UniProt ID | PSMD5_HUMAN | |
---|---|---|
UniProt AC | Q16401 | |
Protein Name | 26S proteasome non-ATPase regulatory subunit 5 | |
Gene Name | PSMD5 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 504 | |
Subcellular Localization | ||
Protein Description | Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5.. | |
Protein Sequence | MAAQALALLREVARLEAPLEELRALHSVLQAVPLNELRQQAAELRLGPLFSLLNENHREKTTLCVSILERLLQAMEPVHVARNLRVDLQRGLIHPDDSVKILTLSQIGRIVENSDAVTEILNNAELLKQIVYCIGGENLSVAKAAIKSLSRISLTQAGLEALFESNLLDDLKSVMKTNDIVRYRVYELIIEISSVSPESLNYCTTSGLVTQLLRELTGEDVLVRATCIEMVTSLAYTHHGRQYLAQEGVIDQISNIIVGADSDPFSSFYLPGFVKFFGNLAVMDSPQQICERYPIFVEKVFEMIESQDPTMIGVAVDTVGILGSNVEGKQVLQKTGTRFERLLMRIGHQSKNAPVELKIRCLDAISSLLYLPPEQQTDDLLRMTESWFSSLSRDPLELFRGISSQPFPELHCAALKVFTAIANQPWAQKLMFNSPGFVEYVVDRSVEHDKASKDAKYELVKALANSKTIAEIFGNPNYLRLRTYLSEGPYYVKPVSTTAVEGAE | |
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 | Acetylation | ------MAAQALALL ------CHHHHHHHH | 14.31 | 22223895 | |
60 | 2-Hydroxyisobutyrylation | LNENHREKTTLCVSI HCCCCCCHHHHHHHH | 46.93 | - | |
61 | Phosphorylation | NENHREKTTLCVSIL CCCCCCHHHHHHHHH | 21.90 | 21406692 | |
62 | Phosphorylation | ENHREKTTLCVSILE CCCCCHHHHHHHHHH | 29.27 | 21406692 | |
66 | Phosphorylation | EKTTLCVSILERLLQ CHHHHHHHHHHHHHH | 22.06 | 21406692 | |
75 | Sulfoxidation | LERLLQAMEPVHVAR HHHHHHHCCHHHHHH | 3.74 | 21406390 | |
98 | Phosphorylation | GLIHPDDSVKILTLS CCCCCCCCEEEEEHH | 32.46 | 20873877 | |
100 | 2-Hydroxyisobutyrylation | IHPDDSVKILTLSQI CCCCCCEEEEEHHHH | 35.63 | - | |
100 | Ubiquitination | IHPDDSVKILTLSQI CCCCCCEEEEEHHHH | 35.63 | - | |
105 | Phosphorylation | SVKILTLSQIGRIVE CEEEEEHHHHCHHHC | 17.95 | 21712546 | |
114 | Phosphorylation | IGRIVENSDAVTEIL HCHHHCCCHHHHHHH | 17.28 | 21712546 | |
132 | Phosphorylation | ELLKQIVYCIGGENL HHHHHHHHHHCCCCH | 4.68 | 28152594 | |
140 | Phosphorylation | CIGGENLSVAKAAIK HHCCCCHHHHHHHHH | 31.45 | 24719451 | |
143 | Ubiquitination | GENLSVAKAAIKSLS CCCHHHHHHHHHHHH | 35.87 | 23000965 | |
144 | Ubiquitination | ENLSVAKAAIKSLSR CCHHHHHHHHHHHHC | 12.51 | 27667366 | |
147 | Ubiquitination | SVAKAAIKSLSRISL HHHHHHHHHHHCCCC | 40.39 | 23000965 | |
148 | Phosphorylation | VAKAAIKSLSRISLT HHHHHHHHHHCCCCH | 26.01 | 28258704 | |
150 | Phosphorylation | KAAIKSLSRISLTQA HHHHHHHHCCCCHHH | 34.36 | 28258704 | |
153 | Phosphorylation | IKSLSRISLTQAGLE HHHHHCCCCHHHHHH | 25.01 | 28258704 | |
155 | Phosphorylation | SLSRISLTQAGLEAL HHHCCCCHHHHHHHH | 15.02 | 28258704 | |
176 | Ubiquitination | DDLKSVMKTNDIVRY HHHHHHHHHCHHHHH | 41.86 | 33845483 | |
210 | Phosphorylation | CTTSGLVTQLLRELT CCHHHHHHHHHHHHH | 20.67 | - | |
215 | Ubiquitination | LVTQLLRELTGEDVL HHHHHHHHHHCCCHH | 51.13 | 23503661 | |
247 | Ubiquitination | GRQYLAQEGVIDQIS HHHHHHHCCCHHHHH | 50.23 | 23503661 | |
253 | Ubiquitination | QEGVIDQISNIIVGA HCCCHHHHHCEEECC | 2.78 | 21963094 | |
279 | Ubiquitination | GFVKFFGNLAVMDSP HHHHHHCCEEECCCH | 21.48 | 24816145 | |
291 | Ubiquitination | DSPQQICERYPIFVE CCHHHHHHHCCHHHH | 57.80 | 29967540 | |
308 | Ubiquitination | FEMIESQDPTMIGVA HHHHHCCCCCEEEEE | 50.33 | 29967540 | |
315 | Ubiquitination | DPTMIGVAVDTVGIL CCCEEEEEEEEEEEC | 6.56 | 27667366 | |
334 | Ubiquitination | EGKQVLQKTGTRFER CCHHHHHHHCCHHHH | 44.77 | 29967540 | |
351 | Ubiquitination | MRIGHQSKNAPVELK HHHCCCCCCCCCCHH | 51.03 | 29967540 | |
358 | Ubiquitination | KNAPVELKIRCLDAI CCCCCCHHHHHHHHH | 18.01 | 27667366 | |
370 | Phosphorylation | DAISSLLYLPPEQQT HHHHHHHCCCHHHCC | 23.58 | - | |
383 | Sulfoxidation | QTDDLLRMTESWFSS CCHHHHHHCHHHHHH | 5.00 | 30846556 | |
384 | Phosphorylation | TDDLLRMTESWFSSL CHHHHHHCHHHHHHC | 22.04 | 29083192 | |
386 | Ubiquitination | DLLRMTESWFSSLSR HHHHHCHHHHHHCCC | 25.02 | 23503661 | |
386 | Phosphorylation | DLLRMTESWFSSLSR HHHHHCHHHHHHCCC | 25.02 | 29083192 | |
389 | Phosphorylation | RMTESWFSSLSRDPL HHCHHHHHHCCCCHH | 24.90 | 29083192 | |
390 | Phosphorylation | MTESWFSSLSRDPLE HCHHHHHHCCCCHHH | 22.38 | 29083192 | |
413 | Ubiquitination | PFPELHCAALKVFTA CCCHHHHHHHHHHHH | 12.70 | 29967540 | |
416 | Ubiquitination | ELHCAALKVFTAIAN HHHHHHHHHHHHHHC | 30.49 | - | |
418 | Ubiquitination | HCAALKVFTAIANQP HHHHHHHHHHHHCCH | 3.50 | 23503661 | |
419 | Phosphorylation | CAALKVFTAIANQPW HHHHHHHHHHHCCHH | 21.82 | 24850871 | |
424 | Ubiquitination | VFTAIANQPWAQKLM HHHHHHCCHHHHHHH | 26.37 | 21963094 | |
429 | Ubiquitination | ANQPWAQKLMFNSPG HCCHHHHHHHHCCCC | 33.89 | 23503661 | |
434 | Phosphorylation | AQKLMFNSPGFVEYV HHHHHHCCCCHHEEE | 18.35 | - | |
440 | Phosphorylation | NSPGFVEYVVDRSVE CCCCHHEEEEECCCC | 10.64 | - | |
450 | Ubiquitination | DRSVEHDKASKDAKY ECCCCCCCCCHHHHH | 57.37 | 24816145 | |
456 | Ubiquitination | DKASKDAKYELVKAL CCCCHHHHHHHHHHH | 49.76 | 29967540 | |
457 | Phosphorylation | KASKDAKYELVKALA CCCHHHHHHHHHHHH | 19.06 | - | |
461 | Ubiquitination | DAKYELVKALANSKT HHHHHHHHHHHCCCH | 50.75 | 23503661 | |
466 | Phosphorylation | LVKALANSKTIAEIF HHHHHHCCCHHHHHH | 26.10 | - | |
467 | Ubiquitination | VKALANSKTIAEIFG HHHHHCCCHHHHHHC | 43.70 | 21963094 | |
478 | Phosphorylation | EIFGNPNYLRLRTYL HHHCCCCHHHHEEEC | 8.41 | 28152594 | |
486 | Phosphorylation | LRLRTYLSEGPYYVK HHHEEECCCCCEEEC | 30.05 | 28555341 | |
490 | Phosphorylation | TYLSEGPYYVKPVST EECCCCCEEECCCCC | 31.57 | 21945579 | |
491 | Phosphorylation | YLSEGPYYVKPVSTT ECCCCCEEECCCCCC | 12.72 | 21945579 | |
493 | Ubiquitination | SEGPYYVKPVSTTAV CCCCEEECCCCCCCC | 24.47 | 24816145 | |
496 | Phosphorylation | PYYVKPVSTTAVEGA CEEECCCCCCCCCCC | 28.68 | 21945579 | |
497 | Phosphorylation | YYVKPVSTTAVEGAE EEECCCCCCCCCCCC | 21.00 | 21945579 | |
498 | Phosphorylation | YVKPVSTTAVEGAE- EECCCCCCCCCCCC- | 22.62 | 21945579 |
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 PSMD5_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSMD5_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 PSMD5_HUMAN !! |
Kegg Disease | ||||||
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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 |
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2. |