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Q02053 (UBA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Names and origin

Protein namesRecommended name:
Ubiquitin-like modifier-activating enzyme 1
Alternative name(s):
Ubiquitin-activating enzyme E1
Ubiquitin-activating enzyme E1 X
Ubiquitin-like modifier-activating enzyme 1 X
Gene names
Name:Uba1
Synonyms:Sbx, Ube1, Ube1ax, Ube1x
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1058 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Monomer. Interacts with GAN (via BTB domain).

Tissue specificity

Ubiquitously expressed. In testis, expressed in A spermatogonia and spermatids but at very low levels in pachytene spermatocytes. Ref.9

Developmental stage

In testis, highly expressed from 14.5 days post coitum (dpc) until the day of birth, with levels falling after 10 days post partum (dpp) but peaking again at 28 dpp. Ref.9

Induction

May be modulated by the thyroid hormone receptor. Ref.8

Post-translational modification

ISGylated. Ref.10

Miscellaneous

There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Sequence caution

The sequence CAA44465.1 differs from that shown. Reason: Frameshift at position 1033.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10581057Ubiquitin-like modifier-activating enzyme 1
PRO_0000194935

Regions

Repeat63 – 1991371-1
Repeat459 – 6111531-2
Nucleotide binding478 – 50730ATP By similarity
Region63 – 6115492 approximate repeats

Sites

Active site6321Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue131Phosphoserine By similarity
Modified residue461Phosphoserine By similarity
Modified residue551Phosphotyrosine Ref.11
Modified residue5281N6-succinyllysine Ref.13
Modified residue6711N6-acetyllysine Ref.13
Modified residue8001Phosphothreonine By similarity
Modified residue8101Phosphoserine By similarity
Modified residue8161Phosphoserine Ref.12
Modified residue8201Phosphoserine Ref.12
Modified residue8351Phosphoserine By similarity
Modified residue9801N6-acetyllysine By similarity

Experimental info

Sequence conflict9631L → V in CAA44465. Ref.6

Secondary structure

................................................ 1058
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02053 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 95D8152ED5C8E037

FASTA1,058117,809
        10         20         30         40         50         60 
MSSSPLSKKR RVSGPDPKPG SNCSPAQSAL SEVSSVPTNG MAKNGSEADI DESLYSRQLY 

        70         80         90        100        110        120 
VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTTQWA DLSSQFYLRE 

       130        140        150        160        170        180 
EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSSFQ VVVLTNSPLE AQLRVGEFCH 

       190        200        210        220        230        240 
SRGIKLVVAD TRGLFGQLFC DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH 

       250        260        270        280        290        300 
GFETGDFVSF SEVQGMIQLN GCQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK 

       310        320        330        340        350        360 
ISFKSLPASL VEPDFVMTDF AKYSRPAQLH IGFQALHQFC ALHNQPPRPR NEEDATELVG 

       370        380        390        400        410        420 
LAQAVNARSP PSVKQNSLDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI 

       430        440        450        460        470        480 
MQWLYFDALE CLPEDKEALT EEKCLPRQNR YDGQVAVFGS DFQEKLSKQK YFLVGAGAIG 

       490        500        510        520        530        540 
CELLKNFAMI GLGCGEGGEV VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN 

       550        560        570        580        590        600 
PYIQVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNIDA RMYMDRRCVY YRKPLLESGT 

       610        620        630        640        650        660 
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA 

       670        680        690        700        710        720 
ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWGDCVTWA CHHWHTQYCN 

       730        740        750        760        770        780 
NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG 

       790        800        810        820        830        840 
SQDRAAVASL LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP 

       850        860        870        880        890        900 
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA 

       910        920        930        940        950        960 
VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV 

       970        980        990       1000       1010       1020 
QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS 

