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P51965

- UB2E1_HUMAN

UniProt

P51965 - UB2E1_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 E1

Gene

UBE2E1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination.2 Publications

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei131 – 1311Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ISG15 ligase activity Source: HGNC
    3. protein binding Source: IntAct
    4. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. cytokine-mediated signaling pathway Source: Reactome
    3. histone H2B ubiquitination Source: UniProtKB
    4. histone monoubiquitination Source: UniProtKB
    5. ISG15-protein conjugation Source: HGNC
    6. mitotic cell cycle Source: Reactome
    7. mitotic spindle assembly checkpoint Source: Reactome
    8. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    9. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    10. protein K48-linked ubiquitination Source: UniProtKB
    11. protein polyubiquitination Source: UniProtKB
    12. protein ubiquitination Source: BHF-UCL
    13. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiP51965.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 E1 (EC:6.3.2.19)
    Alternative name(s):
    UbcH6
    Ubiquitin carrier protein E1
    Ubiquitin-protein ligase E1
    Gene namesi
    Name:UBE2E1
    Synonyms:UBCH6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12477. UBE2E1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37127.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 193192Ubiquitin-conjugating enzyme E2 E1PRO_0000082470Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)

    Post-translational modificationi

    ISGylation suppresses ubiquitin E2 enzyme activity.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP51965.
    PaxDbiP51965.
    PRIDEiP51965.

    PTM databases

    PhosphoSiteiP51965.

    Expressioni

    Gene expression databases

    ArrayExpressiP51965.
    BgeeiP51965.
    CleanExiHS_UBE2E1.
    GenevestigatoriP51965.

    Organism-specific databases

    HPAiHPA030445.

    Interactioni

    Subunit structurei

    Interacts with RNF14.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PAF1Q8N7H52EBI-348546,EBI-2607770
    RNF11Q9Y3C52EBI-348546,EBI-396669
    RNF20Q5VTR22EBI-348546,EBI-2372238
    ZNRF1Q8ND253EBI-348546,EBI-2129250

    Protein-protein interaction databases

    BioGridi113172. 106 interactions.
    IntActiP51965. 62 interactions.
    MINTiMINT-109083.
    STRINGi9606.ENSP00000303709.

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 243
    Helixi42 – 6120
    Beta strandi67 – 748
    Beta strandi78 – 847
    Turni90 – 934
    Beta strandi95 – 1017
    Turni104 – 1085
    Beta strandi112 – 1176
    Helixi133 – 1353
    Turni136 – 1383
    Helixi145 – 15713
    Helixi167 – 1759
    Helixi177 – 19115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XR9X-ray1.79C83-91[»]
    3BZHX-ray1.60A1-193[»]
    4JJQX-ray1.95B5-14[»]
    ProteinModelPortaliP51965.
    SMRiP51965. Positions 21-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51965.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 1810Poly-Ser

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    InParanoidiP51965.
    KOiK06689.
    OMAiLSHRRIP.
    OrthoDBiEOG7PCJGX.
    PhylomeDBiP51965.
    TreeFamiTF101117.

    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.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51965-1) [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

    MSDDDSRAST SSSSSSSSNQ QTEKETNTPK KKESKVSMSK NSKLLSTSAK    50
    RIQKELADIT LDPPPNCSAG PKGDNIYEWR STILGPPGSV YEGGVFFLDI 100
    TFTPEYPFKP PKVTFRTRIY HCNINSQGVI CLDILKDNWS PALTISKVLL 150
    SICSLLTDCN PADPLVGSIA TQYMTNRAEH DRMARQWTKR YAT 193
    Length:193
    Mass (Da):21,404
    Last modified:October 1, 1996 - v1
    Checksum:i2FBC50BE2A6A0008
    GO
    Isoform 2 (identifier: P51965-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-50: MSDDDSRASTSSSSSSSSNQQTEKETNTPKKKESKVSMSKNSKLLSTSAK → MKEVGRPREVRGRPGKS

    Note: No experimental confirmation available.

    Show »
    Length:160
    Mass (Da):18,000
    Checksum:i412FAB80EBA7A2A7
    GO
    Isoform 3 (identifier: P51965-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         51-67: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:176
    Mass (Da):19,499
    Checksum:i4CFBF51A6FB61C8C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311C → R in BI223271. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251E → D.
    Corresponds to variant rs36060625 [ dbSNP | Ensembl ].
    VAR_061868

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5050MSDDD…STSAK → MKEVGRPREVRGRPGKS in isoform 2. 1 PublicationVSP_045884Add
    BLAST
    Alternative sequencei51 – 6717Missing in isoform 3. 1 PublicationVSP_047200Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92963 mRNA. Translation: CAA63539.1.
    AK314854 mRNA. Translation: BAG37371.1.
    AC020626 Genomic DNA. No translation available.
    AC124914 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64329.1.
    CH471055 Genomic DNA. Translation: EAW64331.1.
    CH471055 Genomic DNA. Translation: EAW64332.1.
    BC009139 mRNA. Translation: AAH09139.1.
    BI223271 mRNA. No translation available.
    BI666638 mRNA. No translation available.
    CCDSiCCDS2638.1. [P51965-1]
    CCDS2639.1. [P51965-3]
    CCDS56244.1. [P51965-2]
    RefSeqiNP_001189405.1. NM_001202476.1. [P51965-2]
    NP_003332.1. NM_003341.4. [P51965-1]
    NP_872607.1. NM_182666.2. [P51965-3]
    UniGeneiHs.164853.

