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P49459

- UBE2A_HUMAN

UniProt

P49459 - UBE2A_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 A

Gene

UBE2A

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

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA.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 sitei88 – 881Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin protein ligase binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    2. DNA repair Source: UniProtKB
    3. histone H2A ubiquitination Source: UniProtKB
    4. in utero embryonic development Source: Ensembl
    5. maternal process involved in female pregnancy Source: Ensembl
    6. positive regulation of cell proliferation Source: UniProtKB
    7. postreplication repair Source: UniProtKB
    8. protein autoubiquitination Source: UniProtKB
    9. protein K11-linked ubiquitination Source: UniProtKB
    10. protein K48-linked ubiquitination Source: UniProtKB
    11. protein polyubiquitination Source: Reactome
    12. response to UV Source: UniProtKB
    13. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator, Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiP49459.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 A (EC:6.3.2.19)
    Alternative name(s):
    RAD6 homolog A
    Short name:
    HR6A
    Short name:
    hHR6A
    Ubiquitin carrier protein A
    Ubiquitin-protein ligase A
    Gene namesi
    Name:UBE2A
    Synonyms:RAD6A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12472. UBE2A.

    Subcellular locationi

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. cytosol Source: Reactome
    3. HULC complex Source: UniProtKB
    4. nuclear chromatin Source: Ensembl
    5. XY body Source: Ensembl

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked, syndromic, Nascimento-type (MRXSN) [MIM:300860]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRXSN features include dysmorphic facies, hirsutism, skin and nails abnormalities, obesity, speech anomalies and seizures.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111R → Q in MRXSN. 1 Publication
    VAR_066627
    Natural varianti23 – 231G → R in MRXSN. 1 Publication
    VAR_066628

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300860. phenotype.
    Orphaneti163956. intellectual disability, X-linked, Nascimento type.
    PharmGKBiPA37122.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 152152Ubiquitin-conjugating enzyme E2 APRO_0000082445Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei120 – 1201Phosphoserine; by CDK91 Publication

    Post-translational modificationi

    Phosphorylation at Ser-120 by CDK9 increases activity towards histone H2B.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49459.
    PaxDbiP49459.
    PRIDEiP49459.

    PTM databases

    PhosphoSiteiP49459.

    Expressioni

    Gene expression databases

    ArrayExpressiP49459.
    BgeeiP49459.
    CleanExiHS_UBE2A.
    GenevestigatoriP49459.

    Interactioni

    Subunit structurei

    Interacts with RAD18 and WAC.1 Publication

    Protein-protein interaction databases

    BioGridi113167. 46 interactions.
    DIPiDIP-24260N.
    IntActiP49459. 18 interactions.
    MINTiMINT-267059.
    STRINGi9606.ENSP00000360613.

    Structurei

    3D structure databases

    ProteinModelPortaliP49459.
    SMRiP49459. Positions 2-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiP49459.
    KOiK10573.
    OMAiPVPDNVM.
    OrthoDBiEOG7M0NTH.
    PhylomeDBiP49459.
    TreeFamiTF101128.

    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: P49459-1) [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

    MSTPARRRLM RDFKRLQEDP PAGVSGAPSE NNIMVWNAVI FGPEGTPFED    50
    GTFKLTIEFT EEYPNKPPTV RFVSKMFHPN VYADGSICLD ILQNRWSPTY 100
    DVSSILTSIQ SLLDEPNPNS PANSQAAQLY QENKREYEKR VSAIVEQSWR 150
    DC 152
    Length:152
    Mass (Da):17,315
    Last modified:August 4, 2003 - v2
    Checksum:i0AAEB5B7770E47E2
    GO
    Isoform 2 (identifier: P49459-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         51-80: Missing.

    Show »
    Length:122
    Mass (Da):13,777
    Checksum:iFE5B4840CF115701
    GO
    Isoform 3 (identifier: P49459-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-75: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:77
    Mass (Da):8,833
    Checksum:iE947FEF59BB7F0AE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491E → G in AAA35981. (PubMed:1717990)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111R → Q in MRXSN. 1 Publication
    VAR_066627
    Natural varianti23 – 231G → R in MRXSN. 1 Publication
    VAR_066628

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7575Missing in isoform 3. CuratedVSP_043851Add
    BLAST
    Alternative sequencei51 – 8030Missing in isoform 2. 1 PublicationVSP_043852Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74524 mRNA. Translation: AAA35981.1.
    AK297696 mRNA. Translation: BAG60054.1.
    AK313092 mRNA. Translation: BAG35916.1.
    DQ068065 Genomic DNA. Translation: AAY46159.1.
    AC004913 Genomic DNA. No translation available.
    CH471161 Genomic DNA. Translation: EAW89861.1.
    CH471161 Genomic DNA. Translation: EAW89862.1.
    CH471161 Genomic DNA. Translation: EAW89863.1.
    BC010175 mRNA. Translation: AAH10175.1.
    CCDSiCCDS14580.1. [P49459-1]
    CCDS14581.1. [P49459-2]
    PIRiA41222.
    RefSeqiNP_001269090.1. NM_001282161.1.
    NP_003327.2. NM_003336.3. [P49459-1]
    NP_861427.1. NM_181762.2. [P49459-2]
    UniGeneiHs.379466.

