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Q8TBC4

- UBA3_HUMAN

UniProt

Q8TBC4 - UBA3_HUMAN

Protein

NEDD8-activating enzyme E1 catalytic subunit

Gene

UBA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression.3 Publications

    Enzyme regulationi

    Binding of TP53BP2 to the regulatory subunit NAE1 decreases activity.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei211 – 2111Determines specificity for NEDD8
    Active sitei237 – 2371Glycyl thioester intermediate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi100 – 12425ATP1 PublicationAdd
    BLAST
    Nucleotide bindingi148 – 17124ATP1 PublicationAdd
    BLAST

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. NEDD8 activating enzyme activity Source: RefGenome
    4. protein binding Source: UniProtKB
    5. protein heterodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. endomitotic cell cycle Source: Ensembl
    3. protein neddylation Source: RefGenome
    4. proteolysis Source: ProtInc
    5. regulation of cell cycle Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00885.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NEDD8-activating enzyme E1 catalytic subunit (EC:6.3.2.-)
    Alternative name(s):
    NEDD8-activating enzyme E1C
    Ubiquitin-activating enzyme E1C
    Ubiquitin-like modifier-activating enzyme 3
    Short name:
    Ubiquitin-activating enzyme 3
    Gene namesi
    Name:UBA3
    Synonyms:UBE1C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12470. UBA3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RefGenome
    2. nucleus Source: LIFEdb

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651F → G: Reduces affinity for UBE2M. 1 Publication
    Mutagenesisi148 – 1481I → A: No effect on NEDD8 adenylation. 1 Publication
    Mutagenesisi160 – 1612HI → AA: Reduces affinity for UBE2M.
    Mutagenesisi167 – 1671D → A: Abolishes NEDD8 adenylation. 1 Publication
    Mutagenesisi192 – 1921P → A: Reduces affinity for UBE2M; when associated with A-195 and A-197. 1 Publication
    Mutagenesisi195 – 1951I → A: Reduces affinity for UBE2M; when associated with A-192 and A-197. 1 Publication
    Mutagenesisi197 – 1971P → A: Reduces affinity for UBE2M; when associated with A-192 and A-195. 1 Publication
    Mutagenesisi211 – 2111R → Q: Abolishes specificity for NEDD8. 1 Publication
    Mutagenesisi214 – 2141L → A: Reduces affinity for UBE2M; when associated with A-217. 1 Publication
    Mutagenesisi217 – 2171M → A: Reduces affinity for UBE2M; when associated with A-214. 1 Publication
    Mutagenesisi227 – 2282LY → DD: Strongly reduces NEDD8 adenylation.
    Mutagenesisi237 – 2371C → S: Abolishes thioester intermediate formation. 1 Publication
    Mutagenesisi238 – 2381T → A: No effect on NEDD8 adenylation; impairs thioester intermediate formation. 1 Publication
    Mutagenesisi310 – 3101I → A: No effect on NEDD8 adenylation or thioester intermediate formation; impairs NEDD8 transfer to UBE2M. 1 Publication
    Mutagenesisi331 – 3311I → A: Reduces affinity for UBE2M. 1 Publication
    Mutagenesisi352 – 3576YTYTFE → ATATA: Abolishes NEDD8 adenylation.
    Mutagenesisi368 – 3681S → P: Impairs NEDD8 transfer to UBE2M. 1 Publication
    Mutagenesisi369 – 3691Q → P: No effect on NEDD8 transfer to UBE2M. 1 Publication
    Mutagenesisi370 – 3701L → P: Impairs NEDD8 transfer to UBE2M. 1 Publication
    Mutagenesisi412 – 4121T → A: Impairs NEDD8 transfer to UBE2M. 1 Publication
    Mutagenesisi415 – 4151L → A: Impairs NEDD8 transfer to UBE2M. 1 Publication
    Mutagenesisi418 – 4181V → A: Impairs NEDD8 transfer to UBE2M. 1 Publication
    Mutagenesisi421 – 4211I → A: Impairs NEDD8 transfer to UBE2M. 1 Publication
    Mutagenesisi424 – 4241R → A: No effect on NEDD8 transfer to UBE2M. 1 Publication

    Organism-specific databases

    PharmGKBiPA162407622.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 463462NEDD8-activating enzyme E1 catalytic subunitPRO_0000194941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8TBC4.
    PaxDbiQ8TBC4.
    PRIDEiQ8TBC4.

    PTM databases

    PhosphoSiteiQ8TBC4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ8TBC4.
    BgeeiQ8TBC4.
    CleanExiHS_UBA3.
    GenevestigatoriQ8TBC4.

    Organism-specific databases

    HPAiHPA034873.
    HPA034874.

