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Protein

Ubiquitin-activating enzyme E1 1

Gene

ptr3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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.1 Publication

Catalytic activityi

ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.1 Publication

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 sitei22ATPCombined sources1 Publication1
Binding sitei437ATP; via amide nitrogenCombined sources1 Publication1
Binding sitei463ATPCombined sources1 Publication1
Binding sitei474ATPCombined sources1 Publication1
Binding sitei487ATPCombined sources1 Publication1
Binding sitei513ATP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Active sitei593Glycyl thioester intermediatePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi537 – 538ATPCombined sources1 Publication2

GO - Molecular functioni

  • ATP binding Source: PomBase
  • magnesium ion binding Source: PomBase
  • ubiquitin activating enzyme activity Source: PomBase
  • ubiquitin-protein transferase activity Source: GO_Central

GO - Biological processi

  • modification-dependent protein catabolic process Source: GO_Central
  • protein ubiquitination Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-activating enzyme E1 1 (EC:6.2.1.451 Publication)
Alternative name(s):
Poly(A)+ RNA transport protein 3
Gene namesi
Name:ptr3
ORF Names:SPBC1604.21c, SPBC211.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1604.21c.
PomBaseiSPBC1604.21c. ptr3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi592I → G: Strongly reduces enzyme activity. 1 Publication1
Mutagenesisi598F → A: Nearly abolishes enzyme activity; when associated with A-701. 1 Publication1
Mutagenesisi689F → A: Abolishes enzyme activity; when associated with A-701. 1 Publication1
Mutagenesisi701F → A: Nearly abolishes enzyme activity; when associated with A-598. Abolishes enzyme activity; when associated with A-689. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001949761 – 1012Ubiquitin-activating enzyme E1 1Add BLAST1012

Proteomic databases

MaxQBiO94609.
PRIDEiO94609.

Interactioni

Subunit structurei

Monomer. Interacts with the E2 ubiquitin-conjugating enzyme ubc4.1 Publication

Protein-protein interaction databases

BioGridi277267. 7 interactors.
DIPiDIP-48686N.
MINTiMINT-4685507.

Structurei

Secondary structure

11012
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 27Combined sources11
Helixi29 – 36Combined sources8
Beta strandi39 – 43Combined sources5
Helixi47 – 59Combined sources13
Beta strandi62 – 67Combined sources6
Helixi74 – 78Combined sources5
Helixi85 – 87Combined sources3
Helixi92 – 101Combined sources10
Beta strandi109 – 111Combined sources3
Helixi118 – 122Combined sources5
Beta strandi124 – 128Combined sources5
Helixi133 – 145Combined sources13
Beta strandi149 – 156Combined sources8
Beta strandi159 – 165Combined sources7
Beta strandi170 – 176Combined sources7
Beta strandi182 – 189Combined sources8
Beta strandi193 – 197Combined sources5
Beta strandi209 – 214Combined sources6
Helixi221 – 223Combined sources3
Beta strandi233 – 238Combined sources6
Beta strandi247 – 251Combined sources5
Beta strandi253 – 257Combined sources5
Beta strandi261 – 263Combined sources3
Helixi268 – 271Combined sources4
Beta strandi272 – 274Combined sources3
Helixi282 – 284Combined sources3
Helixi287 – 304Combined sources18
Turni305 – 307Combined sources3
Helixi315 – 331Combined sources17
Helixi340 – 348Combined sources9
Turni349 – 351Combined sources3
Helixi355 – 372Combined sources18
Beta strandi382 – 387Combined sources6
Helixi389 – 391Combined sources3
Beta strandi394 – 396Combined sources3
Helixi400 – 403Combined sources4
Helixi411 – 417Combined sources7
Helixi419 – 426Combined sources8
Beta strandi429 – 433Combined sources5
Helixi437 – 449Combined sources13
Turni450 – 452Combined sources3
Beta strandi454 – 456Combined sources3
Beta strandi458 – 462Combined sources5
Helixi469 – 471Combined sources3
Turni472 – 474Combined sources3
Helixi480 – 482Combined sources3
Helixi487 – 498Combined sources12
Helixi500 – 502Combined sources3
Beta strandi505 – 509Combined sources5
Helixi515 – 517Combined sources3
Turni518 – 520Combined sources3
Helixi523 – 527Combined sources5
Beta strandi530 – 534Combined sources5
Helixi539 – 552Combined sources14
Beta strandi556 – 562Combined sources7
Beta strandi565 – 571Combined sources7
Turni573 – 575Combined sources3
Helixi579 – 581Combined sources3
Helixi592 – 597Combined sources6
Helixi602 – 617Combined sources16
Helixi619 – 627Combined sources9
Helixi633 – 637Combined sources5
Turni638 – 640Combined sources3
Helixi644 – 655Combined sources12
Turni656 – 658Combined sources3
Helixi663 – 678Combined sources16
Helixi680 – 688Combined sources9
Beta strandi698 – 702Combined sources5
Helixi719 – 735Combined sources17
Helixi744 – 752Combined sources9
Turni780 – 782Combined sources3
Helixi788 – 792Combined sources5
Helixi797 – 799Combined sources3
Helixi819 – 833Combined sources15
Helixi841 – 848Combined sources8
Helixi856 – 874Combined sources19
Helixi880 – 882Combined sources3
Beta strandi885 – 889Combined sources5
Helixi890 – 892Combined sources3
Beta strandi894 – 898Combined sources5
Beta strandi905 – 908Combined sources4
Beta strandi911 – 914Combined sources4
Turni915 – 917Combined sources3
Beta strandi919 – 924Combined sources6
Helixi927 – 936Combined sources10
Beta strandi941 – 947Combined sources7
Beta strandi950 – 954Combined sources5
Helixi959 – 963Combined sources5
Turni964 – 967Combined sources4
Helixi970 – 977Combined sources8
Beta strandi988 – 996Combined sources9
Beta strandi1007 – 1011Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4II2X-ray2.20A13-1012[»]
4II3X-ray2.90A/C13-1012[»]
ProteinModelPortaliO94609.
SMRiO94609.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

