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Q9R1T2

- SAE1_MOUSE

UniProt

Q9R1T2 - SAE1_MOUSE

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Protein

SUMO-activating enzyme subunit 1

Gene
Sae1, Aos1, Sua1, Ubl1a1, Uble1a
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Pathwayi

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein C-terminus binding Source: UniProtKB
  3. SUMO activating enzyme activity Source: Ensembl

GO - Biological processi

  1. protein sumoylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_223195. 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: Chromosome 7

Organism-specific databases

MGIiMGI:1929264. Sae1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
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; alternate By similarity
Chaini2 – 350349SUMO-activating enzyme subunit 1, N-terminally processedPRO_0000423291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei2 – 21N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processed By 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.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9R1T2.
SMRiQ9R1T2. Positions 29-349.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00550000075007.
HOGENOMiHOG000172217.
HOVERGENiHBG080782.
InParanoidiQ9R1T2.
KOiK10684.
OMAiRTPVDYF.
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. Align

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

MVEKEEAGGG GGGGISEEEA AQYDRQIRLW GLEAQKRLRA SRVLIVGMKG    50
LGAEIAKNLI LAGVKGLTML DHEQVSPEDP GAQFLIQTGS VGRNRAEASL 100
ERAQNLNPMV DVKVDTEDVE KKPESFFTKF DAVCLTCCSR DVIIKVDQIC 150
HRNSIKFFTG DVFGYHGYTF ANLGEHEFVE EKTKVAKVSQ GVEDGPEAKR 200
AKLDSSETTM VKKKVLFCPV KEALEVDWSG EKAKAALKRT APDYFLLQVL 250
LKFRTDKGRD PTSESYKEDA ELLLQIRNDV FDSLGISPDL LPDDFVRYCF 300
SEMAPVCAVV GGILAQEIVK ALSQRDPPHN NFFFFDGMKG SGIVECLGPQ 350
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. VSP_022004Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS20848.1. [Q9R1T2-1 ]
RefSeqi NP_001272820.1. NM_001285891.1. [Q9R1T2-1 ]
NP_001272821.1. NM_001285892.1. [Q9R1T2-2 ]
NP_062722.1. NM_019748.3. [Q9R1T2-1 ]
UniGenei Mm.258530.

3D structure databases

ProteinModelPortali Q9R1T2.
SMRi Q9R1T2. Positions 29-349.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207998. 3 interactions.
IntActi Q9R1T2. 1 interaction.
MINTi MINT-4139487.

PTM databases

PhosphoSitei Q9R1T2.

2D gel databases

REPRODUCTION-2DPAGE Q9R1T2.

Proteomic databases

MaxQBi Q9R1T2.
PaxDbi Q9R1T2.
PRIDEi Q9R1T2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000094815 ; ENSMUSP00000092409 ; ENSMUSG00000052833 . [Q9R1T2-1 ]
GeneIDi 56459.
KEGGi mmu:56459.
UCSCi uc009fhp.1. mouse. [Q9R1T2-1 ]
uc009fhq.1. mouse. [Q9R1T2-2 ]

Organism-specific databases

CTDi 10055.
MGIi MGI:1929264. Sae1.

Phylogenomic databases

eggNOGi COG0476.
GeneTreei ENSGT00550000075007.
HOGENOMi HOG000172217.
HOVERGENi HBG080782.
InParanoidi Q9R1T2.
KOi K10684.
OMAi RTPVDYF.
OrthoDBi EOG7FR7GW.
PhylomeDBi Q9R1T2.
TreeFami TF315037.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_196647. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_223195. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Miscellaneous databases

NextBioi 312702.
PROi Q9R1T2.
SOURCEi Search...

Gene expression databases

Bgeei Q9R1T2.
CleanExi MM_SAE1.
Genevestigatori Q9R1T2.

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. "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: September 3, 2014
This is version 109 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

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