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Q9UBT2

- SAE2_HUMAN

UniProt

Q9UBT2 - SAE2_HUMAN

Protein

SUMO-activating enzyme subunit 2

Gene

UBA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (16 Feb 2004)
      Previous versions | rss
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    Functioni

    The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.6 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei48 – 481ATP1 Publication
    Binding sitei72 – 721ATP1 Publication
    Metal bindingi158 – 1581Zinc
    Metal bindingi161 – 1611Zinc
    Active sitei173 – 1731Glycyl thioester intermediate2 PublicationsPROSITE-ProRule annotation
    Metal bindingi441 – 4411Zinc
    Metal bindingi444 – 4441Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi24 – 296ATP1 Publication
    Nucleotide bindingi56 – 594ATP1 Publication
    Nucleotide bindingi95 – 962ATP1 Publication
    Nucleotide bindingi117 – 1226ATP1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. enzyme activator activity Source: ProtInc
    3. ligase activity Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct
    6. protein heterodimerization activity Source: UniProtKB
    7. SUMO activating enzyme activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. positive regulation of catalytic activity Source: GOC
    3. post-translational protein modification Source: Reactome
    4. protein sumoylation Source: UniProtKB
    5. SMT3-dependent protein catabolic process Source: RefGenome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SUMO-activating enzyme subunit 2 (EC:6.3.2.-)
    Alternative name(s):
    Anthracycline-associated resistance ARX
    Ubiquitin-like 1-activating enzyme E1B
    Ubiquitin-like modifier-activating enzyme 2
    Gene namesi
    Name:UBA2
    Synonyms:SAE2, UBLE1B
    ORF Names:HRIHFB2115
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:30661. UBA2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention.

    GO - Cellular componenti

    1. cytosol Source: RefGenome
    2. nucleoplasm Source: Reactome
    3. SUMO activating enzyme complex Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561N → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication
    Mutagenesisi57 – 571L → A: Strongly reduces ATP-dependent activation of SUMO proteins. 1 Publication
    Mutagenesisi59 – 591R → A: Strongly reduces ATP-dependent activation of SUMO proteins. 1 Publication
    Mutagenesisi72 – 721K → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication
    Mutagenesisi117 – 1171D → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication
    Mutagenesisi173 – 1731C → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi174 – 1741T → A: Slightly reduced enzyme activity. 1 Publication
    Mutagenesisi184 – 1841H → Q: No effect on enzyme activity. 1 Publication
    Mutagenesisi235 – 2351I → A: Strongly reduced interaction with UBE2I; when associated with A-238. 1 Publication
    Mutagenesisi238 – 2381I → A: Strongly reduced interaction with UBE2I; when associated with A-235. 1 Publication
    Mutagenesisi484 – 4841Missing: Strongly reduced interaction with UBE2I. 1 Publication
    Mutagenesisi485 – 4851G → GGGG: Strongly reduced interaction with UBE2I. 1 Publication

    Organism-specific databases

    PharmGKBiPA162407583.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 640640SUMO-activating enzyme subunit 2PRO_0000194968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki190 – 190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki236 – 236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
    Cross-linki257 – 257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei271 – 2711N6-acetyllysine; alternate1 Publication
    Cross-linki271 – 271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Cross-linki275 – 275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei507 – 5071Phosphoserine1 Publication
    Modified residuei592 – 5921Phosphoserine1 Publication
    Cross-linki611 – 611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei613 – 6131N6-acetyllysine; alternateBy similarity
    Cross-linki613 – 613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Cross-linki617 – 617Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki623 – 623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-236 inhibits enzymatic activity. Sumoylation at the C-terminal lysine cluster plays an essential role in nuclear trafficking.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UBT2.
    PaxDbiQ9UBT2.
    PeptideAtlasiQ9UBT2.
    PRIDEiQ9UBT2.

    PTM databases

    PhosphoSiteiQ9UBT2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UBT2.
    BgeeiQ9UBT2.
    CleanExiHS_UBA2.
    GenevestigatoriQ9UBT2.

    Organism-specific databases

    HPAiHPA041436.

    Interactioni

    Subunit structurei

    Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds to the two domains that are encoded on a single polypeptide chain in ubiquitin-activating enzyme E1. Interacts with UBE2I.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SAE1Q9UBE03EBI-718569,EBI-743154

    Protein-protein interaction databases

    BioGridi115365. 62 interactions.
    DIPiDIP-35136N.
    IntActiQ9UBT2. 5 interactions.
    MINTiMINT-1405216.
    STRINGi9606.ENSP00000246548.

