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Protein

SUMO-activating enzyme subunit 2

Gene

Uba2

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Pathwayi: protein 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481ATPBy similarity
Binding sitei72 – 721ATPBy similarity
Metal bindingi158 – 1581ZincBy similarity
Metal bindingi161 – 1611ZincBy similarity
Active sitei173 – 1731Glycyl thioester intermediatePROSITE-ProRule annotation
Metal bindingi439 – 4391ZincBy similarity
Metal bindingi442 – 4421ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 296ATPBy similarity
Nucleotide bindingi56 – 594ATPBy similarity
Nucleotide bindingi95 – 962ATPBy similarity
Nucleotide bindingi117 – 1226ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-MMU-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
SUMO-activating enzyme subunit 2 (EC:6.3.2.-)
Alternative name(s):
Anthracycline-associated resistance ARX
Ubiquitin-like 1-activating enzyme E1B
Ubiquitin-like modifier-activating enzyme 2
Gene namesi
Name:Uba2
Synonyms:Sae2, Uble1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1858313. Uba2.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638SUMO-activating enzyme subunit 2PRO_0000194969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki190 – 190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei207 – 2071PhosphoserineCombined sources
Cross-linki236 – 236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki236 – 236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki257 – 257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei271 – 2711N6-acetyllysine; alternateCombined sources
Cross-linki271 – 271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki275 – 275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei505 – 5051PhosphoserineBy similarity
Modified residuei548 – 5481PhosphoserineCombined sources
Modified residuei590 – 5901PhosphoserineCombined sources
Cross-linki609 – 609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei611 – 6111N6-acetyllysine; alternateCombined sources
Cross-linki611 – 611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki621 – 621Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-236 inhibits enzymatic activity. Sumoylation at the C-terminal lysine cluster plays an essential role in nuclear trafficking (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Z1F9.
MaxQBiQ9Z1F9.
PaxDbiQ9Z1F9.
PRIDEiQ9Z1F9.

PTM databases

iPTMnetiQ9Z1F9.
PhosphoSiteiQ9Z1F9.
SwissPalmiQ9Z1F9.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in testis.1 Publication

Gene expression databases

BgeeiQ9Z1F9.
CleanExiMM_UBA2.
ExpressionAtlasiQ9Z1F9. baseline and differential.
GenevisibleiQ9Z1F9. MM.

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

GO - Molecular functioni

  • protein heterodimerization activity Source: MGI
  • transcription factor binding Source: MGI

Protein-protein interaction databases

BioGridi206169. 2 interactions.
IntActiQ9Z1F9. 3 interactions.
MINTiMINT-4139526.
STRINGi10090.ENSMUSP00000099807.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1F9.
SMRiQ9Z1F9. Positions 4-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiKOG2013. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00550000074924.
HOGENOMiHOG000216514.
HOVERGENiHBG060266.
InParanoidiQ9Z1F9.
KOiK10685.
OMAiTAYHDSV.
OrthoDBiEOG7S7SDB.
PhylomeDBiQ9Z1F9.
TreeFamiTF300765.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR016040. NAD(P)-bd_dom.
IPR030661. SAE2/Uba2.
IPR000594. ThiF_NAD_FAD-bd.
IPR028077. UAE_UbL_dom.
IPR032426. UBA2_C.
IPR019572. UBA_E1_Cys.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF14732. UAE_UbL. 1 hit.
PF16195. UBA2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF039133. SUMO_E1B. 1 hit.
SUPFAMiSSF69572. SSF69572. 2 hits.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z1F9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSRGLPRE LAEAVSGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD
60 70 80 90 100
TIDVSNLNRQ FLFQKKHVGR SKAQVAKESV LQFHPQANIE AHHDSIMNPD
110 120 130 140 150
YNVEFFRQFI LVMNALDNRA ARNHVNRMCL AADVPLIESG TAGYLGQVTT
160 170 180 190 200
IKKGVTECYE CHPKPTQRTF PGCTIRNTPS EPIHCIVWAK YLFNQLFGEE
210 220 230 240 250
DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST KEWAKSTGYD
260 270 280 290 300
PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEANADQQNE
310 320 330 340 350
PQLGLKDQQV LDVKSYASLF SKSIETLRVH LAEKGDGAEL IWDKDDPPAM
360 370 380 390 400
DFVTSAANLR MHIFSMNMKS RFDIKSMAGN IIPAIATTNA VIAGLIVLEG
410 420 430 440 450
LKILSGKIDQ CRTIFLNKQP NPRKKLLVPC ALDPPNTNCY VCASKPEVTV
460 470 480 490 500
RLNVHKVTVL TLQDKIVKEK FAMVAPDVQI EDGKGTILIS SEEGETEANN
510 520 530 540 550
PKKLSDFGIR NGSRLQADDF LQDYTLLINI LHSEDLGKDV EFEVVGDSPE
560 570 580 590 600
KVGPKQAEDA AKSIANGSDD GAQPSTSTAQ EQDDVLIVDS DEEGPSNSTD
610 620 630
CSGDDKARKR KLEENEAAST KKCRLEQMED PDDVIALD
Length:638
Mass (Da):70,569
Last modified:May 1, 1999 - v1
Checksum:i065C72C1CA7F4CA7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091D → V in BAE37349 (PubMed:16141072).Curated
Sequence conflicti542 – 5421F → L in BAE30671 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21136.1.
RefSeqiNP_057891.1. NM_016682.2.
UniGeneiMm.27560.

