ID RBX1_SCHPO Reviewed; 107 AA.
AC O13959;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 172.
DE RecName: Full=RING-box protein pip1;
DE Short=RING-box protein 1;
DE AltName: Full=Pop-interacting protein 1;
GN Name=pip1; ORFNames=SPAC23H4.18c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH POP1; POP2 AND PCUL1.
RX PubMed=12167173; DOI=10.1186/1471-2091-3-22;
RA Seibert V., Prohl C., Schoultz I., Rhee E., Lopez R., Abderazzaq K.,
RA Zhou C., Wolf D.A.;
RT "Combinatorial diversity of fission yeast SCF ubiquitin ligases by
RT homo- and heterooligomeric assemblies of the F-box proteins Pop1p and
RT Pop2p.";
RL BMC Biochem. 3:22-22(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION IN THE RIK1-ASSOCIATED E3
RP UBIQUITIN LIGASE COMPLEX.
RX PubMed=16024659; DOI=10.1101/gad.1328005;
RA Horn P.J., Bastie J.-N., Peterson C.L.;
RT "A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for
RT heterochromatin formation.";
RL Genes Dev. 19:1705-1714(2005).
RN [4]
RP INTERACTION WITH CUL3.
RX PubMed=14527422; DOI=10.1016/s1097-2765(03)00341-1;
RA Geyer R., Wee S., Anderson S., Yates J. III, Wolf D.A.;
RT "BTB/POZ domain proteins are putative substrate adaptors for cullin 3
RT ubiquitin ligases.";
RL Mol. Cell 12:783-790(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Component of E3 ubiquitin ligase SCF complexes, which mediate
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins. Seems to recruit the E2 ubiquitination enzyme, like
CC UBC3/CDC34, to the complex and brings it into close proximity to the
CC substrate. Component of the rik1-associated E3 ubiquitin ligase complex
CC that shows ubiquitin ligase activity and is required for histone H3K9
CC methylation. H3K9me represents a specific tag for epigenetic
CC transcriptional repression by recruiting swi6/HP1 to methylated
CC histones which leads to transcriptional silencing within centromeric
CC heterochromatin, telomeric regions and at the silent mating-type loci.
CC {ECO:0000269|PubMed:12167173}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF E3 ubiquitin ligase complex containing psh1,
CC pip1, pcul1 and the F-box proteins pop1 and pop2. Instead of the
CC pop1/pop2 heterodimer also homooligomers of pop1 or pop2 may be present
CC in the complex. Component of the rik1-associated E3 ubiquitin ligase
CC complex composed of at least clr4, cul4, pip1, raf1 and raf2. Interacts
CC with cul3. {ECO:0000269|PubMed:12167173, ECO:0000269|PubMed:14527422,
CC ECO:0000269|PubMed:16024659}.
CC -!- INTERACTION:
CC O13959; Q9Y709: skp1; NbExp=6; IntAct=EBI-1112060, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. It coordinates an additional third zinc ion.
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DR EMBL; AF179228; AAD54393.1; -; mRNA.
DR EMBL; CU329670; CAB58559.1; -; Genomic_DNA.
DR PIR; T38310; T38310.
DR RefSeq; NP_593388.1; NM_001018820.2.
DR AlphaFoldDB; O13959; -.
DR SMR; O13959; -.
DR BioGRID; 278387; 12.
DR IntAct; O13959; 9.
DR STRING; 284812.O13959; -.
DR iPTMnet; O13959; -.
DR MaxQB; O13959; -.
DR PaxDb; 4896-SPAC23H4-18c-1; -.
DR EnsemblFungi; SPAC23H4.18c.1; SPAC23H4.18c.1:pep; SPAC23H4.18c.
DR GeneID; 2541897; -.
DR KEGG; spo:SPAC23H4.18c; -.
DR PomBase; SPAC23H4.18c; -.
DR VEuPathDB; FungiDB:SPAC23H4.18c; -.
DR eggNOG; KOG2930; Eukaryota.
DR HOGENOM; CLU_115512_2_1_1; -.
DR InParanoid; O13959; -.
DR OMA; DTCVECQ; -.
DR PhylomeDB; O13959; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O13959; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0043494; C:CLRC complex; IDA:PomBase.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0140851; F:histone H3K14 ubiquitin ligase activity; IDA:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0031507; P:heterochromatin formation; IC:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16485; mRING-H2-C3H2C2D_RBX1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR11210:SF2; E3 UBIQUITIN-PROTEIN LIGASE RBX1; 1.
DR PANTHER; PTHR11210; RING BOX; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..107
FT /note="RING-box protein pip1"
FT /id="PRO_0000056021"
FT ZN_FING 52..97
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 107 AA; 12724 MW; 71C3A3D2BF26DABF CRC64;
MEDEMQIDKK EVEIEQKPPR FEIKKWNAVA LWQWDIVVDN CAICRNHIMD LCIECQANTD
SAAAQECTVA WGTCNHAFHF HCISRWLNTR NVCPLDNREW EFQRYGH
//
