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Protein

SUMO-activating enzyme subunit 1

Gene

Sae1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Pathwayi

GO - Molecular functioni

  1. ATP-dependent protein binding Source: MGI
  2. protein C-terminus binding Source: UniProtKB
  3. protein heterodimerization activity Source: MGI
  4. SUMO activating enzyme activity Source: GO_Central

GO - Biological processi

  1. protein sumoylation Source: UniProtKB
  2. 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_304803. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_304847. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
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, Ubl1a1, Uble1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1929264. Sae1.

Subcellular locationi

  1. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: GO_Central
  2. intracellular membrane-bounded organelle Source: MGI
  3. nucleoplasm Source: MGI
  4. nucleus Source: MGI
  5. SUMO activating enzyme complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350SUMO-activating enzyme subunit 1PRO_0000194967Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 350349SUMO-activating enzyme subunit 1, N-terminally processedPRO_0000423291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processedBy similarity
Modified residuei202 – 2021N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9R1T2.
PaxDbiQ9R1T2.
PRIDEiQ9R1T2.

2D gel databases

REPRODUCTION-2DPAGEQ9R1T2.

PTM databases

PhosphoSiteiQ9R1T2.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in testis.1 Publication

Gene expression databases

BgeeiQ9R1T2.
CleanExiMM_SAE1.
GenevestigatoriQ9R1T2.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi207998. 3 interactions.
IntActiQ9R1T2. 1 interaction.
MINTiMINT-4139487.

Structurei

3D structure databases

SMRiQ9R1T2. Positions 29-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00550000075007.
HOGENOMiHOG000172217.
HOVERGENiHBG080782.
InParanoidiQ9R1T2.
KOiK10684.
OMAiDQLCSKH.
OrthoDBiEOG7FR7GW.
PhylomeDBiQ9R1T2.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R1T2-1) [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 GGGGISEEEA AQYDRQIRLW GLEAQKRLRA SRVLIVGMKG
60 70 80 90 100
LGAEIAKNLI LAGVKGLTML DHEQVSPEDP GAQFLIQTGS VGRNRAEASL
110 120 130 140 150
ERAQNLNPMV DVKVDTEDVE KKPESFFTKF DAVCLTCCSR DVIIKVDQIC
160 170 180 190 200
HRNSIKFFTG DVFGYHGYTF ANLGEHEFVE EKTKVAKVSQ GVEDGPEAKR
210 220 230 240 250
AKLDSSETTM VKKKVLFCPV KEALEVDWSG EKAKAALKRT APDYFLLQVL
260 270 280 290 300
LKFRTDKGRD PTSESYKEDA ELLLQIRNDV FDSLGISPDL LPDDFVRYCF
310 320 330 340 350
SEMAPVCAVV GGILAQEIVK ALSQRDPPHN NFFFFDGMKG SGIVECLGPQ
Length:350
Mass (Da):38,620
Last modified:May 1, 2000 - v1
Checksum:i333108F6E98BABAA
GO
Isoform 2 (identifier: Q9R1T2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-350: ALSQRDPPHNNFFFFDGMKGSGIVECLGPQ → VCLGTMCV

Note: No experimental confirmation available.

Show »
Length:328
Mass (Da):36,135
Checksum:iD979A4D5950C2E4F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei321 – 35030ALSQR…CLGPQ → VCLGTMCV in isoform 2. 1 PublicationVSP_022004Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024303 mRNA. Translation: BAA82876.1.
AK010313 mRNA. Translation: BAB26845.1.
AK011783 mRNA. Translation: BAB27838.1.
AK087556 mRNA. Translation: BAC39925.1.
AK090012 mRNA. Translation: BAC41044.1.
AK154139 mRNA. Translation: BAE32401.1.
AK159672 mRNA. Translation: BAE35276.1.
AK162789 mRNA. Translation: BAE37060.1.
BC068164 mRNA. Translation: AAH68164.1.
CCDSiCCDS20848.1. [Q9R1T2-1]
RefSeqiNP_001272820.1. NM_001285891.1. [Q9R1T2-1]
NP_001272821.1. NM_001285892.1. [Q9R1T2-2]
NP_062722.1. NM_019748.3. [Q9R1T2-1]
UniGeneiMm.258530.

Genome annotation databases

EnsembliENSMUST00000094815; ENSMUSP00000092409; ENSMUSG00000052833. [Q9R1T2-1]
GeneIDi56459.
KEGGimmu:56459.
UCSCiuc009fhp.1. mouse. [Q9R1T2-1]
uc009fhq.1. mouse. [Q9R1T2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024303 mRNA. Translation: BAA82876.1.
AK010313 mRNA. Translation: BAB26845.1.
AK011783 mRNA. Translation: BAB27838.1.
AK087556 mRNA. Translation: BAC39925.1.
AK090012 mRNA. Translation: BAC41044.1.
AK154139 mRNA. Translation: BAE32401.1.
AK159672 mRNA. Translation: BAE35276.1.
AK162789 mRNA. Translation: BAE37060.1.
BC068164 mRNA. Translation: AAH68164.1.
CCDSiCCDS20848.1. [Q9R1T2-1]
RefSeqiNP_001272820.1. NM_001285891.1. [Q9R1T2-1]
NP_001272821.1. NM_001285892.1. [Q9R1T2-2]
NP_062722.1. NM_019748.3. [Q9R1T2-1]
UniGeneiMm.258530.

3D structure databases

SMRiQ9R1T2. Positions 29-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207998. 3 interactions.
IntActiQ9R1T2. 1 interaction.
MINTiMINT-4139487.

PTM databases

PhosphoSiteiQ9R1T2.

2D gel databases

REPRODUCTION-2DPAGEQ9R1T2.

Proteomic databases

MaxQBiQ9R1T2.
PaxDbiQ9R1T2.
PRIDEiQ9R1T2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094815; ENSMUSP00000092409; ENSMUSG00000052833. [Q9R1T2-1]
GeneIDi56459.
KEGGimmu:56459.
UCSCiuc009fhp.1. mouse. [Q9R1T2-1]
uc009fhq.1. mouse. [Q9R1T2-2]

Organism-specific databases

CTDi10055.
MGIiMGI:1929264. Sae1.

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00550000075007.
HOGENOMiHOG000172217.
HOVERGENiHBG080782.
InParanoidiQ9R1T2.
KOiK10684.
OMAiDQLCSKH.
OrthoDBiEOG7FR7GW.
PhylomeDBiQ9R1T2.
TreeFamiTF315037.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiREACT_304803. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_304847. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Miscellaneous databases

ChiTaRSiSae1. mouse.
NextBioi312702.
PROiQ9R1T2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R1T2.
CleanExiMM_SAE1.
GenevestigatoriQ9R1T2.

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. "Mus musculus cDNA similar to human Sua1 complete cds, complete cds."
    Kaneta Y., Takada S., Itoh M., Takagi N.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: BALB/c, C57BL/6J and NOD.
    Tissue: Embryo, Embryonic stem cell, Eye and Thymus.
  3. "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).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "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: IDENTIFICATION, TISSUE SPECIFICITY.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSAE1_MOUSE
AccessioniPrimary (citable) accession number: Q9R1T2
Secondary accession number(s): Q3TRG9, Q3TWJ0, Q9CSW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.