RN112_HUMAN
ID RN112_HUMAN Reviewed; 631 AA.
AC Q9ULX5; O60633; Q7Z5V9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=RING finger protein 112;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Brain finger protein;
DE AltName: Full=Zinc finger protein 179;
GN Name=RNF112; Synonyms=BFP, ZNF179;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=10574464; DOI=10.1093/dnares/6.5.353;
RA Seki N., Hattori A., Muramatsu M., Saito T.;
RT "cDNA cloning of a human brain finger protein, BFP/ZNF179, a member of the
RT RING finger protein family.";
RL DNA Res. 6:353-356(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-127.
RX PubMed=8660987; DOI=10.1006/geno.1996.0203;
RA Matsuda Y., Inoue S., Seki N., Hosoi T., Orimo A., Muramatsu M., Hori T.;
RT "Chromosome mapping of human (ZNF179), mouse, and rat genes for brain
RT finger protein (bfp), a member of the RING finger family.";
RL Genomics 33:325-327(1996).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=28684796; DOI=10.1038/s41598-017-05305-0;
RA Lee K.H., Chen C.L., Lee Y.C., Kao T.J., Chen K.Y., Fang C.Y., Chang W.C.,
RA Chiang Y.H., Huang C.C.;
RT "Znf179 induces differentiation and growth arrest of human primary
RT glioblastoma multiforme in a p53-dependent cell cycle pathway.";
RL Sci. Rep. 7:4787-4787(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays an important role in
CC neuronal differentiation, including neurogenesis and gliogenesis,
CC during brain development. During embryonic development initiates
CC neuronal differentiation by inducing cell cycle arrest at the G0/G1
CC phase through up-regulation of cell-cycle regulatory proteins
CC (PubMed:28684796). Plays a role not only in the fetal period during the
CC development of the nervous system, but also in the adult brain, where
CC it is involved in the maintenance of neural functions and protection of
CC the nervous tissue cells from oxidative stress-induced damage. Exhibits
CC GTPase and E3 ubiquitin-protein ligase activities. Regulates dendritic
CC spine density and synaptic neurotransmission; its ability to hydrolyze
CC GTP is involved in the maintenance of dendritic spine density (By
CC similarity). {ECO:0000250|UniProtKB:Q96DY5,
CC ECO:0000269|PubMed:28684796}.
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:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Self-associates. Interacts with SP1 in an oxidative stress-
CC regulated manner. Interacts with SIGMAR1 in an oxidative stress-
CC regulated manner. Interacts with ZBTB16 (via C2H2-type zinc finger
CC domains 1 and 2). {ECO:0000250|UniProtKB:Q96DY5}.
CC -!- INTERACTION:
CC Q9ULX5; P01023: A2M; NbExp=3; IntAct=EBI-25829984, EBI-640741;
CC Q9ULX5; P05067: APP; NbExp=3; IntAct=EBI-25829984, EBI-77613;
CC Q9ULX5; P05067-2: APP; NbExp=3; IntAct=EBI-25829984, EBI-17264467;
CC Q9ULX5; P54253: ATXN1; NbExp=6; IntAct=EBI-25829984, EBI-930964;
CC Q9ULX5; P09172: DBH; NbExp=3; IntAct=EBI-25829984, EBI-8589586;
CC Q9ULX5; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-25829984, EBI-25840379;
CC Q9ULX5; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-25829984, EBI-21603100;
CC Q9ULX5; P28799: GRN; NbExp=3; IntAct=EBI-25829984, EBI-747754;
CC Q9ULX5; P42858: HTT; NbExp=21; IntAct=EBI-25829984, EBI-466029;
CC Q9ULX5; P51608: MECP2; NbExp=3; IntAct=EBI-25829984, EBI-1189067;
CC Q9ULX5; P19404: NDUFV2; NbExp=3; IntAct=EBI-25829984, EBI-713665;
CC Q9ULX5; Q96CV9: OPTN; NbExp=3; IntAct=EBI-25829984, EBI-748974;
CC Q9ULX5; Q99497: PARK7; NbExp=3; IntAct=EBI-25829984, EBI-1164361;
CC Q9ULX5; Q7Z412: PEX26; NbExp=3; IntAct=EBI-25829984, EBI-752057;
CC Q9ULX5; O14832: PHYH; NbExp=3; IntAct=EBI-25829984, EBI-721853;
CC Q9ULX5; D3DTS7: PMP22; NbExp=3; IntAct=EBI-25829984, EBI-25882629;
CC Q9ULX5; O60260-5: PRKN; NbExp=6; IntAct=EBI-25829984, EBI-21251460;
CC Q9ULX5; P41219: PRPH; NbExp=3; IntAct=EBI-25829984, EBI-752074;
CC Q9ULX5; P49768-2: PSEN1; NbExp=6; IntAct=EBI-25829984, EBI-11047108;
CC Q9ULX5; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25829984, EBI-396669;
CC Q9ULX5; P37840: SNCA; NbExp=3; IntAct=EBI-25829984, EBI-985879;
CC Q9ULX5; P00441: SOD1; NbExp=3; IntAct=EBI-25829984, EBI-990792;
CC Q9ULX5; Q13148: TARDBP; NbExp=6; IntAct=EBI-25829984, EBI-372899;
CC Q9ULX5; P09936: UCHL1; NbExp=3; IntAct=EBI-25829984, EBI-714860;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q96DY5}; Multi-
CC pass membrane protein {ECO:0000255}. Membrane
CC {ECO:0000250|UniProtKB:Q96DY5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96DY5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96DY5}. Nucleus {ECO:0000250|UniProtKB:Q96DY5}.
CC Nucleus, nuclear body {ECO:0000250|UniProtKB:Q96DY5}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q96DY5}. Endosome
CC {ECO:0000250|UniProtKB:Q96DY5}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:Q96DY5}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q96DY5}. Perikaryon
CC {ECO:0000250|UniProtKB:Q96DY5}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q96DY5}. Note=Predominantly in the nucleus, but
CC some amounts were also found in the cytoplasm. Oxidative stress
CC stimulates its shuttling from the cytoplasm into the nucleus. Recruited
CC to nuclear bodies via its interaction with ZBTB16. Localizes to the
CC cell soma and neuritis and only slightly to the nucleus in the neurons
CC of most brain areas. {ECO:0000250|UniProtKB:Q96DY5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULX5-2; Sequence=VSP_042377;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain (PubMed:10574464).
CC Decreased expression in glioma brain tumors as compared to normal
CC brains (at protein level) (PubMed:28684796).
CC {ECO:0000269|PubMed:10574464, ECO:0000269|PubMed:28684796}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q96DY5}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR EMBL; AB026054; BAA84698.1; -; mRNA.
DR EMBL; AC004448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053989; AAH53989.1; -; mRNA.
DR EMBL; AF054587; AAC08584.1; -; Genomic_DNA.
DR CCDS; CCDS58529.1; -. [Q9ULX5-1]
DR PIR; JC7155; JC7155.
DR RefSeq; NP_009079.2; NM_007148.4. [Q9ULX5-1]
DR AlphaFoldDB; Q9ULX5; -.
DR SMR; Q9ULX5; -.
DR BioGRID; 113520; 2.
DR IntAct; Q9ULX5; 23.
DR STRING; 9606.ENSP00000454919; -.
DR iPTMnet; Q9ULX5; -.
DR PhosphoSitePlus; Q9ULX5; -.
DR BioMuta; RNF112; -.
DR DMDM; 378405197; -.
DR MassIVE; Q9ULX5; -.
DR PaxDb; Q9ULX5; -.
DR PeptideAtlas; Q9ULX5; -.
DR PRIDE; Q9ULX5; -.
DR ProteomicsDB; 85146; -. [Q9ULX5-1]
DR ProteomicsDB; 85147; -. [Q9ULX5-2]
DR Antibodypedia; 3002; 162 antibodies from 23 providers.
DR DNASU; 7732; -.
DR Ensembl; ENST00000461366.2; ENSP00000454919.1; ENSG00000128482.16. [Q9ULX5-1]
DR GeneID; 7732; -.