    Interactioni

    Subunit structurei

    Heterodimer of UBA3 and NAE1. Interacts with NEDD8, UBE2F and UBE2M. Binds ESR1 and ESR2 with bound steroid ligand By similarity. Interacts with TBATA By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAD23BP547272EBI-717567,EBI-954531
    UBE2MP610812EBI-717567,EBI-1041660

    Protein-protein interaction databases

    BioGridi114503. 26 interactions.
    IntActiQ8TBC4. 12 interactions.
    MINTiMINT-1375257.
    STRINGi9606.ENSP00000354340.

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni35 – 384
    Helixi39 – 468
    Helixi62 – 687
    Beta strandi72 – 754
    Helixi80 – 9011
    Beta strandi96 – 1005
    Helixi106 – 1083
    Turni109 – 1113
    Helixi117 – 1193
    Helixi124 – 13512
    Beta strandi142 – 1465
    Helixi148 – 1503
    Helixi153 – 1564
    Beta strandi160 – 1645
    Helixi169 – 18113
    Beta strandi185 – 1884
    Beta strandi189 – 1913
    Helixi192 – 1943
    Beta strandi198 – 2047
    Beta strandi207 – 2137
    Turni215 – 2173
    Helixi221 – 2277
    Helixi236 – 2416
    Helixi246 – 25510
    Helixi257 – 2604
    Helixi275 – 29117
    Helixi299 – 3068
    Helixi314 – 33320
    Beta strandi341 – 3466
    Beta strandi348 – 3503
    Beta strandi352 – 3565
    Turni365 – 3673
    Beta strandi372 – 3765
    Beta strandi377 – 3793
    Helixi382 – 39110
    Turni393 – 3953
    Beta strandi401 – 4066
    Beta strandi409 – 4146
    Helixi419 – 43012
    Beta strandi431 – 4333
    Helixi434 – 4363
    Helixi437 – 4404
    Beta strandi443 – 4475
    Beta strandi451 – 4533
    Beta strandi455 – 4606

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R4MX-ray3.00B/D/F/H33-463[»]
    1R4NX-ray3.60B/D/F/H33-463[»]
    1TT5X-ray2.60B/D33-463[»]
    1Y8XX-ray2.40B368-463[»]
    1YOVX-ray2.60B/D22-463[»]
    2LQ7NMR-A369-463[»]
    2NVUX-ray2.80B33-463[»]
    3DBHX-ray2.85B/D/F/H33-463[»]
    3DBLX-ray2.90B/D/F/H33-463[»]
    3DBRX-ray3.05B/D/F/H33-463[»]
    3FN1X-ray2.50A368-463[»]
    3GZNX-ray3.00B/D1-463[»]
    ProteinModelPortaliQ8TBC4.
    SMRiQ8TBC4. Positions 33-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TBC4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 7018Interaction with UBE2M N-terminusAdd
    BLAST
    Regioni157 – 1615Interaction with UBE2M N-terminus
    Regioni192 – 21726Interaction with UBE2M N-terminusAdd
    BLAST
    Regioni227 – 2293Interaction with NEDD8
    Regioni242 – 2487Interaction with NAE1
    Regioni292 – 2954Interaction with NAE1
    Regioni331 – 3388Interaction with UBE2M N-terminus
    Regioni352 – 3576Interaction with NEDD8
    Regioni368 – 46396Interaction with UBE2M core domainAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000166793.
    HOVERGENiHBG082736.
    InParanoidiQ8TBC4.
    KOiK10686.
    OMAiDHIQWIF.
    PhylomeDBiQ8TBC4.
    TreeFamiTF300499.

    Family and domain databases

    Gene3Di1.10.10.520. 1 hit.
    3.10.20.260. 1 hit.
    3.40.50.720. 2 hits.
    InterProiIPR014929. E2_binding.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR023318. Ub_act_enz_dom_a.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018074. UBQ-activ_enz_E1_AS.
    [Graphical view]
    PfamiPF08825. E2_bind. 1 hit.
    PF00899. ThiF. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 1 hit.
    PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TBC4-1) [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