    Structurei

    Secondary structure

    1
    640
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 179
    Beta strandi19 – 235
    Helixi27 – 3913
    Beta strandi43 – 486
    Helixi54 – 585
    Helixi65 – 673
    Helixi72 – 8110
    Beta strandi88 – 947
    Helixi103 – 1064
    Beta strandi110 – 1145
    Helixi119 – 13214
    Beta strandi136 – 1427
    Beta strandi145 – 1517
    Turni153 – 1553
    Beta strandi168 – 1714
    Turni172 – 1765
    Helixi182 – 19716
    Helixi202 – 2043
    Helixi213 – 2153
    Beta strandi225 – 2273
    Beta strandi234 – 2363
    Helixi241 – 2466
    Helixi251 – 2599
    Helixi261 – 2666
    Helixi270 – 2723
    Beta strandi274 – 2763
    Helixi284 – 2896
    Helixi308 – 3103
    Helixi315 – 33521
    Turni337 – 3393
    Helixi349 – 36517
    Helixi373 – 3819
    Helixi388 – 40619
    Helixi410 – 4123
    Beta strandi414 – 4185
    Beta strandi426 – 4338
    Turni442 – 4443
    Beta strandi445 – 4473
    Beta strandi449 – 4546
    Turni456 – 4583
    Helixi461 – 4666
    Helixi467 – 4726
    Beta strandi479 – 4868
    Beta strandi489 – 4913
    Beta strandi493 – 4986
    Helixi501 – 5033
    Helixi506 – 5094
    Beta strandi516 – 5216
    Turni522 – 5254
    Beta strandi526 – 5349
    Beta strandi544 – 5463
    Turni609 – 6113
    Turni614 – 6196
    Helixi620 – 6267
    Helixi627 – 6293
    Beta strandi636 – 6383

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y8QX-ray2.25B/D1-640[»]
    1Y8RX-ray2.75B/E1-640[»]
    2PX9NMR-A166-382[»]
    3KYCX-ray2.45B1-640[»]
    3KYDX-ray2.61B1-549[»]
    DisProtiDP00486.
    ProteinModelPortaliQ9UBT2.
    SMRiQ9UBT2. Positions 4-591, 607-640.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBT2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000216514.
    HOVERGENiHBG060266.
    InParanoidiQ9UBT2.
    KOiK10685.
    OMAiYACLFSK.
    OrthoDBiEOG7S7SDB.
    PhylomeDBiQ9UBT2.
    TreeFamiTF300765.

    Family and domain databases

    Gene3Di1.10.3240.10. 1 hit.
    3.40.50.720. 2 hits.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR028077. UAE_UbL_dom.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018074. UBQ-activ_enz_E1_AS.
    [Graphical view]
    PfamiPF00899. ThiF. 1 hit.
    PF14732. UAE_UbL. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 2 hits.
    PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
    PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBT2-1) [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

    MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD    50
    TIDVSNLNRQ FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD 100
    YNVEFFRQFI LVMNALDNRA ARNHVNRMCL AADVPLIESG TAGYLGQVTT 150
    IKKGVTECYE CHPKPTQRTF PGCTIRNTPS EPIHCIVWAK YLFNQLFGEE 200
    DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST KEWAKSTGYD 250
    PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ 300
    NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS 350
    AMDFVTSAAN LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL 400
    EGLKILSGKI DQCRTIFLNK QPNPRKKLLV PCALDPPNPN CYVCASKPEV 450
    TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV QIEDGKGTIL ISSEEGETEA 500
    NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK DVEFEVVGDA 550
    PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN 600
    ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD 640
    Length:640
    Mass (Da):71,224
    Last modified:February 16, 2004 - v2
    Checksum:iC12D15293BBF90EB
    GO
    Isoform 2 (identifier: Q9UBT2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-96: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:544
    Mass (Da):60,839
    Checksum:i24F5E43AB6FA2B05
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti229 – 2291S → C in AAD12784. (PubMed:9920803)Curated
    Sequence conflicti229 – 2291S → C in AAD23914. (PubMed:10217437)Curated
    Sequence conflicti341 – 3411E → G in CAB66839. (PubMed:11230166)Curated
    Sequence conflicti456 – 4561V → L in BAD92109. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti307 – 3071L → R.2 Publications
    Corresponds to variant rs1043062 [ dbSNP | Ensembl ].
    VAR_017689

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9696Missing in isoform 2. 1 PublicationVSP_056164Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090384 mRNA. Translation: AAD12784.1.
    AF079566 mRNA. Translation: AAD23914.1.
    AF110957 mRNA. Translation: AAD24434.1.
    U35832 mRNA. Translation: AAC99992.1.
    AL136905 mRNA. Translation: CAB66839.1.
    AK124730 mRNA. Translation: BAG54081.1.
    BT009781 mRNA. Translation: AAP88783.1.
    CR456756 mRNA. Translation: CAG33037.1.
    AC008747 Genomic DNA. No translation available.
    BC003153 mRNA. Translation: AAH03153.1.
    AB208872 mRNA. Translation: BAD92109.1.
    AB015337 mRNA. Translation: BAA34795.1.
    CCDSiCCDS12439.1.
    PIRiT46936.
    RefSeqiNP_005490.1. NM_005499.2.
    XP_005258461.1. XM_005258404.1.
    UniGeneiHs.631580.

    Genome annotation databases

    EnsembliENST00000246548; ENSP00000246548; ENSG00000126261.
    ENST00000439527; ENSP00000437484; ENSG00000126261.
    GeneIDi10054.
    KEGGihsa:10054.
    UCSCiuc002nvk.3. human.

    Polymorphism databases

    DMDMi42559898.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090384 mRNA. Translation: AAD12784.1 .
    AF079566 mRNA. Translation: AAD23914.1 .
    AF110957 mRNA. Translation: AAD24434.1 .
    U35832 mRNA. Translation: AAC99992.1 .
    AL136905 mRNA. Translation: CAB66839.1 .
    AK124730 mRNA. Translation: BAG54081.1 .
    BT009781 mRNA. Translation: AAP88783.1 .
    CR456756 mRNA. Translation: CAG33037.1 .
    AC008747 Genomic DNA. No translation available.
    BC003153 mRNA. Translation: AAH03153.1 .
    AB208872 mRNA. Translation: BAD92109.1 .
    AB015337 mRNA. Translation: BAA34795.1 .
    CCDSi CCDS12439.1.
    PIRi T46936.
    RefSeqi NP_005490.1. NM_005499.2.
    XP_005258461.1. XM_005258404.1.
    UniGenei Hs.631580.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y8Q X-ray 2.25 B/D 1-640 [» ]
    1Y8R X-ray 2.75 B/E 1-640 [» ]
    2PX9 NMR - A 166-382 [» ]
    3KYC X-ray 2.45 B 1-640 [» ]
    3KYD X-ray 2.61 B 1-549 [» ]
    DisProti DP00486.
    ProteinModelPortali Q9UBT2.
    SMRi Q9UBT2. Positions 4-591, 607-640.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115365. 62 interactions.
    DIPi DIP-35136N.
    IntActi Q9UBT2. 5 interactions.
    MINTi MINT-1405216.
    STRINGi 9606.ENSP00000246548.

    Chemistry

    ChEMBLi CHEMBL2095174.

    PTM databases

    PhosphoSitei Q9UBT2.

    Polymorphism databases

    DMDMi 42559898.

    Proteomic databases

    MaxQBi Q9UBT2.
    PaxDbi Q9UBT2.
    PeptideAtlasi Q9UBT2.
    PRIDEi Q9UBT2.

    Protocols and materials databases

    DNASUi 10054.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246548 ; ENSP00000246548 ; ENSG00000126261 .
    ENST00000439527 ; ENSP00000437484 ; ENSG00000126261 .
    GeneIDi 10054.
    KEGGi hsa:10054.
    UCSCi uc002nvk.3. human.

    Organism-specific databases

    CTDi 10054.
    GeneCardsi GC19P034919.
    HGNCi HGNC:30661. UBA2.
    HPAi HPA041436.
    MIMi 613295. gene.
    neXtProti NX_Q9UBT2.
    PharmGKBi PA162407583.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000216514.
    HOVERGENi HBG060266.
    InParanoidi Q9UBT2.
    KOi K10685.
    OMAi YACLFSK.
    OrthoDBi EOG7S7SDB.
    PhylomeDBi Q9UBT2.
    TreeFami TF300765.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    Reactomei REACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_163812. SUMO is conjugated to E1 (UBA2:SAE1).

