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Protein

E3 ubiquitin-protein ligase pub1

Gene

pub1

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

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Regulates ubiquitination of cdc25.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei735 – 7351Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • phospholipid binding Source: PomBase
  • ubiquitin protein ligase activity Source: PomBase

GO - Biological processi

  • negative regulation of leucine import in response to ammonium ion Source: PomBase
  • protein localization to Golgi apparatus Source: PomBase
  • protein ubiquitination Source: PomBase
  • regulation of intracellular pH Source: PomBase
  • regulation of transmembrane transport Source: PomBase
  • ubiquitin-dependent protein catabolic process Source: PomBase
  • uracil transport Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19. 5613.
ReactomeiR-SPO-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase pub1 (EC:6.3.2.-)
Gene namesi
Name:pub1
ORF Names:SPAC11G7.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC11G7.02.
PomBaseiSPAC11G7.02. pub1.

Subcellular locationi

  • Membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cell periphery Source: PomBase
  • cytoplasm Source: PomBase
  • Golgi apparatus Source: PomBase
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767E3 ubiquitin-protein ligase pub1PRO_0000120332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei156 – 1561Phosphothreonine1 Publication
Modified residuei178 – 1781Phosphoserine1 Publication
Modified residuei180 – 1801Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92462.

PTM databases

iPTMnetiQ92462.

Interactioni

Protein-protein interaction databases

BioGridi278309. 68 interactions.
MINTiMINT-4701562.

Structurei

3D structure databases

ProteinModelPortaliQ92462.
SMRiQ92462. Positions 207-238, 290-320, 344-377, 388-759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 3216C2PROSITE-ProRule annotationAdd
BLAST
Domaini211 – 23626WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini294 – 31926WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini351 – 37626WW 3PROSITE-ProRule annotationAdd
BLAST
Domaini463 – 767305HECTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi242 – 2476Poly-Ala

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
Contains 3 WW domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000208451.
InParanoidiQ92462.
KOiK10591.
OMAiSSNYNEH.
OrthoDBiEOG735453.
PhylomeDBiQ92462.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTiSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 3 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 3 hits.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92462-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSAQSRRI RVTIVAADGL YKRDVFRFPD PFAVLTVDGE QTHTTTAIKK
60 70 80 90 100
TLNPYWNETF EVNVTDNSTI AIQVFDQKKF KKKGQGFLGV INLRVGDVLD
110 120 130 140 150
LAIGGDEMLT RDLKKSNENT VVHGKIIINL STTAQSTLQV PSSAASGART
160 170 180 190 200
QRTSITNDPQ SSQSSSVSRN PASSRAGSPT RDNAPAASPA SSEPRTFSSF
210 220 230 240 250
EDQYGRLPPG WERRTDNLGR TYYVDHNTRS TTWIRPNLSS VAGAAAAELH
260 270 280 290 300
SSASSANVTE GVQPSSSNAA RRTEASVLTS NATTAGSGEL PPGWEQRYTP
310 320 330 340 350
EGRPYFVDHN TRTTTWVDPR RQQYIRSYGG PNNATIQQQP VSQLGPLPSG
360 370 380 390 400
WEMRLTNTAR VYFVDHNTKT TTWDDPRLPS SLDQNVPQYK RDFRRKLIYF
410 420 430 440 450
LSQPALHPLP GQCHIKVRRN HIFEDSYAEI MRQSATDLKK RLMIKFDGED
460 470 480 490 500
GLDYGGLSRE YFFLLSHEMF NPFYCLFEYS SVDNYTLQIN PHSGINPEHL
510 520 530 540 550
NYFKFIGRVI GLAIFHRRFV DAFFVVSFYK MILQKKVTLQ DMESMDAEYY
560 570 580 590 600
RSLVWILDND ITGVLDLTFS VEDNCFGEVV TIDLKPNGRN IEVTEENKRE
610 620 630 640 650
YVDLVTVWRI QKRIEEQFNA FHEGFSELIP QELINVFDER ELELLIGGIS
660 670 680 690 700
EIDMEDWKKH TDYRSYSEND QIIKWFWELM DEWSNEKKSR LLQFTTGTSR
710 720 730 740 750
IPVNGFKDLQ GSDGPRKFTI EKAGEPNKLP KAHTCFNRLD LPPYTSKKDL
760
DHKLSIAVEE TIGFGQE
Length:767
Mass (Da):87,268
Last modified:December 15, 1998 - v2
Checksum:iF1455A155EB9ACF7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631Q → K in CAA68867 (PubMed:8635463).Curated
Sequence conflicti163 – 1631Q → K in AAB07514 (PubMed:8635463).Curated
Sequence conflicti609 – 6091Missing in CAA68867 (PubMed:8635463).Curated
Sequence conflicti609 – 6091Missing in AAB07514 (PubMed:8635463).Curated
Sequence conflicti661 – 6611T → K in CAA68867 (PubMed:8635463).Curated
Sequence conflicti661 – 6611T → K in AAB07514 (PubMed:8635463).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07592 mRNA. Translation: CAA68867.1.
U66716 mRNA. Translation: AAB07514.1.
CU329670 Genomic DNA. Translation: CAB16207.1.
U62795 Genomic DNA. Translation: AAB63350.1.
PIRiS66562.
T37545.
RefSeqiNP_594396.1. NM_001019819.2.

Genome annotation databases

EnsemblFungiiSPAC11G7.02.1; SPAC11G7.02.1:pep; SPAC11G7.02.
GeneIDi2541818.
KEGGispo:SPAC11G7.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07592 mRNA. Translation: CAA68867.1.
U66716 mRNA. Translation: AAB07514.1.
CU329670 Genomic DNA. Translation: CAB16207.1.
U62795 Genomic DNA. Translation: AAB63350.1.
PIRiS66562.
T37545.
RefSeqiNP_594396.1. NM_001019819.2.

3D structure databases

ProteinModelPortaliQ92462.
SMRiQ92462. Positions 207-238, 290-320, 344-377, 388-759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278309. 68 interactions.
MINTiMINT-4701562.

PTM databases

iPTMnetiQ92462.

Proteomic databases

MaxQBiQ92462.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC11G7.02.1; SPAC11G7.02.1:pep; SPAC11G7.02.
GeneIDi2541818.
KEGGispo:SPAC11G7.02.

Organism-specific databases

EuPathDBiFungiDB:SPAC11G7.02.
PomBaseiSPAC11G7.02. pub1.

Phylogenomic databases

HOGENOMiHOG000208451.
InParanoidiQ92462.
KOiK10591.
OMAiSSNYNEH.
OrthoDBiEOG735453.
PhylomeDBiQ92462.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 5613.
ReactomeiR-SPO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ92462.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTiSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 3 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 3 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 3 hits.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Pub1 acts as an E6-AP-like protein ubiquitiin ligase in the degradation of cdc25."
    Nefsky B., Beach D.
    EMBO J. 15:1301-1312(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Tolerance of low pH in Schizosaccharomyces pombe requires a functioning pub1 ubiquitin ligase."
    Saleki R., Jia Z., Karagiannis J., Young P.G.
    Mol. Gen. Genet. 254:520-528(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: J227.
  3. "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.
  4. "The novel HECT-type ubiquitin-protein ligase Pub2p shares partially overlapping function with Pub1p in Schizosaccharomyces pombe."
    Tamai K.K., Shimoda C.
    J. Cell Sci. 115:1847-1857(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156; SER-178 AND THR-180, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPUB1_SCHPO
AccessioniPrimary (citable) accession number: Q92462
Secondary accession number(s): O14454
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: June 8, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.