RCOR1_HUMAN - dbPTM
RCOR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCOR1_HUMAN
UniProt AC Q9UKL0
Protein Name REST corepressor 1
Gene Name RCOR1
Organism Homo sapiens (Human).
Sequence Length 485
Subcellular Localization Nucleus . Upon infection by HSV-1, it is partially translocated into the cytoplasm in an HSV-1-dependent manner.
Protein Description Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation..
Protein Sequence MPAMVEKGPEVSGKRRGRNNAAASASAAAASAAASAACASPAATAASGAAASSASAAAASAAAAPNNGQNKSLAAAAPNGNSSSNSWEEGSSGSSSDEEHGGGGMRVGPQYQAVVPDFDPAKLARRSQERDNLGMLVWSPNQNLSEAKLDEYIAIAKEKHGYNMEQALGMLFWHKHNIEKSLADLPNFTPFPDEWTVEDKVLFEQAFSFHGKTFHRIQQMLPDKSIASLVKFYYSWKKTRTKTSVMDRHARKQKREREESEDELEEANGNNPIDIEVDQNKESKKEVPPTETVPQVKKEKHSTQAKNRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAEHGKEETNGPSNQKPVKSPDNSIKMPEEEDEAPVLDVRYASAS
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
9PhosphorylationPAMVEKGPEVSGKRR
CCCCCCCCCCCCCCC		36.61-
12PhosphorylationVEKGPEVSGKRRGRN
CCCCCCCCCCCCCCC		50.22-
142-HydroxyisobutyrylationKGPEVSGKRRGRNNA
CCCCCCCCCCCCCCH		40.47-
24PhosphorylationGRNNAAASASAAAAS
CCCCHHHHHHHHHHH		10.8022210691
26PhosphorylationNNAAASASAAAASAA
CCHHHHHHHHHHHHH		11.1522210691
35PhosphorylationAAASAAASAACASPA
HHHHHHHHHHHHCHH		3.7328348404
40PhosphorylationAASAACASPAATAAS
HHHHHHHCHHHHHHH		10.9322210691
44PhosphorylationACASPAATAASGAAA
HHHCHHHHHHHHHHH		26.8822210691
47PhosphorylationSPAATAASGAAASSA
CHHHHHHHHHHHHHH		16.0528348404
52PhosphorylationAASGAAASSASAAAA
HHHHHHHHHHHHHHH		22.0128348404
53PhosphorylationASGAAASSASAAAAS
HHHHHHHHHHHHHHH		10.8022210691
55PhosphorylationGAAASSASAAAASAA
HHHHHHHHHHHHHHH		11.1528348404
60PhosphorylationSASAAAASAAAAPNN
HHHHHHHHHHHCCCC		24.1428348404
72PhosphorylationPNNGQNKSLAAAAPN
CCCCCCCCCCCCCCC		14.9523090842
82PhosphorylationAAAPNGNSSSNSWEE
CCCCCCCCCCCCCCC		53.7628450419
83PhosphorylationAAPNGNSSSNSWEEG
CCCCCCCCCCCCCCC		37.5028450419
84PhosphorylationAPNGNSSSNSWEEGS
CCCCCCCCCCCCCCC		16.3528450419
86PhosphorylationNGNSSSNSWEEGSSG
CCCCCCCCCCCCCCC		59.1128450419
88PhosphorylationNSSSNSWEEGSSGSS
CCCCCCCCCCCCCCC		34.5023090842
89PhosphorylationSSSNSWEEGSSGSSS
CCCCCCCCCCCCCCC		54.2623090842
91PhosphorylationSNSWEEGSSGSSSDE
CCCCCCCCCCCCCCC		28.7223663014
92PhosphorylationNSWEEGSSGSSSDEE
CCCCCCCCCCCCCCC		45.3823663014
93PhosphorylationSWEEGSSGSSSDEEH
CCCCCCCCCCCCCCC		51.2223090842
94PhosphorylationWEEGSSGSSSDEEHG
CCCCCCCCCCCCCCC		68.2223663014
95PhosphorylationEEGSSGSSSDEEHGG
CCCCCCCCCCCCCCC		54.5723663014
96PhosphorylationEGSSGSSSDEEHGGG
CCCCCCCCCCCCCCC		53.4723663014
119UbiquitinationQAVVPDFDPAKLARR
EEECCCCCHHHHHHH		48.3321890473
122UbiquitinationVPDFDPAKLARRSQE
CCCCCHHHHHHHHHH		49.58-
122SumoylationVPDFDPAKLARRSQE
CCCCCHHHHHHHHHH		49.5828112733
