REST_HUMAN - dbPTM
REST_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID REST_HUMAN
UniProt AC Q13127
Protein Name RE1-silencing transcription factor
Gene Name REST
Organism Homo sapiens (Human).
Sequence Length 1097
Subcellular Localization Nucleus . Colocalizes with ZFP90 in the nucleus.
Protein Description Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells. Restricts the expression of neuronal genes by associating with two distinct corepressors, mSin3 and CoREST, which in turn recruit histone deacetylase to the promoters of REST-regulated genes. Mediates repression by recruiting the BHC complex at RE1/NRSE sites which acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. Transcriptional repression by REST-CDYL via the recruitment of histone methyltransferase EHMT2 may be important in transformation suppression..
Protein Sequence MATQVMGQSSGGGGLFTSSGNIGMALPNDMYDLHDLSKAELAAPQLIMLANVALTGEVNGSCCDYLVGEERQMAELMPVGDNNFSDSEEGEGLEESADIKGEPHGLENMELRSLELSVVEPQPVFEASGAPDIYSSNKDLPPETPGAEDKGKSSKTKPFRCKPCQYEAESEEQFVHHIRVHSAKKFFVEESAEKQAKARESGSSTAEEGDFSKGPIRCDRCGYNTNRYDHYTAHLKHHTRAGDNERVYKCIICTYTTVSEYHWRKHLRNHFPRKVYTCGKCNYFSDRKNNYVQHVRTHTGERPYKCELCPYSSSQKTHLTRHMRTHSGEKPFKCDQCSYVASNQHEVTRHARQVHNGPKPLNCPHCDYKTADRSNFKKHVELHVNPRQFNCPVCDYAASKKCNLQYHFKSKHPTCPNKTMDVSKVKLKKTKKREADLPDNITNEKTEIEQTKIKGDVAGKKNEKSVKAEKRDVSKEKKPSNNVSVIQVTTRTRKSVTEVKEMDVHTGSNSEKFSKTKKSKRKLEVDSHSLHGPVNDEESSTKKKKKVESKSKNNSQEVPKGDSKVEENKKQNTCMKKSTKKKTLKNKSSKKSSKPPQKEPVEKGSAQMDPPQMGPAPTEAVQKGPVQVEPPPPMEHAQMEGAQIRPAPDEPVQMEVVQEGPAQKELLPPVEPAQMVGAQIVLAHMELPPPMETAQTEVAQMGPAPMEPAQMEVAQVESAPMQVVQKEPVQMELSPPMEVVQKEPVQIELSPPMEVVQKEPVKIELSPPIEVVQKEPVQMELSPPMGVVQKEPAQREPPPPREPPLHMEPISKKPPLRKDKKEKSNMQSERARKEQVLIEVGLVPVKDSWLLKESVSTEDLSPPSPPLPKENLREEASGDQKLLNTGEGNKEAPLQKVGAEEADESLPGLAANINESTHISSSGQNLNTPEGETLNGKHQTDSIVCEMKMDTDQNTRENLTGINSTVEEPVSPMLPPSAVEEREAVSKTALASPPATMAANESQEIDEDEGIHSHEGSDLSDNMSEGSDDSGLHGARPVPQESSRKNAKEALAVKAAKGDFVCIFCDRSFRKGKDYSKHLNRHLVNVYYLEEAAQGQE
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
85PhosphorylationPVGDNNFSDSEEGEG
CCCCCCCCCCCCCCC		42.2123090842
87PhosphorylationGDNNFSDSEEGEGLE
CCCCCCCCCCCCCCH		36.0323090842
96PhosphorylationEGEGLEESADIKGEP
CCCCCHHHCCCCCCC		23.1323090842
201PhosphorylationKQAKARESGSSTAEE
HHHHHHHHCCCCCCC		38.1228102081
203PhosphorylationAKARESGSSTAEEGD
HHHHHHCCCCCCCCC		33.5228102081
204PhosphorylationKARESGSSTAEEGDF
HHHHHCCCCCCCCCC		34.8528102081
205PhosphorylationARESGSSTAEEGDFS
HHHHCCCCCCCCCCC		39.5225627689
