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Q9UMX0

- UBQL1_HUMAN

UniProt

Q9UMX0 - UBQL1_HUMAN

Protein

Ubiquilin-1

Gene

UBQLN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors. Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation.

    GO - Molecular functioni

    1. kinase binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to hypoxia Source: BHF-UCL
    2. regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
    3. regulation of protein ubiquitination Source: HGNC
    4. response to endoplasmic reticulum stress Source: BHF-UCL

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquilin-1
    Alternative name(s):
    Protein linking IAP with cytoskeleton 1
    Short name:
    PLIC-1
    Short name:
    hPLIC-1
    Gene namesi
    Name:UBQLN1
    Synonyms:DA41, PLIC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12508. UBQLN1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Detected in neuronal processes and at synapses By similarity. Detected in cytosolic puncta that may correspond to autophagosomes.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum Source: HGNC
    3. nucleus Source: HPA
    4. perinuclear region of cytoplasm Source: UniProtKB
    5. proteasome complex Source: UniProtKB-KW
    6. protein complex Source: LIFEdb

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37155.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 589588Ubiquilin-1PRO_0000211008Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications

    Post-translational modificationi

    Phosphorylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UMX0.
    PaxDbiQ9UMX0.
    PRIDEiQ9UMX0.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00071180.

    PTM databases

    PhosphoSiteiQ9UMX0.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed throughout the brain; detected in neurons and in neuropathological lesions, such as neurofibrillary tangles and Lewy bodies. Highly expressed in heart, placenta, pancreas, lung, liver, skeletal muscle and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ9UMX0.
    BgeeiQ9UMX0.
    CleanExiHS_UBQLN1.
    GenevestigatoriQ9UMX0.

    Organism-specific databases

    HPAiCAB037256.
    HPA054143.

    Interactioni

    Subunit structurei

    Binds CD47, NBL1, GABRA1, GABRA2, GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3. Binds UBE3A, BTRC, P4HB, MTOR, PSEN1 and PSEN2. Interacts with the proteasome 19S subunit. Interacts (via ubiquitin-like domain) with TREX1; the interaction is direct and may control TREX1 subcellular location.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADRM1Q161864EBI-741480,EBI-954387
    EPS15P425665EBI-741480,EBI-396684
    PSMD4P550366EBI-741480,EBI-359318
    RIC8AQ9NPQ83EBI-741480,EBI-717509
    SERPINI2O758303EBI-741480,EBI-750144
    UBCP0CG483EBI-741480,EBI-3390054
    UBQLN4Q9NRR58EBI-741480,EBI-711226

    Protein-protein interaction databases

    BioGridi119007. 328 interactions.
    DIPiDIP-41629N.
    IntActiQ9UMX0. 49 interactions.
    MINTiMINT-150317.
    STRINGi9606.ENSP00000365576.

    Structurei

    Secondary structure

    1
    589
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 426
    Beta strandi47 – 526
    Helixi58 – 6912
    Helixi73 – 753
    Beta strandi76 – 805
    Beta strandi83 – 853
    Helixi92 – 943
    Beta strandi101 – 1066
    Turni543 – 5475
    Helixi548 – 5569
    Helixi562 – 57211
    Helixi576 – 5838

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JY5NMR-A541-586[»]
    2JY6NMR-B541-586[»]
    2KLCNMR-A34-112[»]
    ProteinModelPortaliQ9UMX0.
    SMRiQ9UMX0. Positions 1-112, 537-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UMX0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 11175Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini546 – 58641UBAPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The UBA domain mediates binding to PSEN1 and PSEN2. It also binds ubiquitin with micromolar affinity, independently of polyubiquitin linkage type.

    Sequence similaritiesi

    Contains 1 UBA domain.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5272.
    HOVERGENiHBG064537.
    InParanoidiQ9UMX0.
    KOiK04523.
    OMAiPDIMRQX.
    OrthoDBiEOG7HF1J8.
    PhylomeDBiQ9UMX0.
    TreeFamiTF314412.

    Family and domain databases

    InterProiIPR006636. STI1_HS-bd.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR015496. Ubiquilin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR028799. UBQLN1.
    [Graphical view]
    PANTHERiPTHR10677. PTHR10677. 1 hit.
    PTHR10677:SF16. PTHR10677:SF16. 1 hit.
    PfamiPF00627. UBA. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00727. STI1. 4 hits.
    SM00165. UBA. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50030. UBA. 1 hit.
    PS50053. UBIQUITIN_2. 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: Q9UMX0-1) [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

