CGRF1_HUMAN
ID CGRF1_HUMAN Reviewed; 332 AA.
AC Q99675; Q96BX2;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cell growth regulator with RING finger domain protein 1;
DE AltName: Full=Cell growth regulatory gene 19 protein;
DE AltName: Full=RING finger protein 197;
GN Name=CGRRF1; Synonyms=CGR19, RNF197;
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].
RC TISSUE=Fetal brain;
RX PubMed=8968090;
RA Madden S.L., Galella E.A., Riley D., Bertelsen A.H., Beaudry G.A.;
RT "Induction of cell growth regulatory genes by p53.";
RL Cancer Res. 56:5384-5390(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=22361696; DOI=10.1016/j.jprot.2012.01.030;
RA Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R., Uhlen M.,
RA Lundberg E.;
RT "Systematic validation of antibody binding and protein subcellular
RT localization using siRNA and confocal microscopy.";
RL J. Proteomics 75:2236-2251(2012).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=27485036; DOI=10.1038/srep30955;
RA Kaneko M., Iwase I., Yamasaki Y., Takai T., Wu Y., Kanemoto S.,
RA Matsuhisa K., Asada R., Okuma Y., Watanabe T., Imaizumi K., Nomura Y.;
RT "Genome-wide identification and gene expression profiling of ubiquitin
RT ligases for endoplasmic reticulum protein degradation.";
RL Sci. Rep. 6:30955-30955(2016).
RN [5]
RP STRUCTURE BY NMR OF 262-318.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain of the human cell growth regulator
RT with RING finger domain 1 protein.";
RL Submitted (JUL-2007) to the PDB data bank.
CC -!- FUNCTION: Able to inhibit growth in several cell lines.
CC {ECO:0000250|UniProtKB:P97587}.
CC -!- INTERACTION:
CC Q99675; Q8TD06: AGR3; NbExp=3; IntAct=EBI-2130213, EBI-3925742;
CC Q99675; O15155: BET1; NbExp=3; IntAct=EBI-2130213, EBI-749204;
CC Q99675; P21854: CD72; NbExp=3; IntAct=EBI-2130213, EBI-307924;
CC Q99675; O14735: CDIPT; NbExp=3; IntAct=EBI-2130213, EBI-358858;
CC Q99675; O43169: CYB5B; NbExp=3; IntAct=EBI-2130213, EBI-1058710;
CC Q99675; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-2130213, EBI-12118888;
CC Q99675; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-2130213, EBI-12142299;
CC Q99675; O15552: FFAR2; NbExp=3; IntAct=EBI-2130213, EBI-2833872;
CC Q99675; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-2130213, EBI-11955647;
CC Q99675; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-2130213, EBI-13345167;
CC Q99675; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-2130213, EBI-10266796;
CC Q99675; P26715: KLRC1; NbExp=3; IntAct=EBI-2130213, EBI-9018187;
CC Q99675; Q86VI4: LAPTM4B; NbExp=3; IntAct=EBI-2130213, EBI-3267258;
CC Q99675; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-2130213, EBI-12133176;
CC Q99675; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-2130213, EBI-2341610;
CC Q99675; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-2130213, EBI-3923617;
CC Q99675; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-2130213, EBI-12092917;
CC Q99675; Q8TEB9: RHBDD1; NbExp=3; IntAct=EBI-2130213, EBI-9916444;
CC Q99675; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-2130213, EBI-4403649;
CC Q99675; Q99726: SLC30A3; NbExp=3; IntAct=EBI-2130213, EBI-10294651;
CC Q99675; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-2130213, EBI-10262251;
CC Q99675; Q96L08: SUSD3; NbExp=3; IntAct=EBI-2130213, EBI-18194029;
CC Q99675; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-2130213, EBI-2844246;
CC Q99675; Q14656: TMEM187; NbExp=3; IntAct=EBI-2130213, EBI-13046724;
CC Q99675; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-2130213, EBI-12111910;
CC Q99675; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-2130213, EBI-17249488;
CC Q99675; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-2130213, EBI-751210;
CC Q99675; O95159: ZFPL1; NbExp=3; IntAct=EBI-2130213, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22361696}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:27485036}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in
CC testis and the cerebellum. {ECO:0000269|PubMed:27485036}.
CC -!- INDUCTION: Up-regulated by endoplasmic reticulum (ER) stress triggered
CC by thapsigargin or tunicamycin. {ECO:0000269|PubMed:27485036}.
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DR EMBL; U66469; AAC50897.1; -; mRNA.
