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P61289

- PSME3_HUMAN

UniProt

P61289 - PSME3_HUMAN

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Protein
Proteasome activator complex subunit 3
Gene
PSME3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation.6 Publications

GO - Molecular functioni

  1. MDM2/MDM4 family protein binding Source: UniProtKB
  2. endopeptidase activator activity Source: UniProtKB
  3. p53 binding Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. RNA metabolic process Source: Reactome
  4. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  5. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  6. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  7. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  8. apoptotic process Source: Reactome
  9. cellular nitrogen compound metabolic process Source: Reactome
  10. gene expression Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. mitotic cell cycle Source: Reactome
  13. negative regulation of apoptotic process Source: Reactome
  14. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. positive regulation of endopeptidase activity Source: GOC
  17. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  18. protein polyubiquitination Source: Reactome
  19. regulation of apoptotic process Source: Reactome
  20. regulation of cellular amino acid metabolic process Source: Reactome
  21. regulation of proteasomal protein catabolic process Source: UniProtKB
  22. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  23. small molecule metabolic process Source: Reactome
  24. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome activator complex subunit 3
Alternative name(s):
11S regulator complex subunit gamma
Short name:
REG-gamma
Activator of multicatalytic protease subunit 3
Ki nuclear autoantigen
Proteasome activator 28 subunit gamma
Short name:
PA28g
Short name:
PA28gamma
Gene namesi
Name:PSME3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9570. PSME3.

Subcellular locationi

Nucleus. Cytoplasm By similarity
Note: Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase By similarity.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. proteasome activator complex Source: InterPro
  6. proteasome complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881K → E, D, A, C, N, Q, H, F, S, I or P: Assembles into less stable hexamers/heptamers and therefore impairs specificity of activation of trypsin-like subunits of the proteasome. 1 Publication

Organism-specific databases

PharmGKBiPA33916.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 254253Proteasome activator complex subunit 3
PRO_0000161789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei24 – 241Phosphoserine1 Publication
Modified residuei195 – 1951N6-acetyllysine; by P300/CBP1 Publication

Post-translational modificationi

Phosphorylated by MAP3K3 By similarity.
Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates. Deacetylated by SIRT1.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP61289.
PaxDbiP61289.
PRIDEiP61289.

PTM databases

PhosphoSiteiP61289.

Miscellaneous databases

PMAP-CutDBP61289.

Expressioni

Inductioni

Up-regulated in thyroid carcinoma cells.1 Publication

Gene expression databases

ArrayExpressiP61289.
BgeeiP61289.
CleanExiHS_PSME3.
GenevestigatoriP61289.

Organism-specific databases

HPAiCAB008388.
HPA012510.

Interactioni

Subunit structurei

Homoheptamer; the stability of the heptamer is essential for the specific activation of the trypsine-like subunit and inhibition of the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits of the proteasome. Interacts with p53/TP53 and MDM2. Interacts with MAP3K3 By similarity. Associates with the proteasome.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATN1P542593EBI-355546,EBI-945980
COILP384323EBI-355546,EBI-945751
MDM2Q009878EBI-355546,EBI-389668
NCOA3Q9Y6Q95EBI-355546,EBI-81196
SMURF1Q9HCE75EBI-355546,EBI-976466
TP53P046377EBI-355546,EBI-366083
vifP125042EBI-355546,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi115492. 71 interactions.
IntActiP61289. 39 interactions.
MINTiMINT-5002653.
STRINGi9606.ENSP00000293362.

Structurei

3D structure databases

ProteinModelPortaliP61289.
SMRiP61289. Positions 5-64, 112-246.

Family & Domainsi

Domaini

The C-terminal sequences affect heptamer stability and proteasome affinity.1 Publication

Sequence similaritiesi

Belongs to the PA28 family.

Phylogenomic databases

eggNOGiNOG236353.
HOVERGENiHBG053745.
InParanoidiP61289.
KOiK06698.
OMAiFVMPGGM.
PhylomeDBiP61289.
TreeFamiTF106236.

Family and domain databases

Gene3Di1.20.120.180. 1 hit.
1.20.5.120. 1 hit.
InterProiIPR009077. Proteasome_activ_pa28.
IPR003186. Proteasome_activ_pa28_C.
IPR003185. Proteasome_activ_pa28_N.
[Graphical view]
PANTHERiPTHR10660. PTHR10660. 1 hit.
PfamiPF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view]
SUPFAMiSSF47216. SSF47216. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61289-1) [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

MASLLKVDQE VKLKVDSFRE RITSEAEDLV ANFFPKKLLE LDSFLKEPIL    50
NIHDLTQIHS DMNLPVPDPI LLTNSHDGLD GPTYKKRRLD ECEEAFQGTK 100
VFVMPNGMLK SNQQLVDIIE KVKPEIRLLI EKCNTVKMWV QLLIPRIEDG 150
NNFGVSIQEE TVAELRTVES EAASYLDQIS RYYITRAKLV SKIAKYPHVE 200
DYRRTVTEID EKEYISLRLI ISELRNQYVT LHDMILKNIE KIKRPRSSNA 250
ETLY 254
Length:254
Mass (Da):29,506
Last modified:May 10, 2004 - v1
Checksum:i116FAB47D60A26C0
GO
Isoform 2 (identifier: P61289-2) [UniParc] [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-135: T → TPSGKGPHICFDLQ

Show »
Length:267
Mass (Da):30,887
Checksum:i76E7E6ECCC65589F
GO
Isoform 3 (identifier: P61289-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MASLLKVDQEVKL → MEKWILKKIKYLQSGGLSASYYSY

Note: No experimental confirmation. Gene prediction based on EST data.

Show »
Length:265
Mass (Da):30,890
Checksum:iEC200E4F73756C82
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313MASLL…QEVKL → MEKWILKKIKYLQSGGLSAS YYSY in isoform 3.
VSP_055047Add
BLAST
Alternative sequencei135 – 1351T → TPSGKGPHICFDLQ in isoform 2.
VSP_004516

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251E → K in AAB60335. 1 Publication
Sequence conflicti94 – 941E → K in AAA93227. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11292 mRNA. Translation: AAB60335.1.
BT019386 mRNA. Translation: AAV38193.1.
AK292618 mRNA. Translation: BAF85307.1.
AK074999 mRNA. Translation: BAG52046.1.
AC016889 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60893.1.
BC001423 mRNA. Translation: AAH01423.1.
BC002684 mRNA. Translation: AAH02684.1.
BC008020 mRNA. Translation: AAH08020.1.
U25756 Genomic DNA. Translation: AAA93227.1.
CCDSiCCDS11442.1. [P61289-2]
CCDS45689.1.
PIRiI38702. A60537.
RefSeqiNP_005780.2. NM_005789.3. [P61289-1]
NP_789839.1. NM_176863.2. [P61289-2]
UniGeneiHs.152978.

Genome annotation databases

EnsembliENST00000293362; ENSP00000293362; ENSG00000131467. [P61289-2]
ENST00000590720; ENSP00000466794; ENSG00000131467. [P61289-1]
GeneIDi10197.
KEGGihsa:10197.
UCSCiuc002ibp.3. human.
uc002ibq.4. human. [P61289-2]

Polymorphism databases

DMDMi47117724.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U11292 mRNA. Translation: AAB60335.1 .
BT019386 mRNA. Translation: AAV38193.1 .
AK292618 mRNA. Translation: BAF85307.1 .
AK074999 mRNA. Translation: BAG52046.1 .
AC016889 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60893.1 .
BC001423 mRNA. Translation: AAH01423.1 .
BC002684 mRNA. Translation: AAH02684.1 .
BC008020 mRNA. Translation: AAH08020.1 .
U25756 Genomic DNA. Translation: AAA93227.1 .
CCDSi CCDS11442.1. [P61289-2 ]
CCDS45689.1.
PIRi I38702. A60537.
RefSeqi NP_005780.2. NM_005789.3. [P61289-1 ]
NP_789839.1. NM_176863.2. [P61289-2 ]
UniGenei Hs.152978.

3D structure databases

ProteinModelPortali P61289.
SMRi P61289. Positions 5-64, 112-246.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115492. 71 interactions.
IntActi P61289. 39 interactions.
MINTi MINT-5002653.
STRINGi 9606.ENSP00000293362.

PTM databases

PhosphoSitei P61289.

Polymorphism databases

DMDMi 47117724.

Proteomic databases

MaxQBi P61289.
PaxDbi P61289.
PRIDEi P61289.

Protocols and materials databases

DNASUi 10197.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000293362 ; ENSP00000293362 ; ENSG00000131467 . [P61289-2 ]
ENST00000590720 ; ENSP00000466794 ; ENSG00000131467 . [P61289-1 ]
GeneIDi 10197.
KEGGi hsa:10197.
UCSCi uc002ibp.3. human.
uc002ibq.4. human. [P61289-2 ]

Organism-specific databases

CTDi 10197.
GeneCardsi GC17P040985.
HGNCi HGNC:9570. PSME3.
HPAi CAB008388.
HPA012510.
MIMi 605129. gene.
neXtProti NX_P61289.
PharmGKBi PA33916.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236353.
HOVERGENi HBG053745.
InParanoidi P61289.
KOi K06698.
OMAi FVMPGGM.
PhylomeDBi P61289.
TreeFami TF106236.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi PSME3. human.
GeneWikii PSME3.
GenomeRNAii 10197.
NextBioi 38592.
PMAP-CutDB P61289.
PROi P61289.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61289.
Bgeei P61289.
CleanExi HS_PSME3.
Genevestigatori P61289.

Family and domain databases

Gene3Di 1.20.120.180. 1 hit.
1.20.5.120. 1 hit.
InterProi IPR009077. Proteasome_activ_pa28.
IPR003186. Proteasome_activ_pa28_C.
IPR003185. Proteasome_activ_pa28_N.
[Graphical view ]
PANTHERi PTHR10660. PTHR10660. 1 hit.
Pfami PF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view ]
SUPFAMi SSF47216. SSF47216. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus."
    Nikaido T., Shimada K., Shibata M., Hata M., Sakamoto M., Takasaki Y., Sato C., Takahashi T., Nishida Y.
    Clin. Exp. Immunol. 79:209-214(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: B-cell and Fetal brain.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Thymus.
  5. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung, Ovary and Placenta.
  9. Bienvenut W.V., Ramsay A., Leung H.Y.
    Submitted (FEB-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12 AND 111-121, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  10. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-135.
    Tissue: Ovary.
  11. "Characterization of recombinant REGalpha, REGbeta, and REGgamma proteasome activators."
    Realini C., Jensen C.C., Zhang Z., Johnston S.C., Knowlton J.R., Hill C.P., Rechsteiner M.
    J. Biol. Chem. 272:25483-25492(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH THE PROTEASOME, CALCIUM-BINDING.
  12. "Properties of the nuclear proteasome activator PA28gamma (REGgamma)."
    Wilk S., Chen W.-E., Magnusson R.P.
    Arch. Biochem. Biophys. 383:265-271(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  13. "Subcellular localization of proteasomes and their regulatory complexes in mammalian cells."
    Brooks P., Fuertes G., Murray R.Z., Bose S., Knecht E., Rechsteiner M.C., Hendil K.B., Tanaka K., Dyson J., Rivett J.
    Biochem. J. 346:155-161(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "The proteasome activator 11 S REG or PA28: chimeras implicate carboxyl-terminal sequences in oligomerization and proteasome binding but not in the activation of specific proteasome catalytic subunits."
    Li J., Gao X., Joss L., Rechsteiner M.
    J. Mol. Biol. 299:641-654(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH THE PROTEASOME, SUBUNIT.
  15. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Site-specific acetylation of the proteasome activator REGgamma directs its heptameric structure and functions."
    Liu J., Wang Y., Li L., Zhou L., Wei H., Zhou Q., Liu J., Wang W., Ji L., Shan P., Wang Y., Yang Y., Jung S.Y., Zhang P., Wang C., Long W., Zhang B., Li X.
    J. Biol. Chem. 288:16567-16578(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-195, SUBUNIT.
  22. "Lysine 188 substitutions convert the pattern of proteasome activation by REGgamma to that of REGs alpha and beta."
    Li J., Gao X., Ortega J., Nazif T., Joss L., Bogyo M., Steven A.C., Rechsteiner M.
    EMBO J. 20:3359-3369(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY, SUBUNIT, FUNCTION, MUTAGENESIS OF LYS-188.
  23. Cited for: INDUCTION, SUBCELLULAR LOCATION.
  24. "Purification procedures determine the proteasome activation properties of REG gamma (PA28 gamma)."
    Gao X., Li J., Pratt G., Wilk S., Rechsteiner M.
    Arch. Biochem. Biophys. 425:158-164(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation."
    Zhang Z., Zhang R.
    EMBO J. 27:852-864(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53 AND MDM2.

Entry informationi

Entry nameiPSME3_HUMAN
AccessioniPrimary (citable) accession number: P61289
Secondary accession number(s): A8K9A3
, O35563, P97373, Q12920, Q13172, Q9BQD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: September 3, 2014
This is version 114 of the entry and version 1 of the sequence. [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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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