UniProt ID | PRS4_HUMAN | |
---|---|---|
UniProt AC | P62191 | |
Protein Name | 26S proteasome regulatory subunit 4 | |
Gene Name | PSMC1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 440 | |
Subcellular Localization |
Cytoplasm. Nucleus. Membrane Lipid-anchor . |
|
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. PSMC1 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 | MGQSQSGGHGPGGGKKDDKDKKKKYEPPVPTRVGKKKKKTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL | |
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 |
---|---|---|---|---|---|
2 | N-myristoyl glycine | ------MGQSQSGGH ------CCCCCCCCC | 35.53 | - | |
2 | Myristoylation | ------MGQSQSGGH ------CCCCCCCCC | 35.53 | 22223895 | |
4 | Phosphorylation | ----MGQSQSGGHGP ----CCCCCCCCCCC | 22.15 | 19362540 | |
6 | Phosphorylation | --MGQSQSGGHGPGG --CCCCCCCCCCCCC | 52.57 | 26546556 | |
13 | Ubiquitination | SGGHGPGGGKKDDKD CCCCCCCCCCCCCCC | 48.13 | - | |
18 | Ubiquitination | PGGGKKDDKDKKKKY CCCCCCCCCCHHHCC | 70.68 | - | |
23 | Ubiquitination | KDDKDKKKKYEPPVP CCCCCHHHCCCCCCC | 67.34 | - | |
24 | Acetylation | DDKDKKKKYEPPVPT CCCCHHHCCCCCCCC | 64.82 | 25825284 | |
24 | Malonylation | DDKDKKKKYEPPVPT CCCCHHHCCCCCCCC | 64.82 | 26320211 | |
24 | Ubiquitination | DDKDKKKKYEPPVPT CCCCHHHCCCCCCCC | 64.82 | - | |
25 | Ubiquitination | DKDKKKKYEPPVPTR CCCHHHCCCCCCCCC | 42.41 | - | |
25 | Phosphorylation | DKDKKKKYEPPVPTR CCCHHHCCCCCCCCC | 42.41 | 27273156 | |
40 | Phosphorylation | VGKKKKKTKGPDAAS CCCCCCCCCCCCHHH | 50.54 | 23312004 | |
41 | Ubiquitination | GKKKKKTKGPDAASK CCCCCCCCCCCHHHC | 76.85 | - | |
47 | Phosphorylation | TKGPDAASKLPLVTP CCCCCHHHCCCCCCC | 36.12 | 23312004 | |
48 | Ubiquitination | KGPDAASKLPLVTPH CCCCHHHCCCCCCCC | 49.77 | 21890473 | |
48 | Ubiquitination | KGPDAASKLPLVTPH CCCCHHHCCCCCCCC | 49.77 | 21906983 | |
48 | Ubiquitination | KGPDAASKLPLVTPH CCCCHHHCCCCCCCC | 49.77 | 21890473 | |
53 | Phosphorylation | ASKLPLVTPHTQCRL HHCCCCCCCCCHHHH | 19.62 | 30266825 | |
56 | Phosphorylation | LPLVTPHTQCRLKLL CCCCCCCCHHHHHHH | 30.48 | 30266825 | |
58 | Glutathionylation | LVTPHTQCRLKLLKL CCCCCCHHHHHHHHH | 6.06 | 22555962 | |
61 | Ubiquitination | PHTQCRLKLLKLERI CCCHHHHHHHHHHHH | 32.21 | - | |
64 | Ubiquitination | QCRLKLLKLERIKDY HHHHHHHHHHHHHHH | 59.75 | - | |
69 | Ubiquitination | LLKLERIKDYLLMEE HHHHHHHHHHHHHHH | 46.68 | 21890473 | |
69 | Acetylation | LLKLERIKDYLLMEE HHHHHHHHHHHHHHH | 46.68 | 26051181 | |
69 | Ubiquitination | LLKLERIKDYLLMEE HHHHHHHHHHHHHHH | 46.68 | 21906983 | |
69 | Ubiquitination | LLKLERIKDYLLMEE HHHHHHHHHHHHHHH | 46.68 | 21890473 | |
71 | Phosphorylation | KLERIKDYLLMEEEF HHHHHHHHHHHHHHH | 9.20 | 27642862 | |
74 | Sulfoxidation | RIKDYLLMEEEFIRN HHHHHHHHHHHHHHC | 5.86 | 30846556 | |
85 | Sulfoxidation | FIRNQEQMKPLEEKQ HHHCHHHCCCHHHHH | 4.80 | 30846556 | |
86 | Ubiquitination | IRNQEQMKPLEEKQE HHCHHHCCCHHHHHH | 46.26 | 21906983 | |
91 | Acetylation | QMKPLEEKQEEERSK HCCCHHHHHHHHHHC | 54.34 | 26051181 | |
91 | Ubiquitination | QMKPLEEKQEEERSK HCCCHHHHHHHHHHC | 54.34 | 21906983 | |
98 | Ubiquitination | KQEEERSKVDDLRGT HHHHHHHCHHHHCCC | 56.77 | 21890473 | |
98 | Sumoylation | KQEEERSKVDDLRGT HHHHHHHCHHHHCCC | 56.77 | - | |
98 | Ubiquitination | KQEEERSKVDDLRGT HHHHHHHCHHHHCCC | 56.77 | 21906983 | |
98 | Ubiquitination | KQEEERSKVDDLRGT HHHHHHHCHHHHCCC | 56.77 | 21890473 | |
105 | Ubiquitination | KVDDLRGTPMSVGTL CHHHHCCCCCCHHHH | 14.91 | - | |
144 | Ubiquitination | SFVDKDLLEPGCSVL HCCCHHHCCCCCEEH | 12.23 | - | |
147 | Ubiquitination | DKDLLEPGCSVLLNH CHHHCCCCCEEHHCC | 13.63 | - | |
149 | Phosphorylation | DLLEPGCSVLLNHKV HHCCCCCEEHHCCCC | 23.01 | 29978859 | |
155 | Ubiquitination | CSVLLNHKVHAVIGV CEEHHCCCCCEEEEE | 34.34 | - | |
159 | Ubiquitination | LNHKVHAVIGVLMDD HCCCCCEEEEEECCC | 2.06 | - | |
164 | Ubiquitination | HAVIGVLMDDTDPLV CEEEEEECCCCCCCE | 3.99 | - | |
175 | Sumoylation | DPLVTVMKVEKAPQE CCCEEEEEEEECCCC | 42.79 | - | |
178 | Acetylation | VTVMKVEKAPQETYA EEEEEEEECCCCHHH | 69.24 | 25953088 | |
178 | Ubiquitination | VTVMKVEKAPQETYA EEEEEEEECCCCHHH | 69.24 | 21906983 | |
183 | Phosphorylation | VEKAPQETYADIGGL EEECCCCHHHCCCCC | 20.82 | 29978859 | |
184 | Phosphorylation | EKAPQETYADIGGLD EECCCCHHHCCCCCH | 11.09 | 28796482 | |
185 | Acetylation | KAPQETYADIGGLDN ECCCCHHHCCCCCHH | 14.90 | - | |
185 | Ubiquitination | KAPQETYADIGGLDN ECCCCHHHCCCCCHH | 14.90 | - | |
192 | Acetylation | ADIGGLDNQIQEIKE HCCCCCHHHHHHHHH | 45.99 | - | |
192 | Ubiquitination | ADIGGLDNQIQEIKE HCCCCCHHHHHHHHH | 45.99 | - | |
198 | Ubiquitination | DNQIQEIKESVELPL HHHHHHHHHHCCCCC | 43.09 | - | |
200 | Phosphorylation | QIQEIKESVELPLTH HHHHHHHHCCCCCCC | 18.85 | 28796482 | |
206 | Phosphorylation | ESVELPLTHPEYYEE HHCCCCCCCHHHHHH | 33.18 | 28796482 | |
210 | Phosphorylation | LPLTHPEYYEEMGIK CCCCCHHHHHHCCCC | 22.19 | 28796482 | |
211 | Phosphorylation | PLTHPEYYEEMGIKP CCCCHHHHHHCCCCC | 12.07 | 28796482 | |
217 | Ubiquitination | YYEEMGIKPPKGVIL HHHHCCCCCCCEEEE | 49.92 | 21906983 | |
220 | Ubiquitination | EMGIKPPKGVILYGP HCCCCCCCEEEEECC | 74.47 | - | |
220 | Ubiquitination | EMGIKPPKGVILYGP HCCCCCCCEEEEECC | 74.47 | - | |
225 | Phosphorylation | PPKGVILYGPPGTGK CCCEEEEECCCCCCH | 19.23 | 23917254 | |
230 | Phosphorylation | ILYGPPGTGKTLLAK EEECCCCCCHHHHHH | 41.08 | 29083192 | |
232 | Ubiquitination | YGPPGTGKTLLAKAV ECCCCCCHHHHHHHH | 35.52 | 21890473 | |
232 | 2-Hydroxyisobutyrylation | YGPPGTGKTLLAKAV ECCCCCCHHHHHHHH | 35.52 | - | |
232 | Acetylation | YGPPGTGKTLLAKAV ECCCCCCHHHHHHHH | 35.52 | 25953088 | |
232 | Ubiquitination | YGPPGTGKTLLAKAV ECCCCCCHHHHHHHH | 35.52 | 21906983 | |
232 | Ubiquitination | YGPPGTGKTLLAKAV ECCCCCCHHHHHHHH | 35.52 | 21890473 | |
233 | Phosphorylation | GPPGTGKTLLAKAVA CCCCCCHHHHHHHHH | 28.48 | 29083192 | |
237 | Acetylation | TGKTLLAKAVANQTS CCHHHHHHHHHCCCC | 43.28 | 25953088 | |
237 | Ubiquitination | TGKTLLAKAVANQTS CCHHHHHHHHHCCCC | 43.28 | 17370265 | |
243 | Phosphorylation | AKAVANQTSATFLRV HHHHHCCCCHHHHHH | 21.82 | 20873877 | |
244 | Phosphorylation | KAVANQTSATFLRVV HHHHCCCCHHHHHHH | 18.62 | 30624053 | |
246 | Phosphorylation | VANQTSATFLRVVGS HHCCCCHHHHHHHCH | 23.99 | 20873877 | |
253 | Ubiquitination | TFLRVVGSELIQKYL HHHHHHCHHHHHHHH | 20.02 | - | |
258 | Ubiquitination | VGSELIQKYLGDGPK HCHHHHHHHHCCCHH | 35.13 | 21890473 | |
258 | 2-Hydroxyisobutyrylation | VGSELIQKYLGDGPK HCHHHHHHHHCCCHH | 35.13 | - | |
258 | Acetylation | VGSELIQKYLGDGPK HCHHHHHHHHCCCHH | 35.13 | 19608861 | |
258 | Ubiquitination | VGSELIQKYLGDGPK HCHHHHHHHHCCCHH | 35.13 | 21890473 | |
258 | Ubiquitination | VGSELIQKYLGDGPK HCHHHHHHHHCCCHH | 35.13 | 21890473 | |
265 | Acetylation | KYLGDGPKLVRELFR HHHCCCHHHHHHHHH | 66.21 | 23749302 | |
265 | Ubiquitination | KYLGDGPKLVRELFR HHHCCCHHHHHHHHH | 66.21 | 265 | |
277 | Ubiquitination | LFRVAEEHAPSIVFI HHHHHHHHCCCEEEE | 34.15 | - | |
286 | Ubiquitination | PSIVFIDEIDAIGTK CCEEEEEECCCCCCC | 37.64 | - | |
293 | Acetylation | EIDAIGTKRYDSNSG ECCCCCCCCCCCCCC | 43.69 | 25953088 | |
293 | Ubiquitination | EIDAIGTKRYDSNSG ECCCCCCCCCCCCCC | 43.69 | 21906983 | |
295 | Phosphorylation | DAIGTKRYDSNSGGE CCCCCCCCCCCCCCH | 25.86 | 22964224 | |
297 | Phosphorylation | IGTKRYDSNSGGERE CCCCCCCCCCCCHHH | 24.78 | - | |
308 | Phosphorylation | GEREIQRTMLELLNQ CHHHHHHHHHHHHHH | 15.10 | 28176443 | |
309 | Sulfoxidation | EREIQRTMLELLNQL HHHHHHHHHHHHHHC | 2.74 | 30846556 | |
314 | Ubiquitination | RTMLELLNQLDGFDS HHHHHHHHHCCCCCC | 53.66 | - | |
321 | Phosphorylation | NQLDGFDSRGDVKVI HHCCCCCCCCCEEEE | 35.58 | 28176443 | |
322 | Methylation | QLDGFDSRGDVKVIM HCCCCCCCCCEEEEE | 47.37 | 115492847 | |
323 | Ubiquitination | LDGFDSRGDVKVIMA CCCCCCCCCEEEEEE | 48.27 | - | |
326 | Ubiquitination | FDSRGDVKVIMATNR CCCCCCEEEEEECCC | 30.68 | 21906983 | |
340 | Ubiquitination | RIETLDPALIRPGRI CCEECCHHHCCCCCC | 18.45 | - | |
347 | Ubiquitination | ALIRPGRIDRKIEFP HHCCCCCCCCEEECC | 8.13 | - | |
348 | Ubiquitination | LIRPGRIDRKIEFPL HCCCCCCCCEEECCC | 44.45 | - | |
350 | Ubiquitination | RPGRIDRKIEFPLPD CCCCCCCEEECCCCC | 42.72 | - | |
350 | Ubiquitination | RPGRIDRKIEFPLPD CCCCCCCEEECCCCC | 42.72 | - | |
357 | Ubiquitination | KIEFPLPDEKTKKRI EEECCCCCHHHHHHE | 77.14 | - | |
359 | Ubiquitination | EFPLPDEKTKKRIFQ ECCCCCHHHHHHEEE | 73.38 | 35966 | |
369 | Phosphorylation | KRIFQIHTSRMTLAD HHEEEEECCCCCCCC | 21.47 | 30001349 | |
370 | Phosphorylation | RIFQIHTSRMTLADD HEEEEECCCCCCCCC | 13.09 | 23312004 | |
372 | Sulfoxidation | FQIHTSRMTLADDVT EEEECCCCCCCCCCC | 3.45 | 30846556 | |
373 | Phosphorylation | QIHTSRMTLADDVTL EEECCCCCCCCCCCH | 20.06 | 22985185 | |
385 | Sulfoxidation | VTLDDLIMAKDDLSG CCHHHHHHCCCCCCC | 5.01 | 30846556 | |
387 | Ubiquitination | LDDLIMAKDDLSGAD HHHHHHCCCCCCCCC | 34.10 | 21906983 | |
391 | Phosphorylation | IMAKDDLSGADIKAI HHCCCCCCCCCHHHH | 38.64 | 21712546 | |
396 | 2-Hydroxyisobutyrylation | DLSGADIKAICTEAG CCCCCCHHHHHHHHH | 32.04 | - | |
396 | Ubiquitination | DLSGADIKAICTEAG CCCCCCHHHHHHHHH | 32.04 | - | |
399 | Glutathionylation | GADIKAICTEAGLMA CCCHHHHHHHHHHHH | 3.17 | 22555962 | |
405 | Sulfoxidation | ICTEAGLMALRERRM HHHHHHHHHHHHHHH | 3.02 | 21406390 | |
413 | Ubiquitination | ALRERRMKVTNEDFK HHHHHHHCCCHHHHH | 44.06 | 21906983 | |
420 | Ubiquitination | KVTNEDFKKSKENVL CCCHHHHHHHHHHCE | 69.34 | 21890473 | |
420 | 2-Hydroxyisobutyrylation | KVTNEDFKKSKENVL CCCHHHHHHHHHHCE | 69.34 | - | |
420 | Ubiquitination | KVTNEDFKKSKENVL CCCHHHHHHHHHHCE | 69.34 | 21890473 | |
420 | Ubiquitination | KVTNEDFKKSKENVL CCCHHHHHHHHHHCE | 69.34 | 21890473 | |
421 | Ubiquitination | VTNEDFKKSKENVLY CCHHHHHHHHHHCEE | 67.75 | - | |
423 | Ubiquitination | NEDFKKSKENVLYKK HHHHHHHHHHCEEEC | 63.29 | - | |
429 | Acetylation | SKENVLYKKQEGTPE HHHHCEEECCCCCCC | 43.76 | 7396815 | |
429 | Ubiquitination | SKENVLYKKQEGTPE HHHHCEEECCCCCCC | 43.76 | - | |
430 | Sumoylation | KENVLYKKQEGTPEG HHHCEEECCCCCCCC | 39.77 | - | |
430 | Sumoylation | KENVLYKKQEGTPEG HHHCEEECCCCCCCC | 39.77 | - | |
430 | Ubiquitination | KENVLYKKQEGTPEG HHHCEEECCCCCCCC | 39.77 | 2190698 | |
434 | Phosphorylation | LYKKQEGTPEGLYL- EEECCCCCCCCCCC- | 19.88 | 22617229 | |
439 | Phosphorylation | EGTPEGLYL------ CCCCCCCCC------ | 22.63 | 25807930 |
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 PRS4_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRS4_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 PRS4_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 |
"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-258, AND MASS SPECTROMETRY. | |
Myristoylation | |
Reference | PubMed |
"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: MYRISTOYLATION [LARGE SCALE ANALYSIS] AT GLY-2, 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-4, AND MASSSPECTROMETRY. | |
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND MASSSPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237, AND MASSSPECTROMETRY. |