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Q13564

- ULA1_HUMAN

UniProt

Q13564 - ULA1_HUMAN

Protein

NEDD8-activating enzyme E1 regulatory subunit

Gene

NAE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Regulatory 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. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation.3 Publications

    Enzyme regulationi

    Binding of TP53BP2 to the regulatory subunit NAE1 decreases neddylation activity.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei211 – 2111Interaction with UBA3

    GO - Molecular functioni

    1. catalytic activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. protein heterodimerization activity Source: UniProtKB
    4. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. mitotic DNA replication checkpoint Source: UniProtKB
    2. neuron apoptotic process Source: UniProtKB
    3. protein neddylation Source: UniProtKB
    4. regulation of apoptotic process Source: UniProtKB
    5. regulation of neuron apoptotic process Source: UniProtKB
    6. signal transduction Source: ProtInc

    Keywords - Biological processi

    Apoptosis, Cell cycle, Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00885.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NEDD8-activating enzyme E1 regulatory subunit
    Alternative name(s):
    Amyloid beta precursor protein-binding protein 1, 59 kDa
    Short name:
    APP-BP1
    Amyloid protein-binding protein 1
    Proto-oncogene protein 1
    Gene namesi
    Name:NAE1
    Synonyms:APPBP1
    ORF Names:HPP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:621. NAE1.

    Subcellular locationi

    Cell membrane 1 Publication
    Note: Colocalizes with APP in lipid rafts.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: RefGenome
    3. nucleus Source: RefGenome
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi331 – 3311D → A: Impairs the formation of the NEDD8-UBA3 thioester. 1 Publication

    Organism-specific databases

    PharmGKBiPA162396730.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 534533NEDD8-activating enzyme E1 regulatory subunitPRO_0000194951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei6 – 61N6-acetyllysine1 Publication
    Modified residuei341 – 3411N6-acetyllysineBy similarity

    Post-translational modificationi

    Ubiquitinated by TRIP12, leading to its degradation by the proteasome.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ13564.
    PaxDbiQ13564.
    PRIDEiQ13564.

    PTM databases

    PhosphoSiteiQ13564.

    Expressioni

    Tissue specificityi

    Ubiquitous in fetal tissues. Expressed throughout the adult brain.1 Publication

    Gene expression databases

    ArrayExpressiQ13564.
    BgeeiQ13564.
    CleanExiHS_NAE1.
    GenevestigatoriQ13564.

    Organism-specific databases

    HPAiHPA041178.
    HPA042041.

    Interactioni

    Subunit structurei

    Heterodimer of UBA3 and NAE1. The complex binds NEDD8 and UBE2M. Binds APP and TP53BP2.3 Publications

    Protein-protein interaction databases

    BioGridi114402. 32 interactions.
    IntActiQ13564. 6 interactions.
    MINTiMINT-1429663.
    STRINGi9606.ENSP00000290810.