DR EMBL; BC015063; AAH15063.1; -; mRNA.
DR CCDS; CCDS9719.1; -.
DR RefSeq; NP_006559.1; NM_006568.2.
DR PDB; 2EA5; NMR; -; A=264-318.
DR PDBsum; 2EA5; -.
DR AlphaFoldDB; Q99675; -.
DR SMR; Q99675; -.
DR BioGRID; 115910; 108.
DR IntAct; Q99675; 56.
DR MINT; Q99675; -.
DR STRING; 9606.ENSP00000216420; -.
DR iPTMnet; Q99675; -.
DR PhosphoSitePlus; Q99675; -.
DR BioMuta; CGRRF1; -.
DR DMDM; 44887778; -.
DR EPD; Q99675; -.
DR MassIVE; Q99675; -.
DR MaxQB; Q99675; -.
DR PaxDb; Q99675; -.
DR PeptideAtlas; Q99675; -.
DR PRIDE; Q99675; -.
DR ProteomicsDB; 78389; -.
DR Antibodypedia; 152; 171 antibodies from 30 providers.
DR DNASU; 10668; -.
DR Ensembl; ENST00000216420.12; ENSP00000216420.7; ENSG00000100532.13.
DR GeneID; 10668; -.
DR KEGG; hsa:10668; -.
DR MANE-Select; ENST00000216420.12; ENSP00000216420.7; NM_006568.3; NP_006559.1.
DR UCSC; uc001xay.4; human.
DR CTD; 10668; -.
DR DisGeNET; 10668; -.
DR GeneCards; CGRRF1; -.
DR HGNC; HGNC:15528; CGRRF1.
DR HPA; ENSG00000100532; Low tissue specificity.
DR MIM; 606138; gene.
DR neXtProt; NX_Q99675; -.
DR OpenTargets; ENSG00000100532; -.
DR PharmGKB; PA134985671; -.
DR VEuPathDB; HostDB:ENSG00000100532; -.
DR eggNOG; KOG4265; Eukaryota.
DR GeneTree; ENSGT00390000004542; -.
DR HOGENOM; CLU_053217_0_0_1; -.
DR InParanoid; Q99675; -.
DR OMA; EDNREIY; -.
DR OrthoDB; 670633at2759; -.
DR PhylomeDB; Q99675; -.
DR TreeFam; TF328102; -.
DR PathwayCommons; Q99675; -.
DR SignaLink; Q99675; -.
DR BioGRID-ORCS; 10668; 13 hits in 1118 CRISPR screens.
DR ChiTaRS; CGRRF1; human.
DR EvolutionaryTrace; Q99675; -.
DR GenomeRNAi; 10668; -.
DR Pharos; Q99675; Tdark.
DR PRO; PR:Q99675; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q99675; protein.
DR Bgee; ENSG00000100532; Expressed in right testis and 208 other tissues.
DR ExpressionAtlas; Q99675; baseline and differential.
DR Genevisible; Q99675; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042496; CGRF1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15379; PTHR15379; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Endoplasmic reticulum; Growth arrest;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..332
FT /note="Cell growth regulator with RING finger domain
FT protein 1"
FT /id="PRO_0000055869"
FT ZN_FING 274..309
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VARIANT 117
FT /note="C -> Y (in dbSNP:rs11555279)"
FT /id="VAR_052081"
FT CONFLICT 103
FT /note="S -> N (in Ref. 2; AAH15063)"
FT /evidence="ECO:0000305"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2EA5"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:2EA5"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:2EA5"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:2EA5"
SQ SEQUENCE 332 AA; 38242 MW; 2F1FC0D12B710C80 CRC64;
MAAVFLVTLY EYSPLFYIAV VFTCFIVTTG LVLGWFGWDV PVILRNSEET QFSTRVFKKQ
MRQVKNPFGL EITNPSSASI TTGITLTTDC LEDSLLTCYW GCSVQKLYEA LQKHVYCFRI
STPQALEDAL YSEYLYQEQY FIKKDSKEEI YCQLPRDTKI EDFGTVPRSR YPLVALLTLA
DEDDREIYDI ISMVSVIHIP DRTYKLSCRI LYQYLLLAQG QFHDLKQLFM SANNNFTPSN
NSSSEEKNTD RSLLEKVGLS ESEVEPSEEN SKDCVVCQNG TVNWVLLPCR HTCLCDGCVK
YFQQCPMCRQ FVQESFALCS QKEQDKDKPK TL
