GEMC1_XENLA
ID GEMC1_XENLA Reviewed; 316 AA.
AC D3YN49;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Geminin coiled-coil domain-containing protein 1;
DE Short=xGEMC1;
GN Name=gmnc; Synonyms=gemc1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH CDC45L; CDK2 AND TOPBP1, MUTAGENESIS OF
RP THR-153; 163-ARG--LEU-165; SER-177; SER-215; THR-226; SER-239; SER-255;
RP SER-259 AND THR-264, AND PHOSPHORYLATION AT THR-153.
RX PubMed=20383140; DOI=10.1038/ncb2050;
RA Balestrini A., Cosentino C., Errico A., Garner E., Costanzo V.;
RT "GEMC1 is a TopBP1-interacting protein required for chromosomal DNA
RT replication.";
RL Nat. Cell Biol. 12:484-491(2010).
CC -!- FUNCTION: Regulator of DNA replication. Promotes initiation of
CC chromosomal DNA replication by mediating topbp1- and cdk2-dependent
CC recruitment of cdc45l onto replication origins.
CC {ECO:0000269|PubMed:20383140}.
CC -!- SUBUNIT: Interacts with topbp1. Interacts with Cdc45l and the kinase
CC cdk2-cyclin-E (the interaction is direct).
CC {ECO:0000269|PubMed:20383140}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20383140}.
CC Note=Associates with chromatin during pre-replication complex (pre-RC)
CC formation following interaction with topbp1.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues. Enriched in
CC proliferating cells from skin and gut. {ECO:0000269|PubMed:20383140}.
CC -!- PTM: Highly phosphorylated by cdk2; stimulates initiation of DNA
CC replication. {ECO:0000269|PubMed:20383140}.
CC -!- SIMILARITY: Belongs to the GEMC1 family. {ECO:0000305}.
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DR EMBL; GU594151; ADC92603.1; -; mRNA.
DR RefSeq; NP_001166876.1; NM_001173405.1.
DR AlphaFoldDB; D3YN49; -.
DR SMR; D3YN49; -.
DR iPTMnet; D3YN49; -.
DR GeneID; 100379535; -.
DR KEGG; xla:100379535; -.
DR CTD; 100379535; -.
DR Xenbase; XB-GENE-6465509; gmnc.S.
DR OrthoDB; 966768at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 100379535; Expressed in ovary and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IMP:UniProtKB.
DR InterPro; IPR029700; GEMC1.
DR PANTHER; PTHR13372:SF2; PTHR13372:SF2; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Coiled coil; DNA replication; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..316
FT /note="Geminin coiled-coil domain-containing protein 1"
FT /id="PRO_0000395805"
FT REGION 134..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 82..117
FT /evidence="ECO:0000255"
FT COMPBIAS 134..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="Phosphothreonine; by cdk2"
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 153
FT /note="T->A: Can still be phosphorylated by cdk2 in vitro.
FT Abolishes phosphorylation by cdk2; when associated with A-
FT 177; A-215; A-226; A-239; A-255; A-259 and A-264."
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 163..165
FT /note="RNL->ANA: Strongly reduces phosphorylation and
FT interaction with cdk2 without affecting interaction with
FT cdc45l."
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 177
FT /note="S->A: Abolishes phosphorylation by cdk2; when
FT associated with A-153; A-215; A-226; A-239; A-255; A-259
FT and A-264."
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 215
FT /note="S->A: Abolishes phosphorylation by cdk2; when
FT associated with A-153; A-177; A-226; A-239; A-255; A-259
FT and A-264."
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 226
FT /note="T->A: Abolishes phosphorylation by cdk2; when
FT associated with A-153; A-177; A-215; A-239; A-255; A-259
FT and A-264."
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 239
FT /note="S->A: Abolishes phosphorylation by cdk2; when
FT associated with A-153; A-177; A-215; A-226; A-255; A-259
FT and A-264."
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 255
FT /note="S->A: Abolishes phosphorylation by cdk2; when
FT associated with A-153; A-177; A-215; A-226; A-239; A-259
FT and A-264."
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 259
FT /note="S->A: Abolishes phosphorylation by cdk2; when
FT associated with A-153; A-177; A-215; A-226; A-239; A-255
FT and A-264."
FT /evidence="ECO:0000269|PubMed:20383140"
FT MUTAGEN 264
FT /note="T->A: Abolishes phosphorylation by cdk2; when
FT associated with A-153; A-177; A-215; A-226; A-239; A-255
FT and A-259."
FT /evidence="ECO:0000269|PubMed:20383140"
SQ SEQUENCE 316 AA; 34569 MW; 379F2E2D6E25085F CRC64;
MNTILTCQDE YFAGGLGYDC PYFSSTSAST VDVSKETWVS LWASGLLDNR SSNHGPHTQG
QLYNMGNSLQ EDYLFGDQLS SQISANKQLQ DTLLQKEEEL SRLHEENNKL KEFLNSAFVK
TLAEKTKKLL HQNGQSSFCT NPNSRVPFSS NSTPGSKAKR ARRNLYGELT ACEAQSSPVV
EKWVLQTLGL KDVDTIDDSA LANYSAMSLQ PKQDSPSSGY SSAHLTPGHS QAATSCSLSP
SQCSSASLPE SETASPLSSP TYHTPDVAPN KTEVAFSTSL HPHCNVKTHS FPQGQAFVRR
DTQGGWKFTW VPKQSE