    MAESGESGGP PGSQDSAAGA EGAGAPAAAA SAEPKIMKVT VKTPKEKEEF    50
    AVPENSSVQQ FKEEISKRFK SHTDQLVLIF AGKILKDQDT LSQHGIHDGL 100
    TVHLVIKTQN RPQDHSAQQT NTAGSNVTTS STPNSNSTSG SATSNPFGLG 150
    GLGGLAGLSS LGLNTTNFSE LQSQMQRQLL SNPEMMVQIM ENPFVQSMLS 200
    NPDLMRQLIM ANPQMQQLIQ RNPEISHMLN NPDIMRQTLE LARNPAMMQE 250
    MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMLSAAQEQ FGGNPFASLV 300
    SNTSSGEGSQ PSRTENRDPL PNPWAPQTSQ SSSASSGTAS TVGGTTGSTA 350
    SGTSGQSTTA PNLVPGVGAS MFNTPGMQSL LQQITENPQL MQNMLSAPYM 400
    RSMMQSLSQN PDLAAQMMLN NPLFAGNPQL QEQMRQQLPT FLQQMQNPDT 450
    LSAMSNPRAM QALLQIQQGL QTLATEAPGL IPGFTPGLGA LGSTGGSSGT 500
    NGSNATPSEN TSPTAGTTEP GHQQFIQQML QALAGVNPQL QNPEVRFQQQ 550
    LEQLSAMGFL NREANLQALI ATGGDINAAI ERLLGSQPS 589
    Length:589
    Mass (Da):62,519
    Last modified:March 1, 2002 - v2
    Checksum:i8B4756B6113B7025
    GO
    Isoform 2 (identifier: Q9UMX0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         416-443: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:561
    Mass (Da):59,220
    Checksum:i1E0BC42EC5BA4DA6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251A → T in AAH39294. (PubMed:15489334)Curated
    Sequence conflicti41 – 411V → A in BAB20436. (PubMed:10807547)Curated
    Sequence conflicti61 – 611F → S in BAB20436. (PubMed:10807547)Curated
    Sequence conflicti91 – 911L → S in BAB20436. (PubMed:10807547)Curated
    Sequence conflicti125 – 1251S → G in CAB66578. (PubMed:11230166)Curated
    Sequence conflicti202 – 2021P → H in AAH39294. (PubMed:15489334)Curated
    Sequence conflicti537 – 5382NP → YS in BAB20436. (PubMed:10807547)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei416 – 44328Missing in isoform 2. 1 PublicationVSP_009787Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176069 mRNA. Translation: AAD49751.3.
    AF293384 mRNA. Translation: AAG02473.1.
    AB035275 mRNA. Translation: BAB20436.1.
    AL136643 mRNA. Translation: CAB66578.1.
    AL354920 Genomic DNA. Translation: CAI15100.1.
    AL354920 Genomic DNA. Translation: CAI15101.1.
    CH471089 Genomic DNA. Translation: EAW62659.1.
    CH471089 Genomic DNA. Translation: EAW62661.1.
    BC010066 mRNA. Translation: AAH10066.1.
    BC039294 mRNA. Translation: AAH39294.1.
    AK074535 mRNA. No translation available.
    CCDSiCCDS6663.1. [Q9UMX0-1]
    CCDS6664.1. [Q9UMX0-2]
    RefSeqiNP_038466.2. NM_013438.4. [Q9UMX0-1]
    NP_444295.1. NM_053067.2. [Q9UMX0-2]
    UniGeneiHs.9589.

    Genome annotation databases

    EnsembliENST00000257468; ENSP00000257468; ENSG00000135018. [Q9UMX0-2]
    ENST00000376395; ENSP00000365576; ENSG00000135018. [Q9UMX0-1]
    GeneIDi29979.
    KEGGihsa:29979.
    UCSCiuc004amv.3. human. [Q9UMX0-1]
    uc004amw.3. human. [Q9UMX0-2]

    Polymorphism databases

    DMDMi48475013.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176069 mRNA. Translation: AAD49751.3 .
    AF293384 mRNA. Translation: AAG02473.1 .
    AB035275 mRNA. Translation: BAB20436.1 .
    AL136643 mRNA. Translation: CAB66578.1 .
    AL354920 Genomic DNA. Translation: CAI15100.1 .
    AL354920 Genomic DNA. Translation: CAI15101.1 .
    CH471089 Genomic DNA. Translation: EAW62659.1 .
    CH471089 Genomic DNA. Translation: EAW62661.1 .
    BC010066 mRNA. Translation: AAH10066.1 .
    BC039294 mRNA. Translation: AAH39294.1 .
    AK074535 mRNA. No translation available.
    CCDSi CCDS6663.1. [Q9UMX0-1 ]
    CCDS6664.1. [Q9UMX0-2 ]
    RefSeqi NP_038466.2. NM_013438.4. [Q9UMX0-1 ]
    NP_444295.1. NM_053067.2. [Q9UMX0-2 ]
    UniGenei Hs.9589.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JY5 NMR - A 541-586 [» ]
    2JY6 NMR - B 541-586 [» ]
    2KLC NMR - A 34-112 [» ]
    ProteinModelPortali Q9UMX0.
    SMRi Q9UMX0. Positions 1-112, 537-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119007. 328 interactions.
    DIPi DIP-41629N.
    IntActi Q9UMX0. 49 interactions.
    MINTi MINT-150317.
    STRINGi 9606.ENSP00000365576.

