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Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

Uba1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system (PubMed:1511901). 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. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites.By similarity1 Publication

Catalytic activityi

ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei478ATP; via amide nitrogenBy similarity1
Binding sitei504ATPBy similarity1
Binding sitei515ATPBy similarity1
Binding sitei528ATPBy similarity1
Active sitei632Glycyl thioester intermediatePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi576 – 577ATPBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.2.1.B9. 3474.
ReactomeiR-MMU-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 1 (EC:6.2.1.45By similarity)
Alternative name(s):
Ubiquitin-activating enzyme E1
Ubiquitin-activating enzyme E1 X
Ubiquitin-like modifier-activating enzyme 1 X
Gene namesi
Name:Uba1
Synonyms:Sbx, Ube1, Ube1ax, Ube1x
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:98890. Uba1.

Subcellular locationi

  • Cytoplasm By similarity
  • Mitochondrion By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001949352 – 1058Ubiquitin-like modifier-activating enzyme 1Add BLAST1057

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei4PhosphoserineBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei21PhosphoserineCombined sources1
Modified residuei24PhosphoserineCombined sources1
Modified residuei46PhosphoserineCombined sources1
Modified residuei55PhosphotyrosineCombined sources1
Modified residuei528N6-succinyllysineCombined sources1
Modified residuei671N6-acetyllysineCombined sources1
Modified residuei800PhosphothreonineBy similarity1
Modified residuei810PhosphoserineCombined sources1
Modified residuei816PhosphoserineCombined sources1
Modified residuei820PhosphoserineCombined sources1
Modified residuei835PhosphoserineCombined sources1
Modified residuei980N6-acetyllysineBy similarity1

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ02053.
MaxQBiQ02053.
PaxDbiQ02053.
PRIDEiQ02053.

PTM databases

iPTMnetiQ02053.
PhosphoSitePlusiQ02053.
SwissPalmiQ02053.

Expressioni

Tissue specificityi

Ubiquitously expressed. In testis, expressed in A spermatogonia and spermatids but at very low levels in pachytene spermatocytes.1 Publication

Developmental stagei

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.1 Publication

Inductioni

May be modulated by the thyroid hormone receptor.

Gene expression databases

BgeeiENSMUSG00000001924.
CleanExiMM_UBA1.
ExpressionAtlasiQ02053. baseline and differential.
GenevisibleiQ02053. MM.

Interactioni

Subunit structurei

Monomer. Interacts with GAN (via BTB domain).

Protein-protein interaction databases

BioGridi204410. 8 interactors.
IntActiQ02053. 9 interactors.
MINTiMINT-1869675.
STRINGi10090.ENSMUSP00000001989.

Structurei

Secondary structure

11058
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni203 – 205Combined sources3
Beta strandi218 – 225Combined sources8
Beta strandi227 – 234Combined sources8
Beta strandi246 – 255Combined sources10
Helixi257 – 260Combined sources4
Beta strandi265 – 278Combined sources14
Helixi280 – 282Combined sources3
Beta strandi288 – 294Combined sources7
Helixi631 – 635Combined sources5
Helixi641 – 656Combined sources16
Helixi658 – 666Combined sources9
Helixi671 – 677Combined sources7
Helixi683 – 695Combined sources13
Turni696 – 698Combined sources3
Helixi703 – 718Combined sources16
Helixi720 – 728Combined sources9
Beta strandi740 – 742Combined sources3
Helixi759 – 775Combined sources17
Helixi784 – 792Combined sources9
Beta strandi809 – 811Combined sources3
Helixi824 – 832Combined sources9
Helixi836 – 838Combined sources3
Helixi858 – 872Combined sources15
Helixi880 – 886Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z7LX-ray2.80A/B/C626-891[»]
2LZJNMR-A202-312[»]
2V31NMR-A202-312[»]
ProteinModelPortaliQ02053.
SMRiQ02053.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02053.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati63 – 1991-1Add BLAST137
Repeati459 – 6111-2Add BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 6112 approximate repeatsAdd BLAST549

