Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

Uba1

Organism
Rattus norvegicus (Rat)
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. 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 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.By similarity
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 annotationBy similarity1

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

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 1By similarity (EC:6.2.1.45By similarity)
Alternative name(s):
Ubiquitin-activating enzyme E1By similarity
Gene namesi
Name:Uba1Imported
Synonyms:Ube1By similarity
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi1359327. 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_00003650962 – 1058Ubiquitin-like modifier-activating enzyme 1Add BLAST1057

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei4PhosphoserineBy similarity1
Modified residuei13PhosphoserineBy similarity1
Modified residuei21PhosphoserineBy similarity1
Modified residuei24PhosphoserineBy similarity1
Modified residuei46PhosphoserineCombined sources1
Modified residuei55PhosphotyrosineBy similarity1
Modified residuei528N6-succinyllysineBy similarity1
Modified residuei671N6-acetyllysineBy similarity1
Modified residuei800PhosphothreonineBy similarity1
Modified residuei810PhosphoserineBy similarity1
Modified residuei816PhosphoserineBy similarity1
Modified residuei820PhosphoserineBy similarity1
Modified residuei835PhosphoserineCombined sources1
Modified residuei980N6-acetyllysineBy similarity1

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ5U300.
PRIDEiQ5U300.

PTM databases

iPTMnetiQ5U300.
PhosphoSitePlusiQ5U300.

Expressioni

Gene expression databases

BgeeiENSRNOG00000019164.
GenevisibleiQ5U300. RN.

Interactioni

Subunit structurei

Monomer. Interacts with GAN (via BTB domain) (By similarity).By similarity

Protein-protein interaction databases

BioGridi260716. 3 interactors.
STRINGi10116.ENSRNOP00000033950.

Structurei

3D structure databases

ProteinModelPortaliQ5U300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Sequence analysis

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ5U300.
KOiK03178.
OMAiFAMAEPI.
OrthoDBiEOG091G0130.
PhylomeDBiQ5U300.
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.

Q5U300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSPLSKKR RVSGPDPKPG SNCSSAQSVL 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
LVEDFLSGFQ VVVLTNSPLE EQLRVGEFCH SRGIKLVVAD TRGLFGQLFC
210 220 230 240 250
DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFETGDFVSF
260 270 280 290 300
SEVQGMVQLN GCQPIEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
310 320 330 340 350
ISFKSLPASL AEPDFVMTDF AKYSRPAQLH IGFQALHQFC AQHNRPPRPR
360 370 380 390 400
NEEDATELVT LAQAVNARSP PAVQQDNVDE DLIRKLAYVA AGDLAPINAF
410 420 430 440 450
IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEALT EDKCLPRQNR
460 470 480 490 500
YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEV
510 520 530 540 550
VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PYIQVTSHQN
560 570 580 590 600
RVGPDTERIY DDDFFQNLDG VANALDNVDA 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):117,788
Last modified:December 7, 2004 - v1
Checksum:iFAC21190A3014F79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474009 Genomic DNA. Translation: EDL97701.1.
CH474009 Genomic DNA. Translation: EDL97702.1.
BC085791 mRNA. Translation: AAH85791.1.
RefSeqiNP_001014102.1. NM_001014080.1.
XP_006256674.1. XM_006256612.3.
XP_006256675.2. XM_006256613.3.
UniGeneiRn.11800.

Genome annotation databases

EnsembliENSRNOT00000031115; ENSRNOP00000033950; ENSRNOG00000019164.
GeneIDi314432.
KEGGirno:314432.
UCSCiRGD:1359327. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474009 Genomic DNA. Translation: EDL97701.1.
CH474009 Genomic DNA. Translation: EDL97702.1.
BC085791 mRNA. Translation: AAH85791.1.
RefSeqiNP_001014102.1. NM_001014080.1.
XP_006256674.1. XM_006256612.3.
XP_006256675.2. XM_006256613.3.
UniGeneiRn.11800.

3D structure databases

ProteinModelPortaliQ5U300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi260716. 3 interactors.
STRINGi10116.ENSRNOP00000033950.

PTM databases

iPTMnetiQ5U300.
PhosphoSitePlusiQ5U300.

Proteomic databases

PaxDbiQ5U300.
PRIDEiQ5U300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000031115; ENSRNOP00000033950; ENSRNOG00000019164.
GeneIDi314432.
KEGGirno:314432.
UCSCiRGD:1359327. rat.

Organism-specific databases

CTDi7317.
RGDi1359327. Uba1.

Phylogenomic databases

eggNOGiKOG2012. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ5U300.
KOiK03178.
OMAiFAMAEPI.
OrthoDBiEOG091G0130.
PhylomeDBiQ5U300.
TreeFamiTF300586.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ5U300.

Gene expression databases

BgeeiENSRNOG00000019164.
GenevisibleiQ5U300. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q5U300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: December 7, 2004
Last modified: November 30, 2016
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.