DR KEGG; hsa:7732; -.
DR MANE-Select; ENST00000461366.2; ENSP00000454919.1; NM_007148.5; NP_009079.2.
DR UCSC; uc010vyw.3; human. [Q9ULX5-1]
DR CTD; 7732; -.
DR DisGeNET; 7732; -.
DR GeneCards; RNF112; -.
DR HGNC; HGNC:12968; RNF112.
DR HPA; ENSG00000128482; Tissue enhanced (brain).
DR MIM; 601237; gene.
DR neXtProt; NX_Q9ULX5; -.
DR OpenTargets; ENSG00000128482; -.
DR VEuPathDB; HostDB:ENSG00000128482; -.
DR eggNOG; KOG2037; Eukaryota.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160153; -.
DR HOGENOM; CLU_034812_0_0_1; -.
DR InParanoid; Q9ULX5; -.
DR OMA; MGAVNRC; -.
DR OrthoDB; 836337at2759; -.
DR PhylomeDB; Q9ULX5; -.
DR PathwayCommons; Q9ULX5; -.
DR SignaLink; Q9ULX5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7732; 5 hits in 1113 CRISPR screens.
DR ChiTaRS; RNF112; human.
DR GenomeRNAi; 7732; -.
DR Pharos; Q9ULX5; Tbio.
DR PRO; PR:Q9ULX5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9ULX5; protein.
DR Bgee; ENSG00000128482; Expressed in right hemisphere of cerebellum and 138 other tissues.
DR ExpressionAtlas; Q9ULX5; baseline and differential.
DR Genevisible; Q9ULX5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0036474; P:cell death in response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0036473; P:cell death in response to oxidative stress; ISS:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
DR GO; GO:0045687; P:positive regulation of glial cell differentiation; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0033194; P:response to hydroperoxide; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02263; GBP; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; GTP-binding; Membrane; Metal-binding; Neurogenesis;
KW Nucleotide-binding; Nucleus; Reference proteome; Synapse; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..631
FT /note="RING finger protein 112"
FT /id="PRO_0000056301"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 166..397
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT ZN_FING 57..98
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 131..631
FT /note="Interaction with ZBTB16"
FT /evidence="ECO:0000250|UniProtKB:Q96DY5"
FT BINDING 318..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96DY5"
FT VAR_SEQ 374
FT /note="P -> PG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574464"
FT /id="VSP_042377"
SQ SEQUENCE 631 AA; 68298 MW; 770C4F33B1395954 CRC64;
MPRPALSVTS FCHRLGKRER KQSFMGNSGN SWSHTPFPKL ELGLGPQPMA PRELPTCSIC
LERLRDPISL DCGHDFCIRC FSTHRLPGCE PPCCPECRKI CKQKRGLRSL GEKMKLLPQR
PLPPALQETC PVRAEPLLLV RINASGGLIL RMGAINRCLK HPLARDTPVC LLAVLGEQHS
GKSFLLNHLL QGLPGLESGE GGRPRGGEAS LQGCRWGANG LARGIWMWSH PFLLGKEGKK
VAVFLVDTGD AMSPELSRET RIKLCALTTM LSSYQILSTS QELKDTDLDY LEMFVHVAEV
MGKHYGMVPI QHLDLLVRDS SHPNKAGQGH VGNIFQRLSG RYPKVQELLQ GKRARCCLLP
APGRRRMNQG HASPGDTDDD FRHLLGAYVS DVLSAAPQHA KSRCQGYWNE GRAVARGDRR
LLTGQQLAQE IKNLSGWMGR TGPGFTSPDE MAAQLHDLRK VEAAKREFEE YVRQQDVATK
RIFSALRVLP DTMRNLLSTQ KDAILARHGV ALLCKGRDQT LEALEAELQA TAKAFMDSYT
MRFCGHLAAV GGAVGAGLMG LAGGVVGAGM AAAALAAEAG MVAAGAAVGA TGAAVVGGGV
GAGLAATVGC MEKEEDERLL EGDREPLLQE E
