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Q9UHD9

- UBQL2_HUMAN

UniProt

Q9UHD9 - UBQL2_HUMAN

Protein

Ubiquilin-2

Gene

UBQLN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Increases the half-life of proteins destined to be degraded by the proteasome; may modulate proteasome-mediated protein degradation.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cell death Source: UniProtKB-KW

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquilin-2
    Alternative name(s):
    Chap1
    DSK2 homolog
    Protein linking IAP with cytoskeleton 2
    Short name:
    PLIC-2
    Short name:
    hPLIC-2
    Ubiquitin-like product Chap1/Dsk2
    Gene namesi
    Name:UBQLN2
    Synonyms:N4BP4, PLIC2
    ORF Names:HRIHFB2157
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12509. UBQLN2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Where it colocalizes with the proteasome. Associated with fibers in mitotic cells.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: UniProtKB-SubCell
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia (ALS15) [MIM:300857]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS15 may develop frontotemporal dementia.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551S → N in ALS15; uncertain pathological significance. 1 Publication
    VAR_068892
    Natural varianti189 – 1891P → T in ALS15; uncertain pathological significance. 1 Publication
    VAR_068893
    Natural varianti283 – 2831A → T in ALS15. 1 Publication
    VAR_068895
    Natural varianti425 – 4251Q → R in ALS15. 1 Publication
    VAR_068896
    Natural varianti487 – 4871T → I in ALS15. 1 Publication
    VAR_068897
    Natural varianti497 – 4971P → H in ALS15; leads to defective ubiquitin-mediated proteasomal degradation. 1 Publication
    VAR_066562
    Natural varianti497 – 4971P → S in ALS15. 1 Publication
    VAR_066563
    Natural varianti506 – 5061P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation. 1 Publication
    VAR_066564
    Natural varianti509 – 5091P → S in ALS15. 1 Publication
    VAR_066565
    Natural varianti525 – 5251P → S in ALS15. 1 Publication
    VAR_066566

    Keywords - Diseasei

    Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi300857. phenotype.
    Orphaneti803. Amyotrophic lateral sclerosis.
    PharmGKBiPA37156.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 624623Ubiquilin-2PRO_0000211011Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UHD9.
    PaxDbiQ9UHD9.
    PeptideAtlasiQ9UHD9.
    PRIDEiQ9UHD9.

    PTM databases

    PhosphoSiteiQ9UHD9.

    Expressioni

    Inductioni

    Highly expressed in mitotic cells from metaphase to telophase. Expression in non-mitotic cells is very low.

    Gene expression databases

    BgeeiQ9UHD9.
    CleanExiHS_UBQLN2.
    GenevestigatoriQ9UHD9.

    Organism-specific databases

    HPAiCAB013481.
    HPA006431.

    Interactioni

    Subunit structurei

    Binds UBE3A and BTRC. Interacts with the 19S proteasome subunit. Interacts with C9orf72.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADRM1Q161863EBI-947187,EBI-954387
    PSMD4P550363EBI-947187,EBI-359318
    RAD23AP547253EBI-947187,EBI-746453
    RPN13O487264EBI-947187,EBI-7710745From a different organism.

    Protein-protein interaction databases

    BioGridi119006. 61 interactions.
    DIPiDIP-42116N.
    IntActiQ9UHD9. 12 interactions.
    MINTiMINT-1192483.
    STRINGi9606.ENSP00000345195.

