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Q9UBE0

- SAE1_HUMAN

UniProt

Q9UBE0 - SAE1_HUMAN

Protein

SUMO-activating enzyme subunit 1

Gene

SAE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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/SAE2.7 Publications

    Pathwayi

    GO - Molecular functioni

    1. ATP-dependent protein binding Source: UniProtKB
    2. enzyme activator activity Source: ProtInc
    3. protein binding Source: IntAct
    4. protein C-terminus binding Source: UniProtKB
    5. protein heterodimerization activity Source: UniProtKB
    6. ubiquitin 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. protein ubiquitination Source: UniProtKB
    6. regulation of mitotic cell cycle Source: RefGenome
    7. SMT3-dependent protein catabolic process Source: RefGenome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    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 1
    Alternative name(s):
    Ubiquitin-like 1-activating enzyme E1A
    Cleaved into the following chain:
    Gene namesi
    Name:SAE1
    Synonyms:AOS1, SUA1, UBLE1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:30660. SAE1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: RefGenome
    2. intracellular membrane-bounded organelle Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211R → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication
    Mutagenesisi24 – 263RLW → AAA: Abolishes ATP-dependent activation of SUMO proteins.

    Organism-specific databases

    PharmGKBiPA162402387.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 346346SUMO-activating enzyme subunit 1PRO_0000194966Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 346345SUMO-activating enzyme subunit 1, N-terminally processedPRO_0000423290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei2 – 21N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processed1 Publication
    Modified residuei198 – 1981N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UBE0.
    PaxDbiQ9UBE0.
    PeptideAtlasiQ9UBE0.
    PRIDEiQ9UBE0.

    PTM databases

    PhosphoSiteiQ9UBE0.

    Expressioni

    Tissue specificityi

    Expression level increases during S phase and drops in G2 phase (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9UBE0.
    BgeeiQ9UBE0.
    CleanExiHS_SAE1.
    GenevestigatoriQ9UBE0.

    Organism-specific databases

    HPAiHPA041906.
    HPA043552.

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UBA2Q9UBT23EBI-743154,EBI-718569

    Protein-protein interaction databases

    BioGridi115366. 38 interactions.
    DIPiDIP-34587N.
    IntActiQ9UBE0. 6 interactions.
    MINTiMINT-1205002.
    STRINGi9606.ENSP00000270225.

    Structurei

    Secondary structure

    1
    346
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2614
    Helixi28 – 358
    Beta strandi38 – 425
    Helixi46 – 5813
    Beta strandi61 – 666
    Beta strandi73 – 753
    Helixi76 – 783
    Helixi91 – 10111
    Beta strandi106 – 1116
    Helixi115 – 1173
    Helixi120 – 1234
    Beta strandi127 – 1337
    Helixi136 – 14813
    Beta strandi152 – 1609
    Beta strandi162 – 1687
    Beta strandi170 – 1778
    Beta strandi206 – 2127
    Helixi216 – 2194
    Helixi227 – 2337
    Helixi239 – 25214
    Beta strandi253 – 2553
    Helixi259 – 2613
    Helixi262 – 27817
    Turni279 – 2813
    Helixi284 – 2863
    Helixi289 – 2935
    Beta strandi296 – 2983
    Helixi300 – 31920
    Beta strandi327 – 3326
    Turni333 – 3364
    Beta strandi337 – 3415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y8QX-ray2.25A/C1-346[»]
    1Y8RX-ray2.75A/D1-346[»]
    3KYCX-ray2.45A1-346[»]
    3KYDX-ray2.61A1-346[»]
    DisProtiDP00485.
    ProteinModelPortaliQ9UBE0.
    SMRiQ9UBE0. Positions 25-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UBE0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000172217.
    HOVERGENiHBG080782.
    InParanoidiQ9UBE0.
    KOiK10684.
    OMAiRTPVDYF.
    PhylomeDBiQ9UBE0.
    TreeFamiTF315037.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view]
    PfamiPF00899. ThiF. 1 hit.
    [Graphical view]
    PRINTSiPR01849. UBIQUITINACT.
    SUPFAMiSSF69572. SSF69572. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBE0-1) [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

    MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE    50
    IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ 100
    NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS 150
    IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD 200
    SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQVLLKFR 250
    TDKGRDPSSD TYEEDSELLL QIRNDVLDSL GISPDLLPED FVRYCFSEMA 300
    PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPK 346
    Length:346
    Mass (Da):38,450
    Last modified:May 1, 2000 - v1
    Checksum:iE2B10A69FF2ED746
    GO
    Isoform 2 (identifier: Q9UBE0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         245-266: VLLKFRTDKGRDPSSDTYEEDS → GTASPRWPQCVRWLEGFWHRKL
         267-346: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:266
    Mass (Da):29,811
    Checksum:i058AD8B9B2A2EEBB
    GO
    Isoform 3 (identifier: Q9UBE0-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         245-299: VLLKFRTDKG...DFVRYCFSEM → GPVSAGPSSQ...PTCIPCPLPS
         300-346: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:299
    Mass (Da):33,063
    Checksum:i35D1828B2957CCBA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151I → M in BAG51064. 1 PublicationCurated
    Sequence conflicti158 – 1581V → A in AAF29104. (PubMed:11042152)Curated
    Sequence conflicti178 – 1803KTK → ETD in AAF29104. (PubMed:11042152)Curated
    Sequence conflicti186 – 1861Q → H in AAF29104. (PubMed:11042152)Curated
    Sequence conflicti273 – 2731R → G in AAD12785. (PubMed:9920803)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei245 – 29955VLLKF…CFSEM → GPVSAGPSSQQLLLLRWHEG EWDCGVPWPQVNSRFGSPRD ANCSMPTCIPCPLPS in isoform 3. 1 PublicationVSP_045372Add
    BLAST
    Alternative sequencei245 – 26622VLLKF…YEEDS → GTASPRWPQCVRWLEGFWHR KL in isoform 2. 1 PublicationVSP_045373Add
    BLAST
    Alternative sequencei267 – 34680Missing in isoform 2. 1 PublicationVSP_045374Add
    BLAST
    Alternative sequencei300 – 34647Missing in isoform 3. 1 PublicationVSP_045375Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090385 mRNA. Translation: AAD12785.2.
    AF046025 mRNA. Translation: AAD23902.2.
    AF110956 mRNA. Translation: AAD24433.1.
    AF161489 mRNA. Translation: AAF29104.1.
    AL560234 mRNA. No translation available.
    BT007290 mRNA. Translation: AAP35954.1.
    AK021978 mRNA. Translation: BAG51064.1.
    AK315624 mRNA. Translation: BAG37992.1.
    AC008532 Genomic DNA. No translation available.
    AC008755 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW57461.1.
    CH471126 Genomic DNA. Translation: EAW57463.1.
    BC000344 mRNA. Translation: AAH00344.1.
    BC003611 mRNA. Translation: AAH03611.1.
    BC018271 mRNA. Translation: AAH18271.1.
    CCDSiCCDS12696.1. [Q9UBE0-1]
    CCDS54284.1. [Q9UBE0-2]
    CCDS54285.1. [Q9UBE0-3]
    RefSeqiNP_001139185.1. NM_001145713.1. [Q9UBE0-3]
    NP_001139186.1. NM_001145714.1. [Q9UBE0-2]
    NP_005491.1. NM_005500.2. [Q9UBE0-1]
    UniGeneiHs.515500.

    Genome annotation databases

    EnsembliENST00000270225; ENSP00000270225; ENSG00000142230. [Q9UBE0-1]
    ENST00000392776; ENSP00000440818; ENSG00000142230. [Q9UBE0-2]
    ENST00000413379; ENSP00000416557; ENSG00000142230. [Q9UBE0-3]
    GeneIDi10055.
    KEGGihsa:10055.
    UCSCiuc002pgc.3. human. [Q9UBE0-1]
    uc010ekx.3. human.