    PTM databases

    PhosphoSitei Q9UMX0.

    Polymorphism databases

    DMDMi 48475013.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00071180.

    Proteomic databases

    MaxQBi Q9UMX0.
    PaxDbi Q9UMX0.
    PRIDEi Q9UMX0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257468 ; ENSP00000257468 ; ENSG00000135018 . [Q9UMX0-2 ]
    ENST00000376395 ; ENSP00000365576 ; ENSG00000135018 . [Q9UMX0-1 ]
    GeneIDi 29979.
    KEGGi hsa:29979.
    UCSCi uc004amv.3. human. [Q9UMX0-1 ]
    uc004amw.3. human. [Q9UMX0-2 ]

    Organism-specific databases

    CTDi 29979.
    GeneCardsi GC09M086274.
    HGNCi HGNC:12508. UBQLN1.
    HPAi CAB037256.
    HPA054143.
    MIMi 605046. gene.
    neXtProti NX_Q9UMX0.
    PharmGKBi PA37155.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5272.
    HOVERGENi HBG064537.
    InParanoidi Q9UMX0.
    KOi K04523.
    OMAi PDIMRQX.
    OrthoDBi EOG7HF1J8.
    PhylomeDBi Q9UMX0.
    TreeFami TF314412.

    Miscellaneous databases

    ChiTaRSi UBQLN1. human.
    EvolutionaryTracei Q9UMX0.
    GeneWikii UBQLN1.
    GenomeRNAii 29979.
    NextBioi 52732.
    PROi Q9UMX0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UMX0.
    Bgeei Q9UMX0.
    CleanExi HS_UBQLN1.
    Genevestigatori Q9UMX0.

    Family and domain databases

    InterProi IPR006636. STI1_HS-bd.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR015496. Ubiquilin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR028799. UBQLN1.
    [Graphical view ]
    PANTHERi PTHR10677. PTHR10677. 1 hit.
    PTHR10677:SF16. PTHR10677:SF16. 1 hit.
    Pfami PF00627. UBA. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00727. STI1. 4 hits.
    SM00165. UBA. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50030. UBA. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation."
      Mah A.L., Perry G., Smith M.A., Monteiro M.J.
      J. Cell Biol. 151:847-862(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PSEN1 AND PSEN2, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Mah A.L., Monteiro M.J.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome."
      Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L., Gill G., Howley P.M.
      Mol. Cell 6:409-419(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH UBE3A; BTRC AND THE PROTEASOME.
      Tissue: B-cell.
    4. "Molecular cloning and expression analysis of the human DA41 gene and its mapping to chromosome 9q21.2-q21.3."
      Hanaoka E., Ozaki T., Ohira M., Nakamura Y., Suzuki M., Takahashi E., Moriya H., Nakagawara A., Sakiyama S.
      J. Hum. Genet. 45:188-191(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    6. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Muscle.
    9. "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] OF 1-316.
      Tissue: Embryo.
    10. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 71-83; 207-236; 244-253 AND 547-582, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    11. "Characterization of ubiquilin 1, an mTOR-interacting protein."
      Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J.
      Biochim. Biophys. Acta 1542:41-56(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH MTOR, TISSUE SPECIFICITY.
    12. "Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death."
      Ko H.S., Uehara T., Nomura Y.
      J. Biol. Chem. 277:35386-35392(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH P4HB.
    13. "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.
    14. "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].
    15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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].
    19. "The TREX1 C-terminal region controls cellular localization through ubiquitination."
      Orebaugh C.D., Fye J.M., Harvey S., Hollis T., Wilkinson J.C., Perrino F.W.
      J. Biol. Chem. 288:28881-28892(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TREX1, SUBCELLULAR LOCATION.
    20. "Affinity makes the difference: nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains."
      Zhang D., Raasi S., Fushman D.
      J. Mol. Biol. 377:162-180(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 541-586 ALONE AND IN COMPLEX WITH UBIQUITIN.

    Entry informationi

    Entry nameiUBQL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UMX0
    Secondary accession number(s): Q5T6J5
    , Q5T6J9, Q8IXS9, Q8N2Q3, Q9H0T8, Q9H3R4, Q9HAZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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 9
      Human chromosome 9: 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