RN152_HUMAN
ID RN152_HUMAN Reviewed; 203 AA.
AC Q8N8N0; B3KV99; Q52LA4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=E3 ubiquitin-protein ligase RNF152 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:25936802};
DE AltName: Full=RING finger protein 152 {ECO:0000312|HGNC:HGNC:26811};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF152 {ECO:0000305};
GN Name=RNF152 {ECO:0000312|HGNC:HGNC:26811};
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, UBIQUITINATION, AND TISSUE SPECIFICITY.
RX PubMed=21203937; DOI=10.1007/s13238-010-0083-1;
RA Zhang S., Wu W., Wu Y., Zheng J., Suo T., Tang H., Tang J.;
RT "RNF152, a novel lysosome localized E3 ligase with pro-apoptotic
RT activities.";
RL Protein Cell 1:656-663(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, INTERACTION
RP WITH RRAGA, AND REGION.
RX PubMed=25936802; DOI=10.1016/j.molcel.2015.03.033;
RA Deng L., Jiang C., Chen L., Jin J., Wei J., Zhao L., Chen M., Pan W.,
RA Xu Y., Chu H., Wang X., Ge X., Li D., Liao L., Liu M., Li L., Wang P.;
RT "The ubiquitination of RagA GTPase by RNF152 negatively regulates mTORC1
RT activation.";
RL Mol. Cell 58:804-818(2015).
CC -!- FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-63'-linked
CC polyubiquitination of RRAGA in response to amino acid starvation.
CC Thereby, regulates mTORC1 signaling and plays a role in the cellular
CC response to amino acid availability (PubMed:25936802). Also mediates
CC 'Lys-48'-linked polyubiquitination of target proteins and their
CC subsequent targeting to the proteasome for degradation. Induces
CC apoptosis when overexpressed (PubMed:21203937).
CC {ECO:0000269|PubMed:21203937, ECO:0000269|PubMed:25936802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:25936802};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:25936802}.
CC -!- SUBUNIT: Interacts with RRAGA (inactive GDP-bound form); stimulated by
CC amino acid starvation (PubMed:25936802). Interacts with SEC16A (By
CC similarity). {ECO:0000250|UniProtKB:Q8BG47,
CC ECO:0000269|PubMed:25936802}.
CC -!- INTERACTION:
CC Q8N8N0; Q15125: EBP; NbExp=3; IntAct=EBI-2129725, EBI-3915253;
CC Q8N8N0; P48165: GJA8; NbExp=3; IntAct=EBI-2129725, EBI-17458373;
CC Q8N8N0; P43628: KIR2DL3; NbExp=3; IntAct=EBI-2129725, EBI-8632435;
CC Q8N8N0; Q99732: LITAF; NbExp=3; IntAct=EBI-2129725, EBI-725647;
CC Q8N8N0; O95859: TSPAN12; NbExp=3; IntAct=EBI-2129725, EBI-2466403;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:25936802,
CC ECO:0000305|PubMed:21203937}; Single-pass membrane protein
CC {ECO:0000269|PubMed:25936802, ECO:0000305|PubMed:21203937}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21203937}.
CC -!- PTM: Ubiquitinated. Autoubiquitinated in vitro, leading to its
CC degradation by the proteasome (Probable).
CC {ECO:0000305|PubMed:21203937}.
CC -!- SIMILARITY: Belongs to the RNF152 family. {ECO:0000305}.
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DR EMBL; AK096495; BAC04805.1; -; mRNA.
DR EMBL; AK122758; BAG53711.1; -; mRNA.
DR EMBL; AC105094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094004; AAH94004.1; -; mRNA.
DR EMBL; BC111956; AAI11957.1; -; mRNA.
DR CCDS; CCDS11978.1; -.
DR RefSeq; NP_775828.1; NM_173557.2.
DR RefSeq; XP_005266707.1; XM_005266650.3.
DR RefSeq; XP_005266709.1; XM_005266652.3.
