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P61289

- PSME3_HUMAN

UniProt

P61289 - PSME3_HUMAN

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
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (10 May 2004)
      Previous versions | rss
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    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. endopeptidase activator activity Source: UniProtKB
    2. MDM2/MDM4 family protein binding Source: UniProtKB
    3. p53 binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

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

    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 2 Publications. 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

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProt
    6. proteasome activator complex Source: InterPro
    7. proteasome complex Source: ProtInc

    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 – 11Removed2 Publications
    Chaini2 – 254253Proteasome activator complex subunit 3PRO_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 SIRT1.3 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.By similarity6 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. 73 interactions.
    IntActiP61289. 39 interactions.
    MINTiMINT-5002653.
    STRINGi9606.ENSP00000293362.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Belongs to the PA28 family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251E → K in AAB60335. (PubMed:7951316)Curated
    Sequence conflicti94 – 941E → K in AAA93227. (PubMed:7545954)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313MASLL…QEVKL → MEKWILKKIKYLQSGGLSAS YYSY in isoform 3. CuratedVSP_055047Add
    BLAST
    Alternative sequencei135 – 1351T → TPSGKGPHICFDLQ in isoform 2. 1 PublicationVSP_004516

    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.
    CCDS59290.1. [P61289-3]
    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]
    ENST00000441946; ENSP00000409487; ENSG00000131467. [P61289-3]
    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.
    CCDS59290.1. [P61289-3 ]
    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. 73 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 ]
    ENST00000441946 ; ENSP00000409487 ; ENSG00000131467 . [P61289-3 ]
    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

    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: October 1, 2014
    This is version 115 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