SATB1_HUMAN - dbPTM
SATB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SATB1_HUMAN
UniProt AC Q01826
Protein Name DNA-binding protein SATB1
Gene Name SATB1
Organism Homo sapiens (Human).
Sequence Length 763
Subcellular Localization Nucleus matrix. Nucleus, PML body. Organized into a cage-like network anchoring loops of heterochromatin and tethering specialized DNA sequences. When sumoylated, localized in promyelocytic leukemia nuclear bodies (PML NBs).
Protein Description Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma (By similarity). Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes (e.g. PML at the MHC-I locus) and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis..
Protein Sequence MDHLNEATQGKEHSEMSNNVSDPKGPPAKIARLEQNGSPLGRGRLGSTGAKMQGVPLKHSGHLMKTNLRKGTMLPVFCVVEHYENAIEYDCKEEHAEFVLVRKDMLFNQLIEMALLSLGYSHSSAAQAKGLIQVGKWNPVPLSYVTDAPDATVADMLQDVYHVVTLKIQLHSCPKLEDLPPEQWSHTTVRNALKDLLKDMNQSSLAKECPLSQSMISSIVNSTYYANVSAAKCQEFGRWYKHFKKTKDMMVEMDSLSELSQQGANHVNFGQQPVPGNTAEQPPSPAQLSHGSQPSVRTPLPNLHPGLVSTPISPQLVNQQLVMAQLLNQQYAVNRLLAQQSLNQQYLNHPPPVSRSMNKPLEQQVSTNTEVSSEIYQWVRDELKRAGISQAVFARVAFNRTQGLLSEILRKEEDPKTASQSLLVNLRAMQNFLQLPEAERDRIYQDERERSLNAASAMGPAPLISTPPSRPPQVKTATIATERNGKPENNTMNINASIYDEIQQEMKRAKVSQALFAKVAATKSQGWLCELLRWKEDPSPENRTLWENLSMIRRFLSLPQPERDAIYEQESNAVHHHGDRPPHIIHVPAEQIQQQQQQQQQQQQQQQAPPPPQPQQQPQTGPRLPPRQPTVASPAESDEENRQKTRPRTKISVEALGILQSFIQDVGLYPDEEAIQTLSAQLDLPKYTIIKFFQNQRYYLKHHGKLKDNSGLEVDVAEYKEEELLKDLEESVQDKNTNTLFSVKLEEELSVEGNTDINTDLKD
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
1Acetylation-------MDHLNEAT
-------CCHHHHHH		7.08-
24AcetylationSNNVSDPKGPPAKIA
CCCCCCCCCCHHHHH		84.657975543
29UbiquitinationDPKGPPAKIARLEQN
CCCCCHHHHHHHHHC		42.55-
38PhosphorylationARLEQNGSPLGRGRL
HHHHHCCCCCCCCCC		25.2223401153
42MethylationQNGSPLGRGRLGSTG
HCCCCCCCCCCCCCC		34.4483445813
47PhosphorylationLGRGRLGSTGAKMQG
CCCCCCCCCCCCCCC		28.4130576142
48PhosphorylationGRGRLGSTGAKMQGV
CCCCCCCCCCCCCCC		39.0822496350
51SumoylationRLGSTGAKMQGVPLK
CCCCCCCCCCCCCCC		32.8528112733
51AcetylationRLGSTGAKMQGVPLK
CCCCCCCCCCCCCCC		32.8525953088
51UbiquitinationRLGSTGAKMQGVPLK
CCCCCCCCCCCCCCC		32.85-
58UbiquitinationKMQGVPLKHSGHLMK
CCCCCCCCCCCCCCC		29.65-
58 (in isoform 2)Ubiquitination-29.65-
65UbiquitinationKHSGHLMKTNLRKGT
CCCCCCCCCCCCCCC		40.39-
117PhosphorylationLIEMALLSLGYSHSS
HHHHHHHHCCCCCCH		22.1622210691
120PhosphorylationMALLSLGYSHSSAAQ
HHHHHCCCCCCHHHH		14.4322210691
136AcetylationKGLIQVGKWNPVPLS
CCCEEECCCCCCCCH		44.9616630892
175UbiquitinationIQLHSCPKLEDLPPE
EEECCCCCHHHCCHH		69.69-
185PhosphorylationDLPPEQWSHTTVRNA
HCCHHHCCHHHHHHH		15.6219060867
188PhosphorylationPEQWSHTTVRNALKD
HHHCCHHHHHHHHHH		16.4320351170
194UbiquitinationTTVRNALKDLLKDMN
HHHHHHHHHHHHHCC		43.87-
194 (in isoform 2)Ubiquitination-43.87-
194MalonylationTTVRNALKDLLKDMN
HHHHHHHHHHHHHCC		43.8726320211