212PhosphorylationTAEEGDFSKGPIRCD
CCCCCCCCCCCEECC		41.25-
280UbiquitinationRKVYTCGKCNYFSDR
CCEEEECCCCCCCCC		22.81-
325 (in isoform 3)Phosphorylation-16.9022210691
327 (in isoform 3)Phosphorylation-48.2922210691
442PhosphorylationADLPDNITNEKTEIE
CCCCCCCCCCCHHHH		43.5122167270
495PhosphorylationVTTRTRKSVTEVKEM
EEECCCCCCEEEEEE		30.86-
500AcetylationRKSVTEVKEMDVHTG
CCCCEEEEEEEECCC		40.8820167786
510PhosphorylationDVHTGSNSEKFSKTK
EECCCCCCHHCCCCH		43.8124719451
512AcetylationHTGSNSEKFSKTKKS
CCCCCCHHCCCCHHC		55.5520167786
527PhosphorylationKRKLEVDSHSLHGPV
CCCEEECCCCCCCCC		21.8320873877
529PhosphorylationKLEVDSHSLHGPVND
CEEECCCCCCCCCCC		26.4725849741
545AcetylationESSTKKKKKVESKSK
CCCCHHHHHHCCCCC		71.5719820943
546AcetylationSSTKKKKKVESKSKN
CCCHHHHHHCCCCCC		61.1819820953
549PhosphorylationKKKKKVESKSKNNSQ
HHHHHHCCCCCCCCC		45.2626074081
551PhosphorylationKKKVESKSKNNSQEV
HHHHCCCCCCCCCCC		50.3126074081
552AcetylationKKVESKSKNNSQEVP
HHHCCCCCCCCCCCC		64.9819820959
555PhosphorylationESKSKNNSQEVPKGD
CCCCCCCCCCCCCCC		36.7926074081
563PhosphorylationQEVPKGDSKVEENKK
CCCCCCCCHHHHHHH		47.4726074081
569AcetylationDSKVEENKKQNTCMK
CCHHHHHHHHCCCCC		60.0419815497
570AcetylationSKVEENKKQNTCMKK
CHHHHHHHHCCCCCH		61.4319815503
573PhosphorylationEENKKQNTCMKKSTK
HHHHHHCCCCCHHHC		16.1026074081
576AcetylationKKQNTCMKKSTKKKT
HHHCCCCCHHHCHHH		45.8019815513
578PhosphorylationQNTCMKKSTKKKTLK
HCCCCCHHHCHHHHC		39.6826670566
579PhosphorylationNTCMKKSTKKKTLKN
CCCCCHHHCHHHHCC		56.6226670566
582UbiquitinationMKKSTKKKTLKNKSS
CCHHHCHHHHCCCCC		61.72-
587UbiquitinationKKKTLKNKSSKKSSK
CHHHHCCCCCCCCCC		55.29-
588PhosphorylationKKTLKNKSSKKSSKP
HHHHCCCCCCCCCCC		57.7021712546
589PhosphorylationKTLKNKSSKKSSKPP
HHHCCCCCCCCCCCC		45.7921712546
592PhosphorylationKNKSSKKSSKPPQKE
CCCCCCCCCCCCCCC		47.5321712546
734PhosphorylationEPVQMELSPPMEVVQ
CCCCCCCCCCCEEEE		17.4130576142
750PhosphorylationEPVQIELSPPMEVVQ
CCEEEEECCCCCEEE		17.7325159151
766PhosphorylationEPVKIELSPPIEVVQ
CCEEEEECCCEEEEE		18.8130266825
782PhosphorylationEPVQMELSPPMGVVQ
CCEEEECCCCCCCCC		17.4128348404
854PhosphorylationDSWLLKESVSTEDLS
CCEEECCCCCCCCCC		21.5628176443
856PhosphorylationWLLKESVSTEDLSPP
EEECCCCCCCCCCCC		35.0423403867
857PhosphorylationLLKESVSTEDLSPPS
EECCCCCCCCCCCCC		31.2223403867
861PhosphorylationSVSTEDLSPPSPPLP
CCCCCCCCCCCCCCC		47.2730266825
864PhosphorylationTEDLSPPSPPLPKEN
CCCCCCCCCCCCHHH		42.4029255136
940PhosphorylationTLNGKHQTDSIVCEM
CCCCCCCCCCEEEEE		31.2820068231
942PhosphorylationNGKHQTDSIVCEMKM
CCCCCCCCEEEEEEC		21.9520068231