    MADGEEPEKK RRRIEELLAE KMAVDGGCGD TGDWEGRWNH VKKFLERSGP    50
    FTHPDFEPST ESLQFLLDTC KVLVIGAGGL GCELLKNLAL SGFRQIHVID 100
    MDTIDVSNLN RQFLFRPKDI GRPKAEVAAE FLNDRVPNCN VVPHFNKIQD 150
    FNDTFYRQFH IIVCGLDSII ARRWINGMLI SLLNYEDGVL DPSSIVPLID 200
    GGTEGFKGNA RVILPGMTAC IECTLELYPP QVNFPMCTIA SMPRLPEHCI 250
    EYVRMLQWPK EQPFGEGVPL DGDDPEHIQW IFQKSLERAS QYNIRGVTYR 300
    LTQGVVKRII PAVASTNAVI AAVCATEVFK IATSAYIPLN NYLVFNDVDG 350
    LYTYTFEAER KENCPACSQL PQNIQFSPSA KLQEVLDYLT NSASLQMKSP 400
    AITATLEGKN RTLYLQSVTS IEERTRPNLS KTLKELGLVD GQELAVADVT 450
    TPQTVLFKLH FTS 463
    Length:463
    Mass (Da):51,852
    Last modified:December 6, 2005 - v2
    Checksum:i4C16DC0EEDE31A76
    GO
    Isoform 2 (identifier: Q8TBC4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         8-21: Missing.

    Show »
    Length:449
    Mass (Da):50,072
    Checksum:iC624B0B917B2482B
    GO

    Sequence cautioni

    The sequence AAC27648.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461N → Y in CAB55996. (PubMed:11230166)Curated
    Sequence conflicti271 – 2711D → G in CAB55996. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91K → R.2 Publications
    Corresponds to variant rs17852113 [ dbSNP | Ensembl ].
    VAR_023945

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei8 – 2114Missing in isoform 2. 1 PublicationVSP_041127Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL117566 mRNA. Translation: CAB55996.2.
    AK002159 mRNA. Translation: BAG51021.1.
    AK289392 mRNA. Translation: BAF82081.1.
    AC092060 Genomic DNA. No translation available.
    AC109587 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65470.1.
    BC022853 mRNA. Translation: AAH22853.1.
    AF046024 mRNA. Translation: AAC27648.1. Different initiation.
    AB012190 mRNA. Translation: BAA33144.1.
    CCDSiCCDS2909.1. [Q8TBC4-1]
    CCDS2910.1. [Q8TBC4-2]
    PIRiT17306.
    RefSeqiNP_003959.3. NM_003968.3. [Q8TBC4-1]
    NP_937838.1. NM_198195.1. [Q8TBC4-2]
    UniGeneiHs.154320.

    Genome annotation databases

    EnsembliENST00000349511; ENSP00000340041; ENSG00000144744. [Q8TBC4-2]
    ENST00000361055; ENSP00000354340; ENSG00000144744. [Q8TBC4-1]
    GeneIDi9039.
    KEGGihsa:9039.
    UCSCiuc003dno.3. human. [Q8TBC4-1]
    uc003dnq.3. human. [Q8TBC4-2]

    Polymorphism databases

    DMDMi83305811.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL117566 mRNA. Translation: CAB55996.2 .
    AK002159 mRNA. Translation: BAG51021.1 .
    AK289392 mRNA. Translation: BAF82081.1 .
    AC092060 Genomic DNA. No translation available.
    AC109587 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65470.1 .
    BC022853 mRNA. Translation: AAH22853.1 .
    AF046024 mRNA. Translation: AAC27648.1 . Different initiation.
    AB012190 mRNA. Translation: BAA33144.1 .
    CCDSi CCDS2909.1. [Q8TBC4-1 ]
    CCDS2910.1. [Q8TBC4-2 ]
    PIRi T17306.
    RefSeqi NP_003959.3. NM_003968.3. [Q8TBC4-1 ]
    NP_937838.1. NM_198195.1. [Q8TBC4-2 ]
    UniGenei Hs.154320.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1R4M X-ray 3.00 B/D/F/H 33-463 [» ]
    1R4N X-ray 3.60 B/D/F/H 33-463 [» ]
    1TT5 X-ray 2.60 B/D 33-463 [» ]
    1Y8X X-ray 2.40 B 368-463 [» ]
    1YOV X-ray 2.60 B/D 22-463 [» ]
    2LQ7 NMR - A 369-463 [» ]
    2NVU X-ray 2.80 B 33-463 [» ]
    3DBH X-ray 2.85 B/D/F/H 33-463 [» ]
    3DBL X-ray 2.90 B/D/F/H 33-463 [» ]
    3DBR X-ray 3.05 B/D/F/H 33-463 [» ]
    3FN1 X-ray 2.50 A 368-463 [» ]
    3GZN X-ray 3.00 B/D 1-463 [» ]
    ProteinModelPortali Q8TBC4.
    SMRi Q8TBC4. Positions 33-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114503. 26 interactions.
    IntActi Q8TBC4. 12 interactions.
    MINTi MINT-1375257.
    STRINGi 9606.ENSP00000354340.

    Chemistry

    ChEMBLi CHEMBL2016430.

    PTM databases

    PhosphoSitei Q8TBC4.