198UbiquitinationNALKDLLKDMNQSSL
HHHHHHHHHCCHHHH		63.33-
198 (in isoform 2)Ubiquitination-63.33-
203PhosphorylationLLKDMNQSSLAKECP
HHHHCCHHHHHHHCC		23.4723532336
204PhosphorylationLKDMNQSSLAKECPL
HHHCCHHHHHHHCCC		23.6823532336
212PhosphorylationLAKECPLSQSMISSI
HHHHCCCCHHHHHHH		12.8328122231
214PhosphorylationKECPLSQSMISSIVN
HHCCCCHHHHHHHHH		18.0828122231
217PhosphorylationPLSQSMISSIVNSTY
CCCHHHHHHHHHHCC		12.8428122231
218PhosphorylationLSQSMISSIVNSTYY
CCHHHHHHHHHHCCC		21.4528122231
284PhosphorylationNTAEQPPSPAQLSHG
CCCCCCCCHHHCCCC		39.2828464451
298PhosphorylationGSQPSVRTPLPNLHP
CCCCCCCCCCCCCCC		27.3328464451
309PhosphorylationNLHPGLVSTPISPQL
CCCCCCCCCCCCHHH		33.2428634298
310PhosphorylationLHPGLVSTPISPQLV
CCCCCCCCCCCHHHH		19.7028464451
313PhosphorylationGLVSTPISPQLVNQQ
CCCCCCCCHHHHHHH		14.0628464451
331PhosphorylationAQLLNQQYAVNRLLA
HHHHCHHHHHHHHHH		11.6227642862
341O-linked_GlycosylationNRLLAQQSLNQQYLN
HHHHHHHHHHHHHHC		19.7329351928
341PhosphorylationNRLLAQQSLNQQYLN
HHHHHHHHHHHHHHC		19.73-
346PhosphorylationQQSLNQQYLNHPPPV
HHHHHHHHHCCCCCC		10.3328796482
354O-linked_GlycosylationLNHPPPVSRSMNKPL
HCCCCCCCHHCCCCH		25.1429351928
366PhosphorylationKPLEQQVSTNTEVSS
CCHHHHCCCCCHHHH		16.1724247654
421PhosphorylationDPKTASQSLLVNLRA
CCCCCCHHHHHHHHH		22.6025159151
429SulfoxidationLLVNLRAMQNFLQLP
HHHHHHHHHHHHCCC		2.4321406390
451PhosphorylationYQDERERSLNAASAM
HHHHHHHHHHHHHHC		22.6326074081
456PhosphorylationERSLNAASAMGPAPL
HHHHHHHHHCCCCCC		19.1726074081
465PhosphorylationMGPAPLISTPPSRPP
CCCCCCCCCCCCCCC		42.4130576142
466PhosphorylationGPAPLISTPPSRPPQ
CCCCCCCCCCCCCCC		32.0228464451
469PhosphorylationPLISTPPSRPPQVKT
CCCCCCCCCCCCCCE		59.6328450419
481PhosphorylationVKTATIATERNGKPE
CCEEEEEECCCCCCC		31.4622210691
512PhosphorylationEMKRAKVSQALFAKV
HHHHHHHHHHHHHHH		14.72-
524PhosphorylationAKVAATKSQGWLCEL
HHHHHHHCCCHHHHH		29.57-
557PhosphorylationSMIRRFLSLPQPERD
HHHHHHHCCCCCHHC		34.98-
594 (in isoform 2)Phosphorylation-44.6828796482
596 (in isoform 2)Phosphorylation-38.4228796482
598 (in isoform 2)Phosphorylation-38.4228796482
599 (in isoform 2)Phosphorylation-38.4228796482
630PhosphorylationRLPPRQPTVASPAES
CCCCCCCCCCCCCCC		21.9922115753
633PhosphorylationPRQPTVASPAESDEE
CCCCCCCCCCCCCHH		21.9523401153
637PhosphorylationTVASPAESDEENRQK
CCCCCCCCCHHHHHH		53.0523401153
649PhosphorylationRQKTRPRTKISVEAL
HHHCCCCCHHHHHHH		35.10-
652PhosphorylationTRPRTKISVEALGIL
CCCCCHHHHHHHHHH		18.5622468782
661PhosphorylationEALGILQSFIQDVGL
HHHHHHHHHHHHCCC		22.3722468782
710PhosphorylationHGKLKDNSGLEVDVA
CCCCCCCCCCEEEHH		55.6928122231
731PhosphorylationLLKDLEESVQDKNTN
HHHHHHHHHHCCCCC		18.7230576142
735UbiquitinationLEESVQDKNTNTLFS
HHHHHHCCCCCCEEE		48.89-
744SumoylationTNTLFSVKLEEELSV
CCCEEEEEEEEECCC		49.3218408014
744SumoylationTNTLFSVKLEEELSV
CCCEEEEEEEEECCC		49.32-
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 ligaseSMURF2Q9HAU4
