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   28-JAN-2026, entry version 180.
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_006568.3.
DR   PDB; 2EA5; NMR; -; A=264-318.
DR   PDBsum; 2EA5; -.
DR   AlphaFoldDB; Q99675; -.
DR   SMR; Q99675; -.
DR   BioGRID; 115910; 112.
DR   FunCoup; Q99675; 3030.
DR   IntAct; Q99675; 82.
DR   MINT; Q99675; -.
DR   STRING; 9606.ENSP00000216420; -.
DR   iPTMnet; Q99675; -.
DR   PhosphoSitePlus; Q99675; -.
DR   BioMuta; CGRRF1; -.
DR   DMDM; 44887778; -.
DR   jPOST; Q99675; -.
DR   MassIVE; Q99675; -.
DR   PaxDb; 9606-ENSP00000216420; -.
DR   PeptideAtlas; Q99675; -.
DR   ProteomicsDB; 78389; -.
DR   Antibodypedia; 152; 177 antibodies from 30 providers.
DR   DNASU; 10668; -.
DR   Ensembl; ENST00000216420.12; ENSP00000216420.7; ENSG00000100532.14.
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   AGR; HGNC:15528; -.
DR   ClinPGx; PA134985671; -.
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   OpenTargets; ENSG00000100532; -.
DR   VEuPathDB; HostDB:ENSG00000100532; -.
DR   eggNOG; KOG4265; Eukaryota.
DR   GeneTree; ENSGT00390000004542; -.
DR   HOGENOM; CLU_053217_0_0_1; -.
DR   InParanoid; Q99675; -.
DR   OMA; IYCQLPK; -.
DR   OrthoDB; 10251219at2759; -.
DR   PAN-GO; Q99675; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; Q99675; -.
DR   PathwayCommons; Q99675; -.
DR   SignaLink; Q99675; -.
DR   SIGNOR; Q99675; -.
DR   Agora; ENSG00000100532; -.
DR   BioGRID-ORCS; 10668; 14 hits in 1197 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 primordial germ cell in gonad and 210 other cell types or tissues.
DR   ExpressionAtlas; Q99675; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0008270; F:zinc ion binding; 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   GO; GO:0051726; P:regulation of cell cycle; IEA:UniProtKB-KW.
DR   CDD; cd16787; mRING-HC-C3HC5_CGRF1; 1.
DR   FunFam; 3.30.40.10:FF:000421; Cell growth regulator with ring finger domain 1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR042496; CGRF1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15379; CELL GROWTH REGULATOR WITH RING FINGER DOMAIN PROTEIN 1; 1.
DR   PANTHER; PTHR15379:SF2; CELL GROWTH REGULATOR WITH RING FINGER DOMAIN PROTEIN 1; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 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; Proteomics identification; Reference proteome;
KW   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
//