      1030       1040       1050 
RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence of a functionally active cDNA encoding the mouse ubiquitin-activating enzyme E1."
Imai N., Kaneda S., Nagai Y., Seno T., Ayusawa D., Hanaoka F., Yamao F.
Gene 118:279-282(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Strain: C57BL/6J and NOD.
Tissue: Ovary and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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/6.
Tissue: Brain.
[5]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 69-81; 90-97; 175-182; 227-239; 351-368; 375-384; 386-411; 451-465; 471-485; 538-551; 559-581; 593-604; 636-671; 679-693; 785-802; 844-851; 870-880; 890-923; 945-980 AND 1011-1021, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1."
Mitchell M.J., Woods D.R., Tucker P.K., Opp J.S., Bishop C.E.
Nature 354:483-487(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 615-1058.
Strain: 129/Sv.
[7]"Estimating the intensity of male-driven evolution in rodents by using X-linked and Y-linked Ube 1 genes and pseudogenes."
Chang B.H.-J., Li W.H.
J. Mol. Evol. 40:70-77(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 655-763.
Strain: BALB/c AnCr.
Tissue: Liver.
[8]"Isolation of genomic DNA fragments corresponding to genes modulated in vivo by a transcription factor."
Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L., Zaballos A.
Nucleic Acids Res. 22:4132-4138(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION OF EXPRESSION BY THE THYROID HORMONE RECEPTOR.
[9]"Transcriptional analysis of the candidate spermatogenesis gene Ube1y and of the closely related Ube1x shows that they are coexpressed in spermatogonia and spermatids but are repressed in pachytene spermatocytes."
Odorisio T., Mahadevaiah S.K., McCarrey J.R., Burgoyne P.S.
Dev. Biol. 180:336-343(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[10]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[11]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[12]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816 AND SER-820, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"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-671, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[14]"Crystal structure of a fragment of mouse ubiquitin-activating enzyme."
Szczepanowski R.H., Filipek R., Bochtler M.
J. Biol. Chem. 280:22006-22011(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 626-891.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10576 mRNA. Translation: BAA01433.1.
AK088057 mRNA. Translation: BAC40121.1.
AK088528 mRNA. Translation: BAC40405.1.
AK143416 mRNA. Translation: BAE25369.1.
AK171667 mRNA. Translation: BAE42599.1.
AL807240 Genomic DNA. Translation: CAM23092.1.
BC058630 mRNA. Translation: AAH58630.1.
BC145984 mRNA. Translation: AAI45985.1.
X62580 mRNA. Translation: CAA44465.1. Frameshift.
U09051 Genomic DNA. Translation: AAC52169.1.
U09055 Genomic DNA. Translation: AAC52171.1.
PIRI48756.
I63168.
JC1254.
RefSeqNP_001129557.1. NM_001136085.2.
NP_001263245.1. NM_001276316.1.
NP_001263246.1. NM_001276317.1.
NP_033483.2. NM_009457.4.
UniGeneMm.1104.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7LX-ray2.80A/B/C626-891[»]
2LZJNMR-A202-312[»]
2V31NMR-A203-312[»]
ProteinModelPortalQ02053.
SMRQ02053. Positions 50-1053.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204410. 5 interactions.
IntActQ02053. 7 interactions.
MINTMINT-1869675.

PTM databases

PhosphoSiteQ02053.

Proteomic databases

PaxDbQ02053.
PRIDEQ02053.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.
GeneID22201.
KEGGmmu:22201.
UCSCuc009stl.1. mouse.

Organism-specific databases

CTD7317.
MGIMGI:98890. Uba1.

Phylogenomic databases

eggNOGCOG0476.
GeneTreeENSGT00390000016689.
HOGENOMHOG000167329.
HOVERGENHBG054199.
InParanoidQ02053.
KOK03178.
OMAPFFAFSE.
OrthoDBEOG74R1PV.
PhylomeDBQ02053.
TreeFamTF300586.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ02053.
BgeeQ02053.
CleanExMM_UBA1.
GenevestigatorQ02053.

Family and domain databases

Gene3D1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]
PRINTSPR01849. UBIQUITINACT.
SMARTSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 2 hits.
TIGRFAMsTIGR01408. Ube1. 1 hit.
PROSITEPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBA1. mouse.
EvolutionaryTraceQ02053.
NextBio302189.
PROQ02053.
SOURCESearch...

Entry information

Entry nameUBA1_MOUSE
AccessionPrimary (citable) accession number: Q02053
Secondary accession number(s): A6H6S6, P31253, Q542H8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 147 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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