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Q9UBE0

- SAE1_HUMAN

UniProt

Q9UBE0 - SAE1_HUMAN

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Protein
SUMO-activating enzyme subunit 1
Gene
SAE1, AOS1, SUA1, UBLE1A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 C-terminus binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. protein heterodimerization activity Source: UniProtKB
  6. ubiquitin activating enzyme activity Source: UniProtKB

GO - Biological processi

  1. SMT3-dependent protein catabolic process Source: RefGenome
  2. cellular protein metabolic process Source: Reactome
  3. positive regulation of catalytic activity Source: GOC
  4. post-translational protein modification Source: Reactome
  5. protein sumoylation Source: UniProtKB
  6. protein ubiquitination Source: UniProtKB
  7. regulation of mitotic cell cycle Source: RefGenome
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication

Organism-specific databases

PharmGKBiPA162402387.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346SUMO-activating enzyme subunit 1
PRO_0000194966Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 346345SUMO-activating enzyme subunit 1, N-terminally processed
PRO_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-acetyllysine By 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.4 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

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.

Miscellaneous databases

EvolutionaryTraceiQ9UBE0.

Family & Domainsi

Sequence similaritiesi

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei245 – 29955VLLKF…CFSEM → GPVSAGPSSQQLLLLRWHEG EWDCGVPWPQVNSRFGSPRD ANCSMPTCIPCPLPS in isoform 3.
VSP_045372Add
BLAST
Alternative sequencei245 – 26622VLLKF…YEEDS → GTASPRWPQCVRWLEGFWHR KL in isoform 2.
VSP_045373Add
BLAST
Alternative sequencei267 – 34680Missing in isoform 2.
VSP_045374Add
BLAST
Alternative sequencei300 – 34647Missing in isoform 3.
VSP_045375Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 130 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

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