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P60900

- PSA6_HUMAN

UniProt

P60900 - PSA6_HUMAN

Protein

Proteasome subunit alpha type-6

Gene

PSMA6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

    GO - Molecular functioni

    1. endopeptidase activity Source: UniProtKB
    2. NF-kappaB binding Source: BHF-UCL
    3. protein binding Source: IntAct
    4. purine ribonucleoside triphosphate binding Source: BHF-UCL
    5. RNA binding Source: UniProtKB
    6. threonine-type endopeptidase activity Source: UniProtKB-KW

    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 ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
    15. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    16. protein polyubiquitination Source: Reactome
    17. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
    18. regulation of apoptotic process Source: Reactome
    19. regulation of cellular amino acid metabolic process Source: Reactome
    20. regulation of inflammatory response Source: BHF-UCL
    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 - Molecular functioni

    Hydrolase, Protease, Threonine protease

    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.

    Protein family/group databases

    MEROPSiT01.971.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-6 (EC:3.4.25.1)
    Alternative name(s):
    27 kDa prosomal protein
    Short name:
    PROS-27
    Short name:
    p27K
    Macropain iota chain
    Multicatalytic endopeptidase complex iota chain
    Proteasome iota chain
    Gene namesi
    Name:PSMA6
    Synonyms:PROS27
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9535. PSMA6.

    Subcellular locationi

    Cytoplasm. Nucleus. CytoplasmP-body By similarity
    Note: Colocalizes with TRIM5 in the cytoplasmic bodies.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic mRNA processing body Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. myofibril Source: BHF-UCL
    6. nuclear matrix Source: BHF-UCL
    7. nucleoplasm Source: Reactome
    8. nucleus Source: BHF-UCL
    9. polysome Source: BHF-UCL
    10. proteasome core complex Source: UniProtKB
    11. proteasome core complex, alpha-subunit complex Source: BHF-UCL
    12. sarcomere Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33880.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 246246Proteasome subunit alpha type-6PRO_0000124130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi5 – 51O-linked (GlcNAc)By similarity
    Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei102 – 1021N6-acetyllysine1 Publication
    Modified residuei104 – 1041N6-acetyllysine1 Publication
    Modified residuei159 – 1591PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP60900.
    PaxDbiP60900.
    PeptideAtlasiP60900.
    PRIDEiP60900.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00029623.
    SWISS-2DPAGEP60900.
    UCD-2DPAGEP60900.

    PTM databases

    PhosphoSiteiP60900.

    Expressioni

    Gene expression databases

    BgeeiP60900.
    CleanExiHS_PSMA6.
    GenevestigatoriP60900.

    Organism-specific databases

    HPAiHPA003049.

    Interactioni

    Subunit structurei

    The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with ALKBH4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSMA2P257875EBI-357793,EBI-603262
    PSMA3P257884EBI-357793,EBI-348380
    PSMA4P257894EBI-357793,EBI-359310
    PSMA7O1481811EBI-357793,EBI-603272
    UCHL5Q9Y5K54EBI-357793,EBI-1051183

    Protein-protein interaction databases

    BioGridi111660. 101 interactions.
    DIPiDIP-29367N.
    IntActiP60900. 29 interactions.
    MINTiMINT-5001118.
    STRINGi9606.ENSP00000261479.

    Structurei

    3D structure databases

    ProteinModelPortaliP60900.
    SMRiP60900. Positions 2-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091084.
    HOVERGENiHBG107363.
    InParanoidiP60900.
    KOiK02730.
    PhylomeDBiP60900.
    TreeFamiTF106210.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view]
    SMARTiSM00948. Proteasome_A_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P60900-1) [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

    MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI    50
    VTQKKVPDKL LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN 100
    WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ 150
    VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT 200
    CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD 246
    Length:246
    Mass (Da):27,399
    Last modified:April 13, 2004 - v1
    Checksum:i94D1FD3C0A7CC72A
    GO
    Isoform 2 (identifier: P60900-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MSRGSSAGFDRHITIFSPEGRLYQV → MAGLRR

    Note: No experimental confirmation available.

    Show »
    Length:227
    Mass (Da):25,290
    Checksum:i436E2FE91E1BCDE8
    GO
    Isoform 3 (identifier: P60900-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:167
    Mass (Da):18,816
    Checksum:iF46774830B65E327
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591K → C in CAA43964. (PubMed:1888762)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti233 – 2331A → S.
    Corresponds to variant rs15434 [ dbSNP | Ensembl ].
    VAR_051546

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7979Missing in isoform 3. 1 PublicationVSP_054586Add
    BLAST
    Alternative sequencei1 – 2525MSRGS…RLYQV → MAGLRR in isoform 2. 1 PublicationVSP_054587Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59417 mRNA. Translation: CAA42052.1.
    CR456944 mRNA. Translation: CAG33225.1.
    AK298920 mRNA. Translation: BAG61026.1.
    AK302008 mRNA. Translation: BAG63411.1.
    AK313011 mRNA. Translation: BAG35846.1.
    AK316223 mRNA. Translation: BAH14594.1.
    AL121594 Genomic DNA. No translation available.
    AL133163 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW65876.1.
    CH471078 Genomic DNA. Translation: EAW65877.1.
    BC002979 mRNA. Translation: AAH02979.1.
    BC017882 mRNA. Translation: AAH17882.1.
    BC022354 mRNA. Translation: AAH22354.1.
    BC023659 mRNA. Translation: AAH23659.1.
    BC070137 mRNA. Translation: AAH70137.1.
    X61972 mRNA. Translation: CAA43964.1.
    CCDSiCCDS61437.1. [P60900-2]
    CCDS61438.1. [P60900-3]
    CCDS9655.1. [P60900-1]
    PIRiS30274.
    RefSeqiNP_001269161.1. NM_001282232.1. [P60900-3]
    NP_001269162.1. NM_001282233.1. [P60900-3]
    NP_001269163.1. NM_001282234.1. [P60900-2]
    NP_002782.1. NM_002791.2. [P60900-1]
    UniGeneiHs.446260.

