CHTOP_HUMAN - dbPTM
CHTOP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHTOP_HUMAN
UniProt AC Q9Y3Y2
Protein Name Chromatin target of PRMT1 protein
Gene Name CHTOP
Organism Homo sapiens (Human).
Sequence Length 248
Subcellular Localization Nucleus . Nucleus, nucleolus . Nucleus, nucleoplasm . Nucleus speckle . Mostly associated with facultative heterochromatin (By similarity). Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems t
Protein Description Plays an important role in the ligand-dependent activation of estrogen receptor target genes. [PubMed: 19858291 May play a role in the silencing of fetal globin genes]
Protein Sequence MAAQSAPKVVLKSTTKMSLNERFTNMLKNKQPTPVNIRASMQQQQQLASARNRRLAQQMENRPSVQAALKLKQSLKQRLGKSNIQARLGRPIGALARGAIGGRGLPIIQRGLPRGGLRGGRATRTLLRGGMSLRGQNLLRGGRAVAPRMGLRRGGVRGRGGPGRGGLGRGAMGRGGIGGRGRGMIGRGRGGFGGRGRGRGRGRGALARPVLTKEQLDNQLDAYMSKTKGHLDAELDAYMAQTDPETND
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
2Acetylation------MAAQSAPKV
------CCCCCCCEE		17.7622814378
8AcetylationMAAQSAPKVVLKSTT
CCCCCCCEEEEECCC		44.7027452117
8UbiquitinationMAAQSAPKVVLKSTT
CCCCCCCEEEEECCC		44.70-
8 (in isoform 3)Ubiquitination-44.70-
12AcetylationSAPKVVLKSTTKMSL
CCCEEEEECCCCCCH		33.8625953088
12UbiquitinationSAPKVVLKSTTKMSL
CCCEEEEECCCCCCH		33.86-
16AcetylationVVLKSTTKMSLNERF
EEEECCCCCCHHHHH		26.9525953088
16 (in isoform 3)Ubiquitination-26.95-
16UbiquitinationVVLKSTTKMSLNERF
EEEECCCCCCHHHHH		26.95-
28 (in isoform 3)Ubiquitination-51.86-
28UbiquitinationERFTNMLKNKQPTPV
HHHHHHHHCCCCCCC		51.86-
30MalonylationFTNMLKNKQPTPVNI
HHHHHHCCCCCCCCH		56.9426320211
30 (in isoform 3)Ubiquitination-56.94-
30UbiquitinationFTNMLKNKQPTPVNI
HHHHHHCCCCCCCCH		56.94-
30AcetylationFTNMLKNKQPTPVNI
HHHHHHCCCCCCCCH		56.9430587311
33 (in isoform 3)Phosphorylation-37.0624719451
33PhosphorylationMLKNKQPTPVNIRAS
HHHCCCCCCCCHHHH		37.0629255136
40 (in isoform 3)Phosphorylation-13.7927251275
40PhosphorylationTPVNIRASMQQQQQL
CCCCHHHHHHHHHHH		13.7921082442
41SulfoxidationPVNIRASMQQQQQLA
CCCHHHHHHHHHHHH		3.9921406390
49PhosphorylationQQQQQLASARNRRLA
HHHHHHHHHHHHHHH		36.0321712546
59SulfoxidationNRRLAQQMENRPSVQ
HHHHHHHHHCCHHHH		3.0721406390
64PhosphorylationQQMENRPSVQAALKL
HHHHCCHHHHHHHHH		24.5129978859
70UbiquitinationPSVQAALKLKQSLKQ
HHHHHHHHHHHHHHH		49.24-
70 (in isoform 3)Ubiquitination-49.24-
70AcetylationPSVQAALKLKQSLKQ
HHHHHHHHHHHHHHH		49.2425953088
70SumoylationPSVQAALKLKQSLKQ
HHHHHHHHHHHHHHH		49.2428112733
72 (in isoform 3)Ubiquitination-35.93-
81UbiquitinationSLKQRLGKSNIQARL
HHHHHHCCCCHHHHH		44.94-
82 (in isoform 3)Ubiquitination-37.05-
97DimethylationRPIGALARGAIGGRG
CCHHHHHHHCCCCCC		35.61-
97MethylationRPIGALARGAIGGRG
CCHHHHHHHCCCCCC		35.61-
103MethylationARGAIGGRGLPIIQR
HHHCCCCCCCCCCCC		37.96-
110MethylationRGLPIIQRGLPRGGL
CCCCCCCCCCCCCCC		37.90-
110DimethylationRGLPIIQRGLPRGGL
CCCCCCCCCCCCCCC		37.90-
114MethylationIIQRGLPRGGLRGGR
CCCCCCCCCCCCCCH		57.78-
114DimethylationIIQRGLPRGGLRGGR
CCCCCCCCCCCCCCH		57.78-
118MethylationGLPRGGLRGGRATRT
CCCCCCCCCCHHHHH		49.12-
118DimethylationGLPRGGLRGGRATRT
CCCCCCCCCCHHHHH		49.12-
121MethylationRGGLRGGRATRTLLR
CCCCCCCHHHHHHHH		35.29-
121DimethylationRGGLRGGRATRTLLR
CCCCCCCHHHHHHHH		35.29-
128MethylationRATRTLLRGGMSLRG
HHHHHHHHCCCCCCC		42.61-