    Polymorphism databases

    DMDMi42559897.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090385 mRNA. Translation: AAD12785.2 .
    AF046025 mRNA. Translation: AAD23902.2 .
    AF110956 mRNA. Translation: AAD24433.1 .
    AF161489 mRNA. Translation: AAF29104.1 .
    AL560234 mRNA. No translation available.
    BT007290 mRNA. Translation: AAP35954.1 .
    AK021978 mRNA. Translation: BAG51064.1 .
    AK315624 mRNA. Translation: BAG37992.1 .
    AC008532 Genomic DNA. No translation available.
    AC008755 Genomic DNA. No translation available.
    CH471126 Genomic DNA. Translation: EAW57461.1 .
    CH471126 Genomic DNA. Translation: EAW57463.1 .
    BC000344 mRNA. Translation: AAH00344.1 .
    BC003611 mRNA. Translation: AAH03611.1 .
    BC018271 mRNA. Translation: AAH18271.1 .
    CCDSi CCDS12696.1. [Q9UBE0-1 ]
    CCDS54284.1. [Q9UBE0-2 ]
    CCDS54285.1. [Q9UBE0-3 ]
    RefSeqi NP_001139185.1. NM_001145713.1. [Q9UBE0-3 ]
    NP_001139186.1. NM_001145714.1. [Q9UBE0-2 ]
    NP_005491.1. NM_005500.2. [Q9UBE0-1 ]
    UniGenei Hs.515500.

    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 A/C 1-346 [» ]
    1Y8R X-ray 2.75 A/D 1-346 [» ]
    3KYC X-ray 2.45 A 1-346 [» ]
    3KYD X-ray 2.61 A 1-346 [» ]
    DisProti DP00485.
    ProteinModelPortali Q9UBE0.
    SMRi Q9UBE0. Positions 25-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115366. 38 interactions.
    DIPi DIP-34587N.
    IntActi Q9UBE0. 6 interactions.
    MINTi MINT-1205002.
    STRINGi 9606.ENSP00000270225.

    Chemistry

    BindingDBi Q9UBE0.
    ChEMBLi CHEMBL1615388.

    PTM databases

    PhosphoSitei Q9UBE0.

    Polymorphism databases

    DMDMi 42559897.

    Proteomic databases

    MaxQBi Q9UBE0.
    PaxDbi Q9UBE0.
    PeptideAtlasi Q9UBE0.
    PRIDEi Q9UBE0.

    Protocols and materials databases

    DNASUi 10055.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270225 ; ENSP00000270225 ; ENSG00000142230 . [Q9UBE0-1 ]
    ENST00000392776 ; ENSP00000440818 ; ENSG00000142230 . [Q9UBE0-2 ]
    ENST00000413379 ; ENSP00000416557 ; ENSG00000142230 . [Q9UBE0-3 ]
    GeneIDi 10055.
    KEGGi hsa:10055.
    UCSCi uc002pgc.3. human. [Q9UBE0-1 ]
    uc010ekx.3. human.

    Organism-specific databases

    CTDi 10055.
    GeneCardsi GC19P047634.
    HGNCi HGNC:30660. SAE1.
    HPAi HPA041906.
    HPA043552.
    MIMi 613294. gene.
    neXtProti NX_Q9UBE0.
    PharmGKBi PA162402387.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000172217.
    HOVERGENi HBG080782.
    InParanoidi Q9UBE0.
    KOi K10684.
    OMAi RTPVDYF.
    PhylomeDBi Q9UBE0.
    TreeFami TF315037.

    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

    EvolutionaryTracei Q9UBE0.
    GeneWikii SAE1.
    GenomeRNAii 10055.
    NextBioi 37989.
    PROi Q9UBE0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBE0.
    Bgeei Q9UBE0.
    CleanExi HS_SAE1.
    Genevestigatori Q9UBE0.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view ]
    Pfami PF00899. ThiF. 1 hit.
    [Graphical view ]
    PRINTSi PR01849. UBIQUITINACT.
    SUPFAMi SSF69572. SSF69572. 1 hit.
    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), DIMERIZATION, FUNCTION.
      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), DIMERIZATION, FUNCTION.
      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), PROTEIN SEQUENCE OF 1-11; 109-117 AND 186-193, DIMERIZATION, FUNCTION.
      Tissue: Cervix carcinoma.
    4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    5. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: B-cell.
    6. "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] (ISOFORM 1).
    7. "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 3).
    8. "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].
    9. 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: Colon, Lung and Placenta.
    11. "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, TISSUE SPECIFICITY, DIMERIZATION, FUNCTION.
    12. "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.
    13. "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.
    14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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 UBA2; SUMO1 AND ATP, FUNCTION.
    18. "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 UBA2 AND SUMO1, FUNCTION, MUTAGENESIS OF ARG-21 AND 24-ARG--TRP-26.

    Entry informationi

    Entry nameiSAE1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBE0
    Secondary accession number(s): B2RDP5
    , B3KMQ2, F5GXX7, G3XAK6, O95717, Q9P020
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 131 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 19
      Human chromosome 19: 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