PSMD4_MOUSE - dbPTM
PSMD4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSMD4_MOUSE
UniProt AC O35226
Protein Name 26S proteasome non-ATPase regulatory subunit 4
Gene Name Psmd4
Organism Mus musculus (Mouse).
Sequence Length 376
Subcellular Localization
Protein Description Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. Displays a preferred selectivity for longer polyubiquitin chains..
Protein Sequence MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATPGTEDSDDALLKMTINQQEFGRPGLPDLSSMTEEEQIAYAMQMSLQGTEFSQESADMDASSAMDTSDPVKEEDDYDVMQDPEFLQSVLENLPGVDPNNAAIRSVMGALASQATKDGKNDKKEEEKK
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
37S-nitrosocysteineQDAVNIVCHSKTRSN
HHHHHEEEECCCCCC
2.38-
37GlutathionylationQDAVNIVCHSKTRSN
HHHHHEEEECCCCCC
2.3824333276
37S-nitrosylationQDAVNIVCHSKTRSN
HHHHHEEEECCCCCC
2.3820925432
40UbiquitinationVNIVCHSKTRSNPEN
HHEEEECCCCCCCCC
25.0522790023
40 (in isoform 2)Ubiquitination-25.0522790023
41PhosphorylationNIVCHSKTRSNPENN
HEEEECCCCCCCCCC
42.2025293948
43PhosphorylationVCHSKTRSNPENNVG
EEECCCCCCCCCCEE
63.0725293948
53PhosphorylationENNVGLITLANDCEV
CCCEEEEEECCCCEE
25.5125293948
74 (in isoform 2)Ubiquitination-40.6222790023
74UbiquitinationDTGRILSKLHTVQPK
CCCHHHHHCCCCCCC
40.6222790023
87S-nitrosylationPKGKITFCTGIRVAH
CCCCEEEECHHHHHH
2.2620925432
87GlutathionylationPKGKITFCTGIRVAH
CCCCEEEECHHHHHH
2.2624333276
87S-nitrosocysteinePKGKITFCTGIRVAH
CCCCEEEECHHHHHH
2.26-
122 (in isoform 2)Ubiquitination-63.7222790023
122UbiquitinationSPVEDNEKDLVKLAK
CCCCCCHHHHHHHHH
63.72-
122AcetylationSPVEDNEKDLVKLAK
CCCCCCHHHHHHHHH
63.7223236377
122MalonylationSPVEDNEKDLVKLAK
CCCCCCHHHHHHHHH
63.7226320211
126 (in isoform 2)Ubiquitination-50.4522790023
126UbiquitinationDNEKDLVKLAKRLKK
CCHHHHHHHHHHHHH
50.45-
126MalonylationDNEKDLVKLAKRLKK
CCHHHHHHHHHHHHH
50.4526320211
135 (in isoform 2)Ubiquitination-48.2522790023
135UbiquitinationAKRLKKEKVNVDIIN
HHHHHHHCCCEEEEE
48.2522790023
242 (in isoform 3)Phosphorylation-24.2425777480
242 (in isoform 2)Phosphorylation-24.2425777480
242 (in isoform 5)Phosphorylation-24.2425266776
242PhosphorylationARRAAAASAAEAGIA
HHHHHHHHHHHHCCC
24.2425619855
250 (in isoform 2)Phosphorylation-21.9626824392
250 (in isoform 3)Phosphorylation-21.9626824392
250 (in isoform 5)Phosphorylation-21.9621149613
250PhosphorylationAAEAGIATPGTEDSD
HHHHCCCCCCCCCCC
21.9625521595
253 (in isoform 2)Phosphorylation-37.5126824392
253 (in isoform 3)Phosphorylation-37.5126824392
253 (in isoform 5)Phosphorylation-37.5121149613
253PhosphorylationAGIATPGTEDSDDAL
HCCCCCCCCCCCHHH
37.5122942356
256PhosphorylationATPGTEDSDDALLKM
CCCCCCCCCHHHHHH
31.0325521595
259 (in isoform 2)Phosphorylation-21.5626824392
259 (in isoform 3)Phosphorylation-21.5626824392
262UbiquitinationDSDDALLKMTINQQE
CCCHHHHHHHCCHHH
34.54-
348 (in isoform 4)Phosphorylation-35.8225168779
353PhosphorylationPNNAAIRSVMGALAS
CCHHHHHHHHHHHHH
15.4429472430
360PhosphorylationSVMGALASQATKDGK
HHHHHHHHHHHCCCC
22.6229514104
364UbiquitinationALASQATKDGKNDKK
HHHHHHHCCCCCCCH
68.4522790023
364AcetylationALASQATKDGKNDKK
HHHHHHHCCCCCCCH
68.4523806337
364 (in isoform 2)Ubiquitination-68.4522790023
367 (in isoform 2)Ubiquitination-72.59-

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 PSMD4_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSMD4_MOUSE !!

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 PSMD4_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFE2_MOUSENfe2physical
10921894
UBC_MOUSEUbcphysical
10921894
PRS8_MOUSEPsmc5physical
21883213
PSB5_MOUSEPsmb5physical
21883213

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSMD4_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250; THR-253 ANDSER-256, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250, AND MASSSPECTROMETRY.

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