    Structurei

    Secondary structure

    1
    624
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 253
    Beta strandi33 – 386
    Beta strandi43 – 486
    Helixi54 – 6512
    Beta strandi69 – 768
    Beta strandi79 – 824
    Helixi87 – 915
    Beta strandi93 – 10210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J8CNMR-A1-103[»]
    ProteinModelPortaliQ9UHD9.
    SMRiQ9UHD9. Positions 1-103, 578-624.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UHD9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 10775Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Repeati491 – 49331
    Repeati494 – 49632
    Repeati497 – 49933
    Repeati500 – 50234
    Repeati503 – 50535
    Repeati506 – 50836
    Repeati509 – 51137
    Repeati512 – 51438
    Repeati515 – 51739
    Repeati518 – 520310
    Repeati521 – 523311
    Repeati524 – 526312
    Domaini581 – 62141UBAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni491 – 5263612 X 3 AA tandem repeats of P-X-XAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5272.
    HOGENOMiHOG000234878.
    HOVERGENiHBG064537.
    InParanoidiQ9UHD9.
    KOiK04523.
    OMAiLMASPEM.
    OrthoDBiEOG7HF1J8.
    PhylomeDBiQ9UHD9.
    TreeFamiTF314412.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR006636. STI1_HS-bd.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR015496. Ubiquilin.
    IPR028430. Ubiquilin-2.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR10677. PTHR10677. 1 hit.
    PTHR10677:SF5. PTHR10677:SF5. 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.
    SSF48371. SSF48371. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50030. UBA. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UHD9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAENGESSGP PRPSRGPAAA QGSAAAPAEP KIIKVTVKTP KEKEEFAVPE    50
    NSSVQQFKEA ISKRFKSQTD QLVLIFAGKI LKDQDTLIQH GIHDGLTVHL 100
    VIKSQNRPQG QSTQPSNAAG TNTTSASTPR SNSTPISTNS NPFGLGSLGG 150
    LAGLSSLGLS STNFSELQSQ MQQQLMASPE MMIQIMENPF VQSMLSNPDL 200
    MRQLIMANPQ MQQLIQRNPE ISHLLNNPDI MRQTLEIARN PAMMQEMMRN 250
    QDLALSNLES IPGGYNALRR MYTDIQEPML NAAQEQFGGN PFASVGSSSS 300
    SGEGTQPSRT ENRDPLPNPW APPPATQSSA TTSTTTSTGS GSGNSSSNAT 350
    GNTVAAANYV ASIFSTPGMQ SLLQQITENP QLIQNMLSAP YMRSMMQSLS 400
    QNPDLAAQMM LNSPLFTANP QLQEQMRPQL PAFLQQMQNP DTLSAMSNPR 450
    AMQALMQIQQ GLQTLATEAP GLIPSFTPGV GVGVLGTAIG PVGPVTPIGP 500
    IGPIVPFTPI GPIGPIGPTG PAAPPGSTGS GGPTGPTVSS AAPSETTSPT 550
    SESGPNQQFI QQMVQALAGA NAPQLPNPEV RFQQQLEQLN AMGFLNREAN 600
    LQALIATGGD INAAIERLLG SQPS 624
    Length:624
    Mass (Da):65,696
    Last modified:January 23, 2007 - v2
    Checksum:iDF7DF8C4D7B71AC3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti544 – 5441S → R(PubMed:10675567)Curated
    Sequence conflicti544 – 5441S → R(PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551S → N in ALS15; uncertain pathological significance. 1 Publication
    VAR_068892
    Natural varianti189 – 1891P → T in ALS15; uncertain pathological significance. 1 Publication
    VAR_068893
    Natural varianti235 – 2351L → H.
    Corresponds to variant rs17002693 [ dbSNP | Ensembl ].
    VAR_052680
    Natural varianti282 – 2821A → V Probable disease-associated mutation found in a patient with frontotemporal dementia. 1 Publication
    VAR_068894
    Natural varianti283 – 2831A → T in ALS15. 1 Publication
    VAR_068895
    Natural varianti425 – 4251Q → R in ALS15. 1 Publication
    VAR_068896
    Natural varianti487 – 4871T → I in ALS15. 1 Publication
    VAR_068897
    Natural varianti497 – 4971P → H in ALS15; leads to defective ubiquitin-mediated proteasomal degradation. 1 Publication
    VAR_066562
    Natural varianti497 – 4971P → S in ALS15. 1 Publication
    VAR_066563
    Natural varianti506 – 5061P → T in ALS15; leads to defective ubiquitin-mediated proteasomal degradation. 1 Publication
    VAR_066564
    Natural varianti509 – 5091P → S in ALS15. 1 Publication
    VAR_066565
    Natural varianti525 – 5251P → S in ALS15. 1 Publication
    VAR_066566

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF189009 mRNA. Translation: AAF17237.1.
    AF293385 mRNA. Translation: AAG02474.1.
    AL354793 Genomic DNA. Translation: CAD13519.1.
    CH471154 Genomic DNA. Translation: EAW93233.1.
    BC069237 mRNA. Translation: AAH69237.1.
    AL442081 mRNA. Translation: CAC09446.1.
    AB015344 mRNA. Translation: BAA34801.1.
    CCDSiCCDS14374.1.
    RefSeqiNP_038472.2. NM_013444.3.
    UniGeneiHs.179309.

    Genome annotation databases

    EnsembliENST00000338222; ENSP00000345195; ENSG00000188021.
    GeneIDi29978.
    KEGGihsa:29978.
    UCSCiuc004dus.3. human.

    Polymorphism databases

    DMDMi124056593.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF189009 mRNA. Translation: AAF17237.1 .
    AF293385 mRNA. Translation: AAG02474.1 .
    AL354793 Genomic DNA. Translation: CAD13519.1 .
    CH471154 Genomic DNA. Translation: EAW93233.1 .
    BC069237 mRNA. Translation: AAH69237.1 .
    AL442081 mRNA. Translation: CAC09446.1 .
    AB015344 mRNA. Translation: BAA34801.1 .
    CCDSi CCDS14374.1.
    RefSeqi NP_038472.2. NM_013444.3.
    UniGenei Hs.179309.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J8C NMR - A 1-103 [» ]
    ProteinModelPortali Q9UHD9.
    SMRi Q9UHD9. Positions 1-103, 578-624.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119006. 61 interactions.
    DIPi DIP-42116N.
    IntActi Q9UHD9. 12 interactions.
    MINTi MINT-1192483.
    STRINGi 9606.ENSP00000345195.

    PTM databases

    PhosphoSitei Q9UHD9.

    Polymorphism databases

    DMDMi 124056593.

    Proteomic databases

    MaxQBi Q9UHD9.
    PaxDbi Q9UHD9.
    PeptideAtlasi Q9UHD9.
    PRIDEi Q9UHD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338222 ; ENSP00000345195 ; ENSG00000188021 .
    GeneIDi 29978.
    KEGGi hsa:29978.
    UCSCi uc004dus.3. human.

    Organism-specific databases

    CTDi 29978.
    GeneCardsi GC0XP056606.
    GeneReviewsi UBQLN2.
    HGNCi HGNC:12509. UBQLN2.
    HPAi CAB013481.
    HPA006431.
    MIMi 300264. gene.
    300857. phenotype.
    neXtProti NX_Q9UHD9.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    PharmGKBi PA37156.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5272.
    HOGENOMi HOG000234878.
    HOVERGENi HBG064537.
    InParanoidi Q9UHD9.
    KOi K04523.
    OMAi LMASPEM.
    OrthoDBi EOG7HF1J8.
    PhylomeDBi Q9UHD9.
    TreeFami TF314412.

    Miscellaneous databases

    EvolutionaryTracei Q9UHD9.
    GeneWikii UBQLN2.
    GenomeRNAii 29978.
    NextBioi 52728.
    PROi Q9UHD9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UHD9.
    CleanExi HS_UBQLN2.
    Genevestigatori Q9UHD9.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR006636. STI1_HS-bd.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR015496. Ubiquilin.
    IPR028430. Ubiquilin-2.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR10677. PTHR10677. 1 hit.
    PTHR10677:SF5. PTHR10677:SF5. 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.
    SSF48371. SSF48371. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50030. UBA. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch."
      Kaye F.J., Modi S., Ivanovska I., Koonin E.V., Thress K., Kubo A., Kornbluth S., Rose M.D.
      FEBS Lett. 467:348-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STCH.
      Tissue: Lung.
    2. "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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE PROTEASOME AND UBE3A.
      Tissue: B-cell.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Placenta.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-624.
      Tissue: Amygdala.
    7. "Selection system for genes encoding nuclear-targeted proteins."
      Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
      Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-624, SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    8. "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].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking."
      Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A., Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E., Atkin J.D.
      Hum. Mol. Genet. 23:3579-3595(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C9ORF72.
    12. "Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a."
      Walters K.J., Kleijnen M.F., Goh A.M., Wagner G., Howley P.M.
      Biochemistry 41:1767-1777(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-103.
    13. Cited for: VARIANTS ALS15 HIS-497; SER-497; THR-506; SER-509 AND SER-525, CHARACTERIZATION OF VARIANTS ALS15 HIS-497 AND THR-506.
    14. "Screening in ALS and FTD patients reveals 3 novel UBQLN2 mutations outside the PXX domain and a pure FTD phenotype."
      Synofzik M., Maetzler W., Grehl T., Prudlo J., Vom Hagen J.M., Haack T., Rebassoo P., Munz M., Schols L., Biskup S.
      Neurobiol. Aging 33:E13-E17(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ALS15 THR-283 AND ARG-425, VARIANT VAL-282.
    15. "UBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis."
      Williams K.L., Warraich S.T., Yang S., Solski J.A., Fernando R., Rouleau G.A., Nicholson G.A., Blair I.P.
      Neurobiol. Aging 33:E3-E10(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ALS15 ILE-487.
    16. "UBQLN2 mutations are rare in French and French-Canadian amyotrophic lateral sclerosis."
      Daoud H., Suhail H., Szuto A., Camu W., Salachas F., Meininger V., Bouchard J.P., Dupre N., Dion P.A., Rouleau G.A.
      Neurobiol. Aging 33:E1-E5(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ALS15 ASN-155 AND THR-189.

    Entry informationi

    Entry nameiUBQL2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHD9
    Secondary accession number(s): O94798
    , Q5D027, Q9H3W6, Q9HAZ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 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, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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