| UniProt ID | PSMD4_HUMAN | |
|---|---|---|
| UniProt AC | P55036 | |
| Protein Name | 26S proteasome non-ATPase regulatory subunit 4 | |
| Gene Name | PSMD4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 377 | |
| 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 | MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATTGTEDSDDALLKMTISQQEFGRTGLPDLSSMTEEEQIAYAMQMSLQGAEFGQAESADIDASSAMDTSEPAKEEDDYDVMQDPEFLQSVLENLPGVDPNNEAIRNAMGSLASQATKDGKKDKKEEDKK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MVLESTMVCVDN ---CCCCEEEEEECC | 20.03 | 23401153 | |
| 6 | Phosphorylation | --MVLESTMVCVDNS --CCCCEEEEEECCH | 12.30 | 23401153 | |
| 9 | Glutathionylation | VLESTMVCVDNSEYM CCCEEEEEECCHHHH | 1.90 | 22555962 | |
| 13 | Phosphorylation | TMVCVDNSEYMRNGD EEEEECCHHHHHCCC | 26.16 | 23401153 | |
| 15 | Phosphorylation | VCVDNSEYMRNGDFL EEECCHHHHHCCCCC | 10.95 | 23401153 | |
| 37 | S-nitrosylation | QDAVNIVCHSKTRSN HHHHHEEEECCCCCC | 2.38 | 19483679 | |
| 37 | Glutathionylation | QDAVNIVCHSKTRSN HHHHHEEEECCCCCC | 2.38 | 22555962 | |
| 37 | S-nitrosocysteine | QDAVNIVCHSKTRSN HHHHHEEEECCCCCC | 2.38 | - | |
| 40 | Ubiquitination | VNIVCHSKTRSNPEN HHEEEECCCCCCCCC | 25.05 | 21890473 | |
| 40 (in isoform 2) | Ubiquitination | - | 25.05 | 21890473 | |
| 40 (in isoform 1) | Ubiquitination | - | 25.05 | 21890473 | |
| 40 | Acetylation | VNIVCHSKTRSNPEN HHEEEECCCCCCCCC | 25.05 | 25953088 | |
| 41 | Phosphorylation | NIVCHSKTRSNPENN HEEEECCCCCCCCCC | 42.20 | 30377224 | |
| 43 | Phosphorylation | VCHSKTRSNPENNVG EEECCCCCCCCCCEE | 63.07 | 30377224 | |
| 53 | Phosphorylation | ENNVGLITLANDCEV CCCEEEEEECCCCEE | 25.51 | 28348404 | |
| 58 | Glutathionylation | LITLANDCEVLTTLT EEEECCCCEEEEEEC | 3.80 | 22555962 | |
| 62 | Phosphorylation | ANDCEVLTTLTPDTG CCCCEEEEEECCCCC | 25.57 | 28348404 | |
| 63 | Phosphorylation | NDCEVLTTLTPDTGR CCCEEEEEECCCCCH | 25.19 | 28348404 | |
| 65 | Phosphorylation | CEVLTTLTPDTGRIL CEEEEEECCCCCHHH | 19.61 | 28348404 | |
| 74 | Acetylation | DTGRILSKLHTVQPK CCCHHHHHCCCCCCC | 40.62 | 25953088 | |
| 74 (in isoform 2) | Ubiquitination | - | 40.62 | 21890473 | |
| 74 | Ubiquitination | DTGRILSKLHTVQPK CCCHHHHHCCCCCCC | 40.62 | 21890473 | |
| 74 (in isoform 1) | Ubiquitination | - | 40.62 | 21890473 | |
| 81 | Ubiquitination | KLHTVQPKGKITFCT HCCCCCCCCCEEEEC | 56.60 | 21890473 | |
| 81 (in isoform 2) | Ubiquitination | - | 56.60 | 21890473 | |
| 81 (in isoform 1) | Ubiquitination | - | 56.60 | 21890473 | |
| 83 (in isoform 1) | Ubiquitination | - | 44.70 | 21890473 | |
| 83 (in isoform 2) | Ubiquitination | - | 44.70 | 21890473 | |
| 83 | Ubiquitination | HTVQPKGKITFCTGI CCCCCCCCEEEECHH | 44.70 | 21890473 | |
| 87 | S-nitrosylation | PKGKITFCTGIRVAH CCCCEEEECHHHHHH | 2.26 | 19483679 | |
| 87 | S-nitrosocysteine | PKGKITFCTGIRVAH CCCCEEEECHHHHHH | 2.26 | - | |
| 88 | Phosphorylation | KGKITFCTGIRVAHL CCCEEEECHHHHHHH | 31.30 | 28555341 | |
| 98 (in isoform 1) | Ubiquitination | - | 31.00 | 21890473 | |
| 98 (in isoform 2) | Ubiquitination | - | 31.00 | 21890473 | |
| 98 | Acetylation | RVAHLALKHRQGKNH HHHHHHHHHHCCCCC | 31.00 | 26210075 | |
| 98 | Ubiquitination | RVAHLALKHRQGKNH HHHHHHHHHHCCCCC | 31.00 | 9865 | |
| 115 (in isoform 2) | Phosphorylation | - | 22.07 | - | |
| 115 | Phosphorylation | RIIAFVGSPVEDNEK EEEEEECCCCCCCHH | 22.07 | 21815630 | |
| 122 | Sumoylation | SPVEDNEKDLVKLAK CCCCCCHHHHHHHHH | 63.72 | 28112733 | |
| 122 | Acetylation | SPVEDNEKDLVKLAK CCCCCCHHHHHHHHH | 63.72 | 23954790 | |
| 122 | Ubiquitination | SPVEDNEKDLVKLAK CCCCCCHHHHHHHHH | 63.72 | 21890473 | |
| 122 (in isoform 1) | Ubiquitination | - | 63.72 | 21890473 | |
| 122 (in isoform 2) | Ubiquitination | - | 63.72 | 21890473 | |
| 126 | Acetylation | DNEKDLVKLAKRLKK CCHHHHHHHHHHHHH | 50.45 | 23749302 | |
| 126 | Ubiquitination | DNEKDLVKLAKRLKK CCHHHHHHHHHHHHH | 50.45 | 21890473 | |
| 126 | Malonylation | DNEKDLVKLAKRLKK CCHHHHHHHHHHHHH | 50.45 | 26320211 | |
| 126 (in isoform 1) | Ubiquitination | - | 50.45 | 21890473 | |
| 126 (in isoform 2) | Ubiquitination | - | 50.45 | 21890473 | |
| 129 | Ubiquitination | KDLVKLAKRLKKEKV HHHHHHHHHHHHHCC | 69.56 | - | |
| 133 | Ubiquitination | KLAKRLKKEKVNVDI HHHHHHHHHCCCEEE | 68.32 | - | |
| 135 | Ubiquitination | AKRLKKEKVNVDIIN HHHHHHHCCCEEEEE | 48.25 | 21890473 | |
| 135 (in isoform 1) | Ubiquitination | - | 48.25 | 21890473 | |
| 135 (in isoform 2) | Ubiquitination | - | 48.25 | 21890473 | |
| 152 (in isoform 2) | Ubiquitination | - | 49.45 | 21890473 | |
| 152 | Ubiquitination | EEEVNTEKLTAFVNT CCCCCHHHEEEEEHH | 49.45 | 21906983 | |
| 152 (in isoform 1) | Ubiquitination | - | 49.45 | 21890473 | |
| 223 | Phosphorylation | LALALRVSMEEQRQR HHHHHHHCHHHHHHH | 17.65 | 21815630 | |
| 224 | Sulfoxidation | ALALRVSMEEQRQRQ HHHHHHCHHHHHHHH | 6.34 | 30846556 | |
| 242 | Phosphorylation | ARRAAAASAAEAGIA HHHHHHHHHHHHCCC | 24.24 | 23403867 | |
| 250 (in isoform 2) | Phosphorylation | - | 24.68 | 15345747 | |
| 250 | Phosphorylation | AAEAGIATTGTEDSD HHHHCCCCCCCCCCH | 24.68 | 30266825 | |
| 251 | Phosphorylation | AEAGIATTGTEDSDD HHHCCCCCCCCCCHH | 32.84 | 30266825 | |
| 253 | Phosphorylation | AGIATTGTEDSDDAL HCCCCCCCCCCHHHH | 34.23 | 30266825 | |
| 256 | Phosphorylation | ATTGTEDSDDALLKM CCCCCCCCHHHHHHH | 31.03 | 30266825 | |
| 262 (in isoform 1) | Ubiquitination | - | 34.54 | 21890473 | |
| 262 | Ubiquitination | DSDDALLKMTISQQE CCHHHHHHHHHCHHH | 34.54 | 21906983 | |
| 263 | Sulfoxidation | SDDALLKMTISQQEF CHHHHHHHHHCHHHH | 3.97 | 21406390 | |
| 264 | Phosphorylation | DDALLKMTISQQEFG HHHHHHHHHCHHHHH | 18.85 | 23898821 | |
| 265 (in isoform 2) | Ubiquitination | - | 2.91 | 21890473 | |
| 266 | Phosphorylation | ALLKMTISQQEFGRT HHHHHHHCHHHHHCC | 19.35 | 29255136 | |
| 326 | Phosphorylation | PAKEEDDYDVMQDPE CCCCCCCCCHHHCHH | 23.82 | - | |
| 356 | Sulfoxidation | NEAIRNAMGSLASQA HHHHHHHHHHHHHHH | 4.23 | 21406390 | |
| 358 | Phosphorylation | AIRNAMGSLASQATK HHHHHHHHHHHHHHC | 14.00 | 25159151 | |
| 361 | Phosphorylation | NAMGSLASQATKDGK HHHHHHHHHHHCCCC | 26.16 | 28112733 | |
| 364 | Phosphorylation | GSLASQATKDGKKDK HHHHHHHHCCCCCCC | 23.25 | 20068231 | |
| 365 | Acetylation | SLASQATKDGKKDKK HHHHHHHCCCCCCCC | 68.45 | 23954790 | |
| 365 (in isoform 1) | Ubiquitination | - | 68.45 | 21890473 | |
| 365 | Ubiquitination | SLASQATKDGKKDKK HHHHHHHCCCCCCCC | 68.45 | 2190698 | |
| 368 | Acetylation | SQATKDGKKDKKEED HHHHCCCCCCCCHHH | 68.85 | 23749302 | |
| 368 (in isoform 2) | Ubiquitination | - | 68.85 | 21890473 | |
| 369 | Ubiquitination | QATKDGKKDKKEEDK HHHCCCCCCCCHHHC | 79.07 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| - | K | Ubiquitination | E3 ubiquitin ligase | SIAH2 | O43255 | PMID:19240029 |
| - | K | Ubiquitination | E3 ubiquitin ligase | UBE3A | Q05086 | PMID:19240029 |
| - | K | Ubiquitination | E3 ubiquitin ligase | NEDD4 | P46934 | PMID:19240029 |
| - | K | Ubiquitination | E3 ubiquitin ligase | MDM2 | Q00987 | PMID:19240029 |
| - | K | Ubiquitination | E3 ubiquitin ligase | BTRC | Q9Y297 | PMID:19240029 |
| - | K | Ubiquitination | E3 ubiquitin ligase | PRKN | O60260 | PMID:19240029 |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRIM63 | Q969Q1 | PMID:19240029 |
| - | K | Ubiquitination | E3 ubiquitin ligase | STUB1 | Q9UNE7 | PMID:15198682 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SMURF1 | Q9HCE7 | PMID:20804422 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSMD4_HUMAN !! | ||||||
* 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_HUMAN !! | ||||||
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASSSPECTROMETRY. | |
| "ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASSSPECTROMETRY. | |
| "Mass spectrometric characterization of the affinity-purified human26S proteasome complex."; Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; Biochemistry 46:3553-3565(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-358 ANDSER-361, CLEAVAGE OF INITIATOR METHIONINE, AND MASS SPECTROMETRY. | |