    Polymorphism databases

    DMDMi 83305811.

    Proteomic databases

    MaxQBi Q8TBC4.
    PaxDbi Q8TBC4.
    PRIDEi Q8TBC4.

    Protocols and materials databases

    DNASUi 9039.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000349511 ; ENSP00000340041 ; ENSG00000144744 . [Q8TBC4-2 ]
    ENST00000361055 ; ENSP00000354340 ; ENSG00000144744 . [Q8TBC4-1 ]
    GeneIDi 9039.
    KEGGi hsa:9039.
    UCSCi uc003dno.3. human. [Q8TBC4-1 ]
    uc003dnq.3. human. [Q8TBC4-2 ]

    Organism-specific databases

    CTDi 9039.
    GeneCardsi GC03M069103.
    HGNCi HGNC:12470. UBA3.
    HPAi HPA034873.
    HPA034874.
    MIMi 603172. gene.
    neXtProti NX_Q8TBC4.
    PharmGKBi PA162407622.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000166793.
    HOVERGENi HBG082736.
    InParanoidi Q8TBC4.
    KOi K10686.
    OMAi DHIQWIF.
    PhylomeDBi Q8TBC4.
    TreeFami TF300499.

    Enzyme and pathway databases

    UniPathwayi UPA00885 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi UBA3. human.
    EvolutionaryTracei Q8TBC4.
    GeneWikii UBE1C.
    GenomeRNAii 9039.
    NextBioi 33859.
    PROi Q8TBC4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TBC4.
    Bgeei Q8TBC4.
    CleanExi HS_UBA3.
    Genevestigatori Q8TBC4.

    Family and domain databases

    Gene3Di 1.10.10.520. 1 hit.
    3.10.20.260. 1 hit.
    3.40.50.720. 2 hits.
    InterProi IPR014929. E2_binding.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR023318. Ub_act_enz_dom_a.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018074. UBQ-activ_enz_E1_AS.
    [Graphical view ]
    Pfami PF08825. E2_bind. 1 hit.
    PF00899. ThiF. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 1 hit.
    PROSITEi PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Fetal kidney.
    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).
    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] (ISOFORM 1), VARIANT ARG-9.
      Tissue: Prostatic adenocarcinoma.
    6. "Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway."
      Gong L., Yeh E.T.H.
      J. Biol. Chem. 274:12036-12042(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-463 (ISOFORM 1), VARIANT ARG-9, FUNCTION, MUTAGENESIS OF CYS-237, TISSUE SPECIFICITY.
      Tissue: Placenta.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-463, FUNCTION.
    8. "Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer."
      Bohnsack R.N., Haas A.L.
      J. Biol. Chem. 278:26823-26830(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NAE1.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1."
      Walden H., Podgorski M.S., Huang D.T., Miller D.W., Howard R.J., Minor D.L. Jr., Holton J.M., Schulman B.A.
      Mol. Cell 12:1427-1437(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 33-463 IN COMPLEX WITH NAE1; NEDD8 AND ATP, MUTAGENESIS OF ARG-211.
    12. "Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8."
      Walden H., Podgorski M.S., Schulman B.A.
      Nature 422:330-334(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 24-463 IN COMPLEX WITH NAE1, MUTAGENESIS OF ILE-148; ASP-167; 227-LEU-TYR-228; THR-238; ILE-310 AND 352-TYR--TYR-357.
    13. "A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8."
      Huang D.T., Miller D.W., Mathew R., Cassell R., Holton J.M., Roussel M.F., Schulman B.A.
      Nat. Struct. Mol. Biol. 11:927-935(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 33-463 IN COMPLEX WITH NAE1 AND UBE2M, MUTAGENESIS OF PHE-65; 160-HIS-ILE-161; PRO-192; ILE-195; PRO-197; LEU-214; MET-217 AND ILE-331.
    14. "Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1."
      Huang D.T., Paydar A., Zhuang M., Waddell M.B., Holton J.M., Schulman B.A.
      Mol. Cell 17:341-350(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 368-463 IN COMPLEX WITH UBE2M, MUTAGENESIS OF SER-368; GLN-369; LEU-370; THR-412; LEU-415; VAL-418; ILE-421 AND ARG-424.
    15. "E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification."
      Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.
      Mol. Cell 33:483-495(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 368-420 IN COMPLEX WITH UBE2F.

    Entry informationi

    Entry nameiUBA3_HUMAN
    AccessioniPrimary (citable) accession number: Q8TBC4
    Secondary accession number(s): A6NLB5
    , A8K027, O76088, Q9NTU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 129 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

    Miscellaneous

    Arg-211 acts as a selectivity gate, preventing misactivation of ubiquitin by this NEDD8-specific E1 complex.

    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