Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  26S proteasome non-ATPase regulatory subunit 12  

UniProtKB / Swiss-Prot ID :  PSD12_HUMAN

Gene Name (Synonyms) : 
PSMD12  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. 

Protein Sequence MADGGSERADGRIVKMEVDYSATVDQRLPECAKLAKEGRLQEVIETLLSLEKQTRTASDMVSTSRILVAV...
Predicted Secondary Structure CCCCCCCCCCCEEEECCCCHHHHHHHHCCHHHHHHHHCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
358V -> A (in dbSNP:rs2230680). VAR_051558
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADGGS
---CCCCCC
24.93UniProtKB
Link-
52Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LSLEKQTRT
HHHHHHHHH
63.36Phosphositeplus
Link-
92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)MLLSKRRSQ
EEEEECCHH
52.37Phosphositeplus
Link-
121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DLPIKLRLI
CHHHHHHHH
26.14Phosphositeplus
Link-
137PhosphotyrosineEGKIYVEIE
CCEEEEEEH
8.77Phosphositeplus
Link-
147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ARLTKTLAT
HHHHHHHHH
46.24Phosphositeplus
Link-
153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LATIKEQNG
HHHHHHHHC
49.22Phosphositeplus
Link-
160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NGDVKEAAS
HCCHHHHHH
46.50Phosphositeplus
Link-
179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GSMEKKERV
CCHHHHHHH
51.82Phosphositeplus
Link-
212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KINTKFFQE
HHHHHHHCC
39.43Phosphositeplus
Link-
221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENTEKLKLK
CCCHHHHHH
49.21Phosphositeplus
Link-
221N6-acetyllysineENTEKLKLK
CCCHHHHHH
49.21HPRD
Link-
221N6-acetyllysineENTEKLKLK
CCCHHHHHH
49.21Phosphositeplus
Link-
221N6-acetyllysine.ENTEKLKLK
CCCHHHHHH
49.21UniProtKB
Link-
227PhosphotyrosineKLKYYNLMI
HHHHHHHHH
10.55HPRD
Link-
255S-nitrosocysteineYDTPCIQAE
HHCCCCCCC
3.80dbSNO
Link-
330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MELRKGSLE
HHCCCCCCC
66.53Phosphositeplus
Link-
368N6-acetyllysineRIMAKYYTR
HHHHHHCCC
22.78HPRD
Link-
368N6-acetyllysineRIMAKYYTR
HHHHHHCCC
22.78Phosphositeplus
Link-
368N6-acetyllysine.RIMAKYYTR
HHHHHHCCC
22.78UniProtKB
Link-
448Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HLIAKEEMI
HHHHHHHHH
47.41Phosphositeplus
Link-
448N6-acetyllysineHLIAKEEMI
HHHHHHHHH
47.41HPRD
Link-
448N6-acetyllysineHLIAKEEMI
HHHHHHHHH
47.41Phosphositeplus
Link-
448N6-acetyllysine.HLIAKEEMI
HHHHHHHHH
47.41UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TRAF6_HUMANphysical interactionMINT-47941MINT14743216
TRAF6_HUMANphysical interactionDIP:44870EDIP14743216
PSA4_HUMANENSP00000348442STRING
PRS6B_HUMANENSP00000348442STRING
PSMD5_HUMANENSP00000348442STRING
PSMD8_HUMANENSP00000348442STRING
PRS10_HUMANENSP00000348442STRING
PSA3_HUMANENSP00000348442STRING
PSME2_HUMANENSP00000348442STRING
PSD10_HUMANENSP00000348442STRING
PSD7_HUMANENSP00000348442STRING
PSA2_HUMANENSP00000348442STRING
PSB3_HUMANENSP00000348442STRING
PSB7_HUMANENSP00000348442STRING
PRS4_HUMANENSP00000348442STRING
PSA6_HUMANENSP00000348442STRING
PSD11_HUMANENSP00000348442STRING
PSMD9_HUMANENSP00000348442STRING
PSB1_HUMANENSP00000348442STRING
PSDE_HUMANENSP00000348442STRING
PSMD3_HUMANENSP00000348442STRING
PSB6_HUMANENSP00000348442STRING
PSA5_HUMANENSP00000348442STRING
PSB4_HUMANENSP00000348442STRING
PRS7_HUMANENSP00000348442STRING
PSMD6_HUMANENSP00000348442STRING
PRS6A_HUMANENSP00000348442STRING
PSMD1_HUMANENSP00000348442STRING
PSMD2_HUMANENSP00000348442STRING
PRS8_HUMANENSP00000348442STRING
PSD13_HUMANENSP00000348442STRING
PSMF1_HUMANENSP00000348442STRING
PSB5_HUMANENSP00000348442STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-221; LYS-368 AND LYS-448,AND MASS SPECTROMETRY.
"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 2-12, AND ACETYLATION AT ALA-2.
"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 ALA-2, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures