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P68036

- UB2L3_HUMAN

UniProt

P68036 - UB2L3_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 L3

Gene

UBE2L3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.7 Publications

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei86 – 861Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. enzyme binding Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. transcription coactivator activity Source: UniProtKB
    7. ubiquitin protein ligase binding Source: UniProtKB
    8. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: UniProtKB
    2. cellular protein modification process Source: UniProtKB
    3. cellular response to glucocorticoid stimulus Source: UniProtKB
    4. cellular response to steroid hormone stimulus Source: UniProtKB
    5. protein K11-linked ubiquitination Source: UniProtKB
    6. protein polyubiquitination Source: UniProtKB
    7. protein ubiquitination Source: UniProtKB
    8. regulation of transcription, DNA-templated Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW
    10. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiP68036.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 L3 (EC:6.3.2.19)
    Alternative name(s):
    L-UBC
    UbcH7
    Ubiquitin carrier protein L3
    Ubiquitin-conjugating enzyme E2-F1
    Ubiquitin-protein ligase L3
    Gene namesi
    Name:UBE2L3
    Synonyms:UBCE7, UBCH7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:12488. UBE2L3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProtKB
    4. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861C → S: Loss of catalytic activity. Prevents ubiquitin-dependent proteasomal degradation of UBE2L3. 2 Publications
    Mutagenesisi88 – 881P → D: Does not convert into a lysine reactive E2; when associated with D-119. 1 Publication
    Mutagenesisi119 – 1191H → D: Does not convert into a lysine reactive E2; when associated with D-88. 1 Publication

    Organism-specific databases

    Orphaneti536. Systemic lupus erythematosus.
    PharmGKBiPA37137.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 154154Ubiquitin-conjugating enzyme E2 L3PRO_0000082476Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91N6-acetyllysine1 Publication
    Modified residuei131 – 1311N6-acetyllysine1 Publication
    Modified residuei138 – 1381N6-acetyllysine1 Publication

    Post-translational modificationi

    Ubiquitinated. The alteration of UBE2L3 protein levels during the S-phase of the cell cycle is due to ubiquitin-dependent proteasomal degradation.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiP68036.
    PaxDbiP68036.
    PRIDEiP68036.

    2D gel databases

    OGPiP51966.
    UCD-2DPAGEP68036.

    PTM databases

    PhosphoSiteiP68036.

    Expressioni

    Tissue specificityi

    Ubiquitous, with highest expression in testis.

    Gene expression databases

    ArrayExpressiP68036.
    BgeeiP68036.
    CleanExiHS_UBE2L3.
    GenevestigatoriP68036.

    Organism-specific databases

    HPAiHPA045609.

    Interactioni

    Subunit structurei

    Interacts with PARK2; involved in ubiquitination and degradation of misfolded proteins. Interacts with UBE3A; used by the papilloma virus HPV-16 E6 protein to ubiquitinate p53/TP53. Interacts with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they functionally interact to regulate progesterone receptor transcriptional activity. May interact with NR3C1.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARIH2O953763EBI-711173,EBI-711158
    RNF19BQ6ZMZ02EBI-711173,EBI-2466594

    Protein-protein interaction databases

    BioGridi113180. 102 interactions.
    DIPiDIP-6124N.
    IntActiP68036. 22 interactions.
    MINTiMINT-5002693.
    STRINGi9606.ENSP00000344259.

    Structurei

    Secondary structure

    1
    154
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 115
    Beta strandi15 – 173
    Beta strandi23 – 253
    Beta strandi30 – 3910
    Beta strandi43 – 453
    Beta strandi51 – 566
    Turni59 – 635
    Beta strandi67 – 726
    Beta strandi77 – 793
    Beta strandi81 – 844
    Turni88 – 903
    Beta strandi91 – 944
    Helixi101 – 11313
    Beta strandi117 – 1193
    Helixi123 – 1308
    Helixi137 – 1448

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C4ZX-ray2.60D1-154[»]
    1FBVX-ray2.90C1-154[»]
    3SQVX-ray3.30C/D1-154[»]
    3SY2X-ray3.27C/D1-154[»]
    ProteinModelPortaliP68036.
    SMRiP68036. Positions 4-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68036.

    Family & Domainsi

    Domaini

    In contrast to other ubiquitin-conjugating enzymes E2, residues essential for lysine reactivity are absent: Pro and a His residues are present instead of an Asp and an Asp residues in positions 88 and 119,respectively.1 Publication

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    InParanoidiP68036.
    KOiK04552.
    OMAiIALVNDX.
    OrthoDBiEOG7GXPD8.
    PhylomeDBiP68036.
    TreeFamiTF313043.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P68036-1) [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

    MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA    50
    FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK 100
    TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK 150
    RPVD 154
    Length:154
    Mass (Da):17,862
    Last modified:October 11, 2004 - v1
    Checksum:iF5A30243BE3C9985
    GO
    Isoform 2 (identifier: P68036-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         10-41: Missing.

