CBX1_HUMAN - dbPTM
CBX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBX1_HUMAN
UniProt AC P83916
Protein Name Chromobox protein homolog 1
Gene Name CBX1
Organism Homo sapiens (Human).
Sequence Length 185
Subcellular Localization Nucleus . Unassociated with chromosomes during mitosis.
Protein Description Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane..
Protein Sequence MGKKQNKKKVEEVLEEEEEEYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEFLQSQKTAHETDKSEGGKRKADSDSEDKGEESKPKKKKEESEKPRGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEERLTWHSYPSEDDDKKDDKN
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
9SumoylationGKKQNKKKVEEVLEE
CCCCCHHHHHHHHHH		57.3928112733
9AcetylationGKKQNKKKVEEVLEE
CCCCCHHHHHHHHHH		57.3921466224
9MethylationGKKQNKKKVEEVLEE
CCCCCHHHHHHHHHH		57.39-
9UbiquitinationGKKQNKKKVEEVLEE
CCCCCHHHHHHHHHH		57.39-
21PhosphorylationLEEEEEEYVVEKVLD
HHHHHHHHHHHHHHH		17.05-
25UbiquitinationEEEYVVEKVLDRRVV
HHHHHHHHHHHHHHH		36.1721890473
33AcetylationVLDRRVVKGKVEYLL
HHHHHHHCCCCEEEE		50.5917074905
33SumoylationVLDRRVVKGKVEYLL
HHHHHHHCCCCEEEE		50.5928112733
35AcetylationDRRVVKGKVEYLLKW
HHHHHCCCCEEEEEE		26.6123749302
35MethylationDRRVVKGKVEYLLKW
HHHHHCCCCEEEEEE		26.61-
35UbiquitinationDRRVVKGKVEYLLKW
HHHHHCCCCEEEEEE		26.61-
38PhosphorylationVVKGKVEYLLKWKGF
HHCCCCEEEEEECCC		21.9628152594
41UbiquitinationGKVEYLLKWKGFSDE
CCCEEEEEECCCCCC		44.2421890473
41AcetylationGKVEYLLKWKGFSDE
CCCEEEEEECCCCCC		44.2417074917
43UbiquitinationVEYLLKWKGFSDEDN
CEEEEEECCCCCCCC		48.79-
51PhosphorylationGFSDEDNTWEPEENL
CCCCCCCCCCCHHCC		43.4522817900
70PhosphorylationLIAEFLQSQKTAHET
HHHHHHHHHHHHHCC		35.47-
72UbiquitinationAEFLQSQKTAHETDK
HHHHHHHHHHHCCCC		53.58-
73PhosphorylationEFLQSQKTAHETDKS
HHHHHHHHHHCCCCC		26.1326074081
77PhosphorylationSQKTAHETDKSEGGK
HHHHHHCCCCCCCCC		38.5726074081
80PhosphorylationTAHETDKSEGGKRKA
HHHCCCCCCCCCCCC		44.2628985074
84UbiquitinationTDKSEGGKRKADSDS
CCCCCCCCCCCCCCC		62.68-
84AcetylationTDKSEGGKRKADSDS
CCCCCCCCCCCCCCC		62.68129779
89PhosphorylationGGKRKADSDSEDKGE
CCCCCCCCCCCCCCC		48.1429255136
91PhosphorylationKRKADSDSEDKGEES
CCCCCCCCCCCCCCC		52.2029255136
98PhosphorylationSEDKGEESKPKKKKE
CCCCCCCCCCCHHHH		50.3723927012
99SumoylationEDKGEESKPKKKKEE
CCCCCCCCCCHHHHH		65.2228112733
104UbiquitinationESKPKKKKEESEKPR
CCCCCHHHHHCCCCC		75.49-
107PhosphorylationPKKKKEESEKPRGFA
CCHHHHHCCCCCCCC		52.6029396449
109UbiquitinationKKKEESEKPRGFARG
HHHHHCCCCCCCCCC		49.66-
111MethylationKEESEKPRGFARGLE
HHHCCCCCCCCCCCC		65.02-
115MethylationEKPRGFARGLEPERI
CCCCCCCCCCCHHHE		48.22-
126PhosphorylationPERIIGATDSSGELM
HHHEEEEECCCCCEE		31.0725850435
128PhosphorylationRIIGATDSSGELMFL
HEEEEECCCCCEEEE		35.5721712546
129PhosphorylationIIGATDSSGELMFLM
EEEEECCCCCEEEEE		38.8122617229
133SulfoxidationTDSSGELMFLMKWKN
ECCCCCEEEEEEECC		1.7921406390
139UbiquitinationLMFLMKWKNSDEADL
EEEEEEECCCCHHCC		40.8421890473
139AcetylationLMFLMKWKNSDEADL
EEEEEEECCCCHHCC		40.8426051181
150UbiquitinationEADLVPAKEANVKCP
HHCCCCHHHHCCCCC		51.8221906983
150SumoylationEADLVPAKEANVKCP
HHCCCCHHHHCCCCC		51.8228112733
150AcetylationEADLVPAKEANVKCP
HHCCCCHHHHCCCCC		51.8226051181
155UbiquitinationPAKEANVKCPQVVIS
CHHHHCCCCCEEEEE		39.75-
156S-nitrosylationAKEANVKCPQVVISF
HHHHCCCCCEEEEEE		2.1924105792
162PhosphorylationKCPQVVISFYEERLT
CCCEEEEEEEHHHHC		15.34-
164PhosphorylationPQVVISFYEERLTWH
CEEEEEEEHHHHCCC		15.30-
169PhosphorylationSFYEERLTWHSYPSE
EEEHHHHCCCCCCCC		27.6130108239
172PhosphorylationEERLTWHSYPSEDDD
HHHHCCCCCCCCCCC		30.2425159151
173PhosphorylationERLTWHSYPSEDDDK
HHHCCCCCCCCCCCC		9.6328102081
175PhosphorylationLTWHSYPSEDDDKKD
HCCCCCCCCCCCCCC		45.4825159151
180UbiquitinationYPSEDDDKKDDKN--
CCCCCCCCCCCCC--		66.1621890473
181UbiquitinationPSEDDDKKDDKN---
CCCCCCCCCCCC---		77.48-
184UbiquitinationDDDKKDDKN------
CCCCCCCCC------		74.76-
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
51TPhosphorylationKinaseCSNK2A1P68400
GPS
-KUbiquitinationE3 ubiquitin ligaseRNF123Q5XPI4
PMID:23077635
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CBX1_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 CBX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EMSY_HUMANC11orf30physical
14651845
SUV91_HUMANSUV39H1physical
10202156
SUV91_MOUSESuv39h1physical
10202156
RL12_HUMANRPL12physical
16169070
UCHL1_HUMANUCHL1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
TIF1B_HUMANTRIM28physical
11336697
CBX1_HUMANCBX1physical
11336697
CBX3_HUMANCBX3physical
11336697
CBX5_HUMANCBX5physical
11336697
EMSY_HUMANC11orf30physical
16615912
CBX1_HUMANCBX1physical
16615912
TIF1B_HUMANTRIM28physical
18590578
H31_HUMANHIST1H3Aphysical
15960974
TIF1B_HUMANTRIM28physical
10330177
CBX3_HUMANCBX3physical
17314413
CBX5_HUMANCBX5physical
17314413
H31_HUMANHIST1H3Aphysical
11882902
CHD4_HUMANCHD4physical
21888893
POGZ_HUMANPOGZphysical
21888893
ADNP_HUMANADNPphysical
21888893
ADNP2_HUMANADNP2physical
21888893
TIF1B_HUMANTRIM28physical
21888893
XRCC6_HUMANXRCC6physical
21888893
CAF1A_HUMANCHAF1Aphysical
21888893
CBX3_HUMANCBX3physical
21888893
CBX5_HUMANCBX5physical
21888893
H2AB1_HUMANH2AFB1physical
21888893
PCNA_HUMANPCNAphysical
22617335
H31T_HUMANHIST3H3physical
22606318
KLF11_HUMANKLF11physical
22318730
VTNC_HUMANVTNphysical
21988832
Z280D_HUMANZNF280Dphysical
20850016
ADNP_HUMANADNPphysical
20850016
AHDC1_HUMANAHDC1physical
20850016
CHD4_HUMANCHD4physical
20850016
POGZ_HUMANPOGZphysical
20850016
CHAP1_HUMANCHAMP1physical
20850016
TR150_HUMANTHRAP3physical
20850016
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 CBX1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, 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-89 AND SER-175, AND MASSSPECTROMETRY.

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