PMID:30742943
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SATB1_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 SATB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC9_HUMANUBE2Iphysical
16189514
SIN3A_HUMANSIN3Aphysical
12374985
HDAC1_HUMANHDAC1physical
12374985
HDAC2_HUMANHDAC2physical
12374985
BAZ1A_HUMANBAZ1Aphysical
12374985
MTA2_HUMANMTA2physical
12374985
SMCA5_HUMANSMARCA5physical
12374985
RPB11_HUMANPOLR2Jphysical
12036295
CTBP1_HUMANCTBP1physical
19103759
PML_HUMANPMLphysical
17173041
KAT2B_HUMANKAT2Bphysical
16630892
HDAC1_HUMANHDAC1physical
16630892
TAT_HV1H2tatphysical
15713622
TAL1_HUMANTAL1physical
15677454
UBC9_HUMANUBE2Iphysical
20351170
UBR5_HUMANUBR5physical
20351170
TOPRS_HUMANTOPORSphysical
20351170
CBX4_HUMANCBX4physical
20351170
PIAS1_HUMANPIAS1physical
20351170
PIAS3_HUMANPIAS3physical
20351170
PIAS4_HUMANPIAS4physical
20351170
CTNB1_HUMANCTNNB1physical
20126258
SIR1_HUMANSIRT1physical
22328728
SUMO1_HUMANSUMO1physical
18408014
PIAS1_HUMANPIAS1physical
18408014
UBC9_HUMANUBE2Iphysical
18408014
PIAS3_HUMANPIAS3physical
18408014
CBX4_HUMANCBX4physical
18408014
TOPRS_HUMANTOPORSphysical
18408014
PIAS4_HUMANPIAS4physical
18408014
PML_HUMANPMLphysical
18408014
CASP6_HUMANCASP6physical
18408014
EP300_HUMANEP300physical
14605447
CHD3_HUMANCHD3physical
12374985
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 SATB1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"Phosphorylation of SATB1, a global gene regulator, acts as amolecular switch regulating its transcriptional activity in vivo.";
Kumar P.P., Purbey P.K., Sinha C.K., Notani D., Limaye A.,Jayani R.S., Galande S.;
Mol. Cell 22:231-243(2006).
Cited for: FUNCTION, MASS SPECTROMETRY, INTERACTION WITH HDAC1 AND PCAF,MUTAGENESIS OF LYS-136 AND SER-185, ACETYLATION AT LYS-136, ANDPHOSPHORYLATION AT SER-185.
Phosphorylation
ReferencePubMed
"Phosphorylation of SATB1, a global gene regulator, acts as amolecular switch regulating its transcriptional activity in vivo.";
Kumar P.P., Purbey P.K., Sinha C.K., Notani D., Limaye A.,Jayani R.S., Galande S.;
Mol. Cell 22:231-243(2006).
Cited for: FUNCTION, MASS SPECTROMETRY, INTERACTION WITH HDAC1 AND PCAF,MUTAGENESIS OF LYS-136 AND SER-185, ACETYLATION AT LYS-136, ANDPHOSPHORYLATION AT SER-185.
Sumoylation
ReferencePubMed
"SUMO conjugation to the matrix attachment region-binding protein,special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 topromyelocytic nuclear bodies where it undergoes caspase cleavage.";
Tan J.-A.T., Sun Y., Song J., Chen Y., Krontiris T.G., Durrin L.K.;
J. Biol. Chem. 283:18124-18134(2008).
Cited for: SUMOYLATION AT LYS-744, MUTAGENESIS OF LYS-411; LYS-486; LYS-720 ANDLYS-744, SUBCELLULAR LOCATION, AND CLEAVAGE BY CASPASE-6.

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