    Genome annotation databases

    EnsembliENST00000306627; ENSP00000303709; ENSG00000170142. [P51965-1]
    ENST00000346855; ENSP00000329113; ENSG00000170142. [P51965-3]
    ENST00000424381; ENSP00000411351; ENSG00000170142. [P51965-2]
    GeneIDi7324.
    KEGGihsa:7324.
    UCSCiuc003cch.3. human. [P51965-1]
    uc003cci.3. human.
    uc021wua.1. human.

    Polymorphism databases

    DMDMi1717857.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92963 mRNA. Translation: CAA63539.1 .
    AK314854 mRNA. Translation: BAG37371.1 .
    AC020626 Genomic DNA. No translation available.
    AC124914 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64329.1 .
    CH471055 Genomic DNA. Translation: EAW64331.1 .
    CH471055 Genomic DNA. Translation: EAW64332.1 .
    BC009139 mRNA. Translation: AAH09139.1 .
    BI223271 mRNA. No translation available.
    BI666638 mRNA. No translation available.
    CCDSi CCDS2638.1. [P51965-1 ]
    CCDS2639.1. [P51965-3 ]
    CCDS56244.1. [P51965-2 ]
    RefSeqi NP_001189405.1. NM_001202476.1. [P51965-2 ]
    NP_003332.1. NM_003341.4. [P51965-1 ]
    NP_872607.1. NM_182666.2. [P51965-3 ]
    UniGenei Hs.164853.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XR9 X-ray 1.79 C 83-91 [» ]
    3BZH X-ray 1.60 A 1-193 [» ]
    4JJQ X-ray 1.95 B 5-14 [» ]
    ProteinModelPortali P51965.
    SMRi P51965. Positions 21-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113172. 106 interactions.
    IntActi P51965. 62 interactions.
    MINTi MINT-109083.
    STRINGi 9606.ENSP00000303709.

    PTM databases

    PhosphoSitei P51965.

    Polymorphism databases

    DMDMi 1717857.

    Proteomic databases

    MaxQBi P51965.
    PaxDbi P51965.
    PRIDEi P51965.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306627 ; ENSP00000303709 ; ENSG00000170142 . [P51965-1 ]
    ENST00000346855 ; ENSP00000329113 ; ENSG00000170142 . [P51965-3 ]
    ENST00000424381 ; ENSP00000411351 ; ENSG00000170142 . [P51965-2 ]
    GeneIDi 7324.
    KEGGi hsa:7324.
    UCSCi uc003cch.3. human. [P51965-1 ]
    uc003cci.3. human.
    uc021wua.1. human.

    Organism-specific databases

    CTDi 7324.
    GeneCardsi GC03P023847.
    HGNCi HGNC:12477. UBE2E1.
    HPAi HPA030445.
    MIMi 602916. gene.
    neXtProti NX_P51965.
    PharmGKBi PA37127.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    InParanoidi P51965.
    KOi K06689.
    OMAi LSHRRIP.
    OrthoDBi EOG7PCJGX.
    PhylomeDBi P51965.
    TreeFami TF101117.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P51965.

    Miscellaneous databases

    EvolutionaryTracei P51965.
    GeneWikii UBE2E1.
    GenomeRNAii 7324.
    NextBioi 28656.
    PROi P51965.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51965.
    Bgeei P51965.
    CleanExi HS_UBE2E1.
    Genevestigatori P51965.

    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. "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).
    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] (ISOFORM 1).
      Tissue: Amygdala.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [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] (ISOFORMS 1; 2 AND 3).
      Tissue: Cervix carcinoma, Colon and Hypothalamus.
    6. "Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme."
      Takeuchi T., Iwahara S., Saeki Y., Sasajima H., Yokosawa H.
      J. Biochem. 138:711-719(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ISGYLATION AT LYS-136.
    7. "The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide."
      Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R., Wahren-Herlenius M.
      Exp. Cell Res. 314:3605-3613(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUB2E1_HUMAN
    AccessioniPrimary (citable) accession number: P51965
    Secondary accession number(s): B2RBX4, C9J8K2, K4DI90
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 148 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3