    Genome annotation databases

    EnsembliENST00000261479; ENSP00000261479; ENSG00000100902. [P60900-1]
    ENST00000540871; ENSP00000444844; ENSG00000100902. [P60900-2]
    ENST00000555764; ENSP00000452566; ENSG00000100902. [P60900-3]
    GeneIDi5687.
    KEGGihsa:5687.
    UCSCiuc001wtd.3. human. [P60900-1]

    Polymorphism databases

    DMDMi46397659.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59417 mRNA. Translation: CAA42052.1 .
    CR456944 mRNA. Translation: CAG33225.1 .
    AK298920 mRNA. Translation: BAG61026.1 .
    AK302008 mRNA. Translation: BAG63411.1 .
    AK313011 mRNA. Translation: BAG35846.1 .
    AK316223 mRNA. Translation: BAH14594.1 .
    AL121594 Genomic DNA. No translation available.
    AL133163 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW65876.1 .
    CH471078 Genomic DNA. Translation: EAW65877.1 .
    BC002979 mRNA. Translation: AAH02979.1 .
    BC017882 mRNA. Translation: AAH17882.1 .
    BC022354 mRNA. Translation: AAH22354.1 .
    BC023659 mRNA. Translation: AAH23659.1 .
    BC070137 mRNA. Translation: AAH70137.1 .
    X61972 mRNA. Translation: CAA43964.1 .
    CCDSi CCDS61437.1. [P60900-2 ]
    CCDS61438.1. [P60900-3 ]
    CCDS9655.1. [P60900-1 ]
    PIRi S30274.
    RefSeqi NP_001269161.1. NM_001282232.1. [P60900-3 ]
    NP_001269162.1. NM_001282233.1. [P60900-3 ]
    NP_001269163.1. NM_001282234.1. [P60900-2 ]
    NP_002782.1. NM_002791.2. [P60900-1 ]
    UniGenei Hs.446260.

    3D structure databases

    ProteinModelPortali P60900.
    SMRi P60900. Positions 2-245.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111660. 101 interactions.
    DIPi DIP-29367N.
    IntActi P60900. 29 interactions.
    MINTi MINT-5001118.
    STRINGi 9606.ENSP00000261479.

    Chemistry

    ChEMBLi CHEMBL2364701.

    Protein family/group databases

    MEROPSi T01.971.

    PTM databases

    PhosphoSitei P60900.

    Polymorphism databases

    DMDMi 46397659.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00029623.
    SWISS-2DPAGE P60900.
    UCD-2DPAGE P60900.

    Proteomic databases

    MaxQBi P60900.
    PaxDbi P60900.
    PeptideAtlasi P60900.
    PRIDEi P60900.

    Protocols and materials databases

    DNASUi 5687.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261479 ; ENSP00000261479 ; ENSG00000100902 . [P60900-1 ]
    ENST00000540871 ; ENSP00000444844 ; ENSG00000100902 . [P60900-2 ]
    ENST00000555764 ; ENSP00000452566 ; ENSG00000100902 . [P60900-3 ]
    GeneIDi 5687.
    KEGGi hsa:5687.
    UCSCi uc001wtd.3. human. [P60900-1 ]

    Organism-specific databases

    CTDi 5687.
    GeneCardsi GC14P035747.
    HGNCi HGNC:9535. PSMA6.
    HPAi HPA003049.
    MIMi 602855. gene.
    neXtProti NX_P60900.
    PharmGKBi PA33880.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091084.
    HOVERGENi HBG107363.
    InParanoidi P60900.
    KOi K02730.
    PhylomeDBi P60900.
    TreeFami TF106210.

    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

    GeneWikii PSMA6.
    GenomeRNAii 5687.
    NextBioi 22090.
    PROi P60900.
    SOURCEi Search...

    Gene expression databases

    Bgeei P60900.
    CleanExi HS_PSMA6.
    Genevestigatori P60900.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SMARTi SM00948. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The prosomal RNA-binding protein p27K is a member of the alpha-type human prosomal gene family."
      Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R., Nothwang H.G., Dutrillaux B., Scherrer K.
      Mol. Gen. Genet. 237:193-205(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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; 2 AND 3).
      Tissue: Cerebellum and Testis.
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain, Lymph, Skeletal muscle and Skin.
    7. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 12-43; 60-88; 105-116; 154-164; 172-181 AND 229-246, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    8. "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous."
      DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., Dawson P.A., Slaughter C.A.
      Biochim. Biophys. Acta 1079:29-38(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-246 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    9. "Human proteasome subunits from 2-dimensional gels identified by partial sequencing."
      Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.
      Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    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. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-59.
      Tissue: Mammary cancer.
    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-102 AND LYS-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Human ALKBH4 interacts with proteins associated with transcription."
      Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
      PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALKBH4.

    Entry informationi

    Entry nameiPSA6_HUMAN
    AccessioniPrimary (citable) accession number: P60900
    Secondary accession number(s): B2R7J9
    , B4DQR4, B4DXJ9, P34062, Q6IB60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 125 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 14
      Human chromosome 14: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3