SATB2_HUMAN - dbPTM
SATB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SATB2_HUMAN
UniProt AC Q9UPW6
Protein Name DNA-binding protein SATB2
Gene Name SATB2
Organism Homo sapiens (Human).
Sequence Length 733
Subcellular Localization Nucleus matrix .
Protein Description Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, 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 and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper-layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating BCL11B expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation..
Protein Sequence MERRSESPCLRDSPDRRSGSPDVKGPPPVKVARLEQNGSPMGARGRPNGAVAKAVGGLMIPVFCVVEQLDGSLEYDNREEHAEFVLVRKDVLFSQLVETALLALGYSHSSAAQAQGIIKLGRWNPLPLSYVTDAPDATVADMLQDVYHVVTLKIQLQSCSKLEDLPAEQWNHATVRNALKELLKEMNQSTLAKECPLSQSMISSIVNSTYYANVSATKCQEFGRWYKKYKKIKVERVERENLSDYCVLGQRPMHLPNMNQLASLGKTNEQSPHSQIHHSTPIRNQVPALQPIMSPGLLSPQLSPQLVRQQIAMAHLINQQIAVSRLLAHQHPQAINQQFLNHPPIPRAVKPEPTNSSVEVSPDIYQQVRDELKRASVSQAVFARVAFNRTQGLLSEILRKEEDPRTASQSLLVNLRAMQNFLNLPEVERDRIYQDERERSMNPNVSMVSSASSSPSSSRTPQAKTSTPTTDLPIKVDGANINITAAIYDEIQQEMKRAKVSQALFAKVAANKSQGWLCELLRWKENPSPENRTLWENLCTIRRFLNLPQHERDVIYEEESRHHHSERMQHVVQLPPEPVQVLHRQQSQPAKESSPPREEAPPPPPPTEDSCAKKPRSRTKISLEALGILQSFIHDVGLYPDQEAIHTLSAQLDLPKHTIIKFFQNQRYHVKHHGKLKEHLGSAVDVAEYKDEELLTESEENDSEEGSEEMYKVEAEEENADKSKAAPAEIDQR
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
5Phosphorylation---MERRSESPCLRD
---CCCCCCCCCCCC		48.9625850435
7Phosphorylation-MERRSESPCLRDSP
-CCCCCCCCCCCCCC		23.3529255136
13PhosphorylationESPCLRDSPDRRSGS
CCCCCCCCCCCCCCC		23.4329255136
18PhosphorylationRDSPDRRSGSPDVKG
CCCCCCCCCCCCCCC		44.5130266825
20PhosphorylationSPDRRSGSPDVKGPP
CCCCCCCCCCCCCCC		21.1230266825
24SumoylationRSGSPDVKGPPPVKV
CCCCCCCCCCCCCEE		73.4228112733
30SumoylationVKGPPPVKVARLEQN
CCCCCCCEEEEEECC		35.6328112733
39PhosphorylationARLEQNGSPMGARGR
EEEECCCCCCCCCCC		21.1829255136
161SumoylationIQLQSCSKLEDLPAE
HHHHHCCCCCCCCHH		61.2928112733
184UbiquitinationNALKELLKEMNQSTL
HHHHHHHHHHCHHHH		68.4921890473
189PhosphorylationLLKEMNQSTLAKECP
HHHHHCHHHHHHHCC		22.0025627689
198PhosphorylationLAKECPLSQSMISSI
HHHHCCCCHHHHHHH		12.8327080861
200PhosphorylationKECPLSQSMISSIVN
HHCCCCHHHHHHHHH		18.0827080861
233SumoylationYKKYKKIKVERVERE
HHHHCCCEEEEECCC		47.0914701874
233SumoylationYKKYKKIKVERVERE
HHHHCCCEEEEECCC		47.09-
243PhosphorylationRVERENLSDYCVLGQ
EECCCCCCCCCCCCC		37.8129496963
271PhosphorylationLGKTNEQSPHSQIHH
CCCCCCCCCCHHCCC		20.5729496963
280PhosphorylationHSQIHHSTPIRNQVP
CHHCCCCCCCCCCCC		20.5529496963
294PhosphorylationPALQPIMSPGLLSPQ
CCCCCCCCCCCCCCC		19.2825850435
299PhosphorylationIMSPGLLSPQLSPQL
CCCCCCCCCCCCHHH		18.6825850435
303PhosphorylationGLLSPQLSPQLVRQQ
CCCCCCCCHHHHHHH		12.8329496963
