CIP1_MOUSE
ID CIP1_MOUSE Reviewed; 276 AA.
AC D3Z3K2;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase CCNB1IP1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9NPC3};
DE AltName: Full=Cyclin-B1-interacting protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase CCNB1IP1 {ECO:0000305};
GN Name=Ccnb1ip1; Synonyms=Gm288, Hei10, Mei4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 77-LEU--VAL-110.
RX PubMed=17784788; DOI=10.1371/journal.pgen.0030139;
RA Ward J.O., Reinholdt L.G., Motley W.W., Niswander L.M., Deacon D.C.,
RA Griffin L.B., Langlais K.K., Backus V.L., Schimenti K.J., O'Brien M.J.,
RA Eppig J.J., Schimenti J.C.;
RT "Mutation in mouse hei10, an e3 ubiquitin ligase, disrupts meiotic crossing
RT over.";
RL PLoS Genet. 3:E139-E139(2007).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=21779533; DOI=10.3390/genes1030440;
RA Strong E.R., Schimenti J.C.;
RT "Evidence implicating CCNB1IP1, a RING domain-containing protein required
RT for meiotic crossing over in mice, as an E3 SUMO ligase.";
RL Genes (Basel) 1:440-451(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24390283; DOI=10.1038/ng.2858;
RA Qiao H., Prasada Rao H.B., Yang Y., Fong J.H., Cloutier J.M., Deacon D.C.,
RA Nagel K.E., Swartz R.K., Strong E., Holloway J.K., Cohen P.E.,
RA Schimenti J., Ward J., Hunter N.;
RT "Antagonistic roles of ubiquitin ligase HEI10 and SUMO ligase RNF212
RT regulate meiotic recombination.";
RL Nat. Genet. 46:194-199(2014).
CC -!- FUNCTION: Ubiquitin E3 ligase that acts as a limiting factor for
CC crossing-over during meiosis: required during zygonema to limit the
CC colocalization of RNF212 with MutS-gamma-associated recombination sites
CC and thereby establish early differentiation of crossover and non-
CC crossover sites. Later, it is directed by MutL-gamma to stably
CC accumulate at designated crossover sites. Probably promotes the
CC dissociation of RNF212 and MutS-gamma to allow the progression of
CC recombination and the implementation of the final steps of crossing
CC over. Modulates cyclin-B levels and participates in the regulation of
CC cell cycle progression through the G2 phase. Overexpression causes
CC delayed entry into mitosis. {ECO:0000269|PubMed:17784788,
CC ECO:0000269|PubMed:24390283}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9NPC3};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CCNB1, UBE2L3 and NF2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24390283}. Chromosome
CC {ECO:0000269|PubMed:24390283}. Note=Associates to the synaptonemal
CC complex.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the testes and 17 day
CC embryos (corresponding to prophase I in females). Weakly or not
CC expressed in other tissues. {ECO:0000269|PubMed:17784788}.
CC -!- DEVELOPMENTAL STAGE: In spermatocytes, synaptonemal complex-associated
CC Ccnb1ip1 foci are detected by early pachynema and their number peaks
CC during midpachynema. In late-pachytene nuclei, Ccnb1ip1 foci number
CC descrease. At the onset of diplonema, foci are no longer detected (at
CC protein level). {ECO:0000269|PubMed:21779533,
CC ECO:0000269|PubMed:24390283}.
CC -!- PTM: Ubiquitinated; autoubiquitinated. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK1 on serine or threonine residues (in vitro).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Both male and female mice are sterile. Males do
CC not make sperm and have much smaller testes, a characteristic of
CC mutants with meiotic defects. Early stages of meiosis occur normally
CC and full synapsis of homologous chromosomes (homologs) is achieved.
CC However, crossover-specific recombination complexes do not assemble and
CC crossing-overs fail. In spermatocytes, chromosomes fail to congress
CC properly at the metaphase plate, leading to arrest and apoptosis before
CC the first meiotic division. Mutant oocytes have a similar chromosomal
CC phenotype but can undergo meiotic divisions and fertilization before
CC arresting. During late meiotic prophase males, absence of Cdk2 and
CC mismatch repair protein association from chromosome cores is correlated
CC with the premature separation of bivalents at diplonema owing to lack
CC of chiasmata. {ECO:0000269|PubMed:17784788,
CC ECO:0000269|PubMed:24390283}.
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DR EMBL; AC027184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466605; EDL20823.1; -; Genomic_DNA.
DR CCDS; CCDS49477.1; -.
DR RefSeq; NP_001104589.1; NM_001111119.1.
DR AlphaFoldDB; D3Z3K2; -.
DR SMR; D3Z3K2; -.
DR BioGRID; 232042; 35.
DR STRING; 10090.ENSMUSP00000093622; -.
DR PhosphoSitePlus; D3Z3K2; -.
DR PaxDb; D3Z3K2; -.
DR PRIDE; D3Z3K2; -.
DR ProteomicsDB; 283920; -.
DR Antibodypedia; 22006; 231 antibodies from 26 providers.
DR Ensembl; ENSMUST00000095932; ENSMUSP00000093622; ENSMUSG00000071470.
DR GeneID; 239083; -.
DR KEGG; mmu:239083; -.
DR UCSC; uc011zjw.1; mouse.
DR CTD; 57820; -.
DR MGI; MGI:2685134; Ccnb1ip1.
DR VEuPathDB; HostDB:ENSMUSG00000071470; -.
DR eggNOG; ENOG502RMFV; Eukaryota.
DR GeneTree; ENSGT00390000002849; -.
DR HOGENOM; CLU_049340_3_0_1; -.
DR InParanoid; D3Z3K2; -.
DR OMA; HQERMYQ; -.
DR OrthoDB; 1383870at2759; -.
DR PhylomeDB; D3Z3K2; -.
DR TreeFam; TF328863; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 239083; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ccnb1ip1; mouse.
DR PRO; PR:D3Z3K2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; D3Z3K2; protein.
DR Bgee; ENSMUSG00000071470; Expressed in ectoplacental cone and 118 other tissues.
DR ExpressionAtlas; D3Z3K2; baseline and differential.
DR Genevisible; D3Z3K2; MM.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0000795; C:synaptonemal complex; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:UniProtKB.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0051026; P:chiasma assembly; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; TAS:UniProtKB.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR InterPro; IPR042448; CCNB1IP1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR14305; PTHR14305; 1.
DR Pfam; PF14634; zf-RING_5; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Meiosis; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..276
FT /note="E3 ubiquitin-protein ligase CCNB1IP1"
FT /id="PRO_0000425901"
FT ZN_FING 10..52
FT /note="RING-type; atypical"
FT COILED 146..182
FT /evidence="ECO:0000255"
FT MUTAGEN 77..100
FT /note="Missing: In mei4; Sterility in both sexes due to
FT meiotic defects."
SQ SEQUENCE 276 AA; 31386 MW; 8677CFEC187C1465 CRC64;
MSLCEDMLLC NYRKCRIKLS GYAWVTACSH IFCDQHGSGE FSRSPAICPA CNSTLSGKLD
IVRTELSPSE EYKAMVLAGL RPEVVLDISS RALAFWTYQV HQERLYQEYN FSKAENHLKQ
MEKMYMQQIQ SKNIELTSMK GEVISMKKVL EEYKKKFSDI SEKLMERNRQ YQKLQGLYDS
LRLRNITIAS QEGSLEPGMI PQSGVFGFPP GNNSKFSLDH IPVGNQGGGD EDVQFRPFFV
CSPTAPEPIN NFFSFASPSH EAEQQVCSRA FKAKRI