Genome annotation databases

EnsembliENSMUST00000102746; ENSMUSP00000099807; ENSMUSG00000052997.
GeneIDi50995.
KEGGimmu:50995.
UCSCiuc009giu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21136.1.
RefSeqiNP_057891.1. NM_016682.2.
UniGeneiMm.27560.

3D structure databases

ProteinModelPortaliQ9Z1F9.
SMRiQ9Z1F9. Positions 4-589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206169. 2 interactions.
IntActiQ9Z1F9. 3 interactions.
MINTiMINT-4139526.
STRINGi10090.ENSMUSP00000099807.

PTM databases

iPTMnetiQ9Z1F9.
PhosphoSiteiQ9Z1F9.
SwissPalmiQ9Z1F9.

Proteomic databases

EPDiQ9Z1F9.
MaxQBiQ9Z1F9.
PaxDbiQ9Z1F9.
PRIDEiQ9Z1F9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102746; ENSMUSP00000099807; ENSMUSG00000052997.
GeneIDi50995.
KEGGimmu:50995.
UCSCiuc009giu.1. mouse.

Organism-specific databases

CTDi10054.
MGIiMGI:1858313. Uba2.

Phylogenomic databases

eggNOGiKOG2013. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00550000074924.
HOGENOMiHOG000216514.
HOVERGENiHBG060266.
InParanoidiQ9Z1F9.
KOiK10685.
OMAiTAYHDSV.
OrthoDBiEOG7S7SDB.
PhylomeDBiQ9Z1F9.
TreeFamiTF300765.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-MMU-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-MMU-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Miscellaneous databases

ChiTaRSiUba2. mouse.
NextBioi307996.
PROiQ9Z1F9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z1F9.
CleanExiMM_UBA2.
ExpressionAtlasiQ9Z1F9. baseline and differential.
GenevisibleiQ9Z1F9. MM.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR016040. NAD(P)-bd_dom.
IPR030661. SAE2/Uba2.
IPR000594. ThiF_NAD_FAD-bd.
IPR028077. UAE_UbL_dom.
IPR032426. UBA2_C.
IPR019572. UBA_E1_Cys.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
PF14732. UAE_UbL. 1 hit.
PF16195. UBA2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF039133. SUMO_E1B. 1 hit.
SUPFAMiSSF69572. SSF69572. 2 hits.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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].
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-548 AND SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "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-271 AND LYS-611, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSAE2_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1F9
Secondary accession number(s): Q3TQN3
, Q3U819, Q3U9J5, Q8BVX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 126 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

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 one 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.