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Q9R1T2 (SAE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SUMO-activating enzyme subunit 1
Alternative name(s):
Ubiquitin-like 1-activating enzyme E1A
Gene names
Name:Sae1
Synonyms:Aos1, Sua1, Ubl1a1, Uble1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Pathway

Protein modification; protein sumoylation.

Subunit structure

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.

Subcellular location

Nucleus By similarity.

Tissue specificity

Broadly expressed, with highest levels in testis. Ref.4

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSUMO activating enzyme activity

Inferred from electronic annotation. Source: Ensembl

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9R1T2-1)

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.
Isoform 2 (identifier: Q9R1T2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     321-350: ALSQRDPPHNNFFFFDGMKGSGIVECLGPQ → VCLGTMCV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350SUMO-activating enzyme subunit 1
PRO_0000194967
Initiator methionine11Removed; alternate By similarity
Chain2 – 350349SUMO-activating enzyme subunit 1, N-terminally processed
PRO_0000423291

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processed By similarity
Modified residue2021N6-acetyllysine Ref.5

Natural variations

Alternative sequence321 – 35030ALSQR…CLGPQ → VCLGTMCV in isoform 2.
VSP_022004

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 333108F6E98BABAA

FASTA35038,620
        10         20         30         40         50         60 
MVEKEEAGGG GGGGISEEEA AQYDRQIRLW GLEAQKRLRA SRVLIVGMKG LGAEIAKNLI 

        70         80         90        100        110        120 
LAGVKGLTML DHEQVSPEDP GAQFLIQTGS VGRNRAEASL ERAQNLNPMV DVKVDTEDVE 

       130        140        150        160        170        180 
KKPESFFTKF DAVCLTCCSR DVIIKVDQIC HRNSIKFFTG DVFGYHGYTF ANLGEHEFVE 

       190        200        210        220        230        240 
EKTKVAKVSQ GVEDGPEAKR AKLDSSETTM VKKKVLFCPV KEALEVDWSG EKAKAALKRT 

       250        260        270        280        290        300 
APDYFLLQVL LKFRTDKGRD PTSESYKEDA ELLLQIRNDV FDSLGISPDL LPDDFVRYCF 

       310        320        330        340        350 
SEMAPVCAVV GGILAQEIVK ALSQRDPPHN NFFFFDGMKG SGIVECLGPQ 

« Hide

Isoform 2 [UniParc].

Checksum: D979A4D5950C2E4F
Show »

FASTA32836,135

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001272820.1. NM_001285891.1.
NP_001272821.1. NM_001285892.1.
NP_062722.1. NM_019748.3.
UniGeneMm.258530.

3D structure databases

ProteinModelPortalQ9R1T2.
SMRQ9R1T2. Positions 29-349.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207998. 3 interactions.
IntActQ9R1T2. 1 interaction.
MINTMINT-4139487.

PTM databases

PhosphoSiteQ9R1T2.

2D gel databases

REPRODUCTION-2DPAGEQ9R1T2.

Proteomic databases

PaxDbQ9R1T2.
PRIDEQ9R1T2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000094815; ENSMUSP00000092409; ENSMUSG00000052833. [Q9R1T2-1]
GeneID56459.
KEGGmmu:56459.
UCSCuc009fhp.1. mouse. [Q9R1T2-1]
uc009fhq.1. mouse. [Q9R1T2-2]

Organism-specific databases

CTD10055.
MGIMGI:1929264. Sae1.

Phylogenomic databases

eggNOGCOG0476.
GeneTreeENSGT00550000075007.
HOGENOMHOG000172217.
HOVERGENHBG080782.
InParanoidQ9R1T2.
KOK10684.
OMATAAHEFS.
OrthoDBEOG7FR7GW.
PhylomeDBQ9R1T2.
TreeFamTF315037.

Enzyme and pathway databases

UniPathwayUPA00886.

Gene expression databases

BgeeQ9R1T2.
CleanExMM_SAE1.
GenevestigatorQ9R1T2.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamPF00899. ThiF. 1 hit.
[Graphical view]
PRINTSPR01849. UBIQUITINACT.
SUPFAMSSF69572. SSF69572. 1 hit.
ProtoNetSearch...

Other

NextBio312702.
PROQ9R1T2.
SOURCESearch...

Entry information

Entry nameSAE1_MOUSE
AccessionPrimary (citable) accession number: Q9R1T2
Secondary accession number(s): Q3TRG9, Q3TWJ0, Q9CSW9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot