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 13-FEB-2019, entry version 146. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT project: 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., RA Uhlen M., 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 RT regulator 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 -!- 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 CC triggered by thapsigargin or tunicamycin. CC {ECO:0000269|PubMed:27485036}. 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; U66469; AAC50897.1; -; mRNA. DR EMBL; BC015063; AAH15063.1; -; mRNA. DR CCDS; CCDS9719.1; -. DR RefSeq; NP_006559.1; NM_006568.2. DR UniGene; Hs.59106; -. DR PDB; 2EA5; NMR; -; A=264-318. DR PDBsum; 2EA5; -. DR ProteinModelPortal; Q99675; -. DR SMR; Q99675; -. DR BioGrid; 115910; 42. DR IntAct; Q99675; 19. DR MINT; Q99675; -. DR STRING; 9606.ENSP00000216420; -. DR iPTMnet; Q99675; -. DR PhosphoSitePlus; Q99675; -. DR BioMuta; CGRRF1; -. DR DMDM; 44887778; -. DR EPD; Q99675; -. DR MaxQB; Q99675; -. DR PaxDb; Q99675; -. DR PeptideAtlas; Q99675; -. DR PRIDE; Q99675; -. DR ProteomicsDB; 78389; -. DR DNASU; 10668; -. DR Ensembl; ENST00000216420; ENSP00000216420; ENSG00000100532. DR GeneID; 10668; -. DR KEGG; hsa:10668; -. DR UCSC; uc001xay.4; human. DR CTD; 10668; -. DR DisGeNET; 10668; -. DR EuPathDB; HostDB:ENSG00000100532.11; -. DR GeneCards; CGRRF1; -. DR HGNC; HGNC:15528; CGRRF1. DR HPA; HPA002930; -. DR MIM; 606138; gene. DR neXtProt; NX_Q99675; -. DR OpenTargets; ENSG00000100532; -. DR PharmGKB; PA134985671; -. DR eggNOG; ENOG410ITZ9; Eukaryota. DR eggNOG; ENOG4111F4I; LUCA. DR GeneTree; ENSGT00390000004542; -. DR HOGENOM; HOG000111607; -. DR HOVERGEN; HBG050932; -. DR InParanoid; Q99675; -. DR OMA; CDGCVRY; -. DR OrthoDB; 670633at2759; -. DR PhylomeDB; Q99675; -. DR TreeFam; TF328102; -. DR ChiTaRS; CGRRF1; human. DR EvolutionaryTrace; Q99675; -. DR GenomeRNAi; 10668; -. DR PRO; PR:Q99675; -. DR Proteomes; UP000005640; Chromosome 14. DR Bgee; ENSG00000100532; Expressed in 229 organ(s), highest expression level in testis. 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:0007050; P:cell cycle arrest; IEA:UniProtKB-KW. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR SMART; SM00184; RING; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Complete proteome; Endoplasmic reticulum; KW Growth arrest; Metal-binding; Nucleus; Polymorphism; KW Reference proteome; Zinc; Zinc-finger. FT CHAIN 1 332 Cell growth regulator with RING finger FT domain protein 1. FT /FTId=PRO_0000055869. FT ZN_FING 274 309 RING-type. {ECO:0000255|PROSITE- FT ProRule:PRU00175}. FT VARIANT 117 117 C -> Y (in dbSNP:rs11555279). FT /FTId=VAR_052081. FT CONFLICT 103 103 S -> N (in Ref. 2; AAH15063). FT {ECO:0000305}. FT STRAND 275 280 {ECO:0000244|PDB:2EA5}. FT TURN 287 290 {ECO:0000244|PDB:2EA5}. FT HELIX 298 301 {ECO:0000244|PDB:2EA5}. FT TURN 306 308 {ECO:0000244|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 //