960PhosphorylationQNTRENLTGINSTVE
CCHHHHCCCCCCCCC		47.8230624053
971PhosphorylationSTVEEPVSPMLPPSA
CCCCCCCCCCCCHHH		18.4630624053
986PhosphorylationVEEREAVSKTALASP
HHHHHHHHHHHHCCC		31.19-
1024PhosphorylationSDLSDNMSEGSDDSG
CCCCCCCCCCCCCCC		45.09-
1027PhosphorylationSDNMSEGSDDSGLHG
CCCCCCCCCCCCCCC		33.91-
1030PhosphorylationMSEGSDDSGLHGARP
CCCCCCCCCCCCCCC		48.52-
1048UbiquitinationESSRKNAKEALAVKA
HHHHCCHHHHHHHHH		53.57-
1054UbiquitinationAKEALAVKAAKGDFV
HHHHHHHHHHCCCEE		36.70-
1057UbiquitinationALAVKAAKGDFVCIF
HHHHHHHCCCEEEEE		64.96-
1077UbiquitinationRKGKDYSKHLNRHLV
HCCCCHHHHHHHHHE		45.97-
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
861SPhosphorylationKinaseERK2P28482
PSP
861SPhosphorylationKinaseERK1P27361
PSP
864SPhosphorylationKinaseERK2P28482
PSP
864SPhosphorylationKinaseERK1P27361
PSP
1030SPhosphorylationKinasePLK1P53350
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:14523018
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of REST_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 REST_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN3B_MOUSESin3bphysical
10570134
SIN3A_MOUSESin3aphysical
10570134
HDAC1_MOUSEHdac1physical
10570134
RCOR1_HUMANRCOR1physical
10449787
KDM5C_HUMANKDM5Cphysical
17468742
RING2_HUMANRNF2physical
17468742
NCOR1_HUMANNCOR1physical
17468742
HDAC2_HUMANHDAC2physical
17468742
SMCA4_HUMANSMARCA4physical
17023429
HDAC5_HUMANHDAC5physical
17011572
SMCA4_HUMANSMARCA4physical
12192000
SP1_HUMANSP1physical
15528196
TBP_MOUSETbpphysical
15197246
TF2B_MOUSEGtf2bphysical
15197246
TBP_HUMANTBPphysical
15197246
TF2B_HUMANGTF2Bphysical
15197246
SIN3B_HUMANSIN3Bphysical
15197246
SIN3A_HUMANSIN3Aphysical
10491605
HDAC1_HUMANHDAC1physical
10491605
TCP4_HUMANSUB1physical
20080105
GRIA2_HUMANGRIA2physical
21948504
SIN3A_HUMANSIN3Aphysical
21693630
TERF2_HUMANTERF2physical
18818083
FBW1A_HUMANBTRCphysical
18354482
EHMT2_HUMANEHMT2physical
15200951
KC1E_HUMANCSNK1Ephysical
24760862
FBW1A_HUMANBTRCphysical
24760862
FBW1A_HUMANBTRCphysical
25299066
PLK1_HUMANPLK1physical
25453754
TEX14_HUMANTEX14physical
25453754
SCYL1_HUMANSCYL1physical
25453754
FBW1A_HUMANBTRCphysical
25453754
RCOR1_HUMANRCOR1physical
25197063
PIN1_HUMANPIN1physical
25197063
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 REST_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-864, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, AND MASSSPECTROMETRY.

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