    Miscellaneous databases

    ChiTaRSi UBA2. human.
    EvolutionaryTracei Q9UBT2.
    GeneWikii UBA2.
    GenomeRNAii 10054.
    NextBioi 37985.
    PROi Q9UBT2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBT2.
    Bgeei Q9UBT2.
    CleanExi HS_UBA2.
    Genevestigatori Q9UBT2.

    Family and domain databases

    Gene3Di 1.10.3240.10. 1 hit.
    3.40.50.720. 2 hits.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR028077. UAE_UbL_dom.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018074. UBQ-activ_enz_E1_AS.
    [Graphical view ]
    Pfami PF00899. ThiF. 1 hit.
    PF14732. UAE_UbL. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 2 hits.
    PROSITEi PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
    PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2."
      Okuma T., Honda R., Ichikawa G., Tsumagari N., Yasuda H.
      Biochem. Biophys. Res. Commun. 254:693-698(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-307.
      Tissue: Cervix carcinoma.
    2. "Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex."
      Gong L., Li B., Millas S., Yeh E.T.H.
      FEBS Lett. 448:185-189(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-307.
      Tissue: Placenta.
    3. "Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1."
      Desterro J.M.P., Rodriguez M.S., Kemp G.D., Hay R.T.
      J. Biol. Chem. 274:10618-10624(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. Slapak C., Mizunuma N., Terashima M., Yamauchi T., Kufe D.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    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] (ISOFORM 2).
      Tissue: Brain.
    7. "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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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.
    11. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-640 (ISOFORM 1).
      Tissue: Brain.
    12. "Selection system for genes encoding nuclear-targeted proteins."
      Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
      Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 536-640 (ISOFORM 1).
      Tissue: Fetal brain.
    13. "Expression and regulation of the mammalian SUMO-1 E1 enzyme."
      Azuma Y., Tan S.-H., Cavenagh M.M., Ainsztein A.M., Saitoh H., Dasso M.
      FASEB J. 15:1825-1827(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DIMERIZATION, FUNCTION.
    14. "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9."
      Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T.
      J. Biol. Chem. 276:35368-35374(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers."
      Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H., Chock P.B.
      Arch. Biochem. Biophys. 453:70-74(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications."
      Wang J., Lee B., Cai S., Fukui L., Hu W., Chen Y.
      J. Biol. Chem. 284:20340-20348(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2I, FUNCTION, MUTAGENESIS OF ASP-484 AND GLY-485.
    19. "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 LYS-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Small ubiquitin-like modifier (SUMO) modification of E1 Cys domain inhibits E1 Cys domain enzymatic activity."
      Truong K., Lee T.D., Chen Y.
      J. Biol. Chem. 287:15154-15163(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-190; LYS-236; LYS-257; LYS-271 AND LYS-275.
    23. "Sumoylation of SAE2 C terminus regulates SAE nuclear localization."
      Truong K., Lee T.D., Li B., Chen Y.
      J. Biol. Chem. 287:42611-42619(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUMOYLATION AT LYS-611; LYS-613; LYS-617 AND LYS-623.
    24. "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."
      Lois L.M., Lima C.D.
      EMBO J. 24:439-451(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SAE1; SUMO1; ZINC IONS AND ATP, FUNCTION, SUBUNIT, ACTIVE SITE.
    25. "The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications."
      Wang J., Hu W., Cai S., Lee B., Song J., Chen Y.
      Mol. Cell 27:228-237(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 166-382 IN COMPLEX WITH UBE2I, MUTAGENESIS OF ILE-235 AND ILE-238, FUNCTION, INTERACTION WITH UBE2I.
    26. "Active site remodelling accompanies thioester bond formation in the SUMO E1."
      Olsen S.K., Capili A.D., Lu X., Tan D.S., Lima C.D.
      Nature 463:906-912(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH SAE1; SUMO1 AND REACTION INTERMEDIATE, FUNCTION, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF ASN-56; LEU-57; ARG-59; LYS-72; ASP-117; CYS-173; THR-174 AND HIS-184.

    Entry informationi

    Entry nameiSAE2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBT2
    Secondary accession number(s): B3KWB9
    , O95605, Q59H87, Q6IBP6, Q9NTJ1, Q9UED2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: February 16, 2004
    Last modified: October 1, 2014
    This is version 130 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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