122UbiquitinationVPDFDPAKLARRSQE
CCCCCHHHHHHHHHH		49.5822817900
124PhosphorylationDFDPAKLARRSQERD
CCCHHHHHHHHHHHC		30.7322115753
127PhosphorylationPAKLARRSQERDNLG
HHHHHHHHHHHCCCC		30.4023401153
136PhosphorylationERDNLGMLVWSPNQN
HHCCCCEEEECCCCC		13.3925850435
139PhosphorylationNLGMLVWSPNQNLSE
CCCEEEECCCCCCCH		56.4725159151
145PhosphorylationWSPNQNLSEAKLDEY
ECCCCCCCHHHHHHH		53.0425850435
149PhosphorylationQNLSEAKLDEYIAIA
CCCCHHHHHHHHHHH		8.70-
152PhosphorylationSEAKLDEYIAIAKEK
CHHHHHHHHHHHHHH		4.00-
154UbiquitinationAKLDEYIAIAKEKHG
HHHHHHHHHHHHHHC		62.27-
156UbiquitinationLDEYIAIAKEKHGYN
HHHHHHHHHHHHCCC		41.44-
157UbiquitinationDEYIAIAKEKHGYNM
HHHHHHHHHHHCCCH		45.0933845483
180UbiquitinationWHKHNIEKSLADLPN
HHHHHHHHHHHCCCC		24.32-
186PhosphorylationEKSLADLPNFTPFPD
HHHHHCCCCCCCCCC		30.57-
189PhosphorylationLADLPNFTPFPDEWT
HHCCCCCCCCCCCCC		39.55-
2242-HydroxyisobutyrylationIQQMLPDKSIASLVK
HHHHCCCCCHHHHHH		12.14-
228PhosphorylationLPDKSIASLVKFYYS
CCCCCHHHHHHHHHH		32.7024719451
232PhosphorylationSIASLVKFYYSWKKT
CHHHHHHHHHHCCCC		22.5024719451
235PhosphorylationSLVKFYYSWKKTRTK
HHHHHHHHCCCCCCC		36.6627067055
257PhosphorylationARKQKREREESEDEL
HHHHHHHHHHHHHHH		45.6620164059
260PhosphorylationQKREREESEDELEEA
HHHHHHHHHHHHHHH		54.7729255136
283PhosphorylationEVDQNKESKKEVPPT
EECCCCCCCCCCCCC		65.0823312004
294SumoylationVPPTETVPQVKKEKH
CCCCCCCCHHHHHHC		50.39-
294SumoylationVPPTETVPQVKKEKH
CCCCCCCCHHHHHHC		50.39-
297SumoylationTETVPQVKKEKHSTQ
CCCCCHHHHHHCCHH		52.3028112733
349UbiquitinationDMELVSVKRQIQNIK
CHHHHHHHHHHHHHH		3.8324816145
356UbiquitinationKRQIQNIKQTNSALK
HHHHHHHHHHCHHHH		23.85-
357PhosphorylationRQIQNIKQTNSALKE
HHHHHHHHHCHHHHH		38.0621406692
358PhosphorylationQIQNIKQTNSALKEK
HHHHHHHHCHHHHHH		25.4021406692
360PhosphorylationQNIKQTNSALKEKLD
HHHHHHCHHHHHHHC		53.1421406692
363UbiquitinationKQTNSALKEKLDGGI
HHHCHHHHHHHCCCC		8.5229967540
365UbiquitinationTNSALKEKLDGGIEP
HCHHHHHHHCCCCCC		49.7929901268
3652-HydroxyisobutyrylationTNSALKEKLDGGIEP
HCHHHHHHHCCCCCC		49.79-
370PhosphorylationKEKLDGGIEPYRLPE
HHHHCCCCCCCCHHH		16.40-
373PhosphorylationLDGGIEPYRLPEVIQ
HCCCCCCCCHHHHHH		25.4723917254
378UbiquitinationEPYRLPEVIQKCNAR
CCCCHHHHHHHHCCC		20.52-
381UbiquitinationRLPEVIQKCNARWTT
CHHHHHHHHCCCCCC		20.1924816145
415UbiquitinationISDVIGNKSVVQVKN
HHHHHCCCCEEEEEE		7.5523000965
418AcetylationVIGNKSVVQVKNFFV
HHCCCCEEEEEEHHH		30.83-
418UbiquitinationVIGNKSVVQVKNFFV
HHCCCCEEEEEEHHH		30.8321890473
421UbiquitinationNKSVVQVKNFFVNYR
CCCEEEEEEHHHHHH		4.94-
421UbiquitinationNKSVVQVKNFFVNYR
CCCEEEEEEHHHHHH		4.9421890473
421AcetylationNKSVVQVKNFFVNYR
CCCEEEEEEHHHHHH		4.9491123
446PhosphorylationEWEAEHGKEETNGPS
HHHHHHCCCCCCCCC		46.7125850435
449PhosphorylationAEHGKEETNGPSNQK
HHHCCCCCCCCCCCC		31.9821955146
