PSD10_HUMAN - dbPTM
PSD10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSD10_HUMAN
UniProt AC O75832
Protein Name 26S proteasome non-ATPase regulatory subunit 10
Gene Name PSMD10
Organism Homo sapiens (Human).
Sequence Length 226
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.; Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export..
Protein Sequence MEGCVSNLMVCNLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKRMVEG
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
1Acetylation-------MEGCVSNL
-------CCCHHHCE
10.10-
6Phosphorylation--MEGCVSNLMVCNL
--CCCHHHCEEHHHH
28.4623401153
15PhosphorylationLMVCNLAYSGKLEEL
EEHHHHHHCCCHHHH
22.5623401153
18UbiquitinationCNLAYSGKLEELKES
HHHHHCCCHHHHHHH
46.9522817900
23UbiquitinationSGKLEELKESILADK
CCCHHHHHHHHHCCC
53.3322817900
23UbiquitinationSGKLEELKESILADK
CCCHHHHHHHHHCCC
53.3321890473
23UbiquitinationSGKLEELKESILADK
CCCHHHHHHHHHCCC
53.3321890473
25PhosphorylationKLEELKESILADKSL
CHHHHHHHHHCCCCH
22.7029396449
30UbiquitinationKESILADKSLATRTD
HHHHHCCCCHHCCCC
41.5921890473
30UbiquitinationKESILADKSLATRTD
HHHHHCCCCHHCCCC
41.5923000965
30UbiquitinationKESILADKSLATRTD
HHHHHCCCCHHCCCC
41.5921890473
30AcetylationKESILADKSLATRTD
HHHHHCCCCHHCCCC
41.5925953088
302-HydroxyisobutyrylationKESILADKSLATRTD
HHHHHCCCCHHCCCC
41.59-
75PhosphorylationDKDDAGWSPLHIAAS
CCCCCCCCHHHHHHH
19.3720873877
90UbiquitinationAGRDEIVKALLGKGA
CCCHHHHHHHHCCCC
38.6923000965
90UbiquitinationAGRDEIVKALLGKGA
CCCHHHHHHHHCCCC
38.6921890473
90UbiquitinationAGRDEIVKALLGKGA
CCCHHHHHHHHCCCC
38.6921890473
902-HydroxyisobutyrylationAGRDEIVKALLGKGA
CCCHHHHHHHHCCCC
38.69-
95UbiquitinationIVKALLGKGAQVNAV
HHHHHHCCCCCCEEE
51.5523000965
112PhosphorylationNGCTPLHYAASKNRH
CCCCHHHHHHCCCCC
16.1428857561
115PhosphorylationTPLHYAASKNRHEIA
CHHHHHHCCCCCHHE
23.4526437602
116AcetylationPLHYAASKNRHEIAV
HHHHHHCCCCCHHEE
53.9625953088
116MalonylationPLHYAASKNRHEIAV
HHHHHHCCCCCHHEE
53.9626320211
116UbiquitinationPLHYAASKNRHEIAV
HHHHHHCCCCCHHEE
53.9632015554
138PhosphorylationNPDAKDHYEATAMHR
CCCHHHHHHHHHHHH
19.8624927040
138NitrationNPDAKDHYEATAMHR
CCCHHHHHHHHHHHH
19.86-
143SulfoxidationDHYEATAMHRAAAKG
HHHHHHHHHHHHHHC
1.5930846556
149UbiquitinationAMHRAAAKGNLKMIH
HHHHHHHHCCCEEEE
43.5422817900
153UbiquitinationAAAKGNLKMIHILLY
HHHHCCCEEEEEEEH
39.5521906983
193PhosphorylationEEAKLLVSQGASIYI
HHHHHHHHCCCCEEE
23.9029396449
197PhosphorylationLLVSQGASIYIENKE
HHHHCCCCEEEECCC
23.8129396449
199PhosphorylationVSQGASIYIENKEEK
HHCCCCEEEECCCCC
10.3329396449
207PhosphorylationIENKEEKTPLQVAKG
EECCCCCCCCCHHCC
32.2920068231
213UbiquitinationKTPLQVAKGGLGLIL
CCCCCHHCCCHHHHH
55.4421890473
213UbiquitinationKTPLQVAKGGLGLIL
CCCCCHHCCCHHHHH
55.4422817900
2212-HydroxyisobutyrylationGGLGLILKRMVEG--
CCHHHHHHHHHCC--
31.30-
221UbiquitinationGGLGLILKRMVEG--
CCHHHHHHHHHCC--
31.3021906983
221UbiquitinationGGLGLILKRMVEG--
CCHHHHHHHHHCC--
31.3021890473
221AcetylationGGLGLILKRMVEG--
CCHHHHHHHHHCC--
31.3025953088

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 PSD10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSD10_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 PSD10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSMD1_HUMANPSMD1physical
17353931
PSMD2_HUMANPSMD2physical
17353931
PSD11_HUMANPSMD11physical
17353931
PRS8_HUMANPSMC5physical
17353931
PRS6B_HUMANPSMC4physical
17353931
PRS4_HUMANPSMC1physical
17353931
DOK2_HUMANDOK2physical
17353931
PSMD3_HUMANPSMD3physical
17353931
PRS6A_HUMANPSMC3physical
17353931
PRS7_HUMANPSMC2physical
17353931
PSMD7_HUMANPSMD7physical
17353931
PRS10_HUMANPSMC6physical
17353931
PSMD6_HUMANPSMD6physical
17353931
PSD12_HUMANPSMD12physical
17353931
PAAF1_HUMANPAAF1physical
17353931
PSMD4_HUMANPSMD4physical
17353931
PRS6B_HUMANPSMC4physical
11779854
MDM2_HUMANMDM2physical
18332869
PRS6B_HUMANPSMC4physical
19412159
MDM2_HUMANMDM2physical
16023600
TF65_HUMANRELAphysical
17904523
NFKB1_HUMANNFKB1physical
17904523
WWP2_HUMANWWP2physical
22387393
PRS6B_HUMANPSMC4physical
19490896
PRS8_HUMANPSMC5physical
19490896
RB_HUMANRB1physical
10613832
CDK4_HUMANCDK4physical
11900540
CCND2_HUMANCCND2physical
11900540
TF65_HUMANRELAphysical
18040287
GDIR1_HUMANARHGDIAphysical
20628200
RHOA_HUMANRHOAphysical
20628200
MAGA4_HUMANMAGEA4physical
12525503
PRS6B_HUMANPSMC4physical
12525503
RB_HUMANRB1physical
12525503
PSD11_HUMANPSMD11physical
22939629
PSD12_HUMANPSMD12physical
22939629
PSMD1_HUMANPSMD1physical
22939629
PSMD3_HUMANPSMD3physical
22939629
PSMD7_HUMANPSMD7physical
22939629
PSDE_HUMANPSMD14physical
22939629
PSMD2_HUMANPSMD2physical
22939629
PSMD4_HUMANPSMD4physical
22939629
PSD13_HUMANPSMD13physical
22939629
PSMD6_HUMANPSMD6physical
22939629
PSMD8_HUMANPSMD8physical
22939629
OARD1_HUMANOARD1physical
22863883
LMNA_HUMANLMNAphysical
22863883
KPRB_HUMANPRPSAP2physical
22863883
RU2B_HUMANSNRPB2physical
22863883
SQSTM_HUMANSQSTM1physical
22863883
HSP74_HUMANHSPA4physical
24338975
HS90A_HUMANHSP90AA1physical
24338975
CLIC1_HUMANCLIC1physical
24338975
GRSF1_HUMANGRSF1physical
24338975
DDAH1_HUMANDDAH1physical
24338975
MP2K1_HUMANMAP2K1physical
24338975
NCK2_HUMANNCK2physical
24338975
PAAF1_HUMANPAAF1physical
26344197
PRS7_HUMANPSMC2physical
26344197
PRS6A_HUMANPSMC3physical
26344197
PSD11_HUMANPSMD11physical
26344197
PSD13_HUMANPSMD13physical
26344197
PSDE_HUMANPSMD14physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD3_HUMANPSMD3physical
26344197
PSMD7_HUMANPSMD7physical
26344197
EP300_HUMANEP300physical
25400040
HIF1A_HUMANHIF1Aphysical
26364616
KEAP1_HUMANKEAP1physical
27091842

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 PSD10_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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