347MethylationLNHPPIPRAVKPEPT
HCCCCCCCCCCCCCC		53.3797804665
350AcetylationPPIPRAVKPEPTNSS
CCCCCCCCCCCCCCC		42.5526051181
350SumoylationPPIPRAVKPEPTNSS
CCCCCCCCCCCCCCC		42.5514701874
350SumoylationPPIPRAVKPEPTNSS
CCCCCCCCCCCCCCC		42.55-
357PhosphorylationKPEPTNSSVEVSPDI
CCCCCCCCCEECHHH		25.1128555341
361PhosphorylationTNSSVEVSPDIYQQV
CCCCCEECHHHHHHH		11.8929496963
410PhosphorylationDPRTASQSLLVNLRA
CCCCCCHHHHHHHHH		22.6028122231
433PhosphorylationEVERDRIYQDERERS
HHHHHHHHHHHHHHH		15.7130576142
446PhosphorylationRSMNPNVSMVSSASS
HHCCCCCCCCCCCCC		21.8022817900
449PhosphorylationNPNVSMVSSASSSPS
CCCCCCCCCCCCCCC		16.1417287340
450PhosphorylationPNVSMVSSASSSPSS
CCCCCCCCCCCCCCC		22.2817287340
452PhosphorylationVSMVSSASSSPSSSR
CCCCCCCCCCCCCCC		33.0417287340
453PhosphorylationSMVSSASSSPSSSRT
CCCCCCCCCCCCCCC		46.0829978859
454PhosphorylationMVSSASSSPSSSRTP
CCCCCCCCCCCCCCC		26.7228348404
456PhosphorylationSSASSSPSSSRTPQA
CCCCCCCCCCCCCCC		42.7829978859
457PhosphorylationSASSSPSSSRTPQAK
CCCCCCCCCCCCCCC		27.5029978859
458PhosphorylationASSSPSSSRTPQAKT
CCCCCCCCCCCCCCC		44.5029978859
465PhosphorylationSRTPQAKTSTPTTDL
CCCCCCCCCCCCCCC		40.6329255136
466PhosphorylationRTPQAKTSTPTTDLP
CCCCCCCCCCCCCCC		31.5129255136
467PhosphorylationTPQAKTSTPTTDLPI
CCCCCCCCCCCCCCE		29.8629255136
469PhosphorylationQAKTSTPTTDLPIKV
CCCCCCCCCCCCEEE		32.7929255136
470PhosphorylationAKTSTPTTDLPIKVD
CCCCCCCCCCCEEEC		36.4225850435
475SumoylationPTTDLPIKVDGANIN
CCCCCCEEECCCCEE		32.1328112733
501PhosphorylationEMKRAKVSQALFAKV
HHHHHHHHHHHHHHH		14.72-
556PhosphorylationQHERDVIYEEESRHH
HHHCCHHCCCHHCCC		19.6925690035
587PhosphorylationQVLHRQQSQPAKESS
HHHHHHCCCCCCCCC		29.7828450419
593PhosphorylationQSQPAKESSPPREEA
CCCCCCCCCCCCCCC		47.6530266825
594PhosphorylationSQPAKESSPPREEAP
CCCCCCCCCCCCCCC		39.7630266825
607PhosphorylationAPPPPPPTEDSCAKK
CCCCCCCCCCCCCCC		59.1923312004
610PhosphorylationPPPPTEDSCAKKPRS
CCCCCCCCCCCCCCC		15.1125159151
682PhosphorylationKLKEHLGSAVDVAEY
HHHHHHHCCEEHHHH		31.3223312004
724SumoylationEENADKSKAAPAEID
HHCCCHHHCCCCHHC		55.0728112733
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 SATB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SATB2_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 SATB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTA2_HUMANMTA2physical
18333962
HDAC1_HUMANHDAC1physical
18333962
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=Chromosomal aberrations involving SATB2 are found in isolated cleft palate. Translocation t(2
7)
translocation t(2
11).
119540
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SATB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-446; SER-449;SER-450 AND SER-452, AND MASS SPECTROMETRY.

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