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P55036

- PSMD4_HUMAN

UniProt

P55036 - PSMD4_HUMAN

Protein

26S proteasome non-ATPase regulatory subunit 4

Gene

PSMD4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Binds and presumably selects ubiquitin-conjugates for destruction. Displays selectivity for longer polyubiquitin chains. Modulates intestinal fluid secretion.

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. poly(A) RNA binding Source: UniProtKB
    3. 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 ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    15. protein polyubiquitination Source: Reactome
    16. regulation of apoptotic process Source: Reactome
    17. regulation of cellular amino acid metabolic process Source: Reactome
    18. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    19. RNA metabolic process Source: Reactome
    20. small molecule metabolic process Source: Reactome
    21. viral process Source: Reactome

    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 proteasome non-ATPase regulatory subunit 4
    Alternative name(s):
    26S proteasome regulatory subunit RPN10
    26S proteasome regulatory subunit S5A
    Antisecretory factor 1
    Short name:
    AF
    Short name:
    ASF
    Multiubiquitin chain-binding protein
    Gene namesi
    Name:PSMD4
    Synonyms:MCB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9561. PSMD4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA
    5. proteasome accessory complex Source: UniProtKB
    6. proteasome complex Source: ProtInc
    7. proteasome regulatory particle, base subcomplex Source: InterPro

    Keywords - Cellular componenti

    Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33907.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 37737726S proteasome non-ATPase regulatory subunit 4PRO_0000173828Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei250 – 2501PhosphothreonineBy similarity
    Modified residuei266 – 2661Phosphoserine4 Publications
    Modified residuei358 – 3581Phosphoserine1 Publication
    Modified residuei361 – 3611Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP55036.
    PaxDbiP55036.
    PRIDEiP55036.

    PTM databases

    PhosphoSiteiP55036.

    Expressioni

    Gene expression databases

    ArrayExpressiP55036.
    BgeeiP55036.
    CleanExiHS_PSMD4.
    GenevestigatoriP55036.

    Organism-specific databases

    HPAiCAB047300.
    HPA038807.
    HPA039252.

    Interactioni

    Subunit structurei

    The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively. Directly interacts with NUB1. Interacts with SQSTM1. Interacts with UBQLN4. Interacts with UBE3A.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-359318,EBI-359318
    ADRM1Q161862EBI-359318,EBI-954387
    DSK2P485102EBI-359318,EBI-6174From a different organism.
    DSK2BQ9SII83EBI-359318,EBI-4433040From a different organism.
    Pax3P246103EBI-359318,EBI-1208116From a different organism.
    PSMD2Q132003EBI-359318,EBI-357648
    RAD23AP547253EBI-359318,EBI-746453
    RAD23AQ84L323EBI-359318,EBI-6394924From a different organism.
    RAD23BP5472712EBI-359318,EBI-954531
    Rbck1Q629213EBI-359318,EBI-7266339From a different organism.
    SCHIP1Q9P0W52EBI-359318,EBI-1397509
    UBCP0CG488EBI-359318,EBI-3390054
    UBQLN1Q9UMX06EBI-359318,EBI-741480
    UBQLN2Q9UHD93EBI-359318,EBI-947187
    UCHL5Q9Y5K55EBI-359318,EBI-1051183

    Protein-protein interaction databases

    BioGridi111683. 285 interactions.
    DIPiDIP-38189N.
    IntActiP55036. 60 interactions.
    MINTiMINT-105366.
    STRINGi9606.ENSP00000357879.

    Structurei

    Secondary structure

    1
    377
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi201 – 2033
    Beta strandi205 – 2084
    Helixi210 – 2123
    Helixi214 – 24431
    Beta strandi245 – 2495
    Beta strandi268 – 2703
    Beta strandi273 – 2753
    Helixi278 – 29417
    Beta strandi296 – 3005
    Beta strandi302 – 3043

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P9CNMR-A263-307[»]
    1P9DNMR-S263-307[»]
    1UELNMR-B263-307[»]
    1YX4NMR-A196-306[»]
    1YX5NMR-A192-306[»]
    1YX6NMR-A196-306[»]
    2KDENMR-A196-306[»]
    2KDFNMR-A196-306[»]
    ProteinModelPortaliP55036.
    SMRiP55036. Positions 1-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55036.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 188184VWFAPROSITE-ProRule annotationAdd
    BLAST
    Repeati211 – 23020UIM 1Add
    BLAST
    Repeati282 – 30120UIM 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni216 – 2205Essential for ubiquitin-binding
    Regioni287 – 2915Essential for ubiquitin-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi238 – 2469Poly-Ala

    Domaini

    The 2 UIM motifs are involved in the binding to a multi-ubiquitin chain in a cooperative way.

    Sequence similaritiesi

    Belongs to the proteasome subunit S5A family.Curated
    Contains 2 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5148.
    HOGENOMiHOG000165630.
    HOVERGENiHBG000425.
    KOiK03029.
    OrthoDBiEOG70W3DM.
    PhylomeDBiP55036.
    TreeFamiTF106232.

    Family and domain databases

    Gene3Di3.40.50.410. 1 hit.
    InterProiIPR027040. Proteasome_su_Rpn10.
    IPR003903. Ubiquitin-int_motif.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR10223. PTHR10223. 1 hit.
    PfamiPF02809. UIM. 2 hits.
    [Graphical view]
    SMARTiSM00726. UIM. 2 hits.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    PROSITEiPS50330. UIM. 2 hits.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform Rpn10A (identifier: P55036-1) [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

    MVLESTMVCV DNSEYMRNGD FLPTRLQAQQ DAVNIVCHSK TRSNPENNVG    50
    LITLANDCEV LTTLTPDTGR ILSKLHTVQP KGKITFCTGI RVAHLALKHR 100
    QGKNHKMRII AFVGSPVEDN EKDLVKLAKR LKKEKVNVDI INFGEEEVNT 150
    EKLTAFVNTL NGKDGTGSHL VTVPPGPSLA DALISSPILA GEGGAMLGLG 200
    ASDFEFGVDP SADPELALAL RVSMEEQRQR QEEEARRAAA ASAAEAGIAT 250
    TGTEDSDDAL LKMTISQQEF GRTGLPDLSS MTEEEQIAYA MQMSLQGAEF 300
    GQAESADIDA SSAMDTSEPA KEEDDYDVMQ DPEFLQSVLE NLPGVDPNNE 350
    AIRNAMGSLA SQATKDGKKD KKEEDKK 377
    Length:377
    Mass (Da):40,737
    Last modified:October 1, 1996 - v1
    Checksum:iEC712EC4DB1CE9AB
    GO
    Isoform Rpn10E (identifier: P55036-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         255-268: DSDDALLKMTISQQ → GERGGIRSPGTAGC
         269-377: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:268
    Mass (Da):28,612
    Checksum:i6640BF4CD5C91C6E
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei255 – 26814DSDDA…TISQQ → GERGGIRSPGTAGC in isoform Rpn10E. CuratedVSP_005291Add
    BLAST
    Alternative sequencei269 – 377109Missing in isoform Rpn10E. CuratedVSP_005292Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51007 mRNA. Translation: AAC50433.1.
    U24704 mRNA. Translation: AAB54057.1.
    AB033605 mRNA. Translation: BAA97581.1.
    AL391069, AL592424 Genomic DNA. Translation: CAH70329.1.
    AL592424, AL391069 Genomic DNA. Translation: CAI16390.1.
    CH471121 Genomic DNA. Translation: EAW53457.1.
    CH471121 Genomic DNA. Translation: EAW53458.1.
    BC002365 mRNA. Translation: AAH02365.1.
    BC072008 mRNA. Translation: AAH72008.1.
    U72664 mRNA. Translation: AAB68598.1.
    CCDSiCCDS991.1. [P55036-1]
    PIRiS63671.
    RefSeqiNP_002801.1. NM_002810.2. [P55036-1]
    UniGeneiHs.505059.

    Genome annotation databases

    EnsembliENST00000368884; ENSP00000357879; ENSG00000159352. [P55036-1]
    GeneIDi5710.
    KEGGihsa:5710.
    UCSCiuc001exl.3. human. [P55036-1]

    Polymorphism databases

    DMDMi1709796.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51007 mRNA. Translation: AAC50433.1 .
    U24704 mRNA. Translation: AAB54057.1 .
    AB033605 mRNA. Translation: BAA97581.1 .
    AL391069 , AL592424 Genomic DNA. Translation: CAH70329.1 .
    AL592424 , AL391069 Genomic DNA. Translation: CAI16390.1 .
    CH471121 Genomic DNA. Translation: EAW53457.1 .
    CH471121 Genomic DNA. Translation: EAW53458.1 .
    BC002365 mRNA. Translation: AAH02365.1 .
    BC072008 mRNA. Translation: AAH72008.1 .
    U72664 mRNA. Translation: AAB68598.1 .
    CCDSi CCDS991.1. [P55036-1 ]
    PIRi S63671.
    RefSeqi NP_002801.1. NM_002810.2. [P55036-1 ]
    UniGenei Hs.505059.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P9C NMR - A 263-307 [» ]
    1P9D NMR - S 263-307 [» ]
    1UEL NMR - B 263-307 [» ]
    1YX4 NMR - A 196-306 [» ]
    1YX5 NMR - A 192-306 [» ]
    1YX6 NMR - A 196-306 [» ]
    2KDE NMR - A 196-306 [» ]
    2KDF NMR - A 196-306 [» ]
    ProteinModelPortali P55036.
    SMRi P55036. Positions 1-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111683. 285 interactions.
    DIPi DIP-38189N.
    IntActi P55036. 60 interactions.
    MINTi MINT-105366.
    STRINGi 9606.ENSP00000357879.

