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Protein

E3 ubiquitin-protein ligase pub3

Gene

pub3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.

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 sitei754 – 7541Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase pub3 (EC:6.3.2.-)
Gene namesi
Name:pub3
ORF Names:SPBC16E9.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC16E9.11c.
PomBaseiSPBC16E9.11c. pub3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 786786E3 ubiquitin-protein ligase pub3PRO_0000120334Add
BLAST

Proteomic databases

MaxQBiO14326.

Interactioni

Protein-protein interaction databases

BioGridi276500. 78 interactions.
MINTiMINT-4672315.

Structurei

3D structure databases

ProteinModelPortaliO14326.
SMRiO14326. Positions 238-267, 308-338, 362-396, 409-778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090C2PROSITE-ProRule annotationAdd
BLAST
Domaini236 – 26934WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini306 – 33934WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 39734WW 3PROSITE-ProRule annotationAdd
BLAST
Domaini453 – 786334HECTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi144 – 21774Thr-richAdd
BLAST

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.
InParanoidiO14326.
KOiK10591.
OrthoDBiEOG735453.
PhylomeDBiO14326.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
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.

O14326-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQGAKRVRF YIVAADGLSK RDLFRQPDPF AILTVDGEQT HTTKVIKKSV
60 70 80 90 100
NPYWNEGFEV TVKPSSVISI RLFDQKKFKK KDQGFLGLVS FRMREVGSFR
110 120 130 140 150
SNREVSLTRP LKKSSTTNLS VLGNLVLKVA PSKIRAPAGN HSSTTANRTT
160 170 180 190 200
STPTTTTART TRTTPRPTAT TNTSNQSTSN STRNGTSAAT SNGTGTGAGT
210 220 230 240 250
GASHRSSPVT NRQTNNTSAL SNSNAHIMSS FEDQYGRLPP GWERRADSLG
260 270 280 290 300
RTYYVDHNTR TTTWTRPASS TNPVHNTSSD SQRLNHQNRH LPDDSNPSLM
310 320 330 340 350
QSDSGNDLPF GWEMRYTDTG RPYFVDHNTR TTTWVDPRNP LVRPNGGSST
360 370 380 390 400
VGSLMQPQSL SHLGPLPSGW EMRLTNSARV YFVDHNTKTT TWDDPRLPSA
410 420 430 440 450
LDQDVPQYKC DFRRKLIYFR SQPGMRPLPG QCNVKVRRDH IFEDSYAEIM
460 470 480 490 500
RYSAHDLKKR LMIRFDGEDG LDYGGLSREF FFLLSHKMFD PIYCLFEYSA
510 520 530 540 550
VDNYTLQINP HSSINPEHLN YFRFIGRVIG LAIFHRRFLD AFFVVSLYKK
560 570 580 590 600
LLRKKVSLAD MESIDAEFYR SLKWVLENDI TGILDLTFSV EEDHFGEVRT
610 620 630 640 650
VELITNGENI EVTEENKKKY VDLVTEWRVS KRVEQQFNAF YSGFVELVSP
660 670 680 690 700
DLVNVFDERE LELLIGGISD VDVEDWKSHT EYRTYIATDP VIKWFWEIIA
710 720 730 740 750
GWKNEDRSKL LQFATGTSRI PVNGFRDLQG SDGPRKFTIE KAGTPDQLPV
760 770 780
AHTCFNRLDL PDYPSKDTLH EKLSLAVENT VGFGNE
Length:786
Mass (Da):89,260
Last modified:January 1, 1998 - v1
Checksum:i57B7A859F5497B9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti637 – 64913FNAFY…VELVS → LMHFILVLLNWYP (PubMed:9501991).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB16903.1.
AB001023 mRNA. Translation: BAA19217.1.
PIRiT39585.
RefSeqiNP_595793.1. NM_001021694.2.

Genome annotation databases

EnsemblFungiiSPBC16E9.11c.1; SPBC16E9.11c.1:pep; SPBC16E9.11c.
GeneIDi2539956.
KEGGispo:SPBC16E9.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB16903.1.
AB001023 mRNA. Translation: BAA19217.1.
PIRiT39585.
RefSeqiNP_595793.1. NM_001021694.2.

3D structure databases

ProteinModelPortaliO14326.
SMRiO14326. Positions 238-267, 308-338, 362-396, 409-778.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276500. 78 interactions.
MINTiMINT-4672315.

Proteomic databases

MaxQBiO14326.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC16E9.11c.1; SPBC16E9.11c.1:pep; SPBC16E9.11c.
GeneIDi2539956.
KEGGispo:SPBC16E9.11c.

Organism-specific databases

EuPathDBiFungiDB:SPBC16E9.11c.
PomBaseiSPBC16E9.11c. pub3.

Phylogenomic databases

HOGENOMiHOG000208451.
InParanoidiO14326.
KOiK10591.
OrthoDBiEOG735453.
PhylomeDBiO14326.

Enzyme and pathway databases

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

Miscellaneous databases

PROiO14326.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
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

  1. "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.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 637-786.
    Strain: PR745.

Entry informationi

Entry nameiPUB3_SCHPO
AccessioniPrimary (citable) accession number: O14326
Secondary accession number(s): P79055
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: January 1, 1998
Last modified: July 6, 2016
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

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.