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Q9Z1F9 (SAE2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SUMO-activating enzyme subunit 2
EC=6.3.2.-
Alternative name(s):
Anthracycline-associated resistance ARX
Ubiquitin-like 1-activating enzyme E1B
Gene names
Name:Uba2
Synonyms:Sae2, Uble1b
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 638638SUMO-activating enzyme subunit 2
PRO_0000194969

Regions

Nucleotide binding24 – 296ATP By similarity
Nucleotide binding56 – 594ATP By similarity
Nucleotide binding95 – 962ATP By similarity
Nucleotide binding117 – 1226ATP By similarity

Sites

Active site1731Glycyl thioester intermediate Potential
Metal binding1581Zinc By similarity
Metal binding1611Zinc By similarity
Metal binding4391Zinc By similarity
Metal binding4421Zinc By similarity
Binding site481ATP By similarity
Binding site721ATP By similarity

Amino acid modifications

Modified residue2711N6-acetyllysine By similarity
Modified residue3221N6-acetyllysine By similarity
Modified residue5901Phosphoserine By similarity

Experimental info

Sequence conflict2091D → V in BAE37349. Ref.2
Sequence conflict5421F → L in BAE30671. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Z1F9 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 065C72C1CA7F4CA7

FASTA63870,569
        10         20         30         40         50         60 
MALSRGLPRE LAEAVSGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD TIDVSNLNRQ 

        70         80         90        100        110        120 
FLFQKKHVGR SKAQVAKESV LQFHPQANIE AHHDSIMNPD YNVEFFRQFI LVMNALDNRA 

       130        140        150        160        170        180 
ARNHVNRMCL AADVPLIESG TAGYLGQVTT IKKGVTECYE CHPKPTQRTF PGCTIRNTPS 

       190        200        210        220        230        240 
EPIHCIVWAK YLFNQLFGEE DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST 

       250        260        270        280        290        300 
KEWAKSTGYD PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEANADQQNE 

       310        320        330        340        350        360 
PQLGLKDQQV LDVKSYASLF SKSIETLRVH LAEKGDGAEL IWDKDDPPAM DFVTSAANLR 

       370        380        390        400        410        420 
MHIFSMNMKS RFDIKSMAGN IIPAIATTNA VIAGLIVLEG LKILSGKIDQ CRTIFLNKQP 

       430        440        450        460        470        480 
NPRKKLLVPC ALDPPNTNCY VCASKPEVTV RLNVHKVTVL TLQDKIVKEK FAMVAPDVQI 

       490        500        510        520        530        540 
EDGKGTILIS SEEGETEANN PKKLSDFGIR NGSRLQADDF LQDYTLLINI LHSEDLGKDV 

       550        560        570        580        590        600 
EFEVVGDSPE KVGPKQAEDA AKSIANGSDD GAQPSTSTAQ EQDDVLIVDS DEEGPSNSTD 

       610        620        630 
CSGDDKARKR KLEENEAAST KKCRLEQMED PDDVIALD

« Hide

References

« Hide 'large scale' references
[1]Mizunuma N., Terashima M., Yamauchi T., Kufe D.W., Slapak C.A.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: DBA/2J.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion, Bone marrow, Corpora quadrigemina, Head, Kidney and Lung.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 11481243] [Abstract]
Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U35833 mRNA. Translation: AAD10338.1.
AK075938 mRNA. Translation: BAC36068.1.
AK146925 mRNA. Translation: BAE27536.1.
AK151765 mRNA. Translation: BAE30671.1.
AK152415 mRNA. Translation: BAE31200.1.
AK163451 mRNA. Translation: BAE37349.1.
AK164826 mRNA. Translation: BAE37935.1.
AK166133 mRNA. Translation: BAE38590.1.
AK168673 mRNA. Translation: BAE40523.1.
AK169168 mRNA. Translation: BAE40947.1.
BC054768 mRNA. Translation: AAH54768.1.
IPIIPI00130173.
RefSeqNP_057891.1. NM_016682.2.
UniGeneMm.27560.

3D structure databases

ProteinModelPortalQ9Z1F9.
SMRQ9Z1F9. Positions 4-589.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Z1F9. 2 interactions.
STRINGQ9Z1F9.

PTM databases

PhosphoSiteQ9Z1F9.

Proteomic databases

PRIDEQ9Z1F9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102746; ENSMUSP00000099807; ENSMUSG00000052997.
GeneID50995.
KEGGmmu:50995.

Organism-specific databases

CTD10054.
MGIMGI:1858313. Uba2.

Phylogenomic databases

GeneTreeENSGT00550000074924.
HOGENOMHBG326381.
HOVERGENHBG060266.
InParanoidQ9Z1F9.
OMAMDFVAAC.
OrthoDBEOG4PRSQ8.
PhylomeDBQ9Z1F9.

Gene expression databases

ArrayExpressQ9Z1F9.
BgeeQ9Z1F9.
CleanExMM_UBA2.
GenevestigatorQ9Z1F9.
GermOnlineENSMUSG00000052997. Mus musculus.

Family and domain databases

InterProIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018074. UBQ-activ_enz_E1_AS.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
G3DSA:1.10.3240.10. Ub-like_act_enz_cat_cys_dom. 1 hit.
KOK10685.
PfamPF00899. ThiF. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]
SUPFAMSSF69572. MoeB. 1 hit.
PROSITEPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307996.
SOURCESearch...

Entry information

Entry nameSAE2_MOUSE
AccessionPrimary (citable) accession number: Q9Z1F9
Secondary accession number(s): Q3TQN3 expand/collapse secondary AC list , Q3U819, Q3U9J5, Q8BVX9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 1999
Last modified: November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents