMANHDAC2physical
15935060
ARI4A_HUMANARID4Aphysical
11283269
MXI1_HUMANMXI1physical
15467743
SMN_HUMANSMN1physical
14749338
BRMS1_HUMANBRMS1physical
14581478
ACTN4_HUMANACTN4physical
26496610
HDAC1_HUMANHDAC1physical
26496610
KDM5A_HUMANKDM5Aphysical
26496610
RBBP7_HUMANRBBP7physical
26496610
STX3_HUMANSTX3physical
26496610
SAP30_HUMANSAP30physical
26496610
AKA12_HUMANAKAP12physical
26496610
LSM4_HUMANLSM4physical
26496610
SIN3A_HUMANSIN3Aphysical
26496610
PLPL8_HUMANPNPLA8physical
26496610
EMSY_HUMANC11orf30physical
26496610
PHF12_HUMANPHF12physical
26496610
GATD1_HUMANGATAD1physical
26496610
SP130_HUMANSAP130physical
26496610
TNC18_HUMANTNRC18physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIN3B_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory