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P62195

- PRS8_HUMAN

UniProt

P62195 - PRS8_HUMAN

Protein

26S protease regulatory subunit 8

Gene

PSMC5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (21 Jun 2004)
      Previous versions | rss
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    Functioni

    The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi190 – 1978ATPSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. thyrotropin-releasing hormone receptor binding Source: UniProtKB
    5. transcription cofactor activity Source: ProtInc
    6. transcription factor binding Source: UniProtKB

    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 programmed cell death Source: UniProtKB
    14. negative regulation of transcription, DNA-templated Source: Ensembl
    15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    16. positive regulation of inclusion body assembly Source: Ensembl
    17. positive regulation of transcription, DNA-templated Source: UniProtKB
    18. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    19. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    20. protein polyubiquitination Source: Reactome
    21. regulation of apoptotic process Source: Reactome
    22. regulation of cellular amino acid metabolic process Source: Reactome
    23. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    24. RNA metabolic process Source: Reactome
    25. small molecule metabolic process Source: Reactome
    26. transcription from RNA polymerase II promoter Source: ProtInc
    27. viral process Source: Reactome

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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:
    26S protease regulatory subunit 8
    Alternative name(s):
    26S proteasome AAA-ATPase subunit RPT6
    Proteasome 26S subunit ATPase 5
    Proteasome subunit p45
    Thyroid hormone receptor-interacting protein 1
    Short name:
    TRIP1
    p45/SUG
    Gene namesi
    Name:PSMC5
    Synonyms:SUG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9552. PSMC5.

    Subcellular locationi

    Cytoplasm Curated. Nucleus Curated

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic vesicle Source: UniProtKB
    4. cytosol Source: Reactome
    5. cytosolic proteasome complex Source: Ensembl
    6. extracellular vesicular exosome Source: UniProt
    7. inclusion body Source: Ensembl
    8. membrane Source: UniProtKB
    9. nuclear proteasome complex Source: Ensembl
    10. nucleoplasm Source: Reactome
    11. nucleus Source: UniProtKB
    12. proteasome accessory complex Source: UniProtKB
    13. proteasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33897.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 40640526S protease regulatory subunit 8PRO_0000084721Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei222 – 2221N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP62195.
    PaxDbiP62195.
    PRIDEiP62195.

    PTM databases

    PhosphoSiteiP62195.

    Expressioni

    Gene expression databases

    ArrayExpressiP62195.
    BgeeiP62195.
    CleanExiHS_PSMC5.
    GenevestigatoriP62195.

    Organism-specific databases

    HPAiHPA017871.

    Interactioni

    Subunit structurei

    Interacts, in vitro, with the thyroid hormone receptor (in a thyroid hormone T3-dependent manner) and with retinoid X receptor (RXR) By similarity. Interacts with NDC80. Interacts with PAAF1. Interacts with TRIM5. Component of a complex with USP49 and RUVBL1.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P03255-12EBI-357745,EBI-6692439From a different organism.
    Camk2aP112754EBI-357745,EBI-2640645From a different organism.
    Camk2bP084133EBI-357745,EBI-916155From a different organism.
    ERCC3P194474EBI-357745,EBI-1183307
    PAAF1Q9BRP42EBI-357745,EBI-1056358
    PLEKHO1Q53GL09EBI-357745,EBI-949945
    PSMC2P3599810EBI-357745,EBI-359710
    PSMC4P4368611EBI-357745,EBI-743997
    PSMC6P623338EBI-357745,EBI-357669
    PSMD2Q132009EBI-357745,EBI-357648

    Protein-protein interaction databases

    BioGridi111678. 128 interactions.
    IntActiP62195. 42 interactions.
    MINTiMINT-5004394.
    STRINGi9606.ENSP00000310572.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi322 – 33312
    Beta strandi336 – 3383
    Helixi344 – 3496
    Helixi356 – 37217
    Beta strandi376 – 3783
    Helixi380 – 39112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KRKNMR-A320-395[»]
    3KW6X-ray2.10A318-395[»]
    ProteinModelPortaliP62195.
    SMRiP62195. Positions 27-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62195.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Curated

    Phylogenomic databases

    eggNOGiCOG1222.
    HOVERGENiHBG000109.
    InParanoidiP62195.
    KOiK03066.
    OMAiVMGTKKV.
    PhylomeDBiP62195.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR005937. 26S_Psome_P45.
    IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
    PROSITEiPS00674. AAA. 1 hit.
    [Graphical view]

    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. Align

    Isoform 1 (identifier: P62195-1) [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

    MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN    50
    ELNAKVRLLR EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD 100
    KNIDINDVTP NCRVALRNDS YTLHKILPNK VDPLVSLMMV EKVPDSTYEM 150
    IGGLDKQIKE IKEVIELPVK HPELFEALGI AQPKGVLLYG PPGTGKTLLA 200
    RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE HAPSIIFMDE 250
    IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI 300
    LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL 350
    MPGASGAEVK GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS 400
    IKKLWK 406
    Length:406
    Mass (Da):45,626
    Last modified:June 21, 2004 - v1
    Checksum:i29C6410C4A85A7F7
    GO
    Isoform 2 (identifier: P62195-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: Missing.

    Show »
    Length:398
    Mass (Da):44,784
    Checksum:i450BB51DA8C9381D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611E → R in BAA07919. (PubMed:7729537)Curated
    Sequence conflicti127 – 1282LP → ML in AAB88187. (PubMed:9110174)Curated
    Sequence conflicti266 – 2661D → S in AAC41735. (PubMed:7776974)Curated
    Sequence conflicti272 – 2721T → Q in AAC41735. (PubMed:7776974)Curated
    Sequence conflicti300 – 3001I → M in AAC41735. (PubMed:7776974)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035901
    Natural varianti258 – 2581R → W.
    Corresponds to variant rs11543211 [ dbSNP | Ensembl ].
    VAR_048119

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 88Missing in isoform 2. 1 PublicationVSP_045441

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D44467 mRNA. Translation: BAA07919.1.
    L38810 mRNA. Translation: AAC41735.1.
    AK290758 mRNA. Translation: BAF83447.1.
    AK291878 mRNA. Translation: BAF84567.1.
    AC015651 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94270.1.
    CH471109 Genomic DNA. Translation: EAW94271.1.
    CH471109 Genomic DNA. Translation: EAW94272.1.
    BC001932 mRNA. Translation: AAH01932.1.
    BC002367 mRNA. Translation: AAH02367.3.
    AF035309 mRNA. Translation: AAB88187.1.
    CCDSiCCDS11645.1. [P62195-1]
    CCDS56043.1. [P62195-2]
    PIRiS60343.
    S65536.
    RefSeqiNP_001186092.1. NM_001199163.1. [P62195-2]
    NP_002796.4. NM_002805.5. [P62195-1]
    UniGeneiHs.79387.

    Genome annotation databases

    EnsembliENST00000310144; ENSP00000310572; ENSG00000087191. [P62195-1]
    ENST00000375812; ENSP00000364970; ENSG00000087191. [P62195-2]
    ENST00000580864; ENSP00000462495; ENSG00000087191. [P62195-2]
    ENST00000581882; ENSP00000463938; ENSG00000087191. [P62195-2]
    GeneIDi5705.
    KEGGihsa:5705.
    UCSCiuc002jcb.3. human. [P62195-1]