128 (in isoform 4)Methylation-42.61-
128DimethylationRATRTLLRGGMSLRG
HHHHHHHHCCCCCCC		42.61-
134MethylationLRGGMSLRGQNLLRG
HHCCCCCCCCCHHCC		37.03-
134DimethylationLRGGMSLRGQNLLRG
HHCCCCCCCCCHHCC		37.03-
140DimethylationLRGQNLLRGGRAVAP
CCCCCHHCCCCCCCC		49.00-
140MethylationLRGQNLLRGGRAVAP
CCCCCHHCCCCCCCC		49.00-
143MethylationQNLLRGGRAVAPRMG
CCHHCCCCCCCCCCC		28.81-
143DimethylationQNLLRGGRAVAPRMG
CCHHCCCCCCCCCCC		28.81-
148MethylationGGRAVAPRMGLRRGG
CCCCCCCCCCCCCCC		23.28-
148DimethylationGGRAVAPRMGLRRGG
CCCCCCCCCCCCCCC		23.28-
152MethylationVAPRMGLRRGGVRGR
CCCCCCCCCCCCCCC		29.48-
153DimethylationAPRMGLRRGGVRGRG
CCCCCCCCCCCCCCC		51.78-
153MethylationAPRMGLRRGGVRGRG
CCCCCCCCCCCCCCC		51.78-
157MethylationGLRRGGVRGRGGPGR
CCCCCCCCCCCCCCC		32.16-
157DimethylationGLRRGGVRGRGGPGR
CCCCCCCCCCCCCCC		32.16-
159MethylationRRGGVRGRGGPGRGG
CCCCCCCCCCCCCCC		36.01-
159DimethylationRRGGVRGRGGPGRGG
CCCCCCCCCCCCCCC		36.01-
164MethylationRGRGGPGRGGLGRGA
CCCCCCCCCCCCCCC		38.86-
164DimethylationRGRGGPGRGGLGRGA
CCCCCCCCCCCCCCC		38.86-
169MethylationPGRGGLGRGAMGRGG
CCCCCCCCCCCCCCC		34.44-
174MethylationLGRGAMGRGGIGGRG
CCCCCCCCCCCCCCC		27.38-
180UbiquitinationGRGGIGGRGRGMIGR
CCCCCCCCCCCCCCC		26.8221890473
180MethylationGRGGIGGRGRGMIGR
CCCCCCCCCCCCCCC		26.82-
182MethylationGGIGGRGRGMIGRGR
CCCCCCCCCCCCCCC		30.10-
187MethylationRGRGMIGRGRGGFGG
CCCCCCCCCCCCCCC		22.25-
189MethylationRGMIGRGRGGFGGRG
CCCCCCCCCCCCCCC		40.47-
203MethylationGRGRGRGRGALARPV
CCCCCCCCCCCCCCC		26.33-
203DimethylationGRGRGRGRGALARPV
CCCCCCCCCCCCCCC		26.33-
208MethylationRGRGALARPVLTKEQ
CCCCCCCCCCCCHHH		23.78-
212PhosphorylationALARPVLTKEQLDNQ
CCCCCCCCHHHHHHH		32.5429978859
213UbiquitinationLARPVLTKEQLDNQL
CCCCCCCHHHHHHHH		39.02-
214 (in isoform 3)Ubiquitination-51.66-
223PhosphorylationLDNQLDAYMSKTKGH
HHHHHHHHHHHCCCC		11.1129978859
225PhosphorylationNQLDAYMSKTKGHLD
HHHHHHHHHCCCCHH		25.2129978859
226 (in isoform 1)Ubiquitination-37.4121890473
226UbiquitinationQLDAYMSKTKGHLDA
HHHHHHHHCCCCHHH		37.4121890473
226AcetylationQLDAYMSKTKGHLDA
HHHHHHHHCCCCHHH		37.4123236377
227 (in isoform 3)Ubiquitination-34.6421890473
227PhosphorylationLDAYMSKTKGHLDAE
HHHHHHHCCCCHHHH		34.6420068231
228UbiquitinationDAYMSKTKGHLDAEL
HHHHHHCCCCHHHHH		48.332190698
228 (in isoform 1)Ubiquitination-48.3321890473
229 (in isoform 3)Ubiquitination-31.6421890473
238PhosphorylationLDAELDAYMAQTDPE
HHHHHHHHHHHCCCC		7.8330266825
242PhosphorylationLDAYMAQTDPETND-
HHHHHHHCCCCCCC-		43.9430266825
243 (in isoform 3)Phosphorylation-27.2724719451
246PhosphorylationMAQTDPETND-----
HHHCCCCCCC-----		50.5030266825
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
212TPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHTOP_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 CHTOP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
KHDR2_HUMANKHDRBS2physical
25416956
ANM5_HUMANPRMT5physical
25284789
ANM1_HUMANPRMT1physical
25284789
MEP50_HUMANWDR77physical
25284789
ERH_HUMANERHphysical
25284789
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 CHTOP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33 AND SER-40, 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 THR-242, AND MASSSPECTROMETRY.

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