PSMD5_HUMAN - dbPTM
PSMD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAQALALL
------CHHHHHHHH
14.3122223895
602-HydroxyisobutyrylationLNENHREKTTLCVSI
HCCCCCCHHHHHHHH
46.93-
61PhosphorylationNENHREKTTLCVSIL
CCCCCCHHHHHHHHH
21.9021406692
62PhosphorylationENHREKTTLCVSILE
CCCCCHHHHHHHHHH
29.2721406692
66PhosphorylationEKTTLCVSILERLLQ
CHHHHHHHHHHHHHH
22.0621406692
75SulfoxidationLERLLQAMEPVHVAR
HHHHHHHCCHHHHHH
3.7421406390
98PhosphorylationGLIHPDDSVKILTLS
CCCCCCCCEEEEEHH
32.4620873877
1002-HydroxyisobutyrylationIHPDDSVKILTLSQI
CCCCCCEEEEEHHHH
35.63-
100UbiquitinationIHPDDSVKILTLSQI
CCCCCCEEEEEHHHH
35.63-
105PhosphorylationSVKILTLSQIGRIVE
CEEEEEHHHHCHHHC
17.9521712546
114PhosphorylationIGRIVENSDAVTEIL
HCHHHCCCHHHHHHH
17.2821712546
132PhosphorylationELLKQIVYCIGGENL
HHHHHHHHHHCCCCH
4.6828152594
140PhosphorylationCIGGENLSVAKAAIK
HHCCCCHHHHHHHHH
31.4524719451
143UbiquitinationGENLSVAKAAIKSLS
CCCHHHHHHHHHHHH
35.8723000965
144UbiquitinationENLSVAKAAIKSLSR
CCHHHHHHHHHHHHC
12.5127667366
147UbiquitinationSVAKAAIKSLSRISL
HHHHHHHHHHHCCCC
40.3923000965
148PhosphorylationVAKAAIKSLSRISLT
HHHHHHHHHHCCCCH
26.0128258704
150PhosphorylationKAAIKSLSRISLTQA
HHHHHHHHCCCCHHH
34.3628258704
153PhosphorylationIKSLSRISLTQAGLE
HHHHHCCCCHHHHHH
25.0128258704
155PhosphorylationSLSRISLTQAGLEAL
HHHCCCCHHHHHHHH
15.0228258704
176UbiquitinationDDLKSVMKTNDIVRY
HHHHHHHHHCHHHHH
41.8633845483
210PhosphorylationCTTSGLVTQLLRELT
CCHHHHHHHHHHHHH
20.67-
215UbiquitinationLVTQLLRELTGEDVL
HHHHHHHHHHCCCHH
51.1323503661
247UbiquitinationGRQYLAQEGVIDQIS
HHHHHHHCCCHHHHH
50.2323503661
253UbiquitinationQEGVIDQISNIIVGA
HCCCHHHHHCEEECC
2.7821963094
279UbiquitinationGFVKFFGNLAVMDSP
HHHHHHCCEEECCCH
21.4824816145
291UbiquitinationDSPQQICERYPIFVE
CCHHHHHHHCCHHHH
57.8029967540
308UbiquitinationFEMIESQDPTMIGVA
HHHHHCCCCCEEEEE
50.3329967540
315UbiquitinationDPTMIGVAVDTVGIL
CCCEEEEEEEEEEEC
6.5627667366
334UbiquitinationEGKQVLQKTGTRFER
CCHHHHHHHCCHHHH
44.7729967540
351UbiquitinationMRIGHQSKNAPVELK
HHHCCCCCCCCCCHH
51.0329967540
358UbiquitinationKNAPVELKIRCLDAI
CCCCCCHHHHHHHHH
18.0127667366
370PhosphorylationDAISSLLYLPPEQQT
HHHHHHHCCCHHHCC
23.58-
383SulfoxidationQTDDLLRMTESWFSS
CCHHHHHHCHHHHHH
5.0030846556
384PhosphorylationTDDLLRMTESWFSSL
CHHHHHHCHHHHHHC
22.0429083192
386UbiquitinationDLLRMTESWFSSLSR
HHHHHCHHHHHHCCC
25.0223503661
386PhosphorylationDLLRMTESWFSSLSR
HHHHHCHHHHHHCCC
25.0229083192
389PhosphorylationRMTESWFSSLSRDPL
HHCHHHHHHCCCCHH
24.9029083192
390PhosphorylationMTESWFSSLSRDPLE
HCHHHHHHCCCCHHH
22.3829083192
413UbiquitinationPFPELHCAALKVFTA
CCCHHHHHHHHHHHH
12.7029967540
416UbiquitinationELHCAALKVFTAIAN
HHHHHHHHHHHHHHC
30.49-
418UbiquitinationHCAALKVFTAIANQP
HHHHHHHHHHHHCCH
3.5023503661
419PhosphorylationCAALKVFTAIANQPW
HHHHHHHHHHHCCHH
21.8224850871
424UbiquitinationVFTAIANQPWAQKLM
HHHHHHCCHHHHHHH
26.3721963094
429UbiquitinationANQPWAQKLMFNSPG
HCCHHHHHHHHCCCC
33.8923503661
434PhosphorylationAQKLMFNSPGFVEYV
HHHHHHCCCCHHEEE
18.35-
440PhosphorylationNSPGFVEYVVDRSVE
CCCCHHEEEEECCCC
10.64-
450UbiquitinationDRSVEHDKASKDAKY
ECCCCCCCCCHHHHH
57.3724816145
456UbiquitinationDKASKDAKYELVKAL
CCCCHHHHHHHHHHH
49.7629967540
457PhosphorylationKASKDAKYELVKALA
CCCHHHHHHHHHHHH
19.06-
461UbiquitinationDAKYELVKALANSKT
HHHHHHHHHHHCCCH
50.7523503661
466PhosphorylationLVKALANSKTIAEIF
HHHHHHCCCHHHHHH
26.10-
467UbiquitinationVKALANSKTIAEIFG
HHHHHCCCHHHHHHC
43.7021963094
478PhosphorylationEIFGNPNYLRLRTYL
HHHCCCCHHHHEEEC
8.4128152594
486PhosphorylationLRLRTYLSEGPYYVK
HHHEEECCCCCEEEC
30.0528555341
490PhosphorylationTYLSEGPYYVKPVST
EECCCCCEEECCCCC
31.5721945579
491PhosphorylationYLSEGPYYVKPVSTT
ECCCCCEEECCCCCC
12.7221945579
493UbiquitinationSEGPYYVKPVSTTAV
CCCCEEECCCCCCCC
24.4724816145
496PhosphorylationPYYVKPVSTTAVEGA
CEEECCCCCCCCCCC
28.6821945579
497PhosphorylationYYVKPVSTTAVEGAE
EEECCCCCCCCCCCC
21.0021945579
498PhosphorylationYVKPVSTTAVEGAE-
EECCCCCCCCCCCC-
22.6221945579

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSMD5_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRS7_HUMANPSMC2physical
19412159
PRS7_YEASTRPT1physical
19217412
PRS4_YEASTRPT2physical
19217412
RPN2_YEASTRPN2physical
19217412
RPN7_YEASTRPN7physical
19217412
PRS7_HUMANPSMC2physical
19490896
PRS4_HUMANPSMC1physical
19490896
PSMD2_HUMANPSMD2physical
19490896
PSMD4_HUMANPSMD4physical
22921402
PRS7_HUMANPSMC2physical
22921402
A4_HUMANAPPphysical
21832049
TFCP2_HUMANTFCP2physical
25416956
BAG1_HUMANBAG1physical
26344197
DI3L2_HUMANDIS3L2physical
26344197
GCSH_HUMANGCSHphysical
26344197
LAMB1_HUMANLAMB1physical
26344197
MCM3_HUMANMCM3physical
26344197
P4HA1_HUMANP4HA1physical
26344197
PAAF1_HUMANPAAF1physical
26344197
PFKAL_HUMANPFKLphysical
26344197
PFKAM_HUMANPFKMphysical
26344197
PSA3_HUMANPSMA3physical
26344197
PSA4_HUMANPSMA4physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB3_HUMANPSMB3physical
26344197
PSB4_HUMANPSMB4physical
26344197
PSB5_HUMANPSMB5physical
26344197
PSB6_HUMANPSMB6physical
26344197
PSB8_HUMANPSMB8physical
26344197
PSB9_HUMANPSMB9physical
26344197
PRS4_HUMANPSMC1physical
26344197
PRS7_HUMANPSMC2physical
26344197
PRS6A_HUMANPSMC3physical
26344197
PRS10_HUMANPSMC6physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSDE_HUMANPSMD14physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD6_HUMANPSMD6physical
26344197
PSMD7_HUMANPSMD7physical
26344197
PSMD8_HUMANPSMD8physical
26344197
PSMD9_HUMANPSMD9physical
26344197
TBCD_HUMANTBCDphysical
26344197
UBP47_HUMANUSP47physical
26344197
PSMD4_HUMANPSMD4physical
28514442
PSD10_HUMANPSMD10physical
28514442
PSMD1_HUMANPSMD1physical
28514442
PRS6A_HUMANPSMC3physical
28514442
PRS10_HUMANPSMC6physical
28514442
PRS7_HUMANPSMC2physical
28514442
PRS4_HUMANPSMC1physical
28514442
PRS8_HUMANPSMC5physical
28514442
PSD12_HUMANPSMD12physical
28514442
PSMD7_HUMANPSMD7physical
28514442
PSD11_HUMANPSMD11physical
28514442
PSD13_HUMANPSMD13physical
28514442
PSMD6_HUMANPSMD6physical
28514442
PRS6B_HUMANPSMC4physical
28514442
PSMD2_HUMANPSMD2physical
28514442
PSMD3_HUMANPSMD3physical
28514442
ADRM1_HUMANADRM1physical
28514442
PSMD8_HUMANPSMD8physical
28514442

Drug and Disease Associations
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.
Regulatory Network of PSMD5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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