Q02053 (UBA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1058 AA.
Sequence status	Complete.
Protein existence	Evidence 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 an 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ligase activity Inferred from electronic annotation. Source: UniProtKB-KW small protein activating enzyme activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1058

1058

Ubiquitin-like modifier-activating enzyme 1

PRO_0000194935

Regions

Repeat

63 – 199

137

1-1

Repeat

459 – 611

153

1-2

Nucleotide binding

478 – 507

30

ATP By similarity

Region

63 – 611

549

2 approximate repeats

Sites

Active site

632

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

13

1

Phosphoserine By similarity

Modified residue

21

1

Phosphoserine Ref.13

Modified residue

24

1

Phosphoserine Ref.13

Modified residue

31

1

Phosphoserine Ref.13

Modified residue

46

1

Phosphoserine Ref.12

Modified residue

55

1

Phosphotyrosine Ref.11

Modified residue

671

1

N6-acetyllysine By similarity

Modified residue

800

1

Phosphothreonine By similarity

Modified residue

810

1

Phosphoserine By similarity

Modified residue

816

1

Phosphoserine Ref.13

Modified residue

820

1

Phosphoserine Ref.13

Modified residue

835

1

Phosphoserine Ref.13

Modified residue

980

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

963

1

L → V in CAA44465. Ref.6

Secondary structure

1

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1058

Helix Strand Turn

Details...

Beta strand

218 – 224

7

Beta strand

227 – 234

8

Beta strand

247 – 250

4

Beta strand

252 – 255

4

Helix

260 – 262

3

Beta strand

265 – 269

5

Beta strand

271 – 278

8

Beta strand

291 – 293

3

Helix

631 – 635

5

Helix

641 – 656

16

Helix

658 – 666

9

Helix

671 – 677

7

Helix

683 – 695

13

Turn

696 – 698

3

Helix

703 – 718

16

Helix

720 – 728

9

Beta strand

740 – 742

3

Helix

759 – 775

17

Helix

784 – 792

9

Beta strand

809 – 811

3

Helix

824 – 832

9

Helix

836 – 838

3

Helix

858 – 872

15

Helix

880 – 886

7

Sequences

	Sequence		Length	Mass (Da)
	Q02053 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 95D8152ED5C8E037	FASTA	1,058	117,809
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. Tissue: Mast cell.
[12]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY. Tissue: Liver.
[13]	"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-21; SER-24; SER-31; SER-816; SER-820 AND SER-835, MASS SPECTROMETRY. Tissue: Liver.
[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.

IPI

IPI00123313.

PIR

I48756.
I63168.
JC1254.

RefSeq

NP_001129557.1. NM_001136085.2.
NP_001263245.1. NM_001276316.1.
NP_001263246.1. NM_001276317.1.
NP_033483.2. NM_009457.4.

UniGene

Mm.1104.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z7L	X-ray	2.80	A/B/C	626-891	[»]
2V31	NMR	-	A	203-312	[»]

ProteinModelPortal

Q02053.

SMR

Q02053. Positions 48-1053.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q02053. 4 interactions.

MINT

MINT-1869675.

PTM databases

PhosphoSite

Q02053.

Proteomic databases

PaxDb

Q02053.

PRIDE

Q02053.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.

GeneID

22201.

KEGG

mmu:22201.

UCSC

uc009stl.1. mouse.

Organism-specific databases

CTD

7317.

MGI

MGI:98890. Uba1.

Phylogenomic databases

eggNOG

COG0476.

GeneTree

ENSGT00390000016689.

HOGENOM

HOG000167329.

HOVERGEN

HBG054199.

InParanoid

Q02053.

KO

K03178.

OrthoDB

EOG4QZ7K4.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q02053.

Bgee

Q02053.

CleanEx

MM_UBA1.

Genevestigator

Q02053.

GermOnline

ENSMUSG00000001924. Mus musculus.

Family and domain databases

Gene3D

1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.

InterPro

IPR009036. 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]

Pfam

PF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view]

PRINTS

PR01849. UBIQUITINACT.

SMART

SM00985. UBA_e1_C. 1 hit.
[Graphical view]

SUPFAM

SSF69572. MoeB. 2 hits.

TIGRFAMs

TIGR01408. Ube1. 1 hit.

PROSITE

PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UBA1. mouse.

EvolutionaryTrace

Q02053.

NextBio

302189.

SOURCE

Search...

Entry information

Entry name

UBA1_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program