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Protein

26S proteasome regulatory subunit 7

Gene

PSMC2

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. PSMC2 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi216 – 223ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandATP-binding, Nucleotide-binding

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

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome regulatory subunit 7
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT1
Proteasome 26S subunit ATPase 2
Protein MSS1
Gene namesi
Name:PSMC2
Synonyms:MSS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000161057.10
HGNCiHGNC:9548 PSMC2
MIMi154365 gene
neXtProtiNX_P35998

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

Cytoplasm, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5701
OpenTargetsiENSG00000161057
PharmGKBiPA33893

Chemistry databases

ChEMBLiCHEMBL2364701

Polymorphism and mutation databases

BioMutaiPSMC2
DMDMi547930

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000847092 – 43326S proteasome regulatory subunit 7Add BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei116N6-acetyllysineCombined sources1
Modified residuei422N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP35998
MaxQBiP35998
PaxDbiP35998
PeptideAtlasiP35998
PRIDEiP35998
ProteomicsDBi55172

2D gel databases

OGPiP35998
REPRODUCTION-2DPAGEiIPI00021435
P35998

PTM databases

iPTMnetiP35998
PhosphoSitePlusiP35998
SwissPalmiP35998

Expressioni

Inductioni

Expression is not cell cycle-dependent and occurs throughout the cell cycle.1 Publication

Gene expression databases

BgeeiENSG00000161057
CleanExiHS_PSMC2
ExpressionAtlasiP35998 baseline and differential
GenevisibleiP35998 HS

Organism-specific databases

HPAiHPA019238
HPA049621

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 including PSMC2 and few additional components (PubMed:27428775, PubMed:27342858). Interacts with NDC80/HEC; this interaction is detected only during M phase. Interacts and SQSTM1 (PubMed:15340068). Interacts with PAAF1 (PubMed:15831487). Directly interacts with TRIM5 (PubMed:22078707).7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111674, 172 interactors
CORUMiP35998
DIPiDIP-27554N
IntActiP35998, 60 interactors
MINTiP35998
STRINGi9606.ENSP00000292644

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GJQelectron microscopy4.50H1-433[»]
5GJRelectron microscopy3.50H/v1-433[»]
5L4Gelectron microscopy4.02H1-433[»]
5LN3electron microscopy6.80H1-433[»]
5M32electron microscopy3.80c1-433[»]
5T0Celectron microscopy3.80AA/BA1-433[»]
5T0Gelectron microscopy4.40A1-433[»]
5T0Helectron microscopy6.80A1-433[»]
5T0Ielectron microscopy8.00A1-433[»]
5T0Jelectron microscopy8.00A1-433[»]
5VGZelectron microscopy3.70A73-155[»]
5VHFelectron microscopy5.70A73-424[»]
5VHHelectron microscopy6.10A73-424[»]
5VHIelectron microscopy6.80A73-424[»]
5VHJelectron microscopy8.50A180-424[»]
5VHMelectron microscopy8.30A159-424[»]
5VHNelectron microscopy7.30A159-424[»]
5VHOelectron microscopy8.30A158-424[»]
5VHPelectron microscopy7.90A159-424[»]
5VHQelectron microscopy8.90A159-424[»]
5VHRelectron microscopy7.70A159-424[»]
5VHSelectron microscopy8.80A73-424[»]
ProteinModelPortaliP35998
SMRiP35998
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0729 Eukaryota
COG1222 LUCA
GeneTreeiENSGT00550000074978
HOGENOMiHOG000225143
HOVERGENiHBG000109
InParanoidiP35998
KOiK03061
OMAiNKYQIHL
OrthoDBiEOG091G096W
PhylomeDBiP35998
TreeFamiTF105661

Family and domain databases

InterProiView protein in InterPro
IPR005937 26S_Psome_P45-like
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR027417 P-loop_NTPase
IPR035245 PSMC2
PANTHERiPTHR23073:SF13 PTHR23073:SF13, 1 hit
PfamiView protein in Pfam
PF00004 AAA, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01242 26Sp45, 1 hit
PROSITEiView protein in PROSITE
PS00674 AAA, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35998-1) [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
MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED
60 70 80 90 100
DIQQLLKKIN ELTGIKESDT GLAPPALWDL AADKQTLQSE QPLQVARCTK
110 120 130 140 150
IINADSEDPK YIINVKQFAK FVVDLSDQVA PTDIEEGMRV GVDRNKYQIH
160 170 180 190 200
IPLPPKIDPT VTMMQVEEKP DVTYSDVGGC KEQIEKLREV VETPLLHPER
210 220 230 240 250
FVNLGIEPPK GVLLFGPPGT GKTLCARAVA NRTDACFIRV IGSELVQKYV
260 270 280 290 300
GEGARMVREL FEMARTKKAC LIFFDEIDAI GGARFDDGAG GDNEVQRTML
310 320 330 340 350
ELINQLDGFD PRGNIKVLMA TNRPDTLDPA LMRPGRLDRK IEFSLPDLEG
360 370 380 390 400
RTHIFKIHAR SMSVERDIRF ELLARLCPNS TGAEIRSVCT EAGMFAIRAR
410 420 430
RKIATEKDFL EAVNKVIKSY AKFSATPRYM TYN
Length:433
Mass (Da):48,634
Last modified:January 23, 2007 - v3
Checksum:i85FD95F6DF7A3E84
GO
Isoform 2 (identifier: P35998-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.

Note: No experimental confirmation available.
Show »
Length:296
Mass (Da):33,274
Checksum:iFB08EBF831391C10
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15D → V in BAE45763 (PubMed:12880961).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0561781 – 137Missing in isoform 2. 1 PublicationAdd BLAST137

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11094 mRNA Translation: BAA01868.1
AB075520 mRNA Translation: BAE45763.1
AK298821 mRNA Translation: BAH12878.1
AC004668 Genomic DNA No translation available.
AC093701 Genomic DNA No translation available.
CH236947 Genomic DNA Translation: EAL24412.1
CH471070 Genomic DNA Translation: EAW83332.1
BC002589 mRNA Translation: AAH02589.1
CCDSiCCDS5731.1 [P35998-1]
PIRiS24353
RefSeqiNP_001191382.1, NM_001204453.1
NP_002794.1, NM_002803.3 [P35998-1]
UniGeneiHs.437366

Genome annotation databases

EnsembliENST00000292644; ENSP00000292644; ENSG00000161057 [P35998-1]
ENST00000435765; ENSP00000391211; ENSG00000161057 [P35998-1]
GeneIDi5701
KEGGihsa:5701
UCSCiuc003vbs.4 human [P35998-1]

Keywords - Coding sequence diversityi

Alternative splicing

Entry informationi

Entry nameiPRS7_HUMAN
AccessioniPrimary (citable) accession number: P35998
Secondary accession number(s): A4D0Q1
, B7Z5E2, Q3LIA5, Q9UDI3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 190 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 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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