PSB4_HUMAN - dbPTM
PSB4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSB4_HUMAN
UniProt AC P28070
Protein Name Proteasome subunit beta type-4
Gene Name PSMB4
Organism Homo sapiens (Human).
Sequence Length 264
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1..
Protein Sequence MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE
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
1Acetylation-------MEAFLGSR
-------CCCCCCCC
8.2722223895
9PhosphorylationEAFLGSRSGLWAGGP
CCCCCCCCCCCCCCC
39.6824114839
22PhosphorylationGPAPGQFYRIPSTPD
CCCCCCEEECCCCCC
10.3520068231
26PhosphorylationGQFYRIPSTPDSFMD
CCEEECCCCCCCCCC
50.6425106551
27PhosphorylationQFYRIPSTPDSFMDP
CEEECCCCCCCCCCH
26.2625106551
30PhosphorylationRIPSTPDSFMDPASA
ECCCCCCCCCCHHHH
24.5528450419
44PhosphorylationALYRGPITRTQNPMV
HHHCCCCCCCCCCCC
30.6922210691
46PhosphorylationYRGPITRTQNPMVTG
HCCCCCCCCCCCCCC
24.8520068231
50SulfoxidationITRTQNPMVTGTSVL
CCCCCCCCCCCEEEE
5.7421406390
52PhosphorylationRTQNPMVTGTSVLGV
CCCCCCCCCEEEEEE
28.6121406692
54PhosphorylationQNPMVTGTSVLGVKF
CCCCCCCEEEEEEEE
13.2920068231
55PhosphorylationNPMVTGTSVLGVKFE
CCCCCCEEEEEEEEC
19.3820068231
74PhosphorylationIAADMLGSYGSLARF
EEEEHHCCCHHHHHH
23.5128348404
75PhosphorylationAADMLGSYGSLARFR
EEEHHCCCHHHHHHH
14.6720090780
77PhosphorylationDMLGSYGSLARFRNI
EHHCCCHHHHHHHCC
15.6028348404
85PhosphorylationLARFRNISRIMRVNN
HHHHHCCHHHEEECC
21.2124719451
93PhosphorylationRIMRVNNSTMLGASG
HHEEECCCCCCCCCC
15.2521712546
94PhosphorylationIMRVNNSTMLGASGD
HEEECCCCCCCCCCC
20.6624719451
99PhosphorylationNSTMLGASGDYADFQ
CCCCCCCCCCHHHHH
30.3328102081
102PhosphorylationMLGASGDYADFQYLK
CCCCCCCHHHHHHHH
16.177918633
107PhosphorylationGDYADFQYLKQVLGQ
CCHHHHHHHHHHHCC
18.8320090780
109SumoylationYADFQYLKQVLGQMV
HHHHHHHHHHHCCHH
33.17-
109UbiquitinationYADFQYLKQVLGQMV
HHHHHHHHHHHCCHH
33.17-
115SulfoxidationLKQVLGQMVIDEELL
HHHHHCCHHCCHHHC
2.4330846556
127PhosphorylationELLGDGHSYSPRAIH
HHCCCCCCCCHHHHH
32.6024719451
128PhosphorylationLLGDGHSYSPRAIHS
HCCCCCCCCHHHHHH
19.6127080861
129PhosphorylationLGDGHSYSPRAIHSW
CCCCCCCCHHHHHHH
15.7827282143
147UbiquitinationAMYSRRSKMNPLWNT
HHHHCHHHCCCCCCE
40.67-
186PhosphorylationAPSLATGYGAYLAQP
CCCHHCCHHHHHHHH
8.33-
189PhosphorylationLATGYGAYLAQPLLR
HHCCHHHHHHHHHHH
9.75-
201AcetylationLLREVLEKQPVLSQT
HHHHHHHHCCCCCHH
56.6023236377
201UbiquitinationLLREVLEKQPVLSQT
HHHHHHHHCCCCCHH
56.6021906983
206PhosphorylationLEKQPVLSQTEARDL
HHHCCCCCHHHHHHH
34.9823663014
208PhosphorylationKQPVLSQTEARDLVE
HCCCCCHHHHHHHHH
28.3923663014
222PhosphorylationERCMRVLYYRDARSY
HHHHHHHHHHCCCCC
8.1328152594
223PhosphorylationRCMRVLYYRDARSYN
HHHHHHHHHCCCCCC
9.6128152594
228PhosphorylationLYYRDARSYNRFQIA
HHHHCCCCCCCEEEE
28.60-
236PhosphorylationYNRFQIATVTEKGVE
CCCEEEEEEECCCEE
29.59-
238PhosphorylationRFQIATVTEKGVEIE
CEEEEEEECCCEEEE
27.85-
240UbiquitinationQIATVTEKGVEIEGP
EEEEEECCCEEEECC
59.9121906983
249PhosphorylationVEIEGPLSTETNWDI
EEEECCCCCCCCHHH
27.6022817900
250PhosphorylationEIEGPLSTETNWDIA
EEECCCCCCCCHHHH
55.2928348404
252PhosphorylationEGPLSTETNWDIAHM
ECCCCCCCCHHHHHH
41.5228348404
259SulfoxidationTNWDIAHMISGFE--
CCHHHHHHHHCCC--
1.6030846556
261PhosphorylationWDIAHMISGFE----
HHHHHHHHCCC----
29.8327251275

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 PSB4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSB4_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 PSB4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OAZ1_HUMANOAZ1physical
11571290
PRP19_HUMANPRPF19physical
15660529
NUB1_HUMANNUB1physical
16707496
UBD_HUMANUBDphysical
16707496
PRS8_HUMANPSMC5physical
16707496
PSB3_HUMANPSMB3physical
17948026
PSB5_HUMANPSMB5physical
17948026
PSB7_HUMANPSMB7physical
17948026
PSB8_HUMANPSMB8physical
17948026
POMP_HUMANPOMPphysical
17948026
PSB10_HUMANPSMB10physical
17948026
CRBN_HUMANCRBNphysical
23026050
A4_HUMANAPPphysical
21832049
PSB5_HUMANPSMB5physical
22939629
PSB6_HUMANPSMB6physical
22939629
PSB7_HUMANPSMB7physical
22939629
PSB8_HUMANPSMB8physical
22939629
PSMD7_HUMANPSMD7physical
22939629
PSMD1_HUMANPSMD1physical
22939629
PSMD2_HUMANPSMD2physical
22939629
PSMD3_HUMANPSMD3physical
22939629
PSMD8_HUMANPSMD8physical
22939629
PSMD4_HUMANPSMD4physical
22939629
PSMD6_HUMANPSMD6physical
22939629
PSDE_HUMANPSMD14physical
22939629
PSD13_HUMANPSMD13physical
22939629
PSD11_HUMANPSMD11physical
22939629
PSME3_HUMANPSME3physical
22939629
PSD12_HUMANPSMD12physical
22939629
PSMD5_HUMANPSMD5physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
SYAP1_HUMANSYAP1physical
22939629
YBOX1_HUMANYBX1physical
22939629
ROA2_HUMANHNRNPA2B1physical
22863883
PSA2_HUMANPSMA2physical
22863883
PSA3_HUMANPSMA3physical
22863883
PSA4_HUMANPSMA4physical
22863883
PSA5_HUMANPSMA5physical
22863883
PSB1_HUMANPSMB1physical
22863883
PSB2_HUMANPSMB2physical
22863883
PSB3_HUMANPSMB3physical
22863883
PSB5_HUMANPSMB5physical
22863883
PSB6_HUMANPSMB6physical
22863883
PSB7_HUMANPSMB7physical
22863883
PSMD9_HUMANPSMD9physical
24720748
PSA5_HUMANPSMA5physical
24720748
ROA1_HUMANHNRNPA1physical
24720748
PRS8_HUMANPSMC5physical
24720748
FSD2_HUMANFSD2physical
25416956
PSB2_HUMANPSMB2physical
26186194
PSD13_HUMANPSMD13physical
26186194
PSA2_HUMANPSMA2physical
26186194
PSA3_HUMANPSMA3physical
26186194
PSB1_HUMANPSMB1physical
26186194
PSA6_HUMANPSMA6physical
26186194
PSME4_HUMANPSME4physical
26186194
PSA7L_HUMANPSMA8physical
26186194
PSA7_HUMANPSMA7physical
26186194
PSD11_HUMANPSMD11physical
26186194
PSME1_HUMANPSME1physical
26186194
PSB7_HUMANPSMB7physical
26186194
PSD12_HUMANPSMD12physical
26186194
FBX7_HUMANFBXO7physical
26186194
POMP_HUMANPOMPphysical
26186194
PSA5_HUMANPSMA5physical
26186194
PSA4_HUMANPSMA4physical
26186194
PSMG2_HUMANPSMG2physical
26186194
PSB6_HUMANPSMB6physical
26186194
PSB5_HUMANPSMB5physical
26186194
PSB3_HUMANPSMB3physical
26186194
PSME2_HUMANPSME2physical
26186194
PSMF1_HUMANPSMF1physical
26186194
PSB9_HUMANPSMB9physical
26186194
CPSF2_HUMANCPSF2physical
26344197
NELFE_HUMANNELFEphysical
26344197
PEX19_HUMANPEX19physical
26344197
PEPL_HUMANPPLphysical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA4_HUMANPSMA4physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB3_HUMANPSMB3physical
26344197
PSB5_HUMANPSMB5physical
26344197
PSB6_HUMANPSMB6physical
26344197
PSB8_HUMANPSMB8physical
26344197
PSB9_HUMANPSMB9physical
26344197
PRS8_HUMANPSMC5physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD6_HUMANPSMD6physical
26344197
U2AF2_HUMANU2AF2physical
26344197
SAE2_HUMANUBA2physical
26344197
PSA7L_HUMANPSMA8physical
28514442
PSB7_HUMANPSMB7physical
28514442
PSME4_HUMANPSME4physical
28514442
PSB9_HUMANPSMB9physical
28514442
PSME2_HUMANPSME2physical
28514442
POMP_HUMANPOMPphysical
28514442
FBX7_HUMANFBXO7physical
28514442
PSME1_HUMANPSME1physical
28514442
PSMF1_HUMANPSMF1physical
28514442
PSA3_HUMANPSMA3physical
28514442
PSA7_HUMANPSMA7physical
28514442
PSMG2_HUMANPSMG2physical
28514442
PSA2_HUMANPSMA2physical
28514442
PSB5_HUMANPSMB5physical
28514442
PSA6_HUMANPSMA6physical
28514442
PSA4_HUMANPSMA4physical
28514442
PSA5_HUMANPSMA5physical
28514442
PSB6_HUMANPSMB6physical
28514442
PSMG1_HUMANPSMG1physical
28514442
PSD11_HUMANPSMD11physical
28514442
PSMD2_HUMANPSMD2physical
28539385

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 PSB4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, AND MASSSPECTROMETRY.

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