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Protein

SUMO-activating enzyme subunit 1

Gene

SAE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Pathway:iprotein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

GO - Molecular functioni

  • ATP-dependent protein binding Source: UniProtKB
  • enzyme activator activity Source: ProtInc
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • ubiquitin activating enzyme activity Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • positive regulation of catalytic activity Source: GOC
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • post-translational protein modification Source: Reactome
  • protein sumoylation Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • regulation of mitotic cell cycle Source: GO_Central
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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:30660. SAE1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: GO_Central
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • SUMO activating enzyme complex 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.

Polymorphism and mutation databases

BioMutaiSAE1.
DMDMi42559897.

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

BgeeiQ9UBE0.
CleanExiHS_SAE1.
ExpressionAtlasiQ9UBE0. baseline and differential.
GenevisibleiQ9UBE0. HS.

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. 40 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 – 2614Combined sources
Helixi28 – 358Combined sources
Beta strandi38 – 425Combined sources
Helixi46 – 5813Combined sources
Beta strandi61 – 666Combined sources
Beta strandi73 – 753Combined sources
Helixi76 – 783Combined sources
Helixi91 – 10111Combined sources
Beta strandi106 – 1116Combined sources
Helixi115 – 1173Combined sources
Helixi120 – 1234Combined sources
Beta strandi127 – 1337Combined sources
Helixi136 – 14813Combined sources
Beta strandi152 – 1609Combined sources
Beta strandi162 – 1687Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi206 – 2127Combined sources
Helixi216 – 2194Combined sources
Helixi227 – 2337Combined sources
Helixi239 – 25214Combined sources
Beta strandi253 – 2553Combined sources
Helixi259 – 2613Combined sources
Helixi262 – 27817Combined sources
Turni279 – 2813Combined sources
Helixi284 – 2863Combined sources
Helixi289 – 2935Combined sources
Beta strandi296 – 2983Combined sources
Helixi300 – 31920Combined sources
Beta strandi327 – 3326Combined sources
Turni333 – 3364Combined sources
Beta strandi337 – 3415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000075007.
HOGENOMiHOG000172217.
HOVERGENiHBG080782.
InParanoidiQ9UBE0.
KOiK10684.
OMAiSSDTYGE.
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. AlignAdd to basket

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

        10         20         30         40         50
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE
60 70 80 90 100
IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ
110 120 130 140 150
NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS
160 170 180 190 200
IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD
210 220 230 240 250
SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQVLLKFR
260 270 280 290 300
TDKGRDPSSD TYEEDSELLL QIRNDVLDSL GISPDLLPED FVRYCFSEMA
310 320 330 340
PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPK
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 (Ref. 6) Curated
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000392776; ENSP00000440818; ENSG00000142230. [Q9UBE0-2]
ENST00000413379; ENSP00000416557; ENSG00000142230. [Q9UBE0-3]
GeneIDi10055.
KEGGihsa:10055.
UCSCiuc002pgc.3. human. [Q9UBE0-1]
uc010ekx.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi115366. 40 interactions.
DIPiDIP-34587N.
IntActiQ9UBE0. 6 interactions.
MINTiMINT-1205002.
STRINGi9606.ENSP00000270225.

Chemistry

BindingDBiQ9UBE0.
ChEMBLiCHEMBL2095174.

PTM databases

PhosphoSiteiQ9UBE0.

Polymorphism and mutation databases

BioMutaiSAE1.
DMDMi42559897.

Proteomic databases

MaxQBiQ9UBE0.
PaxDbiQ9UBE0.
PeptideAtlasiQ9UBE0.
PRIDEiQ9UBE0.

Protocols and materials databases

DNASUi10055.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10055.
GeneCardsiGC19P047634.
HGNCiHGNC:30660. SAE1.
HPAiHPA041906.
HPA043552.
MIMi613294. gene.
neXtProtiNX_Q9UBE0.
PharmGKBiPA162402387.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00550000075007.
HOGENOMiHOG000172217.
HOVERGENiHBG080782.
InParanoidiQ9UBE0.
KOiK10684.
OMAiSSDTYGE.
PhylomeDBiQ9UBE0.
TreeFamiTF315037.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9UBE0.
GeneWikiiSAE1.
GenomeRNAii10055.
NextBioi37989.
PROiQ9UBE0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBE0.
CleanExiHS_SAE1.
ExpressionAtlasiQ9UBE0. baseline and differential.
GenevisibleiQ9UBE0. HS.

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.
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "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.
  19. "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: July 22, 2015
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.