450PhosphorylationEHGKEETNGPSNQKP
HHCCCCCCCCCCCCC		53.9821406692
453PhosphorylationKEETNGPSNQKPVKS
CCCCCCCCCCCCCCC		56.9021955146
457PhosphorylationNGPSNQKPVKSPDNS
CCCCCCCCCCCCCCC		37.4122115753
460PhosphorylationSNQKPVKSPDNSIKM
CCCCCCCCCCCCCCC		49.3629255136
461PhosphorylationNQKPVKSPDNSIKMP
CCCCCCCCCCCCCCC		30.8520873877
464PhosphorylationPVKSPDNSIKMPEEE
CCCCCCCCCCCCCCC		4.8730266825
466SumoylationKSPDNSIKMPEEEDE
CCCCCCCCCCCCCCC		71.2028112733
466UbiquitinationKSPDNSIKMPEEEDE
CCCCCCCCCCCCCCC		71.20-
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 RCOR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RCOR1_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 RCOR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
12032298
KDM1A_HUMANKDM1Aphysical
12032298
HM20B_HUMANHMG20Bphysical
12032298
HDAC2_HUMANHDAC2physical
12032298
PF21A_HUMANPHF21Aphysical
15325272
KDM1A_HUMANKDM1Aphysical
11171972
ZN217_HUMANZNF217physical
11171972
HDAC1_HUMANHDAC1physical
11171972
HDAC2_HUMANHDAC2physical
11171972
REST_HUMANRESTphysical
10449787
MECP2_HUMANMECP2physical
12399542
ZMYM2_HUMANZMYM2physical
18806873
KDM1A_HUMANKDM1Aphysical
18806873
HDAC1_HUMANHDAC1physical
18806873
CTBP1_HUMANCTBP1physical
19242095
KDM5B_HUMANKDM5Bphysical
19242095
ZN217_HUMANZNF217physical
19242095
ZN217_HUMANZNF217physical
17130829
KDM1A_HUMANKDM1Aphysical
16956976
HSP74_HUMANHSPA4physical
18657505
ESCO2_HUMANESCO2physical
18501190
SMCE1_HUMANSMARCE1physical
12192000
HDAC1_HUMANHDAC1physical
12192000
HDAC2_HUMANHDAC2physical
12192000
KDM1A_HUMANKDM1Aphysical
16079794
H31_HUMANHIST1H3Aphysical
16079794
HDAC1_HUMANHDAC1physical
15897453
REST_HUMANRESTphysical
15897453
HDAC1_HUMANHDAC1physical
11102443
HDAC2_HUMANHDAC2physical
11102443
KDM1A_HUMANKDM1Aphysical
11102443
CTBP1_HUMANCTBP1physical
17967884
ESCO2_HUMANESCO2physical
20331966
TCP4_HUMANSUB1physical
20080105
H31T_HUMANHIST3H3physical
12700765
KDM1A_HUMANKDM1Aphysical
22143567
RCOR1_HUMANRCOR1physical
21300290
SNAI1_HUMANSNAI1physical
21300290
KDM1A_HUMANKDM1Aphysical
21602794
KDM1A_HUMANKDM1Aphysical
20389281
DDX46_HUMANDDX46physical
26344197
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
YETS4_HUMANYEATS4physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
VPS50_HUMANCCDC132physical
27173435
CCD93_HUMANCCDC93physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
EIPR1_HUMANTSSC1physical
27173435
RABE1_HUMANRABEP1physical
27173435
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 RCOR1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-257, ANDMASS SPECTROMETRY.
"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-257, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-457, ANDMASS SPECTROMETRY.

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