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Q5U300

- UBA1_RAT

UniProt

Q5U300 - UBA1_RAT

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Protein
Ubiquitin-like modifier-activating enzyme 1
Gene
Uba1, Ube1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei632 – 6321Glycyl thioester intermediate By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi478 – 50730ATP By similarityBy similarity
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ubiquitin activating enzyme activity Source: RefGenome
  3. ubiquitin-protein transferase activity Source: RefGenome

GO - Biological processi

  1. modification-dependent protein catabolic process Source: RefGenome
  2. protein ubiquitination Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 1
Alternative name(s):
Ubiquitin-activating enzyme E1
Gene namesi
Name:Uba1
Synonyms:Ube1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome X

Organism-specific databases

RGDi1359327. Uba1.

Subcellular locationi

Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
  3. mitochondrion Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 10581057Ubiquitin-like modifier-activating enzyme 1
PRO_0000365096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei4 – 41Phosphoserine By similarity
Modified residuei13 – 131Phosphoserine By similarityBy similarity
Modified residuei46 – 461Phosphoserine By similarityBy similarity
Modified residuei55 – 551Phosphotyrosine By similarityBy similarity
Modified residuei528 – 5281N6-succinyllysine By similarity
Modified residuei671 – 6711N6-acetyllysine By similarity
Modified residuei800 – 8001Phosphothreonine By similarityBy similarity
Modified residuei810 – 8101Phosphoserine By similarity
Modified residuei816 – 8161Phosphoserine By similarityBy similarity
Modified residuei820 – 8201Phosphoserine By similarityBy similarity
Modified residuei835 – 8351Phosphoserine By similarityBy similarity
Modified residuei980 – 9801N6-acetyllysine By similarity

Post-translational modificationi

ISGylated By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ5U300.
PRIDEiQ5U300.

PTM databases

PhosphoSiteiQ5U300.

Expressioni

Gene expression databases

GenevestigatoriQ5U300.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi260716. 3 interactions.
STRINGi10116.ENSRNOP00000033950.

Structurei

3D structure databases

ProteinModelPortaliQ5U300.
SMRiQ5U300. Positions 48-1057.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati63 – 1991371-1
Add
BLAST
Repeati459 – 6111531-2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 6115492 approximate repeats
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOGENOMiHOG000167329.
HOVERGENiHBG054199.
InParanoidiQ5U300.
KOiK03178.
OMAiPFFAFSE.
OrthoDBiEOG74R1PV.
PhylomeDBiQ5U300.
TreeFamiTF300586.

Family and domain databases

Gene3Di1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProiIPR009036. 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]
PfamiPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[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

MSSSPLSKKR RVSGPDPKPG SNCSSAQSVL SEVSSVPTNG MAKNGSEADI     50
DESLYSRQLY VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT 100
LHDQGTTQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVTAYTGP 150
LVEDFLSGFQ VVVLTNSPLE EQLRVGEFCH SRGIKLVVAD TRGLFGQLFC 200
DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFETGDFVSF 250
SEVQGMVQLN GCQPIEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK 300
ISFKSLPASL AEPDFVMTDF AKYSRPAQLH IGFQALHQFC AQHNRPPRPR 350
NEEDATELVT LAQAVNARSP PAVQQDNVDE DLIRKLAYVA AGDLAPINAF 400
IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEALT EDKCLPRQNR 450
YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEV 500
VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PYIQVTSHQN 550
RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT 600
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD 650
EFEGLFKQPA ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP 700
QTWGDCVTWA CHHWHTQYCN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH 750
PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG SQDRAAVASL LQSVQVPEFT 800
PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP GFKMYPIDFE 850
KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA 900
VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ 950
EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF 1000
FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV 1050
PYVRYTIR 1058
Length:1,058
Mass (Da):117,788
Last modified:December 7, 2004 - v1
Checksum:iFAC21190A3014F79
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006256612.1.
UniGeneiRn.11800.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CH474009 Genomic DNA. Translation: EDL97701.1 .
CH474009 Genomic DNA. Translation: EDL97702.1 .
BC085791 mRNA. Translation: AAH85791.1 .
RefSeqi NP_001014102.1. NM_001014080.1.
XP_006256674.1. XM_006256612.1.
UniGenei Rn.11800.

3D structure databases

ProteinModelPortali Q5U300.
SMRi Q5U300. Positions 48-1057.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 260716. 3 interactions.
STRINGi 10116.ENSRNOP00000033950.

PTM databases

PhosphoSitei Q5U300.

Proteomic databases

PaxDbi Q5U300.
PRIDEi Q5U300.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000031115 ; ENSRNOP00000033950 ; ENSRNOG00000019164 .
GeneIDi 314432.
KEGGi rno:314432.
UCSCi RGD:1359327. rat.

Organism-specific databases

CTDi 7317.
RGDi 1359327. Uba1.

Phylogenomic databases

eggNOGi COG0476.
GeneTreei ENSGT00390000016689.
HOGENOMi HOG000167329.
HOVERGENi HBG054199.
InParanoidi Q5U300.
KOi K03178.
OMAi PFFAFSE.
OrthoDBi EOG74R1PV.
PhylomeDBi Q5U300.
TreeFami TF300586.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi 667673.
PROi Q5U300.

Gene expression databases

Genevestigatori Q5U300.

Family and domain databases

Gene3Di 1.10.3240.10. 1 hit.
3.40.50.720. 4 hits.
InterProi 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 ]
Pfami PF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 2 hits.
[Graphical view ]
PRINTSi PR01849. UBIQUITINACT.
SMARTi SM00985. UBA_e1_C. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 2 hits.
TIGRFAMsi TIGR01408. Ube1. 1 hit.
PROSITEi PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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: Brown Norway.
    Tissue: Kidney.
  3. Maurya D.K., Bhargava P.
    Submitted (JAN-2009) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

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: September 3, 2014
This is version 88 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.

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

External Data

Dasty 3

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