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ02053.
KOiK03178.
OMAiFAMAEPI.
OrthoDBiEOG091G0130.
PhylomeDBiQ02053.
TreeFamiTF300586.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSPLSKKR RVSGPDPKPG SNCSPAQSAL SEVSSVPTNG MAKNGSEADI
60 70 80 90 100
DESLYSRQLY VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT
110 120 130 140 150
LHDQGTTQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVTAYTGP
160 170 180 190 200
LVEDFLSSFQ VVVLTNSPLE AQLRVGEFCH SRGIKLVVAD TRGLFGQLFC
210 220 230 240 250
DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFETGDFVSF
260 270 280 290 300
SEVQGMIQLN GCQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
310 320 330 340 350
ISFKSLPASL VEPDFVMTDF AKYSRPAQLH IGFQALHQFC ALHNQPPRPR
360 370 380 390 400
NEEDATELVG LAQAVNARSP PSVKQNSLDE DLIRKLAYVA AGDLAPINAF
410 420 430 440 450
IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEALT EEKCLPRQNR
460 470 480 490 500
YDGQVAVFGS DFQEKLSKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEV
510 520 530 540 550
VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PYIQVTSHQN
560 570 580 590 600
RVGPDTERIY DDDFFQNLDG VANALDNIDA RMYMDRRCVY YRKPLLESGT
610 620 630 640 650
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD
660 670 680 690 700
EFEGLFKQPA ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP
710 720 730 740 750
QTWGDCVTWA CHHWHTQYCN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH
760 770 780 790 800
PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG SQDRAAVASL LQSVQVPEFT
810 820 830 840 850
PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP GFKMYPIDFE
860 870 880 890 900
KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA
910 920 930 940 950
VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ
960 970 980 990 1000
EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF
1010 1020 1030 1040 1050
FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV

PYVRYTIR
Length:1,058
Mass (Da):117,809
Last modified:April 1, 1993 - v1
Checksum:i95D8152ED5C8E037
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti963L → V in CAA44465 (PubMed:1684224).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30044.1.
PIRiI48756.
I63168.
JC1254.
RefSeqiNP_001129557.1. NM_001136085.2.
NP_001263245.1. NM_001276316.1.
NP_001263246.1. NM_001276317.1.
NP_033483.2. NM_009457.4.
UniGeneiMm.1104.

Genome annotation databases

EnsembliENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.
GeneIDi22201.
KEGGimmu:22201.
UCSCiuc009stl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30044.1.
PIRiI48756.
I63168.
JC1254.
RefSeqiNP_001129557.1. NM_001136085.2.
NP_001263245.1. NM_001276316.1.
NP_001263246.1. NM_001276317.1.
NP_033483.2. NM_009457.4.
UniGeneiMm.1104.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z7LX-ray2.80A/B/C626-891[»]
2LZJNMR-A202-312[»]
2V31NMR-A202-312[»]
ProteinModelPortaliQ02053.
SMRiQ02053.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204410. 8 interactors.
IntActiQ02053. 9 interactors.
MINTiMINT-1869675.
STRINGi10090.ENSMUSP00000001989.

PTM databases

iPTMnetiQ02053.
PhosphoSitePlusiQ02053.
SwissPalmiQ02053.

Proteomic databases

EPDiQ02053.
MaxQBiQ02053.
PaxDbiQ02053.
PRIDEiQ02053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.
GeneIDi22201.
KEGGimmu:22201.
UCSCiuc009stl.2. mouse.

Organism-specific databases

CTDi7317.
MGIiMGI:98890. Uba1.

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ02053.
KOiK03178.
OMAiFAMAEPI.
OrthoDBiEOG091G0130.
PhylomeDBiQ02053.
TreeFamiTF300586.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.2.1.B9. 3474.
ReactomeiR-MMU-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiUba1. mouse.
EvolutionaryTraceiQ02053.
PROiQ02053.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000001924.
CleanExiMM_UBA1.
ExpressionAtlasiQ02053. baseline and differential.
GenevisibleiQ02053. MM.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR032420. E1_4HB.
IPR032418. E1_FCCH.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_E1_C.
IPR019572. UBA_E1_Cys.
IPR018075. UBQ-activ_enz_E1.
IPR018074. UBQ-activ_enz_E1_CS.
IPR033127. UBQ-activ_enz_E1_Cys_AS.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF16191. E1_4HB. 1 hit.
PF16190. E1_FCCH. 1 hit.
PF09358. E1_UFD. 1 hit.
PF00899. ThiF. 2 hits.
PF10585. UBA_e1_thiolCys. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.
PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBA1_MOUSE
AccessioniPrimary (citable) accession number: Q02053
Secondary accession number(s): A6H6S6, P31253, Q542H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 30, 2016
This is version 177 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.