O13959 (RBX1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RING-box protein pip1
Short name=RING-box protein 1

Alternative name(s):
Pop-interacting protein 1

Gene names

Name:	pip1
ORF Names:	SPAC23H4.18c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	107 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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. Ref.1 Ref.3 Ref.4
Subcellular location	Cytoplasm. Nucleus Ref.1 Ref.5.
Domain	The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion.
Sequence similarities	Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle Inferred from sequence orthology. Source: PomBase protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: PomBase regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Cul4B-RING ubiquitin ligase complex Traceable author statement Ref.3. Source: PomBase cytosol Inferred from direct assay Ref.5. Source: PomBase nucleus Inferred from direct assay Ref.1Ref.5. Source: PomBase
Molecular_function	ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: PomBase zinc ion binding Inferred from sequence model. Source: PomBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
skp1	Q9Y709	6	EBI-1112060,EBI-1172248

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 107	107	RING-box protein pip1		PRO_0000056021
Regions
	Zinc finger	52 – 97	46	RING-type
Sites
	Metal binding	41	1	Zinc 1 By similarity
	Metal binding	44	1	Zinc 1 By similarity
	Metal binding	52	1	Zinc 3 By similarity
	Metal binding	55	1	Zinc 3 By similarity
	Metal binding	67	1	Zinc 3 By similarity
	Metal binding	74	1	Zinc 2 By similarity
	Metal binding	76	1	Zinc 2 By similarity
	Metal binding	79	1	Zinc 1 By similarity
	Metal binding	81	1	Zinc 3 By similarity
	Metal binding	82	1	Zinc 1 By similarity
	Metal binding	93	1	Zinc 2 By similarity
	Metal binding	96	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13959 [UniParc]. Last modified May 1, 2000. Version 2. Checksum: 71C3A3D2BF26DABF	FASTA	107	12,724
	10 20 30 40 50 60 MEDEMQIDKK EVEIEQKPPR FEIKKWNAVA LWQWDIVVDN CAICRNHIMD LCIECQANTD 70 80 90 100 SAAAQECTVA WGTCNHAFHF HCISRWLNTR NVCPLDNREW EFQRYGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF179228 mRNA. Translation: AAD54393.1. CU329670 Genomic DNA. Translation: CAB58559.1.
PIR	T38310.
RefSeq	NP_593388.1. NM_001018820.2.
3D structure databases
ProteinModelPortal	O13959.
SMR	O13959. Positions 20-107.
ModBase	Search...
Protein-protein interaction databases
IntAct	O13959. 9 interactions.
MINT	MINT-4669323.
STRING	4896.SPAC23H4.18c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC23H4.18c.1; SPAC23H4.18c.1:pep; SPAC23H4.18c.
GeneID	2541897.
KEGG	spo:SPAC23H4.18c.
Organism-specific databases
PomBase	SPAC23H4.18c.
Phylogenomic databases
eggNOG	COG5194.
HOGENOM	HOG000171951.
KO	K03868.
OMA	NRDWEFQ.
OrthoDB	EOG4V46J5.
Enzyme and pathway databases
UniPathway	UPA00143.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR024766. Znf_RING_H2. [Graphical view]
Pfam	PF12678. zf-rbx1. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802984.

Entry information

Entry name

RBX1_SCHPO

Accession

Primary (citable) accession number: O13959

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program