Skip Header

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

O94609

- UBA1_SCHPO

UniProt

O94609 - UBA1_SCHPO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin-activating enzyme E1 1

Gene

ptr3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei593 – 5931Glycyl thioester intermediatePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi437 – 46630ATPBy similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: PomBase
  2. magnesium ion binding Source: PomBase
  3. ubiquitin activating enzyme activity Source: PomBase

GO - Biological processi

  1. mRNA export from nucleus Source: PomBase
  2. 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

ReactomeiREACT_268591. ISG15 antiviral mechanism.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-activating enzyme E1 1
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
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC1604.21c.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10121012Ubiquitin-activating enzyme E1 1PRO_0000194976Add
BLAST

Proteomic databases

MaxQBiO94609.
PaxDbiO94609.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi277267. 1 interaction.
DIPiDIP-48686N.
MINTiMINT-4685507.
STRINGi4896.SPBC1604.21c-1.

Structurei

Secondary structure

1
1012
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2711Combined sources
Helixi29 – 368Combined sources
Beta strandi39 – 435Combined sources
Helixi47 – 5913Combined sources
Beta strandi62 – 676Combined sources
Helixi74 – 785Combined sources
Helixi85 – 873Combined sources
Helixi92 – 10110Combined sources
Beta strandi109 – 1113Combined sources
Helixi118 – 1225Combined sources
Beta strandi124 – 1285Combined sources
Helixi133 – 14513Combined sources
Beta strandi149 – 1568Combined sources
Beta strandi159 – 1657Combined sources
Beta strandi170 – 1767Combined sources
Beta strandi182 – 1898Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi209 – 2146Combined sources
Helixi221 – 2233Combined sources
Beta strandi233 – 2386Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi261 – 2633Combined sources
Helixi268 – 2714Combined sources
Beta strandi272 – 2743Combined sources
Helixi282 – 2843Combined sources
Helixi287 – 30418Combined sources
Turni305 – 3073Combined sources
Helixi315 – 33117Combined sources
Helixi340 – 3489Combined sources
Turni349 – 3513Combined sources
Helixi355 – 37218Combined sources
Beta strandi382 – 3876Combined sources
Helixi389 – 3913Combined sources
Beta strandi394 – 3963Combined sources
Helixi400 – 4034Combined sources
Helixi411 – 4177Combined sources
Helixi419 – 4268Combined sources
Beta strandi429 – 4335Combined sources
Helixi437 – 44913Combined sources
Turni450 – 4523Combined sources
Beta strandi454 – 4563Combined sources
Beta strandi458 – 4625Combined sources
Helixi469 – 4713Combined sources
Turni472 – 4743Combined sources
Helixi480 – 4823Combined sources
Helixi487 – 49812Combined sources
Helixi500 – 5023Combined sources
Beta strandi505 – 5095Combined sources
Helixi515 – 5173Combined sources
Turni518 – 5203Combined sources
Helixi523 – 5275Combined sources
Beta strandi530 – 5345Combined sources
Helixi539 – 55214Combined sources
Beta strandi556 – 5627Combined sources
Beta strandi565 – 5717Combined sources
Turni573 – 5753Combined sources
Helixi579 – 5813Combined sources
Helixi592 – 5976Combined sources
Helixi602 – 61716Combined sources
Helixi619 – 6279Combined sources
Helixi633 – 6375Combined sources
Turni638 – 6403Combined sources
Helixi644 – 65512Combined sources
Turni656 – 6583Combined sources
Helixi663 – 67816Combined sources
Helixi680 – 6889Combined sources
Beta strandi698 – 7025Combined sources
Helixi719 – 73517Combined sources
Helixi744 – 7529Combined sources
Helixi788 – 7925Combined sources
Helixi797 – 7993Combined sources
Helixi819 – 83315Combined sources
Helixi841 – 8488Combined sources
Helixi856 – 87419Combined sources
Helixi880 – 8823Combined sources
Beta strandi885 – 8895Combined sources
Helixi890 – 8923Combined sources
Beta strandi894 – 8985Combined sources
Beta strandi905 – 9084Combined sources
Beta strandi911 – 9144Combined sources
Turni915 – 9173Combined sources
Beta strandi919 – 9246Combined sources
Helixi927 – 93610Combined sources
Beta strandi941 – 9477Combined sources
Beta strandi950 – 9545Combined sources
Helixi959 – 9635Combined sources
Turni964 – 9674Combined sources
Helixi970 – 9778Combined sources
Beta strandi988 – 9969Combined sources
Beta strandi1007 – 10115Combined sources

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiCOG0476.
HOGENOMiHOG000167329.
InParanoidiO94609.
KOiK03178.
OMAiKFHPVKQ.
OrthoDBiEOG7FZ07P.
PhylomeDBiO94609.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
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.
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 .
PIRi T50344.
T52000.
RefSeqi XP_001713148.1. XM_001713096.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4II2 X-ray 2.20 A 13-1012 [» ]
4II3 X-ray 2.90 A/C 13-1012 [» ]
ProteinModelPortali O94609.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 277267. 1 interaction.
DIPi DIP-48686N.
MINTi MINT-4685507.
STRINGi 4896.SPBC1604.21c-1.

Proteomic databases

MaxQBi O94609.
PaxDbi O94609.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC1604.21c.1 ; SPBC1604.21c.1:pep ; SPBC1604.21c .
GeneIDi 2540744.
KEGGi spo:SPBC1604.21c.

Organism-specific databases

PomBasei SPBC1604.21c.

Phylogenomic databases

eggNOGi COG0476.
HOGENOMi HOG000167329.
InParanoidi O94609.
KOi K03178.
OMAi KFHPVKQ.
OrthoDBi EOG7FZ07P.
PhylomeDBi O94609.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_268591. ISG15 antiviral mechanism.

Miscellaneous databases

NextBioi 20801866.
PROi O94609.

Family and domain databases

Gene3Di 1.10.3240.10. 2 hits.
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 PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and molecular characterization of mRNA transport mutants in Schizosaccharomyces pombe."
    Azad A.K., Tani T., Shiki N., Tsuneyoshi S., Urushiyama S., Ohshima Y.
    Mol. Biol. Cell 8:825-841(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

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 26, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3