BRX1_HUMAN - dbPTM
BRX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRX1_HUMAN
UniProt AC Q8TDN6
Protein Name Ribosome biogenesis protein BRX1 homolog
Gene Name BRIX1
Organism Homo sapiens (Human).
Sequence Length 353
Subcellular Localization Nucleus, nucleolus.
Protein Description Required for biogenesis of the 60S ribosomal subunit..
Protein Sequence MAATKRKRRGGFAVQAKKPKRNEIDAEPPAKRHATAEEVEEEERDRIPGPVCKGKWKNKERILIFSSRGINFRTRHLMQDLRMLMPHSKADTKMDRKDKLFVINEVCEMKNCNKCIYFEAKKKQDLYMWLSNSPHGPSAKFLVQNIHTLAELKMTGNCLKGSRPLLSFDPAFDELPHYALLKELLIQIFSTPRYHPKSQPFVDHVFTFTILDNRIWFRNFQIIEEDAALVEIGPRFVLNLIKIFQGSFGGPTLYENPHYQSPNMHRRVIRSITAAKYREKQQVKDVQKLRKKEPKTLLPHDPTADVFVTPAEEKPIEIQWVKPEPKVDLKARKKRIYKRQRKMKQRMDSGKTK
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
9MethylationAATKRKRRGGFAVQA
CCCCCCCCCCCCEEE		53.25-
17AcetylationGGFAVQAKKPKRNEI
CCCCEEECCCCCCCC		53.1425953088
18AcetylationGFAVQAKKPKRNEID
CCCEEECCCCCCCCC		59.8025953088
312-HydroxyisobutyrylationIDAEPPAKRHATAEE
CCCCCCHHHCCCHHH		50.95-
31UbiquitinationIDAEPPAKRHATAEE
CCCCCCHHHCCCHHH		50.9524816145
31AcetylationIDAEPPAKRHATAEE
CCCCCCHHHCCCHHH		50.9525953088
35PhosphorylationPPAKRHATAEEVEEE
CCHHHCCCHHHHHHH		28.6023312004
53UbiquitinationRIPGPVCKGKWKNKE
CCCCCCCCCCCCCCC		64.8532015554
53AcetylationRIPGPVCKGKWKNKE
CCCCCCCCCCCCCCC		64.8526051181
82MethylationRHLMQDLRMLMPHSK
HHHHHHHHHHCCCCC		25.20-
89AcetylationRMLMPHSKADTKMDR
HHHCCCCCCCCCCCC		47.4426051181
992-HydroxyisobutyrylationTKMDRKDKLFVINEV
CCCCCCCCEEEEEHH		47.03-
99AcetylationTKMDRKDKLFVINEV
CCCCCCCCEEEEEHH		47.0326051181
109SulfoxidationVINEVCEMKNCNKCI
EEEHHHHHCCCCCCE		2.9821406390
110AcetylationINEVCEMKNCNKCIY
EEHHHHHCCCCCCEE		35.7326051181
114AcetylationCEMKNCNKCIYFEAK
HHHCCCCCCEEEEEC		24.9826051181
121AcetylationKCIYFEAKKKQDLYM
CCEEEEECCHHCEEH		53.9925953088
1232-HydroxyisobutyrylationIYFEAKKKQDLYMWL
EEEEECCHHCEEHHH		48.62-
127PhosphorylationAKKKQDLYMWLSNSP
ECCHHCEEHHHHCCC		8.4417360941
131PhosphorylationQDLYMWLSNSPHGPS
HCEEHHHHCCCCCHH		21.5421406692
133PhosphorylationLYMWLSNSPHGPSAK
EEHHHHCCCCCHHHH		18.2021406692
138PhosphorylationSNSPHGPSAKFLVQN
HCCCCCHHHHHHHHC		49.0021406692
153AcetylationIHTLAELKMTGNCLK
HHHHHHHEHHCCCCC		26.3926051181
153UbiquitinationIHTLAELKMTGNCLK
HHHHHHHEHHCCCCC		26.3929967540
160AcetylationKMTGNCLKGSRPLLS
EHHCCCCCCCCCCCC		57.9726051181
160SumoylationKMTGNCLKGSRPLLS
EHHCCCCCCCCCCCC		57.9728112733
162PhosphorylationTGNCLKGSRPLLSFD
HCCCCCCCCCCCCCC		29.1921406692
167PhosphorylationKGSRPLLSFDPAFDE
CCCCCCCCCCCCCCC		34.9721406692
178PhosphorylationAFDELPHYALLKELL
