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Q9NRR5

- UBQL4_HUMAN

UniProt

Q9NRR5 - UBQL4_HUMAN

Protein

Ubiquilin-4

Gene

UBQLN4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (15 Mar 2004)
      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.1 Publication

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. polyubiquitin binding Source: UniProtKB
    3. protein 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:C1orf6, CIP75, UBIN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1237. UBQLN4.

    Subcellular locationi

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

    GO - Cellular componenti

    1. centrosome Source: HPA
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. endoplasmic reticulum membrane Source: UniProtKB
    5. intracellular membrane-bounded organelle Source: HPA
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25619.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 601601Ubiquilin-4PRO_0000211015Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei98 – 981Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated; this does not lead to proteasomal degradation. May undergo both 'Lys-48'- and 'Lys-63'-linked polyubiquitination.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NRR5.
    PaxDbiQ9NRR5.
    PRIDEiQ9NRR5.

    PTM databases

    PhosphoSiteiQ9NRR5.

    Expressioni

    Tissue specificityi

    Highly expressed in pancreas, kidney, skeletal muscle, heart and throughout the brain, and at lower levels in placenta, lung and liver.1 Publication

    Gene expression databases

    BgeeiQ9NRR5.
    CleanExiHS_UBQLN4.
    GenevestigatoriQ9NRR5.

    Organism-specific databases

    HPAiHPA027920.

    Interactioni

    Subunit structurei

    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 By similarity. Homodimer. Interacts (via UBA domain) with ubiquitin and with polyubiquitin chains. Interacts (via ubiquitin-like domain) with PSMD4, a regulatory subunit of the 26S proteasome. Interacts with ATXN1/SCA1. Interaction with ATXN1 inhibits polyubiquitination of UBQLN4 and interferes with PSMD4 binding.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-711226,EBI-711226
    ATXN1P542536EBI-711226,EBI-930964
    FKBP2P268852EBI-711226,EBI-719873
    MAP1LC3AQ9H4923EBI-711226,EBI-720768
    MLLT6P551982EBI-711226,EBI-740216
    PDLIM7Q9NR122EBI-711226,EBI-350517
    RAI2Q9Y5P33EBI-711226,EBI-746228
    TRIM32Q130493EBI-711226,EBI-742790
    UBQLN1Q9UMX08EBI-711226,EBI-741480
    ZNF205O952012EBI-711226,EBI-747343

    Protein-protein interaction databases

    BioGridi121223. 180 interactions.
    IntActiQ9NRR5. 151 interactions.
    MINTiMINT-1373057.
    STRINGi9606.ENSP00000357292.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRR5.
    SMRiQ9NRR5. Positions 13-83, 555-601.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 8775Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini553 – 59846UBAPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5272.
    HOVERGENiHBG064537.
    InParanoidiQ9NRR5.
    KOiK04523.
    OMAiFGMSRTT.
    OrthoDBiEOG7HF1J8.
    PhylomeDBiQ9NRR5.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRR5-1) [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

    MAEPSGAETR PPIRVTVKTP KDKEEIVICD RASVKEFKEE ISRRFKAQQD    50
    QLVLIFAGKI LKDGDTLNQH GIKDGLTVHL VIKTPQKAQD PAAATASSPS 100
    TPDPASAPST TPASPATPAQ PSTSGSASSD AGSGSRRSSG GGPSPGAGEG 150
    SPSATASILS GFGGILGLGS LGLGSANFME LQQQMQRQLM SNPEMLSQIM 200
    ENPLVQDMMS NPDLMRHMIM ANPQMQQLME RNPEISHMLN NPELMRQTME 250
    LARNPAMMQE MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMFSAAREQ 300
    FGNNPFSSLA GNSDSSSSQP LRTENREPLP NPWSPSPPTS QAPGSGGEGT 350
    GGSGTSQVHP TVSNPFGINA ASLGSGMFNS PEMQALLQQI SENPQLMQNV 400
    ISAPYMRSMM QTLAQNPDFA AQMMVNVPLF AGNPQLQEQL RLQLPVFLQQ 450
    MQNPESLSIL TNPRAMQALL QIQQGLQTLQ TEAPGLVPSL GSFGISRTPA 500
    PSAGSNAGST PEAPTSSPAT PATSSPTGAS SAQQQLMQQM IQLLAGSGNS 550
    QVQTPEVRFQ QQLEQLNSMG FINREANLQA LIATGGDINA AIERLLGSQL 600
    S 601
    Length:601
    Mass (Da):63,853
    Last modified:March 15, 2004 - v2
    Checksum:iE57B9FFEF90793FE
    GO
    Isoform 2 (identifier: Q9NRR5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         93-226: AATASSPSTP...HMIMANPQMQ → PPAAPSLPAA...AAQLHGLHQS
         227-601: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:226
    Mass (Da):24,527
    Checksum:i69101551F1551A93
    GO

    Sequence cautioni

    The sequence AAF19084.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH06410.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1892QL → HV in AAF80171. (PubMed:11001934)Curated
    Sequence conflicti298 – 2981R → Q in AAF80171. (PubMed:11001934)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti495 – 4951I → M.2 Publications
    Corresponds to variant rs2297792 [ dbSNP | Ensembl ].
    VAR_052685

