PSME2_HUMAN - dbPTM
PSME2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSME2_HUMAN
UniProt AC Q9UL46
Protein Name Proteasome activator complex subunit 2
Gene Name PSME2
Organism Homo sapiens (Human).
Sequence Length 239
Subcellular Localization
Protein Description Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome..
Protein Sequence MAKPCGVRLSGEARKQVEVFRQNLFQEAEEFLYRFLPQKIIYLNQLLQEDSLNVADLTSLRAPLDIPIPDPPPKDDEMETDKQEKKEVHKCGFLPGNEKVLSLLALVKPEVWTLKEKCILVITWIQHLIPKIEDGNDFGVAIQEKVLERVNAVKTKVEAFQTTISKYFSERGDAVAKASKETHVMDYRALVHERDEAAYGELRAMVLDLRAFYAELYHIISSNLEKIVNPKGEEKPSMY
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------MAKPCGVRL
------CCCCCCCCC		25.2122814378
3"N6,N6-dimethyllysine"-----MAKPCGVRLS
-----CCCCCCCCCC		39.27-
3Acetylation-----MAKPCGVRLS
-----CCCCCCCCCC		39.2727452117
3Methylation-----MAKPCGVRLS
-----CCCCCCCCCC		39.27-
3Ubiquitination-----MAKPCGVRLS
-----CCCCCCCCCC		39.27-
8MethylationMAKPCGVRLSGEARK
CCCCCCCCCCHHHHH		14.39115389285
10PhosphorylationKPCGVRLSGEARKQV
CCCCCCCCHHHHHHH		24.8323401153
15UbiquitinationRLSGEARKQVEVFRQ
CCCHHHHHHHHHHHH		66.79-
15MalonylationRLSGEARKQVEVFRQ
CCCHHHHHHHHHHHH		66.7926320211
15AcetylationRLSGEARKQVEVFRQ
CCCHHHHHHHHHHHH		66.7926051181
39UbiquitinationLYRFLPQKIIYLNQL
HHHHHHHHHHHHHHH		29.18-
78SulfoxidationPPPKDDEMETDKQEK
CCCCCCCCCCCHHHH		9.6330846556
102PhosphorylationPGNEKVLSLLALVKP
CCCHHHHHHHHHHCH		25.0728450419
108UbiquitinationLSLLALVKPEVWTLK
HHHHHHHCHHHCCCH		35.99-
115UbiquitinationKPEVWTLKEKCILVI
CHHHCCCHHHHHHHH		47.99-
115AcetylationKPEVWTLKEKCILVI
CHHHCCCHHHHHHHH		47.9926051181
145UbiquitinationFGVAIQEKVLERVNA
CHHHHHHHHHHHHHH		35.4321890473
155UbiquitinationERVNAVKTKVEAFQT
HHHHHHHHHHHHHHH		33.4521890473
162PhosphorylationTKVEAFQTTISKYFS
HHHHHHHHHHHHHHH		21.4620068231
163PhosphorylationKVEAFQTTISKYFSE
HHHHHHHHHHHHHHH		16.6920068231
165PhosphorylationEAFQTTISKYFSERG
HHHHHHHHHHHHHHC		21.1520068231
166UbiquitinationAFQTTISKYFSERGD
HHHHHHHHHHHHHCH		46.60-
167PhosphorylationFQTTISKYFSERGDA
HHHHHHHHHHHHCHH		12.9228152594
179PhosphorylationGDAVAKASKETHVMD
CHHHHHHCCCCCCCC		30.2528258704
180AcetylationDAVAKASKETHVMDY
HHHHHHCCCCCCCCH		72.0611921605
185SulfoxidationASKETHVMDYRALVH
HCCCCCCCCHHHHHH		2.6630846556
187NitrationKETHVMDYRALVHER
CCCCCCCHHHHHHHH		4.62-
199PhosphorylationHERDEAAYGELRAMV
HHHHHHHHHHHHHHH		20.4121253578
217PhosphorylationRAFYAELYHIISSNL
HHHHHHHHHHHHCCH		5.18-
231AcetylationLEKIVNPKGEEKPSM
HHHHCCCCCCCCCCC		73.9926051181
231SuccinylationLEKIVNPKGEEKPSM
HHHHCCCCCCCCCCC		73.9923954790
235UbiquitinationVNPKGEEKPSMY---
CCCCCCCCCCCC---		37.78-
235AcetylationVNPKGEEKPSMY---
CCCCCCCCCCCC---		37.7825953088
237PhosphorylationPKGEEKPSMY-----
CCCCCCCCCC-----		41.6126356563
239PhosphorylationGEEKPSMY-------
CCCCCCCC-------		21.5326356563
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 PSME2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSME2_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 PSME2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSME2_HUMANPSME2physical
16189514
PSME1_HUMANPSME1physical
9346951
PSB9_HUMANPSMB9physical
11745344
PSB6_HUMANPSMB6physical
11745344
PSA4_HUMANPSMA4physical
11745344
PSMD6_HUMANPSMD6physical
11745344
PSB7_HUMANPSMB7physical
11745344
PSB8_HUMANPSMB8physical
11745344
PSB10_HUMANPSMB10physical
11745344
A4_HUMANAPPphysical
21832049
PTMA_HUMANPTMAphysical
22939629
GARS_HUMANGARSphysical
22939629
TENN_HUMANTNNphysical
22939629
PSME1_HUMANPSME1physical
22863883
PSME2_HUMANPSME2physical
9325261
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 PSME2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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