CCCCCCHHHHHHHHH		9.3021406692
197AcetylationSTPRYHPKSQPFVDH
CCCCCCCCCCCCCCE		48.7026051181
247PhosphorylationLIKIFQGSFGGPTLY
HHHHHCCCCCCCCCC		15.2224732914
252PhosphorylationQGSFGGPTLYENPHY
CCCCCCCCCCCCCCC		45.2923927012
254PhosphorylationSFGGPTLYENPHYQS
CCCCCCCCCCCCCCC		19.0123927012
259PhosphorylationTLYENPHYQSPNMHR
CCCCCCCCCCCHHHH		16.3723927012
261PhosphorylationYENPHYQSPNMHRRV
CCCCCCCCCHHHHHH		15.8623401153
271PhosphorylationMHRRVIRSITAAKYR
HHHHHHHHHHHHHHH		17.1128555341
276AcetylationIRSITAAKYREKQQV
HHHHHHHHHHHHHHH		42.2319608861
2762-HydroxyisobutyrylationIRSITAAKYREKQQV
HHHHHHHHHHHHHHH		42.23-
276UbiquitinationIRSITAAKYREKQQV
HHHHHHHHHHHHHHH		42.2319608861
284UbiquitinationYREKQQVKDVQKLRK
HHHHHHHHHHHHHHH		48.0924816145
303PhosphorylationTLLPHDPTADVFVTP
CCCCCCCCCCEEEEC		41.3623898821
309PhosphorylationPTADVFVTPAEEKPI
CCCCEEEECCCCCCE		12.8127422710
314SumoylationFVTPAEEKPIEIQWV
EEECCCCCCEEEEEC		42.6828112733
314UbiquitinationFVTPAEEKPIEIQWV
EEECCCCCCEEEEEC		42.6829967540
322NeddylationPIEIQWVKPEPKVDL
CEEEEECCCCCCCCH		40.4832015554
322UbiquitinationPIEIQWVKPEPKVDL
CEEEEECCCCCCCCH		40.4832015554
322SumoylationPIEIQWVKPEPKVDL
CEEEEECCCCCCCCH		40.4828112733
322SumoylationPIEIQWVKPEPKVDL
CEEEEECCCCCCCCH		40.48-
322AcetylationPIEIQWVKPEPKVDL
CEEEEECCCCCCCCH		40.4825953088
326UbiquitinationQWVKPEPKVDLKARK
EECCCCCCCCHHHHH		46.87-
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 BRX1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRX1_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 BRX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAE2_HUMANUBA2physical
16169070
U119A_HUMANUNC119physical
16169070
CD48_HUMANCD48physical
16169070
SETB1_HUMANSETDB1physical
16169070
RL5_HUMANRPL5physical
22939629
EBP2_HUMANEBNA1BP2physical
22939629
UTP15_HUMANUTP15physical
22939629
DDX56_HUMANDDX56physical
26344197
PUM3_HUMANKIAA0020physical
26344197
MK67I_HUMANNIFKphysical
26344197
NOC3L_HUMANNOC3Lphysical
26344197
NSA2_HUMANNSA2physical
26344197
PABP1_HUMANPABPC1physical
26344197
PABP3_HUMANPABPC3physical
26344197
PABP4_HUMANPABPC4physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL26_HUMANRPL26physical
26344197
RL27_HUMANRPL27physical
26344197
RL4_HUMANRPL4physical
26344197
RL5_HUMANRPL5physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS7_HUMANRPS7physical
26344197
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 BRX1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-276, AND MASS SPECTROMETRY.

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