DR RefSeq; XP_011524180.1; XM_011525878.2.
DR RefSeq; XP_011524181.1; XM_011525879.2.
DR RefSeq; XP_016881101.1; XM_017025612.1.
DR RefSeq; XP_016881102.1; XM_017025613.1.
DR AlphaFoldDB; Q8N8N0; -.
DR SMR; Q8N8N0; -.
DR BioGRID; 128647; 29.
DR IntAct; Q8N8N0; 9.
DR STRING; 9606.ENSP00000316628; -.
DR MoonDB; Q8N8N0; Predicted.
DR iPTMnet; Q8N8N0; -.
DR PhosphoSitePlus; Q8N8N0; -.
DR BioMuta; RNF152; -.
DR DMDM; 41017760; -.
DR MassIVE; Q8N8N0; -.
DR PaxDb; Q8N8N0; -.
DR PeptideAtlas; Q8N8N0; -.
DR PRIDE; Q8N8N0; -.
DR Antibodypedia; 71070; 10 antibodies from 7 providers.
DR DNASU; 220441; -.
DR Ensembl; ENST00000312828.4; ENSP00000316628.3; ENSG00000176641.11.
DR GeneID; 220441; -.
DR KEGG; hsa:220441; -.
DR MANE-Select; ENST00000312828.4; ENSP00000316628.3; NM_173557.3; NP_775828.1.
DR UCSC; uc002lih.2; human.
DR CTD; 220441; -.
DR DisGeNET; 220441; -.
DR GeneCards; RNF152; -.
DR HGNC; HGNC:26811; RNF152.
DR HPA; ENSG00000176641; Tissue enhanced (brain, choroid plexus, kidney).
DR MIM; 616512; gene.
DR neXtProt; NX_Q8N8N0; -.
DR OpenTargets; ENSG00000176641; -.
DR PharmGKB; PA134984811; -.
DR VEuPathDB; HostDB:ENSG00000176641; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00730000111317; -.
DR HOGENOM; CLU_1414689_0_0_1; -.
DR InParanoid; Q8N8N0; -.
DR OMA; REIRCPW; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q8N8N0; -.
DR TreeFam; TF331690; -.
DR PathwayCommons; Q8N8N0; -.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; Q8N8N0; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 220441; 11 hits in 1112 CRISPR screens.
DR ChiTaRS; RNF152; human.
DR GenomeRNAi; 220441; -.
DR Pharos; Q8N8N0; Tbio.
DR PRO; PR:Q8N8N0; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q8N8N0; protein.
DR Bgee; ENSG00000176641; Expressed in right lobe of liver and 97 other tissues.
DR ExpressionAtlas; Q8N8N0; baseline and differential.
DR Genevisible; Q8N8N0; HS.
DR GO; GO:0031301; C:integral component of organelle membrane; IMP:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IDA:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033609; RNF152.
DR InterPro; IPR045744; RNF152_C.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR25464:SF1; PTHR25464:SF1; 1.
DR Pfam; PF19325; RNF152_C; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Lysosome; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..203
FT /note="E3 ubiquitin-protein ligase RNF152"
FT /id="PRO_0000056111"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 12..55
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 106..165
FT /note="Necessary for interaction with RRAGA"
FT /evidence="ECO:0000269|PubMed:25936802"
FT CONFLICT 12
FT /note="C -> S (in Ref. 1; BAG53711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 22357 MW; 0DFA570D00744BFA CRC64;
METLSQDSLL ECQICFNYYS PRRRPKLLDC KHTCCSVCLQ QMRTSQKDVR CPWCRGVTKL
PPGFSVSQLP DDPEVLAVIA IPHTSEHTPV FIKLPSNGCY MLPLPISKER ALLPGDMGCR
LLPGSQQKSV TVVTIPAEQQ PLQGGAPQEA VEEEQDRRGV VKSSTWSGVC TVILVACVLV
FLLGIVLHNM SCISKRFTVI SCG
