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UniProtKB - Q13200 (PSMD2_HUMAN)

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Protein

26S proteasome non-ATPase regulatory subunit 2

Gene

PSMD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication
Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6798695 Neutrophil degranulation
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MoonDBiQ13200 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 2
Alternative name(s):
26S proteasome regulatory subunit RPN1
26S proteasome regulatory subunit S2
26S proteasome subunit p97
Protein 55.11
Tumor necrosis factor type 1 receptor-associated protein 2
Gene namesi
Name:PSMD2
Synonyms:TRAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000175166.16
HGNCiHGNC:9559 PSMD2
MIMi606223 gene
neXtProtiNX_Q13200

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5708
OpenTargetsiENSG00000175166
PharmGKBiPA33905

Chemistry databases

ChEMBLiCHEMBL2364701

Polymorphism and mutation databases

BioMutaiPSMD2
DMDMi6174930

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001738101 – 90826S proteasome non-ATPase regulatory subunit 2Add BLAST908

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei16PhosphoserineCombined sources1
Modified residuei24PhosphothreonineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei147PhosphoserineCombined sources1
Modified residuei194PhosphotyrosineCombined sources1
Modified residuei361PhosphoserineCombined sources1
Modified residuei363PhosphoserineCombined sources1
Modified residuei551N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13200
MaxQBiQ13200
PaxDbiQ13200
PeptideAtlasiQ13200
PRIDEiQ13200
ProteomicsDBi59219

PTM databases

iPTMnetiQ13200
PhosphoSitePlusiQ13200
SwissPalmiQ13200

Expressioni

Tissue specificityi

Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung and placenta.

Gene expression databases

BgeeiENSG00000175166
CleanExiHS_PSMD2
ExpressionAtlasiQ13200 baseline and differential
GenevisibleiQ13200 HS

Organism-specific databases

HPAiHPA045192

Interactioni

Subunit structurei

Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases and few additional components including PSMD2 (PubMed:27428775, PubMed:27342858). Interacts with RPGRIP1L (By similarity).By similarity2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111681, 186 interactors
CORUMiQ13200
DIPiDIP-38204N
IntActiQ13200, 153 interactors
MINTiQ13200
STRINGi9606.ENSP00000310129

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50Z1-908[»]
5GJRelectron microscopy3.50AC/Z1-908[»]
5L4Kelectron microscopy4.50Z1-908[»]
5LN3electron microscopy6.80Z1-908[»]
5T0Celectron microscopy3.80Af/Bf1-908[»]
5T0Gelectron microscopy4.40f164-908[»]
5T0Helectron microscopy6.80f164-908[»]
5T0Ielectron microscopy8.00f164-908[»]
5T0Jelectron microscopy8.00f164-908[»]
5VHFelectron microscopy5.70f6-853[»]
5VHHelectron microscopy6.10f6-853[»]
5VHIelectron microscopy6.80f6-853[»]
5VHJelectron microscopy8.50f70-853[»]
5VHMelectron microscopy8.30f6-853[»]
5VHNelectron microscopy7.30f6-853[»]
5VHOelectron microscopy8.30f6-853[»]
5VHPelectron microscopy7.90f70-853[»]
5VHQelectron microscopy8.90f6-853[»]
5VHRelectron microscopy7.70f6-853[»]
5VHSelectron microscopy8.80f70-853[»]
ProteinModelPortaliQ13200
SMRiQ13200
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati409 – 442PC 1Add BLAST34
Repeati443 – 479PC 2Add BLAST37
Repeati480 – 514PC 3Add BLAST35
Repeati517 – 551PC 4Add BLAST35
Repeati560 – 589PC 5Add BLAST30
Repeati692 – 723PC 6Add BLAST32
Repeati742 – 757PC 7Add BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi623 – 641Glu/Lys-richAdd BLAST19

Sequence similaritiesi

Belongs to the proteasome subunit S2 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2005 Eukaryota
COG5110 LUCA
GeneTreeiENSGT00550000074983
HOGENOMiHOG000176022
HOVERGENiHBG001842
InParanoidiQ13200
KOiK03028
OMAiMVDICAY
OrthoDBiEOG091G04TC
PhylomeDBiQ13200
TreeFamiTF105739

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR016643 26S_Psome_Rpn1
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR002015 Proteasome/cyclosome_rpt
PANTHERiPTHR10943:SF1 PTHR10943:SF1, 1 hit
PfamiView protein in Pfam
PF01851 PC_rep, 2 hits
PIRSFiPIRSF015965 26S_Psome_Rpn1, 1 hit
SUPFAMiSSF48371 SSF48371, 4 hits

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13200-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK 
        60         70         80         90        100
QLQDELEMLV ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR 
       110        120        130        140        150
PHYGKLKEIY ENMAPGENKR FAADIISVLA MTMSGERECL KYRLVGSQEE 
       160        170        180        190        200
LASWGHEYVR HLAGEVAKEW QELDDAEKVQ REPLLTLVKE IVPYNMAHNA 
       210        220        230        240        250
EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV PEPENSALLR 
       260        270        280        290        300
CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR 
       310        320        330        340        350
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK 
       360        370        380        390        400
THLENNRFGG SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY 
       410        420        430        440        450
KNKDHGMLSA AASLGMILLW DVDGGLTQID KYLYSSEDYI KSGALLACGI 
       460        470        480        490        500
VNSGVRNECD PALALLSDYV LHNSNTMRLG SIFGLGLAYA GSNREDVLTL 
       510        520        530        540        550
LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ TIMEKSETEL 
       560        570        580        590        600
KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY 
       610        620        630        640        650
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ 
       660        670        680        690        700
GVAVLGIALI AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS 
       710        720        730        740        750
NPRLNILDTL SKFSHDADPE VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ 
       760        770        780        790        800
YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP YHSDRQLMSQ VAVAGLLTVL 
       810        820        830        840        850
VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL PVSVRVGQAV 
       860        870        880        890        900
DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL 

RKNPNYDL
Length:908
Mass (Da):100,200
Last modified:July 15, 1999 - v3
Checksum:iFAD71E7B26101BE3
GO
Isoform 2 (identifier: Q13200-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: MEEGGRDKAP...WGHEYVRHLA → MSMS

Note: No experimental confirmation available.
Show »
Length:749
Mass (Da):82,193
Checksum:i4007D2AAADF807A6
GO
Isoform 3 (identifier: Q13200-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.

Note: No experimental confirmation available.
Show »
Length:778
Mass (Da):85,606
Checksum:i5564271C57A5959D
GO

Sequence cautioni

The sequence AAA87705 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10P → R in CAA60167 (PubMed:7601280).Curated1
Sequence conflicti21P → S (PubMed:9126987).Curated1
Sequence conflicti32E → G (PubMed:9126987).Curated1
Sequence conflicti43Q → L (PubMed:9126987).Curated1
Sequence conflicti57E → V (PubMed:9126987).Curated1
Sequence conflicti60V → A in BAA11226 (PubMed:8774743).Curated1
Sequence conflicti226Y → S in AAA87705 (PubMed:9126987).Curated1
Sequence conflicti260S → T in CAA60167 (PubMed:7601280).Curated1
Sequence conflicti281 – 283IFT → SS in AAA87705 (PubMed:9126987).Curated3
Sequence conflicti415G → A in BAA11226 (PubMed:8774743).Curated1
Sequence conflicti731M → MGM (PubMed:9126987).Curated1
Sequence conflicti776L → P in BAG63219 (PubMed:14702039).Curated1
Sequence conflicti900 – 908LRKNPNYDL → FGRTPIMISK (PubMed:15489334).Curated9
Sequence conflicti900 – 908LRKNPNYDL → FGRTPIMISK (PubMed:7601280).Curated9

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051554176A → T. Corresponds to variant dbSNP:rs11545172Ensembl.1
Natural variantiVAR_051555313E → D1 PublicationCorresponds to variant dbSNP:rs11545169Ensembl.1
Natural variantiVAR_067451724N → Y2 PublicationsCorresponds to variant dbSNP:rs17856236Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0550651 – 163MEEGG…VRHLA → MSMS in isoform 2. 1 PublicationAdd BLAST163
Alternative sequenceiVSP_0550661 – 130Missing in isoform 3. 1 PublicationAdd BLAST130

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78151 mRNA Translation: BAA11226.1
BT009736 mRNA Translation: AAP88738.1
AK301759 mRNA Translation: BAG63219.1
AK302177 mRNA Translation: BAG63543.1
AC078797 Genomic DNA No translation available.
BC002368 mRNA Translation: AAH02368.1
BC002997 mRNA Translation: AAH02997.1
BC007897 mRNA Translation: AAH07897.1
U12596 mRNA Translation: AAA87705.1 Different initiation.
X86446 mRNA Translation: CAA60167.1
CCDSiCCDS3258.1 [Q13200-1]
CCDS63853.1 [Q13200-3]
CCDS63854.1 [Q13200-2]
RefSeqiNP_001265637.1, NM_001278708.1 [Q13200-3]
NP_001265638.1, NM_001278709.1 [Q13200-2]
NP_002799.3, NM_002808.4 [Q13200-1]
UniGeneiHs.518464

Genome annotation databases

EnsembliENST00000310118; ENSP00000310129; ENSG00000175166 [Q13200-1]
ENST00000435761; ENSP00000402618; ENSG00000175166 [Q13200-2]
ENST00000439383; ENSP00000416028; ENSG00000175166 [Q13200-3]
GeneIDi5708
KEGGihsa:5708
UCSCiuc003fnn.3 human [Q13200-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSMD2_HUMAN
AccessioniPrimary (citable) accession number: Q13200
Secondary accession number(s): B4DX07
, B4DXY1, E7EW34, E9PCS3, Q12932, Q15321, Q53XQ4, Q96I12
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: June 20, 2018
This is version 189 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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