    Genome annotation databases

    EnsembliENST00000346330; ENSP00000335027; ENSG00000077721. [P49459-2]
    ENST00000371558; ENSP00000360613; ENSG00000077721. [P49459-1]
    GeneIDi7319.
    KEGGihsa:7319.
    UCSCiuc004erl.3. human. [P49459-1]
    uc004erm.3. human. [P49459-2]

    Polymorphism databases

    DMDMi33518639.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74524 mRNA. Translation: AAA35981.1 .
    AK297696 mRNA. Translation: BAG60054.1 .
    AK313092 mRNA. Translation: BAG35916.1 .
    DQ068065 Genomic DNA. Translation: AAY46159.1 .
    AC004913 Genomic DNA. No translation available.
    CH471161 Genomic DNA. Translation: EAW89861.1 .
    CH471161 Genomic DNA. Translation: EAW89862.1 .
    CH471161 Genomic DNA. Translation: EAW89863.1 .
    BC010175 mRNA. Translation: AAH10175.1 .
    CCDSi CCDS14580.1. [P49459-1 ]
    CCDS14581.1. [P49459-2 ]
    PIRi A41222.
    RefSeqi NP_001269090.1. NM_001282161.1.
    NP_003327.2. NM_003336.3. [P49459-1 ]
    NP_861427.1. NM_181762.2. [P49459-2 ]
    UniGenei Hs.379466.

    3D structure databases

    ProteinModelPortali P49459.
    SMRi P49459. Positions 2-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113167. 46 interactions.
    DIPi DIP-24260N.
    IntActi P49459. 18 interactions.
    MINTi MINT-267059.
    STRINGi 9606.ENSP00000360613.

    PTM databases

    PhosphoSitei P49459.

    Polymorphism databases

    DMDMi 33518639.

    Proteomic databases

    MaxQBi P49459.
    PaxDbi P49459.
    PRIDEi P49459.

    Protocols and materials databases

    DNASUi 7319.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346330 ; ENSP00000335027 ; ENSG00000077721 . [P49459-2 ]
    ENST00000371558 ; ENSP00000360613 ; ENSG00000077721 . [P49459-1 ]
    GeneIDi 7319.
    KEGGi hsa:7319.
    UCSCi uc004erl.3. human. [P49459-1 ]
    uc004erm.3. human. [P49459-2 ]

    Organism-specific databases

    CTDi 7319.
    GeneCardsi GC0XP118708.
    HGNCi HGNC:12472. UBE2A.
    MIMi 300860. phenotype.
    312180. gene.
    neXtProti NX_P49459.
    Orphaneti 163956. intellectual disability, X-linked, Nascimento type.
    PharmGKBi PA37122.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233454.
    HOVERGENi HBG063308.
    InParanoidi P49459.
    KOi K10573.
    OMAi PVPDNVM.
    OrthoDBi EOG7M0NTH.
    PhylomeDBi P49459.
    TreeFami TF101128.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P49459.

    Miscellaneous databases

    ChiTaRSi UBE2A. human.
    GeneWikii UBE2A.
    GenomeRNAii 7319.
    NextBioi 28614.
    PROi P49459.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49459.
    Bgeei P49459.
    CleanExi HS_UBE2A.
    Genevestigatori P49459.

    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. "Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6."
      Koken M.H.M., Reynolds P., Jaspers-Dekker I., Prakash L., Prakash S., Bootsma D., Hoeijmakers J.H.J.
      Proc. Natl. Acad. Sci. U.S.A. 88:8865-8869(1991) [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] (ISOFORMS 1 AND 2).
      Tissue: Subthalamic nucleus.
    3. NIEHS SNPs program
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Skin.
    7. "The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions."
      Kim J., Hake S.B., Roeder R.G.
      Mol. Cell 20:759-770(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "UBE2A, which encodes a ubiquitin-conjugating enzyme, is mutated in a novel X-linked mental retardation syndrome."
      Nascimento R.M., Otto P.A., de Brouwer A.P., Vianna-Morgante A.M.
      Am. J. Hum. Genet. 79:549-555(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MRXSN.
    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. "WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription."
      Zhang F., Yu X.
      Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WAC.
    12. "Phosphorylation by cyclin-dependent kinase-9 controls ubiquitin-conjugating enzyme-2A function."
      Shchebet A., Karpiuk O., Kremmer E., Eick D., Johnsen S.A.
      Cell Cycle 11:2122-2127(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-120.
    13. "Novel missense mutations in the ubiquitination-related gene UBE2A cause a recognizable X-linked mental retardation syndrome."
      Budny B., Badura-Stronka M., Materna-Kiryluk A., Tzschach A., Raynaud M., Latos-Bielenska A., Ropers H.H.
      Clin. Genet. 77:541-551(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MRXSN GLN-11 AND ARG-23.

    Entry informationi

    Entry nameiUBE2A_HUMAN
    AccessioniPrimary (citable) accession number: P49459
    Secondary accession number(s): A6NFE9
    , A6NGR2, A6NMF5, B2R7R9, D3DWI1, Q4TTG1, Q96FX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: August 4, 2003
    Last modified: October 1, 2014
    This is version 136 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 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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