Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P63146

- UBE2B_HUMAN

UniProt

P63146 - UBE2B_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 B

Gene

UBE2B

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'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth.5 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. canonical Wnt signaling pathway Source: UniProtKB
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. cellular response to insulin stimulus Source: Ensembl
    4. chiasma assembly Source: Ensembl
    5. DNA repair Source: UniProtKB
    6. histone H2A ubiquitination Source: UniProtKB
    7. histone lysine demethylation Source: Ensembl
    8. in utero embryonic development Source: Ensembl
    9. maintenance of chromatin silencing Source: Ensembl
    10. negative regulation of apoptotic process Source: Ensembl
    11. negative regulation of cAMP-mediated signaling Source: UniProtKB
    12. negative regulation of histone phosphorylation Source: Ensembl
    13. positive regulation of reciprocal meiotic recombination Source: Ensembl
    14. postreplication repair Source: UniProtKB
    15. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    16. protein autoubiquitination Source: UniProtKB
    17. protein K11-linked ubiquitination Source: UniProtKB
    18. protein K48-linked ubiquitination Source: UniProtKB
    19. protein K63-linked ubiquitination Source: UniProtKB
    20. protein monoubiquitination Source: UniProtKB
    21. protein polyubiquitination Source: UniProtKB
    22. protein stabilization Source: UniProtKB
    23. protein ubiquitination Source: UniProtKB
    24. response to drug Source: UniProtKB
    25. response to hypoxia Source: Ensembl
    26. response to UV Source: UniProtKB
    27. spermatogenesis Source: UniProtKB
    28. sperm axoneme assembly Source: Ensembl
    29. synaptonemal complex organization Source: Ensembl
    30. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    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.
    SignaLinkiP63146.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-conjugating enzyme E2 B (EC:6.3.2.19)
    Alternative name(s):
    RAD6 homolog B
    Short name:
    HR6B
    Short name:
    hHR6B
    Ubiquitin carrier protein B
    Ubiquitin-conjugating enzyme E2-17 kDa
    Ubiquitin-protein ligase B
    Gene namesi
    Name:UBE2B
    Synonyms:RAD6B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:12473. UBE2B.

    Subcellular locationi

    Cell membrane By similarity. Nucleus By similarity
    Note: In peripheral neurons, expressed both at the plasma membrane and in nuclei.By similarity

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. HULC complex Source: UniProtKB
    4. nuclear chromatin Source: Ensembl
    5. nucleus Source: UniProtKB
    6. plasma membrane Source: UniProtKB-SubCell
    7. replication fork Source: UniProtKB
    8. XY body Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37123.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 152152Ubiquitin-conjugating enzyme E2 BPRO_0000082447Add
    BLAST

    Proteomic databases

    MaxQBiP63146.
    PaxDbiP63146.
    PRIDEiP63146.

    Expressioni

    Gene expression databases

    ArrayExpressiP63146.
    BgeeiP63146.
    CleanExiHS_UBE2B.
    GenevestigatoriP63146.

    Interactioni

    Subunit structurei

    Interacts with RAD18, UBR2 and WAC.2 Publications

    Protein-protein interaction databases

    BioGridi113168. 58 interactions.
    DIPiDIP-29832N.
    IntActiP63146. 16 interactions.
    MINTiMINT-97455.
    STRINGi9606.ENSP00000265339.

    Structurei

    Secondary structure

    1
    152
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1815
    Beta strandi24 – 296
    Beta strandi32 – 4110
    Turni47 – 504
    Beta strandi52 – 587
    Turni61 – 655
    Beta strandi69 – 746
    Beta strandi85 – 873
    Helixi90 – 923
    Turni93 – 953
    Helixi102 – 11312
    Helixi124 – 1329
    Helixi134 – 14714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JASNMR-A1-152[»]
    1NXAmodel-A1-152[»]
    2Y4WNMR-A1-152[»]
    2YB6X-ray1.50A1-152[»]
    2YBFX-ray2.00A1-152[»]
    ProteinModelPortaliP63146.
    SMRiP63146. Positions 3-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63146.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233454.
    HOVERGENiHBG063308.
    InParanoidiP63146.
    KOiK10574.
    OMAiIVEQSWV.
    OrthoDBiEOG7M0NTH.
    PhylomeDBiP63146.
    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]

    Sequencei

    Sequence statusi: Complete.

    P63146-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPARRRLM RDFKRLQEDP PVGVSGAPSE NNIMQWNAVI FGPEGTPFED    50
    GTFKLVIEFS EEYPNKPPTV RFLSKMFHPN VYADGSICLD ILQNRWSPTY 100
    DVSSILTSIQ SLLDEPNPNS PANSQAAQLY QENKREYEKR VSAIVEQSWN 150
    DS 152
    Length:152
    Mass (Da):17,312
    Last modified:September 27, 2004 - v1
    Checksum:iCFDEEEE7E06840BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 232VG → C(PubMed:1883845)Curated
    Sequence conflicti41 – 411F → I(PubMed:1883845)Curated
    Sequence conflicti54 – 541K → R(PubMed:1883845)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74525 mRNA. Translation: AAA35982.1.
    X53251 mRNA. Translation: CAA37339.1.
    BT007071 mRNA. Translation: AAP35734.1.
    CR407634 mRNA. Translation: CAG28562.1.
    DQ090910 Genomic DNA. Translation: AAY68224.1.
    AK312012 mRNA. Translation: BAG34950.1.
    CH471062 Genomic DNA. Translation: EAW62257.1.
    CH471062 Genomic DNA. Translation: EAW62258.1.
    BC005979 mRNA. Translation: AAH05979.1.
    BC008404 mRNA. Translation: AAH08404.1.
    BC008470 mRNA. Translation: AAH08470.1.
    CCDSiCCDS4174.1.
    PIRiB41222.
    RefSeqiNP_003328.1. NM_003337.3.
    UniGeneiHs.612096.
    Hs.730071.

    Genome annotation databases

    EnsembliENST00000265339; ENSP00000265339; ENSG00000119048.
    GeneIDi7320.
    KEGGihsa:7320.
    UCSCiuc003kzh.3. human.

    Polymorphism databases

    DMDMi52783814.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74525 mRNA. Translation: AAA35982.1 .
    X53251 mRNA. Translation: CAA37339.1 .
    BT007071 mRNA. Translation: AAP35734.1 .
    CR407634 mRNA. Translation: CAG28562.1 .
    DQ090910 Genomic DNA. Translation: AAY68224.1 .
    AK312012 mRNA. Translation: BAG34950.1 .
    CH471062 Genomic DNA. Translation: EAW62257.1 .
    CH471062 Genomic DNA. Translation: EAW62258.1 .
    BC005979 mRNA. Translation: AAH05979.1 .
    BC008404 mRNA. Translation: AAH08404.1 .
    BC008470 mRNA. Translation: AAH08470.1 .
    CCDSi CCDS4174.1.
    PIRi B41222.
    RefSeqi NP_003328.1. NM_003337.3.
    UniGenei Hs.612096.
    Hs.730071.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JAS NMR - A 1-152 [» ]
    1NXA model - A 1-152 [» ]
    2Y4W NMR - A 1-152 [» ]
    2YB6 X-ray 1.50 A 1-152 [» ]
    2YBF X-ray 2.00 A 1-152 [» ]
    ProteinModelPortali P63146.
    SMRi P63146. Positions 3-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113168. 58 interactions.
    DIPi DIP-29832N.
    IntActi P63146. 16 interactions.
    MINTi MINT-97455.
    STRINGi 9606.ENSP00000265339.

    Polymorphism databases

    DMDMi 52783814.

    Proteomic databases

    MaxQBi P63146.
    PaxDbi P63146.
    PRIDEi P63146.

    Protocols and materials databases

    DNASUi 7320.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265339 ; ENSP00000265339 ; ENSG00000119048 .
    GeneIDi 7320.
    KEGGi hsa:7320.
    UCSCi uc003kzh.3. human.

    Organism-specific databases

    CTDi 7320.
    GeneCardsi GC05P133706.
    HGNCi HGNC:12473. UBE2B.
    MIMi 179095. gene.
    neXtProti NX_P63146.
    PharmGKBi PA37123.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233454.
    HOVERGENi HBG063308.
    InParanoidi P63146.
    KOi K10574.
    OMAi IVEQSWV.
    OrthoDBi EOG7M0NTH.
    PhylomeDBi P63146.
    TreeFami TF101128.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki P63146.

    Miscellaneous databases

    ChiTaRSi UBE2B. human.
    EvolutionaryTracei P63146.
    GeneWikii UBE2B.
    GenomeRNAii 7320.
    NextBioi 28622.
    PROi P63146.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63146.
    Bgeei P63146.
    CleanExi HS_UBE2B.
    Genevestigatori P63146.

    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. "The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the yeast DNA repair gene RAD6."
      Schneider R., Eckerskorn C., Lottspeich F., Schweiger M.
      EMBO J. 9:1431-1435(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Placenta.
    2. "Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating enzyme encoded by yeast DNA repair gene RAD6."
      Woffendin C., Chen Z.Y., Staskus K., Retzel E.F., Plagemann P.G.
      Biochim. Biophys. Acta 1090:81-85(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "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], FUNCTION.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Tissue: Brain.
    7. NIEHS SNPs program
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [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].
      Tissue: Bone marrow and Brain.
    10. "The human RAD18 gene product interacts with HHR6A and HHR6B."
      Xin H., Lin W., Sumanasekera W., Zhang Y., Wu X., Wang Z.
      Nucleic Acids Res. 28:2847-2854(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD18.
    11. "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.
    12. "Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination."
      Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.
      J. Cell Biol. 175:703-708(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen."
      Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., Hurwitz J., Prakash L., Prakash S., Haracska L.
      Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "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.
    15. "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.
    16. "The NMR structure of the class I human ubiquitin-conjugating enzyme 2b."
      Miura T., Klaus W., Ross A., Guntert P., Senn H.
      J. Biomol. NMR 22:89-92(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiUBE2B_HUMAN
    AccessioniPrimary (citable) accession number: P63146
    Secondary accession number(s): B2R503
    , D3DQA2, P23567, Q4PJ15, Q9D0J6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: September 27, 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 5
      Human chromosome 5: 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