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei93 – 226134AATAS…NPQMQ → PPAAPSLPAADAEPRVTLHP YQSPSHAGIAADPAGTTDLA DRGPWAGTQPWLLWDIPDPS TLSRQQRRVYARGPHFLTSH ASHIFSNRGFQRPAATHAAD DPAFGWKWKLTGADARSEIS AAAGAAQLHGLHQS in isoform 2. 1 PublicationVSP_041187Add
    BLAST
    Alternative sequencei227 – 601375Missing in isoform 2. 1 PublicationVSP_041188Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF188240 mRNA. Translation: AAF80171.1.
    AK098368 mRNA. No translation available.
    AK314413 mRNA. Translation: BAG37034.1.
    AL355388 Genomic DNA. Translation: CAH72633.1.
    AL355388 Genomic DNA. Translation: CAH72634.1.
    BC006410 mRNA. Translation: AAH06410.1. Different initiation.
    BC018403 mRNA. Translation: AAH18403.1.
    BC063841 mRNA. Translation: AAH63841.1.
    AF113544 mRNA. Translation: AAF19084.1. Different initiation.
    CCDSiCCDS1127.1. [Q9NRR5-1]
    RefSeqiNP_064516.2. NM_020131.3. [Q9NRR5-1]
    UniGeneiHs.283739.

    Genome annotation databases

    EnsembliENST00000368309; ENSP00000357292; ENSG00000160803. [Q9NRR5-1]
    GeneIDi56893.
    KEGGihsa:56893.
    UCSCiuc001fna.3. human. [Q9NRR5-1]

    Polymorphism databases

    DMDMi45476982.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF188240 mRNA. Translation: AAF80171.1 .
    AK098368 mRNA. No translation available.
    AK314413 mRNA. Translation: BAG37034.1 .
    AL355388 Genomic DNA. Translation: CAH72633.1 .
    AL355388 Genomic DNA. Translation: CAH72634.1 .
    BC006410 mRNA. Translation: AAH06410.1 . Different initiation.
    BC018403 mRNA. Translation: AAH18403.1 .
    BC063841 mRNA. Translation: AAH63841.1 .
    AF113544 mRNA. Translation: AAF19084.1 . Different initiation.
    CCDSi CCDS1127.1. [Q9NRR5-1 ]
    RefSeqi NP_064516.2. NM_020131.3. [Q9NRR5-1 ]
    UniGenei Hs.283739.

    3D structure databases

    ProteinModelPortali Q9NRR5.
    SMRi Q9NRR5. Positions 13-83, 555-601.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121223. 180 interactions.
    IntActi Q9NRR5. 151 interactions.
    MINTi MINT-1373057.
    STRINGi 9606.ENSP00000357292.

    PTM databases

    PhosphoSitei Q9NRR5.

    Polymorphism databases

    DMDMi 45476982.

    Proteomic databases

    MaxQBi Q9NRR5.
    PaxDbi Q9NRR5.
    PRIDEi Q9NRR5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368309 ; ENSP00000357292 ; ENSG00000160803 . [Q9NRR5-1 ]
    GeneIDi 56893.
    KEGGi hsa:56893.
    UCSCi uc001fna.3. human. [Q9NRR5-1 ]

    Organism-specific databases

    CTDi 56893.
    GeneCardsi GC01M156005.
    HGNCi HGNC:1237. UBQLN4.
    HPAi HPA027920.
    MIMi 605440. gene.
    neXtProti NX_Q9NRR5.
    PharmGKBi PA25619.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5272.
    HOVERGENi HBG064537.
    InParanoidi Q9NRR5.
    KOi K04523.
    OMAi FGMSRTT.
    OrthoDBi EOG7HF1J8.
    PhylomeDBi Q9NRR5.
    TreeFami TF314412.

    Miscellaneous databases

    ChiTaRSi UBQLN4. human.
    GenomeRNAii 56893.
    NextBioi 62315.
    PROi Q9NRR5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NRR5.
    CleanExi HS_UBQLN4.
    Genevestigatori Q9NRR5.

    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. "Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein."
      Davidson J.D., Riley B., Burright E.N., Duvick L.A., Zoghbi H.Y., Orr H.T.
      Hum. Mol. Genet. 9:2305-2312(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH ATXN1/SCA1, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "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 AND 2), VARIANT MET-495.
      Tissue: Brain.
    3. "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].
    4. "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, Colon and PNS.
    5. "Identification of two paralogous regions mapping to the short and long arms of human chromosome 2 comprising LIS1 pseudogenes."
      Fogli A., Giglio S., Lo Nigro C., Zollo M., Viggiano L., Rocchi M., Archidiacono N., Zuffardi O., Carrozzo R.
      Cytogenet. Cell Genet. 86:225-232(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-601 (ISOFORM 1), VARIANT MET-495.
    6. "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: FUNCTION, INTERACTION WITH UBIQUITIN; ATXN1 AND PSMD4, SUBUNIT, SUBCELLULAR LOCATION, UBIQUITINATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBQL4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRR5
    Secondary accession number(s): A6ND44
    , B2RAY7, Q5VYA0, Q5VYA1, Q9BR98, Q9UHX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: March 15, 2004
    Last modified: October 1, 2014
    This is version 123 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3