    Structurei

    Secondary structure

    1
    534
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1210
    Helixi14 – 3017
    Beta strandi32 – 365
    Helixi40 – 5011
    Turni51 – 533
    Beta strandi55 – 606
    Helixi67 – 726
    Helixi78 – 803
    Helixi85 – 9410
    Beta strandi104 – 1074
    Helixi109 – 1146
    Helixi117 – 1226
    Beta strandi124 – 1307
    Helixi133 – 14513
    Beta strandi150 – 1567
    Beta strandi159 – 1657
    Beta strandi169 – 1724
    Beta strandi185 – 1873
    Helixi190 – 1978
    Beta strandi201 – 2044
    Helixi209 – 2113
    Helixi214 – 22512
    Turni226 – 2294
    Helixi236 – 24914
    Beta strandi257 – 2593
    Helixi262 – 27514
    Helixi283 – 2897
    Helixi292 – 2954
    Beta strandi299 – 3013
    Helixi303 – 31614
    Turni317 – 3215
    Helixi336 – 36631
    Turni367 – 3693
    Beta strandi372 – 3754
    Helixi377 – 3859
    Helixi387 – 3893
    Beta strandi391 – 3933
    Helixi398 – 4025
    Turni404 – 4063
    Helixi409 – 4157
    Helixi423 – 43917
    Turni447 – 4493
    Helixi450 – 46718
    Helixi476 – 4849
    Turni485 – 4873
    Helixi491 – 51020
    Beta strandi520 – 5234
    Turni524 – 5274
    Beta strandi528 – 5314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1R4MX-ray3.00A/C/E/G1-534[»]
    1R4NX-ray3.60A/C/E/G1-534[»]
    1TT5X-ray2.60A/C1-534[»]
    1YOVX-ray2.60A/C1-534[»]
    2NVUX-ray2.80A1-534[»]
    3DBHX-ray2.85A/C/E/G1-534[»]
    3DBLX-ray2.90A/C/E/G1-534[»]
    3DBRX-ray3.05A/C/E/G1-534[»]
    3GZNX-ray3.00A/C1-534[»]
    ProteinModelPortaliQ13564.
    SMRiQ13564. Positions 6-534.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13564.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni331 – 34414Interaction with UBA3Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000216537.
    HOVERGENiHBG079761.
    KOiK04532.
    OMAiTNQYVPI.
    PhylomeDBiQ13564.
    TreeFamiTF313972.

    Family and domain databases

    Gene3Di3.40.50.720. 3 hits.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view]
    PfamiPF00899. ThiF. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13564-1) [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

    MAQLGKLLKE QKYDRQLRLW GDHGQEALES AHVCLINATA TGTEILKNLV    50
    LPGIGSFTII DGNQVSGEDA GNNFFLQRSS IGKNRAEAAM EFLQELNSDV 100
    SGSFVEESPE NLLDNDPSFF CRFTVVVATQ LPESTSLRLA DVLWNSQIPL 150
    LICRTYGLVG YMRIIIKEHP VIESHPDNAL EDLRLDKPFP ELREHFQSYD 200
    LDHMEKKDHS HTPWIVIIAK YLAQWYSETN GRIPKTYKEK EDFRDLIRQG 250
    ILKNENGAPE DEENFEEAIK NVNTALNTTQ IPSSIEDIFN DDRCINITKQ 300
    TPSFWILARA LKEFVAKEGQ GNLPVRGTIP DMIADSGKYI KLQNVYREKA 350
    KKDAAAVGNH VAKLLQSIGQ APESISEKEL KLLCSNSAFL RVVRCRSLAE 400
    EYGLDTINKD EIISSMDNPD NEIVLYLMLR AVDRFHKQQG RYPGVSNYQV 450
    EEDIGKLKSC LTGFLQEYGL SVMVKDDYVH EFCRYGAAEP HTIAAFLGGA 500
    AAQEVIKIIT KQFVIFNNTY IYSGMSQTSA TFQL 534
    Length:534
    Mass (Da):60,246
    Last modified:November 1, 1996 - v1
    Checksum:i5EC8D3ACE6374F21
    GO
    Isoform 2 (identifier: Q13564-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MAQLGKLLKEQKYDRQL → MDAQQTKTNEA

    Note: No experimental confirmation available.

    Show »
    Length:528
    Mass (Da):59,420
    Checksum:iF3732BF1F365C633
    GO
    Isoform 3 (identifier: Q13564-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-89: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:445
    Mass (Da):50,624
    Checksum:i0E6DF500733F61E6
    GO
    Isoform 4 (identifier: Q13564-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         53-53: G → GNVG

    Show »
    Length:537
    Mass (Da):60,517
    Checksum:i9F3D01503E29A668
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti268 – 2681A → V in BAG53511. (PubMed:14702039)Curated
    Sequence conflicti285 – 2851I → T in BAG53511. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011S → F.
    Corresponds to variant rs363212 [ dbSNP | Ensembl ].
    VAR_052435

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8989Missing in isoform 3. CuratedVSP_054258Add
    BLAST
    Alternative sequencei1 – 1717MAQLG…YDRQL → MDAQQTKTNEA in isoform 2. 1 PublicationVSP_042895Add
    BLAST
    Alternative sequencei53 – 531G → GNVG in isoform 4. 1 PublicationVSP_054259