    Polymorphism databases

    DMDMi49065819.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D44467 mRNA. Translation: BAA07919.1 .
    L38810 mRNA. Translation: AAC41735.1 .
    AK290758 mRNA. Translation: BAF83447.1 .
    AK291878 mRNA. Translation: BAF84567.1 .
    AC015651 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94270.1 .
    CH471109 Genomic DNA. Translation: EAW94271.1 .
    CH471109 Genomic DNA. Translation: EAW94272.1 .
    BC001932 mRNA. Translation: AAH01932.1 .
    BC002367 mRNA. Translation: AAH02367.3 .
    AF035309 mRNA. Translation: AAB88187.1 .
    CCDSi CCDS11645.1. [P62195-1 ]
    CCDS56043.1. [P62195-2 ]
    PIRi S60343.
    S65536.
    RefSeqi NP_001186092.1. NM_001199163.1. [P62195-2 ]
    NP_002796.4. NM_002805.5. [P62195-1 ]
    UniGenei Hs.79387.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KRK NMR - A 320-395 [» ]
    3KW6 X-ray 2.10 A 318-395 [» ]
    ProteinModelPortali P62195.
    SMRi P62195. Positions 27-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111678. 128 interactions.
    IntActi P62195. 42 interactions.
    MINTi MINT-5004394.
    STRINGi 9606.ENSP00000310572.

    PTM databases

    PhosphoSitei P62195.

    Polymorphism databases

    DMDMi 49065819.

    Proteomic databases

    MaxQBi P62195.
    PaxDbi P62195.
    PRIDEi P62195.

    Protocols and materials databases

    DNASUi 5705.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310144 ; ENSP00000310572 ; ENSG00000087191 . [P62195-1 ]
    ENST00000375812 ; ENSP00000364970 ; ENSG00000087191 . [P62195-2 ]
    ENST00000580864 ; ENSP00000462495 ; ENSG00000087191 . [P62195-2 ]
    ENST00000581882 ; ENSP00000463938 ; ENSG00000087191 . [P62195-2 ]
    GeneIDi 5705.
    KEGGi hsa:5705.
    UCSCi uc002jcb.3. human. [P62195-1 ]

    Organism-specific databases

    CTDi 5705.
    GeneCardsi GC17P061904.
    HGNCi HGNC:9552. PSMC5.
    HPAi HPA017871.
    MIMi 601681. gene.
    neXtProti NX_P62195.
    PharmGKBi PA33897.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1222.
    HOVERGENi HBG000109.
    InParanoidi P62195.
    KOi K03066.
    OMAi VMGTKKV.
    PhylomeDBi P62195.

    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 PSMC5. human.
    EvolutionaryTracei P62195.
    GeneWikii PSMC5.
    GenomeRNAii 5705.
    NextBioi 22166.
    PROi P62195.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62195.
    Bgeei P62195.
    CleanExi HS_PSMC5.
    Genevestigatori P62195.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR005937. 26S_Psome_P45.
    IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01242. 26Sp45. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of a new putative ATPase subunit p45 of the human 26S proteasome, a homolog of yeast transcriptional factor Sug1p."
      Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N., Slaughter C.A., Noda C., Tanaka K.
      FEBS Lett. 363:151-156(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Hepatoma.
    2. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
      Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
      Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Skeletal muscle.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 carcinoma.
    6. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-406.
      Tissue: Brain.
    7. "HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins."
      Chen Y., Sharp Z.D., Lee W.-H.
      J. Biol. Chem. 272:24081-24087(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDC80.
    8. "Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins."
      Zheng L., Chen Y., Lee W.-H.
      Mol. Cell. Biol. 19:5417-5428(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDC80.
    9. "Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases."
      Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.
      Mol. Cell. Biol. 25:3842-3853(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAAF1.
    10. "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.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
      Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
      Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM5.
    15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."
      Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S., Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M., Giles K.E., Ma L., Wang H.
      Genes Dev. 27:1581-1595(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH USP49 AND RUVBL1.
    18. "Crystal structure of a domain of 26s proteasome regulatory subunit 8 from Homo sapiens. Northeast structural genomics consortium target ID HR3102A."
      Northeast structural genomics consortium (NESG)
      Submitted (JAN-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 318-395, STRUCTURE BY NMR OF 320-395.
    19. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-60.

    Entry informationi

    Entry nameiPRS8_HUMAN
    AccessioniPrimary (citable) accession number: P62195
    Secondary accession number(s): A8K3Z3
    , A8K763, O35051, O43208, P47210, P52915, P52916
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2004
    Last sequence update: June 21, 2004
    Last modified: October 1, 2014
    This is version 113 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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

    External Data

    Dasty 3