RFPL1_HUMAN
ID RFPL1_HUMAN Reviewed; 317 AA.
AC O75677; Q6IC06; Q9UJ97;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ret finger protein-like 1;
DE AltName: Full=RING finger protein 78;
GN Name=RFPL1; Synonyms=RFPL1L, RNF78;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-127 AND LEU-139 DEL.
RX PubMed=10508838; DOI=10.1101/gr.9.9.803;
RA Seroussi E., Kedra D., Pan H.-Q., Peyrad M., Schwartz C., Scambler P.,
RA Donnai D., Roe B.A., Dumanski J.P.;
RT "Duplications on human chromosome 22 reveal a novel Ret finger protein-like
RT gene family with sense and endogenous antisense transcripts.";
RL Genome Res. 9:803-814(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-127 AND LEU-139
RP DEL.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-317, AND VARIANTS THR-127 AND
RP LEU-139 DEL.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, PHOSPHORYLATION, CHARACTERIZATION
RP OF VARIANT ARG-148--317-LYS DEL, VARIANT GLN-243--317-LYS DEL, AND
RP MUTAGENESIS OF 65-ASN--GLN-124; SER-200 AND SER-287.
RX PubMed=20725088; DOI=10.1038/cdd.2010.102;
RA Bonnefont J., Laforge T., Plastre O., Beck B., Sorce S., Dehay C.,
RA Krause K.H.;
RT "Primate-specific RFPL1 gene controls cell-cycle progression through cyclin
RT B1/Cdc2 degradation.";
RL Cell Death Differ. 18:293-303(2011).
CC -!- FUNCTION: Negatively regulates the G2-M phase transition, possibly by
CC promoting cyclin B1/CCNB1 and CDK1 proteasomal degradation and thereby
CC preventing their accumulation during interphase.
CC {ECO:0000269|PubMed:20725088}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20725088}. Nucleus
CC {ECO:0000269|PubMed:20725088}. Note=A higher concentration is observed
CC in the cytoplasm compared to the nucleus.
CC {ECO:0000269|PubMed:20725088}.
CC -!- TISSUE SPECIFICITY: Seems to be expressed in prostate and less
CC abundantly in adult brain, fetal liver, and fetal kidney.
CC -!- DOMAIN: The B30.2/SPRY domain is required for the negative regulation
CC of cell proliferation. {ECO:0000269|PubMed:20725088}.
CC -!- PTM: Phosphorylated by PKC and CDK1 (PubMed:20725088). The
CC antiproliferative effect seems to be positively regulated by PKC
CC phosphorylation and negatively by CDK1 phosphorylation
CC (PubMed:20725088). {ECO:0000269|PubMed:20725088}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA09043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA09044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ010228; CAA09043.1; ALT_INIT; mRNA.
DR EMBL; AJ010229; CAA09044.1; ALT_INIT; mRNA.
DR EMBL; CR456562; CAG30448.1; -; mRNA.
DR EMBL; BC104768; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13857.2; -.
DR RefSeq; NP_066306.2; NM_021026.2.
DR RefSeq; XP_011528600.1; XM_011530298.2.
DR RefSeq; XP_011528601.1; XM_011530299.2.
DR RefSeq; XP_016884389.1; XM_017028900.1.
DR RefSeq; XP_016884390.1; XM_017028901.1.
DR RefSeq; XP_016884391.1; XM_017028902.1.
DR AlphaFoldDB; O75677; -.
DR SMR; O75677; -.
DR BioGRID; 111920; 15.
DR IntAct; O75677; 1.
DR STRING; 9606.ENSP00000346342; -.
DR iPTMnet; O75677; -.
DR PhosphoSitePlus; O75677; -.
DR BioMuta; RFPL1; -.
DR jPOST; O75677; -.
DR MassIVE; O75677; -.
DR PaxDb; O75677; -.
DR PeptideAtlas; O75677; -.
DR PRIDE; O75677; -.
DR Antibodypedia; 24513; 76 antibodies from 16 providers.
DR DNASU; 5988; -.
DR Ensembl; ENST00000354373.2; ENSP00000346342.2; ENSG00000128250.5.
DR GeneID; 5988; -.
DR KEGG; hsa:5988; -.
DR UCSC; uc003afn.3; human.
DR CTD; 5988; -.
DR DisGeNET; 5988; -.
DR GeneCards; RFPL1; -.
DR HGNC; HGNC:9977; RFPL1.
DR HPA; ENSG00000128250; Tissue enhanced (adrenal gland, brain, retina).
DR MIM; 605968; gene.
DR neXtProt; NX_O75677; -.
DR OpenTargets; ENSG00000128250; -.
DR PharmGKB; PA34346; -.
DR VEuPathDB; HostDB:ENSG00000128250; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000163408; -.
DR HOGENOM; CLU_013137_7_1_1; -.
DR InParanoid; O75677; -.
DR OMA; QTEIICA; -.
DR OrthoDB; 1139938at2759; -.
DR PhylomeDB; O75677; -.
DR TreeFam; TF317532; -.
DR PathwayCommons; O75677; -.
DR SignaLink; O75677; -.
DR BioGRID-ORCS; 5988; 5 hits in 1035 CRISPR screens.
DR ChiTaRS; RFPL1; human.
DR GenomeRNAi; 5988; -.
DR Pharos; O75677; Tdark.
DR PRO; PR:O75677; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O75677; protein.
DR Bgee; ENSG00000128250; Expressed in prefrontal cortex and 46 other tissues.
DR Genevisible; O75677; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051782; P:negative regulation of cell division; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2001272; P:positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd15821; SPRY_PRY_RFPL; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR022723; RDM_domain_RFPL.
DR InterPro; IPR038908; RFPL.
DR InterPro; IPR037960; SPRY/PRY_RFPL.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR25462:SF279; PTHR25462:SF279; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF11002; RDM; 1.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..317
FT /note="Ret finger protein-like 1"
FT /id="PRO_0000056030"
FT DOMAIN 107..301
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 40..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VARIANT 94
FT /note="W -> R (in dbSNP:rs16987627)"
FT /id="VAR_039572"
FT VARIANT 127
FT /note="M -> T (in dbSNP:rs3804076)"
FT /evidence="ECO:0000269|PubMed:10508838,
FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:15489334"
FT /id="VAR_020115"
FT VARIANT 139
FT /note="Missing (in dbSNP:rs3842466)"
FT /evidence="ECO:0000269|PubMed:10508838,
FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:15489334"
FT /id="VAR_039573"
FT VARIANT 148..317
FT /note="Missing (increased cell proliferation;
FT dbSNP:rs16987628)"
FT /evidence="ECO:0000269|PubMed:20725088"
FT /id="VAR_080854"
FT VARIANT 243..317
FT /note="Missing (in dbSNP:rs12484086)"
FT /evidence="ECO:0000269|PubMed:20725088"
FT /id="VAR_080855"
FT MUTAGEN 65..124
FT /note="Missing: Increased cell proliferation."
FT /evidence="ECO:0000269|PubMed:20725088"
FT MUTAGEN 200
FT /note="S->A: Reduced phosphorylation by PKC, increased cell
FT proliferation, reduced apoptosis and lack of cyclin
FT B1/CCNB1 and CDK1 degradation."
FT /evidence="ECO:0000269|PubMed:20725088"
FT MUTAGEN 200
FT /note="S->E: No effect on cell proliferation."
FT /evidence="ECO:0000269|PubMed:20725088"
FT MUTAGEN 287
FT /note="S->E: Increased cell proliferation, reduced
FT apoptosis and lack of cyclin B1/CCNB1 and CDK1
FT degradation."
FT /evidence="ECO:0000269|PubMed:20725088"
FT MUTAGEN 287
FT /note="S->G: Reduced phosphorylation by CDK1."
FT /evidence="ECO:0000269|PubMed:20725088"
FT CONFLICT 289
FT /note="P -> S (in Ref. 2; CAG30448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35491 MW; 75FDDED7BF51B8CA CRC64;
MKRLSLVTTN RLSPHGNFLP LCTFPLAVDM AALFQEASSC PVCSDYLEKP MSLECGCAVC
FKCINSLQKE PHGEDLLCCC CSMVSQKNKI RPSWQLERLA SHIKELEPKL KKILQMNPRM
RKFQVDMTLD ADTANNFLLI SDDLRSVRSG CITQNRQDLA ERFDVSICIL GSPRFTCGRH
YWEVDVGTST EWDLGVCRES VHRKGRIHLT TERGFWTVSL RDGSRLSAST VPLTFLFVDR
KLQRVGIFLD MGMQNVSFFD AEGGSHVYTF RSVSAEEPLH LFFAPPSPPN GDKSVLSICP
VINPGTTDAP VHPGEAK