HOGENOMiHOG000167329.
InParanoidiO94609.
KOiK03178.
OMAiKMKSDCA.
OrthoDBiEOG092C3FGE.
PhylomeDBiO94609.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
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.
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.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94609-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNNMNIDQT DQNTIDEGLY SRQLYVLGHE AMKQMSQSNV LIIGCKGLGV
60 70 80 90 100
EIAKNVCLAG VKSVTLYDPQ PTRIEDLSSQ YFLTEDDIGV PRAKVTVSKL
110 120 130 140 150
AELNQYVPVS VVDELSTEYL KNFKCVVVTE TSLTKQLEIN DFTHKNHIAY
160 170 180 190 200
IAADSRGLFG SIFCDFGENF ICTDTDGNEP LTGMIASITD DGVVTMLEET
210 220 230 240 250
RHGLENGDFV KFTEVKGMPG LNDGTPRKVE VKGPYTFSIG SVKDLGSAGY
260 270 280 290 300
NGVFTQVKVP TKISFKSLRE SLKDPEYVYP DFGKMMRPPQ YHIAFQALSA
310 320 330 340 350
FADAHEGSLP RPRNDIDAAE FFEFCKKIAS TLQFDVELDE KLIKEISYQA
360 370 380 390 400
RGDLVAMSAF LGGAVAQEVL KATTSKFYPL KQYFYFDSLE SLPSSVTISE
410 420 430 440 450
ETCKPRGCRY DGQIAVFGSE FQEKIASLST FLVGAGAIGC EMLKNWAMMG
460 470 480 490 500
VATGESGHIS VTDMDSIEKS NLNRQFLFRP RDVGKLKSEC ASTAVSIMNP
510 520 530 540 550
SLTGKITSYQ ERVGPESEGI FGDEFFEKLS LVTNALDNVE ARMYVDRRCV
560 570 580 590 600
FFEKPLLESG TLGTKGNTQV VVPHLTESYG SSQDPPEKSF PICTLKNFPN
610 620 630 640 650
RIEHTIAWAR DLFEGLFKQP IDNVNMYLSS PNFLETSLKT SSNPREVLEN
660 670 680 690 700
IRDYLVTEKP LSFEECIMWA RLQFDKFFNN NIQQLLFNFP KDSVTSTGQP
710 720 730 740 750
FWSGPKRAPT PLSFDIHNRE HFDFIVAAAS LYAFNYGLKS ETDPAIYERV
760 770 780 790 800
LAGYNPPPFA PKSGIKIQVN ENEEAPETAA NKDKQELKSI ADSLPPPSSL
810 820 830 840 850
VGFRLTPAEF EKDDDSNHHI DFITAASNLR AMNYDITPAD RFKTKFVAGK
860 870 880 890 900
IVPAMCTSTA VVSGLVCLEL VKLVDGKKKI EEYKNGFFNL AIGLFTFSDP
910 920 930 940 950
IASPKMKVNG KEIDKIWDRY NLPDCTLQEL IDYFQKEEGL EVTMLSSGVS
960 970 980 990 1000
LLYANFQPPK KLAERLPLKI SELVEQITKK KLEPFRKHLV LEICCDDANG
1010
EDVEVPFICI KL
Length:1,012
Mass (Da):112,949
Last modified:May 1, 1999 - v1
Checksum:iAB5207808ACC6C2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87259 Genomic DNA. Translation: BAA75198.1.
CU329671 Genomic DNA. Translation: CAA22354.1.
PIRiT50344.
T52000.
RefSeqiXP_001713148.1. XM_001713096.2.

Genome annotation databases

EnsemblFungiiSPBC1604.21c.1; SPBC1604.21c.1:pep; SPBC1604.21c.
GeneIDi2540744.
KEGGispo:SPBC1604.21c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87259 Genomic DNA. Translation: BAA75198.1.
CU329671 Genomic DNA. Translation: CAA22354.1.
PIRiT50344.
T52000.
RefSeqiXP_001713148.1. XM_001713096.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4II2X-ray2.20A13-1012[»]
4II3X-ray2.90A/C13-1012[»]
ProteinModelPortaliO94609.
SMRiO94609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277267. 7 interactors.
DIPiDIP-48686N.
MINTiMINT-4685507.

Proteomic databases

MaxQBiO94609.
PRIDEiO94609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1604.21c.1; SPBC1604.21c.1:pep; SPBC1604.21c.
GeneIDi2540744.
KEGGispo:SPBC1604.21c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1604.21c.
PomBaseiSPBC1604.21c. ptr3.

Phylogenomic databases

HOGENOMiHOG000167329.
InParanoidiO94609.
KOiK03178.
OMAiKMKSDCA.
OrthoDBiEOG092C3FGE.
PhylomeDBiO94609.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-SPO-8866652. Synthesis of active ubiquitin: roles of E1 and E2 enzymes.

Miscellaneous databases

PROiO94609.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
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.
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.
PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBA1_SCHPO
AccessioniPrimary (citable) accession number: O94609
Secondary accession number(s): Q9P7R2, Q9USY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.