    Show »
    Length:122
    Mass (Da):14,121
    Checksum:iB6D14D8ABF26E365
    GO
    Isoform 3 (identifier: P68036-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: MAASRRLMK → MQVAAGTRGD...AGYRRAHGPE

    Note: No experimental confirmation available.

    Show »
    Length:212
    Mass (Da):24,004
    Checksum:iFBA57DE90E19DA78
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151R → S in BAG61806. (PubMed:14702039)Curated
    Sequence conflicti23 – 231R → C in AAG17922. 1 PublicationCurated
    Sequence conflicti118 – 1181E → K in AAG17922. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 99MAASRRLMK → MQVAAGTRGDTRLQEVALLP QLFDLLVLGQRRARLLRQVP SALAGKDLAQLQAGATLAGY RRAHGPE in isoform 3. 1 PublicationVSP_047342
    Alternative sequencei10 – 4132Missing in isoform 2. 1 PublicationVSP_045152Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81003 mRNA. Translation: AAB36017.1.
    X92962 mRNA. Translation: CAA63538.1.
    AJ000519 mRNA. Translation: CAA04156.1.
    AF300336 Genomic DNA. Translation: AAG17922.1.
    CR456606 mRNA. Translation: CAG30492.1.
    AK293179 mRNA. Translation: BAG56722.1.
    AK299985 mRNA. Translation: BAG61806.1.
    AK311761 mRNA. Translation: BAG34704.1.
    AP000553 Genomic DNA. No translation available.
    AP000557 Genomic DNA. No translation available.
    AP000558 Genomic DNA. No translation available.
    CH471095 Genomic DNA. Translation: EAW59459.1.
    BC053368 mRNA. Translation: AAH53368.1.
    CCDSiCCDS13790.1. [P68036-1]
    CCDS58795.1. [P68036-3]
    CCDS58796.1. [P68036-2]
    RefSeqiNP_001243284.1. NM_001256355.1. [P68036-3]
    NP_001243285.1. NM_001256356.1. [P68036-2]
    NP_003338.1. NM_003347.3. [P68036-1]
    UniGeneiHs.108104.

    Genome annotation databases

    EnsembliENST00000342192; ENSP00000344259; ENSG00000185651. [P68036-1]
    ENST00000458578; ENSP00000400906; ENSG00000185651. [P68036-3]
    ENST00000545681; ENSP00000445931; ENSG00000185651. [P68036-2]
    GeneIDi7332.
    KEGGihsa:7332.
    UCSCiuc002zuz.2. human. [P68036-1]
    uc011aig.3. human.

    Polymorphism databases

    DMDMi54039805.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81003 mRNA. Translation: AAB36017.1 .
    X92962 mRNA. Translation: CAA63538.1 .
    AJ000519 mRNA. Translation: CAA04156.1 .
    AF300336 Genomic DNA. Translation: AAG17922.1 .
    CR456606 mRNA. Translation: CAG30492.1 .
    AK293179 mRNA. Translation: BAG56722.1 .
    AK299985 mRNA. Translation: BAG61806.1 .
    AK311761 mRNA. Translation: BAG34704.1 .
    AP000553 Genomic DNA. No translation available.
    AP000557 Genomic DNA. No translation available.
    AP000558 Genomic DNA. No translation available.
    CH471095 Genomic DNA. Translation: EAW59459.1 .
    BC053368 mRNA. Translation: AAH53368.1 .
    CCDSi CCDS13790.1. [P68036-1 ]
    CCDS58795.1. [P68036-3 ]
    CCDS58796.1. [P68036-2 ]
    RefSeqi NP_001243284.1. NM_001256355.1. [P68036-3 ]
    NP_001243285.1. NM_001256356.1. [P68036-2 ]
    NP_003338.1. NM_003347.3. [P68036-1 ]
    UniGenei Hs.108104.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C4Z X-ray 2.60 D 1-154 [» ]
    1FBV X-ray 2.90 C 1-154 [» ]
    3SQV X-ray 3.30 C/D 1-154 [» ]
    3SY2 X-ray 3.27 C/D 1-154 [» ]
    ProteinModelPortali P68036.
    SMRi P68036. Positions 4-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113180. 102 interactions.
    DIPi DIP-6124N.
    IntActi P68036. 22 interactions.
    MINTi MINT-5002693.
    STRINGi 9606.ENSP00000344259.

    PTM databases

    PhosphoSitei P68036.

    Polymorphism databases

    DMDMi 54039805.

    2D gel databases

    OGPi P51966.
    UCD-2DPAGE P68036.

    Proteomic databases

    MaxQBi P68036.
    PaxDbi P68036.
    PRIDEi P68036.

    Protocols and materials databases

    DNASUi 7332.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342192 ; ENSP00000344259 ; ENSG00000185651 . [P68036-1 ]
    ENST00000458578 ; ENSP00000400906 ; ENSG00000185651 . [P68036-3 ]
    ENST00000545681 ; ENSP00000445931 ; ENSG00000185651 . [P68036-2 ]
    GeneIDi 7332.
    KEGGi hsa:7332.
    UCSCi uc002zuz.2. human. [P68036-1 ]
    uc011aig.3. human.