    PTM databases

    PhosphoSitei P55036.

    Polymorphism databases

    DMDMi 1709796.

    Proteomic databases

    MaxQBi P55036.
    PaxDbi P55036.
    PRIDEi P55036.

    Protocols and materials databases

    DNASUi 5710.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368884 ; ENSP00000357879 ; ENSG00000159352 . [P55036-1 ]
    GeneIDi 5710.
    KEGGi hsa:5710.
    UCSCi uc001exl.3. human. [P55036-1 ]

    Organism-specific databases

    CTDi 5710.
    GeneCardsi GC01P151227.
    HGNCi HGNC:9561. PSMD4.
    HPAi CAB047300.
    HPA038807.
    HPA039252.
    MIMi 601648. gene.
    neXtProti NX_P55036.
    PharmGKBi PA33907.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5148.
    HOGENOMi HOG000165630.
    HOVERGENi HBG000425.
    KOi K03029.
    OrthoDBi EOG70W3DM.
    PhylomeDBi P55036.
    TreeFami TF106232.

    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 PSMD4. human.
    EvolutionaryTracei P55036.
    GeneWikii PSMD4.
    GenomeRNAii 5710.
    NextBioi 22186.
    PROi P55036.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55036.
    Bgeei P55036.
    CleanExi HS_PSMD4.
    Genevestigatori P55036.

    Family and domain databases

    Gene3Di 3.40.50.410. 1 hit.
    InterProi IPR027040. Proteasome_su_Rpn10.
    IPR003903. Ubiquitin-int_motif.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR10223. PTHR10223. 1 hit.
    Pfami PF02809. UIM. 2 hits.
    [Graphical view ]
    SMARTi SM00726. UIM. 2 hits.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    PROSITEi PS50330. UIM. 2 hits.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of a pituitary gland protein modulating intestinal fluid secretion."
      Johansson E., Loennroth I., Lange S., Jonson I., Jennische E., Loennroth C.
      J. Biol. Chem. 270:20615-20620(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 63-75 AND 130-140.
      Tissue: Pituitary.
    2. Loennroth I.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease."
      Ferrell K., Deveraux Q., van Nocker S., Rechsteiner M.
      FEBS Lett. 381:143-148(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    4. "Developmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomes."
      Kawahara H., Kasahara M., Nishiyama A., Ohsumi K., Goto T., Kishimoto T., Saeki Y., Yokosawa H., Shimbara N., Murata S., Chiba T., Suzuki K., Tanaka K.
      EMBO J. 19:4144-4153(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Tissue: Fetal brain.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Liver and Lung.
    8. "Proteolysis of presenilin 1 is associated with the 26S proteasome and is altered in Alzheimer's disease."
      Fraser P.E., Levesque G., Rogaeva E.A., Yu G., St George-Hyslop P.H.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 70-377.
      Tissue: Brain.
    9. "Purification and characterization of the antisecretory factor: a protein in the central nervous system and in the gut which inhibits intestinal hypersecretion induced by cholera toxin."
      Loennroth I., Lange S.
      Biochim. Biophys. Acta 883:138-144(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a."
      Young P., Deveraux Q., Beal R.E., Pickart C.M., Rechsteiner M.
      J. Biol. Chem. 273:5461-5467(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYUBIQUITIN BINDING SITES.
    11. "Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1."
      Kamitani T., Kito K., Fukuda-Kamitani T., Yeh E.T.H.
      J. Biol. Chem. 276:46655-46660(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUB1.
    12. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    13. "The effects of the polyglutamine repeat protein ataxin-1 on the UbL-UBA protein A1Up."
      Riley B.E., Xu Y., Zoghbi H.Y., Orr H.T.
      J. Biol. Chem. 279:42290-42301(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBQLN4.
    14. "Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation."
      Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., Wooten M.W.
      Mol. Cell. Biol. 24:8055-8068(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SQSTM1.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes."
      Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M., Harper J.W., Howley P.M.
      Mol. Cell. Biol. 32:3095-3106(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE3A.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Structural determinants for the binding of ubiquitin-like domains to the proteasome."
      Mueller T.D., Feigon J.
      EMBO J. 22:4634-4645(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 263-306 IN COMPLEX WITH HR23A UBIQUITIN-LIKE DOMAIN.
    24. "Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B."
      Fujiwara K., Tenno T., Sugasawa K., Jee J.-G., Ohki I., Kojima C., Tochio H., Hiroaki H., Hanaoka F., Shirakawa M.
      J. Biol. Chem. 279:4760-4767(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 260-307 IN COMPLEX WITH HR23B UBIQUITIN-LIKE DOMAIN.

    Entry informationi

    Entry nameiPSMD4_HUMAN
    AccessioniPrimary (citable) accession number: P55036
    Secondary accession number(s): D3DV16, Q5VWC5, Q9NS92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 149 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3