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Protein

E3 ubiquitin-protein ligase dbl4

Gene

dbl4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri131 – 17848RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri198 – 26467IBR-typeSequence analysisAdd
BLAST
Zinc fingeri291 – 32030RING-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase dbl4By similarityCurated (EC:6.3.2.-By similarity)
Alternative name(s):
DNA-break-localizing protein 41 Publication
Histone E3 ligase 1By similarity
Gene namesi
Name:dbl41 Publication
ORF Names:SPAC328.02Imported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC328.02.
PomBaseiSPAC328.02. dbl4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: PomBase
  • nucleus Source: PomBase
  • site of double-strand break Source: PomBase
  • ubiquitin ligase complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504E3 ubiquitin-protein ligase dbl4PRO_0000310488Add
BLAST

Proteomic databases

MaxQBiQ9P3U4.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi279580. 1 interaction.
MINTiMINT-4703733.

Structurei

3D structure databases

ProteinModelPortaliQ9P3U4.
SMRiQ9P3U4. Positions 283-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RBR family.Curated
Contains 1 IBR-type zinc finger.Sequence analysis
Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri131 – 17848RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri198 – 26467IBR-typeSequence analysisAdd
BLAST
Zinc fingeri291 – 32030RING-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOGENOMiHOG000216612.
InParanoidiQ9P3U4.
KOiK11968.
OMAiNTINWIL.
OrthoDBiEOG7N9059.
PhylomeDBiQ9P3U4.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P3U4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLLDDEFY EEEFENDLLD ASEFEDEFDE DAEIDDDGFT VERKRRRAHS
60 70 80 90 100
VSYRVVSVRD LRASLNEKIN QLTSIIDLTR EQVLGLYRYF KWNRERLLER
110 120 130 140 150
YIDAPEESLQ KAGVGLSGSK QREVVHHEGT CEICYDEGCL PFFSAECDHE
160 170 180 190 200
FCLACYRQYL DSRISEGESV IQCPEESCTQ IVSIQSITKV LDEKSLDRYH
210 220 230 240 250
RLLDRSFVDD NDHLRWCPAP DCEFAIECHV TQASLSSVVP TVTCNCGKQF
260 270 280 290 300
CFGCGHDNHQ PTICPLVKIW LQKCQDDSET ANWIHANTKE CPKCSTTIEK
310 320 330 340 350
NGGCNHMTCK KCKYEFCWVC LGPWTEHGNN WYTCNRYEEK SSTSARDSQS
360 370 380 390 400
KSRASLERYL HYYNRFANHE QSAKLDHELY EHTHKRMTQM QVDSNLSWVE
410 420 430 440 450
VQFLKNAVDI LFQCRQTLKW TYAFAYYLAR NNQTEIFEDN QRDLELAVEN
460 470 480 490 500
LSELCERPCQ DCSLSVFKQR VLDKTVYVRS RRDVLLDDTA RGLAEGRWEY

VVDV
Length:504
Mass (Da):58,939
Last modified:October 1, 2000 - v1
Checksum:iAA71065239F401CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB95997.1.
RefSeqiNP_594204.1. NM_001019627.2.

Genome annotation databases

EnsemblFungiiSPAC328.02.1; SPAC328.02.1:pep; SPAC328.02.
GeneIDi2543148.
KEGGispo:SPAC328.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB95997.1.
RefSeqiNP_594204.1. NM_001019627.2.

3D structure databases

ProteinModelPortaliQ9P3U4.
SMRiQ9P3U4. Positions 283-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279580. 1 interaction.
MINTiMINT-4703733.

Proteomic databases

MaxQBiQ9P3U4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC328.02.1; SPAC328.02.1:pep; SPAC328.02.
GeneIDi2543148.
KEGGispo:SPAC328.02.

Organism-specific databases

EuPathDBiFungiDB:SPAC328.02.
PomBaseiSPAC328.02. dbl4.

Phylogenomic databases

HOGENOMiHOG000216612.
InParanoidiQ9P3U4.
KOiK11968.
OMAiNTINWIL.
OrthoDBiEOG7N9059.
PhylomeDBiQ9P3U4.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ9P3U4.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. "A proteome-wide visual screen identifies fission yeast proteins localizing to DNA double-strand breaks."
    Yu Y., Ren J.Y., Zhang J.M., Suo F., Fang X.F., Wu F., Du L.L.
    DNA Repair 12:433-443(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiHEL1_SCHPO
AccessioniPrimary (citable) accession number: Q9P3U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 95 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

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.