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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
37 | S-nitrosocysteine | QDAVNIVCHSKTRSN HHHHHEEEECCCCCC | 2.38 | - | |
37 | Glutathionylation | QDAVNIVCHSKTRSN HHHHHEEEECCCCCC | 2.38 | 24333276 | |
37 | S-nitrosylation | QDAVNIVCHSKTRSN HHHHHEEEECCCCCC | 2.38 | 20925432 | |
40 | Ubiquitination | VNIVCHSKTRSNPEN HHEEEECCCCCCCCC | 25.05 | 22790023 | |
40 (in isoform 2) | Ubiquitination | - | 25.05 | 22790023 | |
41 | Phosphorylation | NIVCHSKTRSNPENN HEEEECCCCCCCCCC | 42.20 | 25293948 | |
43 | Phosphorylation | VCHSKTRSNPENNVG EEECCCCCCCCCCEE | 63.07 | 25293948 | |
53 | Phosphorylation | ENNVGLITLANDCEV CCCEEEEEECCCCEE | 25.51 | 25293948 | |
74 (in isoform 2) | Ubiquitination | - | 40.62 | 22790023 | |
74 | Ubiquitination | DTGRILSKLHTVQPK CCCHHHHHCCCCCCC | 40.62 | 22790023 | |
87 | S-nitrosylation | PKGKITFCTGIRVAH CCCCEEEECHHHHHH | 2.26 | 20925432 | |
87 | Glutathionylation | PKGKITFCTGIRVAH CCCCEEEECHHHHHH | 2.26 | 24333276 | |
87 | S-nitrosocysteine | PKGKITFCTGIRVAH CCCCEEEECHHHHHH | 2.26 | - | |
122 (in isoform 2) | Ubiquitination | - | 63.72 | 22790023 | |
122 | Ubiquitination | SPVEDNEKDLVKLAK CCCCCCHHHHHHHHH | 63.72 | - | |
122 | Acetylation | SPVEDNEKDLVKLAK CCCCCCHHHHHHHHH | 63.72 | 23236377 | |
122 | Malonylation | SPVEDNEKDLVKLAK CCCCCCHHHHHHHHH | 63.72 | 26320211 | |
126 (in isoform 2) | Ubiquitination | - | 50.45 | 22790023 | |
126 | Ubiquitination | DNEKDLVKLAKRLKK CCHHHHHHHHHHHHH | 50.45 | - | |
126 | Malonylation | DNEKDLVKLAKRLKK CCHHHHHHHHHHHHH | 50.45 | 26320211 | |
135 (in isoform 2) | Ubiquitination | - | 48.25 | 22790023 | |
135 | Ubiquitination | AKRLKKEKVNVDIIN HHHHHHHCCCEEEEE | 48.25 | 22790023 | |
242 (in isoform 3) | Phosphorylation | - | 24.24 | 25777480 | |
242 (in isoform 2) | Phosphorylation | - | 24.24 | 25777480 | |
242 (in isoform 5) | Phosphorylation | - | 24.24 | 25266776 | |
242 | Phosphorylation | ARRAAAASAAEAGIA HHHHHHHHHHHHCCC | 24.24 | 25619855 | |
250 (in isoform 2) | Phosphorylation | - | 21.96 | 26824392 | |
250 (in isoform 3) | Phosphorylation | - | 21.96 | 26824392 | |
250 (in isoform 5) | Phosphorylation | - | 21.96 | 21149613 | |
250 | Phosphorylation | AAEAGIATPGTEDSD HHHHCCCCCCCCCCC | 21.96 | 25521595 | |
253 (in isoform 2) | Phosphorylation | - | 37.51 | 26824392 | |
253 (in isoform 3) | Phosphorylation | - | 37.51 | 26824392 | |
253 (in isoform 5) | Phosphorylation | - | 37.51 | 21149613 | |
253 | Phosphorylation | AGIATPGTEDSDDAL HCCCCCCCCCCCHHH | 37.51 | 22942356 | |
256 | Phosphorylation | ATPGTEDSDDALLKM CCCCCCCCCHHHHHH | 31.03 | 25521595 | |
259 (in isoform 2) | Phosphorylation | - | 21.56 | 26824392 | |
259 (in isoform 3) | Phosphorylation | - | 21.56 | 26824392 | |
262 | Ubiquitination | DSDDALLKMTINQQE CCCHHHHHHHCCHHH | 34.54 | - | |
348 (in isoform 4) | Phosphorylation | - | 35.82 | 25168779 | |
353 | Phosphorylation | PNNAAIRSVMGALAS CCHHHHHHHHHHHHH | 15.44 | 29472430 | |
360 | Phosphorylation | SVMGALASQATKDGK HHHHHHHHHHHCCCC | 22.62 | 29514104 | |
364 | Ubiquitination | ALASQATKDGKNDKK HHHHHHHCCCCCCCH | 68.45 | 22790023 | |
364 | Acetylation | ALASQATKDGKNDKK HHHHHHHCCCCCCCH | 68.45 | 23806337 | |
364 (in isoform 2) | Ubiquitination | - | 68.45 | 22790023 | |
367 (in isoform 2) | Ubiquitination | - | 72.59 | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSMD4_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NFE2_MOUSE | Nfe2 | physical | 10921894 | |
UBC_MOUSE | Ubc | physical | 10921894 | |
PRS8_MOUSE | Psmc5 | physical | 21883213 | |
PSB5_MOUSE | Psmb5 | physical | 21883213 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |