| UniProt ID | PRS6B_HUMAN | |
|---|---|---|
| UniProt AC | P43686 | |
| Protein Name | 26S proteasome regulatory subunit 6B | |
| Gene Name | PSMC4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 418 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| 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. PSMC4 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.. | |
| Protein Sequence | MEEIGILVEKAQDEIPALSVSRPQTGLSFLGPEPEDLEDLYSRYKKLQQELEFLEVQEEYIKDEQKNLKKEFLHAQEEVKRIQSIPLVIGQFLEAVDQNTAIVGSTTGSNYYVRILSTIDRELLKPNASVALHKHSNALVDVLPPEADSSIMMLTSDQKPDVMYADIGGMDIQKQEVREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTAAFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQNVNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFSTITSKMNLSEEVDLEDYVARPDKISGADINSICQESGMLAVRENRYIVLAKDFEKAYKTVIKKDEQEHEFYK | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MEEIGILV -------CCCCCEEE | 10.60 | 22223895 | |
| 1 | Sulfoxidation | -------MEEIGILV -------CCCCCEEE | 10.60 | 28465586 | |
| 19 | Phosphorylation | QDEIPALSVSRPQTG HHCCCCCEECCCCCC | 21.83 | 25159151 | |
| 21 | Phosphorylation | EIPALSVSRPQTGLS CCCCCEECCCCCCCC | 34.56 | 25159151 | |
| 25 (in isoform 1) | Phosphorylation | - | 42.65 | - | |
| 25 | Phosphorylation | LSVSRPQTGLSFLGP CEECCCCCCCCCCCC | 42.65 | 25159151 | |
| 28 (in isoform 1) | Phosphorylation | - | 21.55 | - | |
| 28 | Phosphorylation | SRPQTGLSFLGPEPE CCCCCCCCCCCCCCC | 21.55 | 25159151 | |
| 41 | Phosphorylation | PEDLEDLYSRYKKLQ CCCHHHHHHHHHHHH | 11.92 | 25693802 | |
| 42 | Phosphorylation | EDLEDLYSRYKKLQQ CCHHHHHHHHHHHHH | 36.11 | 25693802 | |
| 45 | Ubiquitination | EDLYSRYKKLQQELE HHHHHHHHHHHHHHH | 45.99 | - | |
| 46 | Ubiquitination | DLYSRYKKLQQELEF HHHHHHHHHHHHHHH | 42.46 | - | |
| 62 | Ubiquitination | EVQEEYIKDEQKNLK HHHHHHHHHHHHHHH | 55.07 | 21906983 | |
| 62 (in isoform 1) | Ubiquitination | - | 55.07 | 21890473 | |
| 66 | Ubiquitination | EYIKDEQKNLKKEFL HHHHHHHHHHHHHHH | 63.30 | - | |
| 70 | Ubiquitination | DEQKNLKKEFLHAQE HHHHHHHHHHHHHHH | 57.79 | 21890473 | |
| 70 (in isoform 1) | Ubiquitination | - | 57.79 | 21890473 | |
| 80 | Ubiquitination | LHAQEEVKRIQSIPL HHHHHHHHHHHHHCC | 47.25 | 21906983 | |
| 80 (in isoform 1) | Ubiquitination | - | 47.25 | 21890473 | |
| 84 | Phosphorylation | EEVKRIQSIPLVIGQ HHHHHHHHHCCHHHH | 24.65 | 21406692 | |
| 86 (in isoform 1) | Phosphorylation | - | 26.31 | - | |
| 94 (in isoform 2) | Ubiquitination | - | 48.19 | 21890473 | |
| 100 | Phosphorylation | LEAVDQNTAIVGSTT HHHHCCCEEEEEECC | 16.48 | 21406692 | |
| 105 | Phosphorylation | QNTAIVGSTTGSNYY CCEEEEEECCCCCHH | 16.35 | 21406692 | |
| 106 | Phosphorylation | NTAIVGSTTGSNYYV CEEEEEECCCCCHHE | 29.28 | 21406692 | |
| 107 | Phosphorylation | TAIVGSTTGSNYYVR EEEEEECCCCCHHEE | 40.07 | 21406692 | |
| 109 | Phosphorylation | IVGSTTGSNYYVRIL EEEECCCCCHHEEEH | 21.40 | 21406692 | |
| 111 | Phosphorylation | GSTTGSNYYVRILST EECCCCCHHEEEHHH | 12.68 | 21406692 | |
| 112 | Phosphorylation | STTGSNYYVRILSTI ECCCCCHHEEEHHHC | 6.36 | 21406692 | |
| 117 | Phosphorylation | NYYVRILSTIDRELL CHHEEEHHHCCHHHH | 22.42 | 20068231 | |
| 118 | Phosphorylation | YYVRILSTIDRELLK HHEEEHHHCCHHHHC | 24.37 | 20068231 | |
| 125 | Acetylation | TIDRELLKPNASVAL HCCHHHHCCCCEEEE | 49.18 | 27452117 | |
| 125 | Ubiquitination | TIDRELLKPNASVAL HCCHHHHCCCCEEEE | 49.18 | 21890473 | |
| 125 (in isoform 1) | Ubiquitination | - | 49.18 | 21890473 | |
| 133 (in isoform 1) | Phosphorylation | - | 18.95 | - | |
| 134 | Methylation | NASVALHKHSNALVD CCEEEEECCCCCEEE | 49.97 | 115977375 | |
| 161 (in isoform 2) | Ubiquitination | - | 44.87 | 21890473 | |
| 164 | Phosphorylation | DQKPDVMYADIGGMD CCCCCEEEEECCCCC | 10.85 | 20068231 | |
| 174 | Ubiquitination | IGGMDIQKQEVREAV CCCCCCCHHHHHHHH | 49.08 | - | |
| 181 (in isoform 2) | Ubiquitination | - | 7.13 | 21890473 | |
| 186 (in isoform 2) | Ubiquitination | - | 23.68 | - | |
| 192 | Ubiquitination | LTHFELYKQIGIDPP CCHHHHHHHHCCCCC | 48.33 | 21890473 | |
| 192 (in isoform 1) | Ubiquitination | - | 48.33 | 21890473 | |
| 204 | Sulfoxidation | DPPRGVLMYGPPGCG CCCCCEEEECCCCCC | 3.19 | 30846556 | |
| 205 | Phosphorylation | PPRGVLMYGPPGCGK CCCCEEEECCCCCCH | 23.48 | 22817900 | |
| 207 (in isoform 1) | Acetylation | - | 12.48 | - | |
| 207 | Acetylation | RGVLMYGPPGCGKTM CCEEEECCCCCCHHH | 12.48 | 19608861 | |
| 207 | Ubiquitination | RGVLMYGPPGCGKTM CCEEEECCCCCCHHH | 12.48 | 19608861 | |
| 207 (in isoform 2) | Ubiquitination | - | 12.48 | 21890473 | |
| 212 | Ubiquitination | YGPPGCGKTMLAKAV ECCCCCCHHHHHHHH | 34.53 | 21906983 | |
| 212 (in isoform 1) | Ubiquitination | - | 34.53 | 21890473 | |
| 213 | Phosphorylation | GPPGCGKTMLAKAVA CCCCCCHHHHHHHHH | 11.60 | 24719451 | |
| 217 | Acetylation | CGKTMLAKAVAHHTT CCHHHHHHHHHHHHH | 39.16 | 25953088 | |
| 217 | Ubiquitination | CGKTMLAKAVAHHTT CCHHHHHHHHHHHHH | 39.16 | - | |
| 224 (in isoform 2) | Ubiquitination | - | 16.19 | - | |
| 238 | Acetylation | VGSEFVQKYLGEGPR HCHHHHHHHHCCCCH | 36.82 | 21466224 | |
| 238 | Ubiquitination | VGSEFVQKYLGEGPR HCHHHHHHHHCCCCH | 36.82 | 21890473 | |
| 238 (in isoform 1) | Ubiquitination | - | 36.82 | 21890473 | |
| 239 | Phosphorylation | GSEFVQKYLGEGPRM CHHHHHHHHCCCCHH | 11.66 | 28152594 | |
| 242 (in isoform 2) | Ubiquitination | - | 64.53 | 21890473 | |
| 255 | Ubiquitination | RDVFRLAKENAPAII HHHHHHHHHCCCEEE | 56.97 | 22053931 | |
| 255 (in isoform 1) | Ubiquitination | - | 56.97 | 21890473 | |
| 272 | Phosphorylation | DEIDAIATKRFDAQT ECCCHHHHCCCCCCC | 19.35 | 20068231 | |
| 273 | Ubiquitination | EIDAIATKRFDAQTG CCCHHHHCCCCCCCC | 41.88 | 21906983 | |
| 273 (in isoform 1) | Ubiquitination | - | 41.88 | 21890473 | |
| 283 | Methylation | DAQTGADREVQRILL CCCCCCCHHHHHHHH | 45.51 | 115492863 | |
| 296 | Sulfoxidation | LLELLNQMDGFDQNV HHHHHHHCCCCCCCC | 5.46 | 28183972 | |
| 316 | Phosphorylation | MATNRADTLDPALLR EECCCCCCCCHHHCC | 31.88 | 21406692 | |
| 330 | Acetylation | RPGRLDRKIEFPLPD CCCCCCCCEECCCCC | 46.37 | 26051181 | |
| 330 | Malonylation | RPGRLDRKIEFPLPD CCCCCCCCEECCCCC | 46.37 | 26320211 | |
| 330 | Ubiquitination | RPGRLDRKIEFPLPD CCCCCCCCEECCCCC | 46.37 | - | |
| 338 | Methylation | IEFPLPDRRQKRLIF EECCCCCHHHHHHHH | 40.78 | 115492855 | |
| 346 | Phosphorylation | RQKRLIFSTITSKMN HHHHHHHHHHHHCCC | 16.35 | 21406692 | |
| 347 | Phosphorylation | QKRLIFSTITSKMNL HHHHHHHHHHHCCCC | 19.95 | 21406692 | |
| 349 | Phosphorylation | RLIFSTITSKMNLSE HHHHHHHHHCCCCCC | 23.53 | 21406692 | |
| 350 | Phosphorylation | LIFSTITSKMNLSEE HHHHHHHHCCCCCCC | 26.51 | 21406692 | |
| 366 (in isoform 1) | Acetylation | - | 29.88 | - | |
| 366 | Acetylation | DLEDYVARPDKISGA CHHHHCCCCCCCCCC | 29.88 | 19608861 | |
| 366 | Ubiquitination | DLEDYVARPDKISGA CHHHHCCCCCCCCCC | 29.88 | 19608861 | |
| 366 (in isoform 2) | Ubiquitination | - | 29.88 | 21890473 | |
| 370 (in isoform 1) | Acetylation | - | 6.31 | - | |
| 370 | Acetylation | YVARPDKISGADINS HCCCCCCCCCCCHHH | 6.31 | 19608861 | |
| 370 | Ubiquitination | YVARPDKISGADINS HCCCCCCCCCCCHHH | 6.31 | 19608861 | |
| 370 (in isoform 2) | Ubiquitination | - | 6.31 | 21890473 | |
| 377 | Phosphorylation | ISGADINSICQESGM CCCCCHHHHHHHHCC | 25.69 | 26126808 | |
| 378 (in isoform 2) | Ubiquitination | - | 2.13 | 21890473 | |
| 379 | Glutathionylation | GADINSICQESGMLA CCCHHHHHHHHCCEE | 3.54 | 22555962 | |
| 382 | Phosphorylation | INSICQESGMLAVRE HHHHHHHHCCEEEEC | 12.01 | 26126808 | |
| 384 | Sulfoxidation | SICQESGMLAVRENR HHHHHHCCEEEECCE | 2.78 | 21406390 | |
| 397 | Acetylation | NRYIVLAKDFEKAYK CEEEEEECCHHHHHH | 59.81 | 19608861 | |
| 397 | Malonylation | NRYIVLAKDFEKAYK CEEEEEECCHHHHHH | 59.81 | 26320211 | |
| 397 | Ubiquitination | NRYIVLAKDFEKAYK CEEEEEECCHHHHHH | 59.81 | 19608861 | |
| 397 (in isoform 1) | Ubiquitination | - | 59.81 | 21890473 | |
| 401 | Acetylation | VLAKDFEKAYKTVIK EEECCHHHHHHHHHC | 57.94 | 19608861 | |
| 401 | Malonylation | VLAKDFEKAYKTVIK EEECCHHHHHHHHHC | 57.94 | 26320211 | |
| 401 | Ubiquitination | VLAKDFEKAYKTVIK EEECCHHHHHHHHHC | 57.94 | 21906983 | |
| 401 (in isoform 1) | Ubiquitination | - | 57.94 | 21890473 | |
| 404 | Acetylation | KDFEKAYKTVIKKDE CCHHHHHHHHHCHHH | 40.97 | 25953088 | |
| 404 | Ubiquitination | KDFEKAYKTVIKKDE CCHHHHHHHHHCHHH | 40.97 | - | |
| 408 | Ubiquitination | KAYKTVIKKDEQEHE HHHHHHHCHHHHHCC | 50.24 | - | |
| 409 | Acetylation | AYKTVIKKDEQEHEF HHHHHHCHHHHHCCC | 56.21 | 26051181 | |
| 409 | Ubiquitination | AYKTVIKKDEQEHEF HHHHHHCHHHHHCCC | 56.21 | 2190698 | |
| 409 (in isoform 1) | Ubiquitination | - | 56.21 | 21890473 | |
| 417 | Phosphorylation | DEQEHEFYK------ HHHHCCCCC------ | 16.89 | 25159151 | |
| 418 | Acetylation | EQEHEFYK------- HHHCCCCC------- | 60.22 | 68813 | |
| 418 | Ubiquitination | EQEHEFYK------- HHHCCCCC------- | 60.22 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 25 | T | Phosphorylation | Kinase | DYRK2 | Q92630 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRS6B_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 PRS6B_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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| Acetylation | |
| Reference | PubMed |
| "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 MET-1, AND MASS SPECTROMETRY. | |
| "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. | |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238; LYS-397 AND LYS-401,AND MASS SPECTROMETRY. | |
| 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-21 AND SER-28, 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-28, AND MASSSPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY. | |