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50939 mRNA. Translation: AAC50477.1.
    AY197612 mRNA. Translation: AAP35030.1.
    AK097680 mRNA. Translation: BAG53511.1.
    AK298159 mRNA. Translation: BAH12735.1.
    AK312784 mRNA. Translation: BAG35647.1.
    AC004638 Genomic DNA. Translation: AAC23784.1.
    AC044802 Genomic DNA. No translation available.
    AL136798 mRNA. Translation: CAB66732.1.
    CH471092 Genomic DNA. Translation: EAW83042.1.
    BC000480 mRNA. Translation: AAH00480.1.
    BC013301 mRNA. Translation: AAH13301.1.
    CCDSiCCDS10820.1. [Q13564-1]
    CCDS42171.1. [Q13564-2]
    CCDS42172.1. [Q13564-3]
    CCDS67050.1. [Q13564-4]
    RefSeqiNP_001018169.1. NM_001018159.1. [Q13564-2]
    NP_001018170.1. NM_001018160.1. [Q13564-3]
    NP_001273429.1. NM_001286500.1. [Q13564-4]
    NP_003896.1. NM_003905.3. [Q13564-1]
    XP_005256272.1. XM_005256215.1. [Q13564-3]
    UniGeneiHs.460978.

    Genome annotation databases

    EnsembliENST00000290810; ENSP00000290810; ENSG00000159593. [Q13564-1]
    ENST00000359087; ENSP00000351990; ENSG00000159593. [Q13564-4]
    ENST00000379463; ENSP00000368776; ENSG00000159593. [Q13564-2]
    ENST00000394074; ENSP00000377637; ENSG00000159593. [Q13564-3]
    GeneIDi8883.
    KEGGihsa:8883.
    UCSCiuc002eqe.3. human. [Q13564-2]
    uc002eqf.3. human. [Q13564-1]

    Polymorphism databases

    DMDMi50400302.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50939 mRNA. Translation: AAC50477.1 .
    AY197612 mRNA. Translation: AAP35030.1 .
    AK097680 mRNA. Translation: BAG53511.1 .
    AK298159 mRNA. Translation: BAH12735.1 .
    AK312784 mRNA. Translation: BAG35647.1 .
    AC004638 Genomic DNA. Translation: AAC23784.1 .
    AC044802 Genomic DNA. No translation available.
    AL136798 mRNA. Translation: CAB66732.1 .
    CH471092 Genomic DNA. Translation: EAW83042.1 .
    BC000480 mRNA. Translation: AAH00480.1 .
    BC013301 mRNA. Translation: AAH13301.1 .
    CCDSi CCDS10820.1. [Q13564-1 ]
    CCDS42171.1. [Q13564-2 ]
    CCDS42172.1. [Q13564-3 ]
    CCDS67050.1. [Q13564-4 ]
    RefSeqi NP_001018169.1. NM_001018159.1. [Q13564-2 ]
    NP_001018170.1. NM_001018160.1. [Q13564-3 ]
    NP_001273429.1. NM_001286500.1. [Q13564-4 ]
    NP_003896.1. NM_003905.3. [Q13564-1 ]
    XP_005256272.1. XM_005256215.1. [Q13564-3 ]
    UniGenei Hs.460978.

    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 A/C/E/G 1-534 [» ]
    1R4N X-ray 3.60 A/C/E/G 1-534 [» ]
    1TT5 X-ray 2.60 A/C 1-534 [» ]
    1YOV X-ray 2.60 A/C 1-534 [» ]
    2NVU X-ray 2.80 A 1-534 [» ]
    3DBH X-ray 2.85 A/C/E/G 1-534 [» ]
    3DBL X-ray 2.90 A/C/E/G 1-534 [» ]
    3DBR X-ray 3.05 A/C/E/G 1-534 [» ]
    3GZN X-ray 3.00 A/C 1-534 [» ]
    ProteinModelPortali Q13564.
    SMRi Q13564. Positions 6-534.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114402. 32 interactions.
    IntActi Q13564. 6 interactions.
    MINTi MINT-1429663.
    STRINGi 9606.ENSP00000290810.

