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Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

Uba1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

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

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

  • ATP binding Source: UniProtKB-KW
  • ubiquitin activating enzyme activity Source: MGI

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processUbl conjugation pathway
LigandATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:98890 Uba1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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, 15 interactors
ELMiQ02053
IntActiQ02053, 11 interactors
MINTiQ02053
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
OMAiLKNWSMM
OrthoDBiEOG091G0130
PhylomeDBiQ02053
TreeFamiTF300586

Family and domain databases

Gene3Di3.10.290.60, 1 hit
InterProiView protein in InterPro
IPR032420 E1_4HB
IPR032418 E1_FCCH
IPR000594 ThiF_NAD_FAD-bd
IPR018965 Ub-activating_enz_E1_C
IPR038252 UBA_E1_C_sf
IPR019572 UBA_E1_Cys
IPR035985 Ubiquitin-activating_enz
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
PfamiView protein in Pfam
PF16191 E1_4HB, 1 hit
PF16190 E1_FCCH, 1 hit
PF09358 E1_UFD, 1 hit
PF00899 ThiF, 2 hits
PF10585 UBA_e1_thiolCys, 1 hit
PRINTSiPR01849 UBIQUITINACT
SMARTiView protein in SMART
SM00985 UBA_e1_C, 1 hit
SUPFAMiSSF69572 SSF69572, 2 hits
TIGRFAMsiTIGR01408 Ube1, 1 hit
PROSITEiView protein in PROSITE
PS00536 UBIQUITIN_ACTIVAT_1, 1 hit
PS00865 UBIQUITIN_ACTIVAT_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiUBA1_MOUSE
AccessioniPrimary (citable) accession number: Q02053
Secondary accession number(s): A6H6S6, P31253, Q542H8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: March 28, 2018
This is version 188 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health