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Protein

RING-box protein pip1

Gene

pip1

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

Component of E3 ubiquitin ligase SCF complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recruit the E2 ubiquitination enzyme, like UBC3/CDC34, to the complex and brings it into close proximity to the substrate. Component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.1 Publication

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
Metal bindingi41 – 411Zinc 1By similarity
Metal bindingi44 – 441Zinc 1By similarity
Metal bindingi52 – 521Zinc 3By similarity
Metal bindingi55 – 551Zinc 3By similarity
Metal bindingi67 – 671Zinc 3By similarity
Metal bindingi74 – 741Zinc 2By similarity
Metal bindingi76 – 761Zinc 2By similarity
Metal bindingi79 – 791Zinc 1By similarity
Metal bindingi81 – 811Zinc 3By similarity
Metal bindingi82 – 821Zinc 1By similarity
Metal bindingi93 – 931Zinc 2By similarity
Metal bindingi96 – 961Zinc 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri52 – 9746RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-5632684. Hedgehog 'on' state.
R-SPO-5696395. Formation of Incision Complex in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
RING-box protein pip1
Short name:
RING-box protein 1
Alternative name(s):
Pop-interacting protein 1
Gene namesi
Name:pip1
ORF Names:SPAC23H4.18c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC23H4.18c.
PomBaseiSPAC23H4.18c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nuclear SCF ubiquitin ligase complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 107107RING-box protein pip1PRO_0000056021Add
BLAST

Proteomic databases

MaxQBiO13959.

Interactioni

Subunit structurei

Part of a SCF E3 ubiquitin ligase complex containing psh1, pip1, pcul1 and the F-box proteins pop1 and pop2. Instead of the pop1/pop2 heterodimer also homooligomers of pop1 or pop2 may be present in the complex. Component of the rik1-associated E3 ubiquitin ligase complex composed of at least clr4, cul4, pip1, raf1 and raf2. Interacts with cul3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
skp1Q9Y7096EBI-1112060,EBI-1172248

Protein-protein interaction databases

BioGridi278387. 11 interactions.
IntActiO13959. 9 interactions.
MINTiMINT-4669323.

Structurei

3D structure databases

ProteinModelPortaliO13959.
SMRiO13959. Positions 20-107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion.

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri52 – 9746RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000171951.
InParanoidiO13959.
KOiK03868.
OMAiECQANQS.
OrthoDBiEOG73Z363.
PhylomeDBiO13959.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDEMQIDKK EVEIEQKPPR FEIKKWNAVA LWQWDIVVDN CAICRNHIMD
60 70 80 90 100
LCIECQANTD SAAAQECTVA WGTCNHAFHF HCISRWLNTR NVCPLDNREW

EFQRYGH
Length:107
Mass (Da):12,724
Last modified:May 1, 2000 - v2
Checksum:i71C3A3D2BF26DABF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF179228 mRNA. Translation: AAD54393.1.
CU329670 Genomic DNA. Translation: CAB58559.1.
PIRiT38310.
RefSeqiNP_593388.1. NM_001018820.2.

Genome annotation databases

EnsemblFungiiSPAC23H4.18c.1; SPAC23H4.18c.1:pep; SPAC23H4.18c.
GeneIDi2541897.
KEGGispo:SPAC23H4.18c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF179228 mRNA. Translation: AAD54393.1.
CU329670 Genomic DNA. Translation: CAB58559.1.
PIRiT38310.
RefSeqiNP_593388.1. NM_001018820.2.

3D structure databases

ProteinModelPortaliO13959.
SMRiO13959. Positions 20-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278387. 11 interactions.
IntActiO13959. 9 interactions.
MINTiMINT-4669323.

Proteomic databases

MaxQBiO13959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC23H4.18c.1; SPAC23H4.18c.1:pep; SPAC23H4.18c.
GeneIDi2541897.
KEGGispo:SPAC23H4.18c.

Organism-specific databases

EuPathDBiFungiDB:SPAC23H4.18c.
PomBaseiSPAC23H4.18c.

Phylogenomic databases

HOGENOMiHOG000171951.
InParanoidiO13959.
KOiK03868.
OMAiECQANQS.
OrthoDBiEOG73Z363.
PhylomeDBiO13959.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-5632684. Hedgehog 'on' state.
R-SPO-5696395. Formation of Incision Complex in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

NextBioi20802984.
PROiO13959.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Combinatorial diversity of fission yeast SCF ubiquitin ligases by homo- and heterooligomeric assemblies of the F-box proteins Pop1p and Pop2p."
    Seibert V., Prohl C., Schoultz I., Rhee E., Lopez R., Abderazzaq K., Zhou C., Wolf D.A.
    BMC Biochem. 3:22-22(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POP1; POP2 AND PCUL1.
  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.
  3. "A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for heterochromatin formation."
    Horn P.J., Bastie J.-N., Peterson C.L.
    Genes Dev. 19:1705-1714(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE RIK1-ASSOCIATED E3 UBIQUITIN LIGASE COMPLEX.
  4. "BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases."
    Geyer R., Wee S., Anderson S., Yates J. III, Wolf D.A.
    Mol. Cell 12:783-790(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CUL3.
  5. "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].

Entry informationi

Entry nameiRBX1_SCHPO
AccessioniPrimary (citable) accession number: O13959
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.