    Chemistry

    ChEMBLi CHEMBL2016431.
    DrugBanki DB00171. Adenosine triphosphate.

    PTM databases

    PhosphoSitei Q13564.

    Polymorphism databases

    DMDMi 50400302.

    Proteomic databases

    MaxQBi Q13564.
    PaxDbi Q13564.
    PRIDEi Q13564.

    Protocols and materials databases

    DNASUi 8883.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290810 ; ENSP00000290810 ; ENSG00000159593 . [Q13564-1 ]
    ENST00000359087 ; ENSP00000351990 ; ENSG00000159593 . [Q13564-4 ]
    ENST00000379463 ; ENSP00000368776 ; ENSG00000159593 . [Q13564-2 ]
    ENST00000394074 ; ENSP00000377637 ; ENSG00000159593 . [Q13564-3 ]
    GeneIDi 8883.
    KEGGi hsa:8883.
    UCSCi uc002eqe.3. human. [Q13564-2 ]
    uc002eqf.3. human. [Q13564-1 ]

    Organism-specific databases

    CTDi 8883.
    GeneCardsi GC16M066836.
    HGNCi HGNC:621. NAE1.
    HPAi HPA041178.
    HPA042041.
    MIMi 603385. gene.
    neXtProti NX_Q13564.
    PharmGKBi PA162396730.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000216537.
    HOVERGENi HBG079761.
    KOi K04532.
    OMAi TNQYVPI.
    PhylomeDBi Q13564.
    TreeFami TF313972.

    Enzyme and pathway databases

    UniPathwayi UPA00885 .

    Miscellaneous databases

    ChiTaRSi NAE1. human.
    EvolutionaryTracei Q13564.
    GeneWikii APPBP1.
    GenomeRNAii 8883.
    NextBioi 33357.
    PROi Q13564.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13564.
    Bgeei Q13564.
    CleanExi HS_NAE1.
    Genevestigatori Q13564.

    Family and domain databases

    Gene3Di 3.40.50.720. 3 hits.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view ]
    Pfami PF00899. ThiF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein."
      Chow N., Korenberg J.R., Chen X.-N., Neve R.L.
      J. Biol. Chem. 271:11339-11346(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH APP, TISSUE SPECIFICITY.
      Tissue: Fetal brain and Fetal skeletal muscle.
    2. "Identification of a new human protooncogene."
      Kim J.W.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    6. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Muscle.
    9. "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: FUNCTION.
    10. "The amyloid precursor protein-binding protein APP-BP1 drives the cell cycle through the S-M checkpoint and causes apoptosis in neurons."
      Chen Y., McPhie D.L., Hirschberg J., Neve R.L.
      J. Biol. Chem. 275:8929-8935(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UBA3.
    11. "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 UBA3.
    12. "APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain."
      Chen Y., Liu W., McPhie D.L., Hassinger L., Neve R.L.
      J. Cell Biol. 163:27-33(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APP, SUBCELLULAR LOCATION.
    13. "ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and decreases APP-BP1-induced cell proliferation and neuronal apoptosis."
      Chen Y., Liu W., Naumovski L., Neve R.L.
      J. Neurochem. 85:801-809(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53BP2.
    14. "TRIP12 functions as an E3 ubiquitin ligase of APP-BP1."
      Park Y., Yoon S.K., Yoon J.B.
      Biochem. Biophys. Res. Commun. 374:294-298(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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 5-534 IN COMPLEX WITH UBA3; NEDD8 AND ATP.
    19. "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 5-534 IN COMPLEX WITH UBA3, MUTAGENESIS OF ASP-331.
    20. "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) IN COMPLEX WITH UBA3 AND UBE2M.

    Entry informationi

    Entry nameiULA1_HUMAN
    AccessioniPrimary (citable) accession number: Q13564
    Secondary accession number(s): A6NCK0
    , A6NFN4, A8MU28, B2R700, B3KUP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 135 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

    Miscellaneous

    NAE1 and UBA3 correspond to the N-terminal and the C-terminal part of yeast UBA3. In yeast the two subunits form a single polypeptide chain.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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