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Q99NB8

- UBQL4_MOUSE

UniProt

Q99NB8 - UBQL4_MOUSE

Protein

Ubiquilin-4

Gene

Ubqln4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Plays a role in the regulation of proteasomal protein degradation. Depending on the case, may promote or inhibit proteasomal protein degradation.2 Publications

    GO - Molecular functioni

    1. polyubiquitin binding Source: UniProtKB

    GO - Biological processi

    1. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquilin-4
    Alternative name(s):
    Ataxin-1 interacting ubiquitin-like protein
    Short name:
    A1Up
    Ataxin-1 ubiquitin-like-interacting protein A1U
    Connexin43-interacting protein of 75 kDa
    Short name:
    CIP75
    Gene namesi
    Name:Ubqln4
    Synonyms:Cip75, Ubin
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:2150152. Ubqln4.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm. Endoplasmic reticulum Curated. Cytoplasmperinuclear region
    Note: Colocalizes with the proteasome, both in nucleus and cytoplasm By similarity. May associate with the endoplasmic reticulum.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: MGI
    3. cytosolic proteasome complex Source: Ensembl
    4. endoplasmic reticulum membrane Source: MGI
    5. nuclear proteasome complex Source: Ensembl
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 596596Ubiquilin-4PRO_0000211016Add
    BLAST

    Post-translational modificationi

    Ubiquitinated; this does not lead to proteasomal degradation. May undergo both 'Lys-48'- and 'Lys-63'-linked polyubiquitination By similarity.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ99NB8.
    PaxDbiQ99NB8.
    PRIDEiQ99NB8.

    PTM databases

    PhosphoSiteiQ99NB8.

    Expressioni

    Tissue specificityi

    Detected in testis, ovary, thyroid, kidney, thymus, heart, liver, lung and spleen (at protein level). Highly expressed in heart, skeletal muscle, kidney, liver and brain. Detected at lower levels in testis, lung and spleen.2 Publications

    Gene expression databases

    BgeeiQ99NB8.
    CleanExiMM_UBQLN4.
    GenevestigatoriQ99NB8.

    Interactioni

    Subunit structurei

    Homodimer. Binds ATXN1/SCA1. Interaction with ATXN1 inhibits polyubiquitination of UBQLN4 and interferes with PSMD4 binding By similarity. Interacts (via ubiquitin-like domain) with PSMD4, a regulatory subunit of the proteasome. Binds signal sequences of proteins that are targeted to the endoplasmic reticulum. Interacts (via UBA domain) with GJA1 (not ubiquitinated) and with ubiquitin; both compete for the same binding site. Interacts (via UBA domain) with polyubiquitin chains and polyubiquitinated proteins.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi220488. 1 interaction.
    IntActiQ99NB8. 4 interactions.
    MINTiMINT-4139382.

    Structurei

    Secondary structure

    1
    596
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi551 – 56212
    Turni563 – 5653
    Helixi569 – 57911
    Helixi583 – 59210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KNZNMR-A549-596[»]
    ProteinModelPortaliQ99NB8.
    SMRiQ99NB8. Positions 13-83, 549-596.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99NB8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 8775Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini548 – 59346UBAPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi174 – 25784Met-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5272.
    GeneTreeiENSGT00390000005720.
    HOGENOMiHOG000234878.
    HOVERGENiHBG064537.
    InParanoidiQ99NB8.
    KOiK04523.
    OMAiVAVNIRC.
    OrthoDBiEOG7HF1J8.
    PhylomeDBiQ99NB8.
    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.
    [Graphical view]
    PANTHERiPTHR10677. PTHR10677. 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]

    Sequencei

    Sequence statusi: Complete.

    Q99NB8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEPSGAETR PQIRVTVKTP KDKEEIVICD QASVKEFKEE ISRRFKAQQD    50
    QLVLIFAGKI LKDGDTLSQH GIKDGLTVHL VIKTPQKAQD PVTAAASPPS 100
    TPDSASAPST TPASPAAAPV QPCSSGNTTS DAGSGGGPSP VAAEGPSSAT 150
    ASILSGFGGI LGLGSLGLGS ANFMELQQQM QRQLMSNPEM LSQIMENPLV 200
    QDMMSNPDLM RHMIMANPQM QQLMERNPEI SHMLNNPELM RQTMELARNP 250
    AMMQEMMRNQ DRALSNLESV PGGYNALRRM YTDIQEPMFT AAREQFGNNP 300
    FSSLAGNSDN SSSQPLRTEN REPLPNPWSP SPPTSQAPGS GGEGTGGSGT 350
    SQVHPTVSNP FGINAASLGS GMFNSPEMQA LLQQISENPQ LMQNVISAPY 400
    MRTMMQTLAQ NPDFAAQMMV NVPLFAGNPQ LQEQLRLQLP VFLQQMQNPE 450
    SLSILTNPRA MQALLQIQQG LQTLQTEAPG LVPSLGSFGT PRTSVPLAGS 500
    NSGSSAEAPT SSPGVPATSP PSAGSNAQQQ LMQQMIQLLS GSGNSQVPMP 550
    EVRFQQQLEQ LNSMGFINRE ANLQALIATG GDINAAIERL LGSQLS 596
    Length:596
    Mass (Da):63,506
    Last modified:June 1, 2001 - v1
    Checksum:i77CC85B49FD083C4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040050 mRNA. Translation: BAB40326.1.
    BC017686 mRNA. Translation: AAH17686.1.
    AK077511 mRNA. Translation: BAC36837.1.
    CCDSiCCDS17479.1.
    RefSeqiNP_277068.1. NM_033526.2.
    UniGeneiMm.303059.

    Genome annotation databases

    EnsembliENSMUST00000008748; ENSMUSP00000008748; ENSMUSG00000008604.
    GeneIDi94232.
    KEGGimmu:94232.
    UCSCiuc008pvq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040050 mRNA. Translation: BAB40326.1 .
    BC017686 mRNA. Translation: AAH17686.1 .
    AK077511 mRNA. Translation: BAC36837.1 .
    CCDSi CCDS17479.1.
    RefSeqi NP_277068.1. NM_033526.2.
    UniGenei Mm.303059.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KNZ NMR - A 549-596 [» ]
    ProteinModelPortali Q99NB8.
    SMRi Q99NB8. Positions 13-83, 549-596.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 220488. 1 interaction.
    IntActi Q99NB8. 4 interactions.
    MINTi MINT-4139382.

    PTM databases

    PhosphoSitei Q99NB8.

    Proteomic databases

    MaxQBi Q99NB8.
    PaxDbi Q99NB8.
    PRIDEi Q99NB8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000008748 ; ENSMUSP00000008748 ; ENSMUSG00000008604 .
    GeneIDi 94232.
    KEGGi mmu:94232.
    UCSCi uc008pvq.1. mouse.

    Organism-specific databases

    CTDi 56893.
    MGIi MGI:2150152. Ubqln4.

    Phylogenomic databases

    eggNOGi COG5272.
    GeneTreei ENSGT00390000005720.
    HOGENOMi HOG000234878.
    HOVERGENi HBG064537.
    InParanoidi Q99NB8.
    KOi K04523.
    OMAi VAVNIRC.
    OrthoDBi EOG7HF1J8.
    PhylomeDBi Q99NB8.
    TreeFami TF314412.

    Miscellaneous databases

    EvolutionaryTracei Q99NB8.
    NextBioi 352243.
    PROi Q99NB8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99NB8.
    CleanExi MM_UBQLN4.
    Genevestigatori Q99NB8.

    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.
    [Graphical view ]
    PANTHERi PTHR10677. PTHR10677. 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. "Molecular cloning of a novel ubiquitin-like protein, UBIN, that binds to ER targeting signal sequences."
      Matsuda M., Koide T., Yorihuzi T., Hosokawa N., Nagata K.
      Biochem. Biophys. Res. Commun. 280:535-540(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SIGNAL SEQUENCES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    2. "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: Kidney.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 549-596.
      Strain: C57BL/6J.
      Tissue: Embryo.
    4. "A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43."
      Li X., Su V., Kurata W.E., Jin C., Lau A.F.
      J. Biol. Chem. 283:5748-5759(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PSMD4 AND GJA1.
    5. "Ubiquitin-independent proteasomal degradation of endoplasmic reticulum-localized connexin43 mediated by CIP75."
      Su V., Nakagawa R., Koval M., Lau A.F.
      J. Biol. Chem. 285:40979-40990(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBIQUITIN AND GJA1, TISSUE SPECIFICITY.
    6. Cited for: STRUCTURE BY NMR OF 549-596, INTERACTION WITH GJA1.

    Entry informationi

    Entry nameiUBQL4_MOUSE
    AccessioniPrimary (citable) accession number: Q99NB8
    Secondary accession number(s): Q8BP88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3