    Organism-specific databases

    CTDi 7332.
    GeneCardsi GC22P021903.
    HGNCi HGNC:12488. UBE2L3.
    HPAi HPA045609.
    MIMi 603721. gene.
    neXtProti NX_P68036.
    Orphaneti 536. Systemic lupus erythematosus.
    PharmGKBi PA37137.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    InParanoidi P68036.
    KOi K04552.
    OMAi IALVNDX.
    OrthoDBi EOG7GXPD8.
    PhylomeDBi P68036.
    TreeFami TF313043.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P68036.

    Miscellaneous databases

    ChiTaRSi UBE2L3. human.
    EvolutionaryTracei P68036.
    GeneWikii UBE2L3.
    GenomeRNAii 7332.
    NextBioi 28696.
    PROi P68036.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68036.
    Bgeei P68036.
    CleanExi HS_UBE2L3.
    Genevestigatori P68036.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3."
      Robinson P.A., Leek J.P., Thompson J., Carr I.M., Bailey A., Moynihan T.P., Coletta P.L., Lench N.J., Markham A.F.
      Mamm. Genome 6:725-731(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5."
      Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M.
      J. Biol. Chem. 271:2795-2800(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3."
      Moynihan T.P., Cole C.G., Dunham I., O'Neil L., Markham A.F., Robinson P.A.
      Genomics 51:124-127(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    4. "Is retroposition a common way of spreading ubiquitin-conjugating enzyme genes throughout mammalian genomes?"
      Poloumienko A.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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; 2 AND 3).
      Tissue: Adrenal gland and Thalamus.
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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.
    10. "Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-'N-end rule' protein substrates."
      Blumenfeld N., Gonen H., Mayer A., Smith C.E., Siegel N.R., Schwartz A.L., Ciechanover A.
      J. Biol. Chem. 269:9574-9581(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 53-67; 67-74 AND 101-122.
    11. "Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7."
      Ardley H.C., Moynihan T.P., Markham A.F., Robinson P.A.
      Biochim. Biophys. Acta 1491:57-64(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROMOTER ANALYSIS.
    12. "Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase."
      Shimura H., Hattori N., Kubo S., Mizuno Y., Asakawa S., Minoshima S., Shimizu N., Iwai K., Chiba T., Tanaka K., Suzuki T.
      Nat. Genet. 25:302-305(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PARK2, MUTAGENESIS OF CYS-86.
    13. "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity."
      Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.
      Biochem. Biophys. Res. Commun. 281:706-713(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF19A.
    14. "Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7."
      Ardley H.C., Tan N.G.S., Rose S.A., Markham A.F., Robinson P.A.
      J. Biol. Chem. 276:19640-19647(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARIH1, SUBCELLULAR LOCATION.
    15. "A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels."
      Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.
      Mol. Cell. Biol. 23:2109-2122(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCNB1IP1.
    16. "The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors."
      Verma S., Ismail A., Gao X., Fu G., Li X., O'Malley B.W., Nawaz Z.
      Mol. Cell. Biol. 24:8716-8726(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NCOA1.
    17. "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis."
      Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.
      FEBS Lett. 580:940-947(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF144B.
    18. "UbcH7 interacts with the glucocorticoid receptor and mediates receptor autoregulation."
      Garside H., Waters C., Berry A., Rice L., Ardley H.C., White A., Robinson P.A., Ray D.
      J. Endocrinol. 190:621-629(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
    19. "NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase."
      Fortier J.M., Kornbluth J.
      J. Immunol. 176:6454-6463(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF19B.
    20. Cited for: FUNCTION, INTERACTION WITH ARIH2.
    21. "Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7."
      Whitcomb E.A., Dudek E.J., Liu Q., Taylor A.
      Mol. Biol. Cell 20:1-9(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF CYS-86.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-131 AND LYS-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
      David Y., Ziv T., Admon A., Navon A.
      J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids."
      Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.
      Nature 474:105-108(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, INTERACTION WITH PARK2 AND ARIH1, MUTAGENESIS OF PRO-88 AND HIS-119.
    26. "Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade."
      Huang L., Kinnucan E., Wang G., Beaudenon S., Howley P.M., Huibregtse J.M., Pavletich N.P.
      Science 286:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBE3A.
    27. "Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases."
      Zheng N., Wang P., Jeffrey P.D., Pavletich N.P.
      Cell 102:533-539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH 47-434 OF CBL AND ZAP70.

    Entry informationi

    Entry nameiUB2L3_HUMAN
    AccessioniPrimary (citable) accession number: P68036
    Secondary accession number(s): B2R4A7
    , B4DDG1, B4DSZ4, E7EWS7, P51966, P70653, Q9HAV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 112 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 22
      Human chromosome 22: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3