RN138_HUMAN
ID RN138_HUMAN Reviewed; 245 AA.
AC Q8WVD3; B2RE17; Q9H8K2; Q9UF87; Q9UKI6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=E3 ubiquitin-protein ligase RNF138 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Nemo-like kinase-associated RING finger protein {ECO:0000303|PubMed:16714285};
DE Short=NLK-associated RING finger protein {ECO:0000303|PubMed:16714285};
DE Short=hNARF {ECO:0000303|PubMed:16714285};
DE AltName: Full=RING finger protein 138 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF138 {ECO:0000305};
GN Name=RNF138 {ECO:0000312|HGNC:HGNC:17765};
GN Synonyms=NARF {ECO:0000303|PubMed:16714285}; ORFNames=HSD-4, HSD4;
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] (ISOFORM 1).
RC TISSUE=Testis;
RA Wang L., Miao S., Yang J., Zhang X., Li M.;
RT "A new spermatogenesis-related gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-245 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH NLK.
RX PubMed=16714285; DOI=10.1074/jbc.m602089200;
RA Yamada M., Ohnishi J., Ohkawara B., Iemura S., Satoh K., Hyodo-Miura J.,
RA Kawachi K., Natsume T., Shibuya H.;
RT "NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates
RT the ubiquitylation and degradation of T cell factor/lymphoid enhancer
RT factor (TCF/LEF).";
RL J. Biol. Chem. 281:20749-20760(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH XRCC5,
RP DOMAIN, AND MUTAGENESIS OF CYS-18 AND CYS-54.
RX PubMed=26502055; DOI=10.1038/ncb3259;
RA Ismail I.H., Gagne J.P., Genois M.M., Strickfaden H., McDonald D., Xu Z.,
RA Poirier G.G., Masson J.Y., Hendzel M.J.;
RT "The RNF138 E3 ligase displaces Ku to promote DNA end resection and
RT regulate DNA repair pathway choice.";
RL Nat. Cell Biol. 17:1446-1457(2015).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBBP8, AND MUTAGENESIS OF
RP 18-CYS--CYS-21.
RX PubMed=26502057; DOI=10.1038/ncb3260;
RA Schmidt C.K., Galanty Y., Sczaniecka-Clift M., Coates J., Jhujh S.,
RA Demir M., Cornwell M., Beli P., Jackson S.P.;
RT "Systematic E2 screening reveals a UBE2D-RNF138-CtIP axis promoting DNA
RT repair.";
RL Nat. Cell Biol. 17:1458-1470(2015).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in DNA damage response
CC by promoting DNA resection and homologous recombination
CC (PubMed:26502055, PubMed:26502057). Recruited to sites of double-strand
CC breaks following DNA damage and specifically promotes double-strand
CC break repair via homologous recombination (PubMed:26502055,
CC PubMed:26502057). Two different, non-exclusive, mechanisms have been
CC proposed. According to a report, regulates the choice of double-strand
CC break repair by favoring homologous recombination over non-homologous
CC end joining (NHEJ): acts by mediating ubiquitination of XRCC5/Ku80,
CC leading to remove the Ku complex from DNA breaks, thereby promoting
CC homologous recombination (PubMed:26502055). According to another
CC report, cooperates with UBE2Ds E2 ubiquitin ligases (UBE2D1, UBE2D2,
CC UBE2D3 or UBE2D4) to promote homologous recombination by mediating
CC ubiquitination of RBBP8/CtIP (PubMed:26502057). Together with NLK,
CC involved in the ubiquitination and degradation of TCF/LEF
CC (PubMed:16714285). Also exhibits auto-ubiquitination activity in
CC combination with UBE2K (PubMed:16714285). May act as a negative
CC regulator in the Wnt/beta-catenin-mediated signaling pathway
CC (PubMed:16714285). {ECO:0000269|PubMed:16714285,
CC ECO:0000269|PubMed:26502055, ECO:0000269|PubMed:26502057}.
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.
CC {ECO:0000269|PubMed:16714285, ECO:0000269|PubMed:26502055,
CC ECO:0000269|PubMed:26502057}.
CC -!- SUBUNIT: Interacts with NLK (PubMed:16714285). Interacts with
CC XRCC5/Ku80 (PubMed:26502055). Interacts with RBBP8/CtIP
CC (PubMed:26502057). {ECO:0000269|PubMed:16714285,
CC ECO:0000269|PubMed:26502055, ECO:0000269|PubMed:26502057}.
CC -!- INTERACTION:
CC Q8WVD3; P07550: ADRB2; NbExp=3; IntAct=EBI-749039, EBI-491169;
CC Q8WVD3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-749039, EBI-10976677;
CC Q8WVD3; O95967: EFEMP2; NbExp=3; IntAct=EBI-749039, EBI-743414;
CC Q8WVD3; P22607: FGFR3; NbExp=3; IntAct=EBI-749039, EBI-348399;
CC Q8WVD3; Q16595: FXN; NbExp=3; IntAct=EBI-749039, EBI-949340;
CC Q8WVD3; Q14957: GRIN2C; NbExp=3; IntAct=EBI-749039, EBI-8285963;
CC Q8WVD3; P28799: GRN; NbExp=3; IntAct=EBI-749039, EBI-747754;
CC Q8WVD3; P06396: GSN; NbExp=3; IntAct=EBI-749039, EBI-351506;
CC Q8WVD3; P01112: HRAS; NbExp=3; IntAct=EBI-749039, EBI-350145;
CC Q8WVD3; O43464: HTRA2; NbExp=3; IntAct=EBI-749039, EBI-517086;
CC Q8WVD3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-749039, EBI-1055254;
CC Q8WVD3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-749039, EBI-10975473;
CC Q8WVD3; P02545: LMNA; NbExp=3; IntAct=EBI-749039, EBI-351935;
CC Q8WVD3; P35240-4: NF2; NbExp=3; IntAct=EBI-749039, EBI-1014514;
CC Q8WVD3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-749039, EBI-741158;
CC Q8WVD3; D3DTS7: PMP22; NbExp=3; IntAct=EBI-749039, EBI-25882629;
CC Q8WVD3; O60260-5: PRKN; NbExp=3; IntAct=EBI-749039, EBI-21251460;
CC Q8WVD3; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-749039, EBI-396669;
CC Q8WVD3; P37840: SNCA; NbExp=3; IntAct=EBI-749039, EBI-985879;
CC Q8WVD3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-749039, EBI-5235340;
CC Q8WVD3; Q13148: TARDBP; NbExp=3; IntAct=EBI-749039, EBI-372899;
CC Q8WVD3; Q86WV8: TSC1; NbExp=3; IntAct=EBI-749039, EBI-12806590;
CC Q8WVD3; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-749039, EBI-8994397;
CC Q8WVD3; P61086: UBE2K; NbExp=11; IntAct=EBI-749039, EBI-473850;
CC Q8WVD3; Q9Y649; NbExp=3; IntAct=EBI-749039, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:26502055,
CC ECO:0000269|PubMed:26502057}. Note=Recruited at DNA damage sites
CC (PubMed:26502055). Localizes to sites of double-strand break:
CC localization to double-strand break sites is mediated by the zinc
CC fingers (PubMed:26502055, PubMed:26502057).
CC {ECO:0000269|PubMed:26502055, ECO:0000269|PubMed:26502057}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WVD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVD3-2; Sequence=VSP_021732;
CC -!- DOMAIN: The zinc finger domains (C2H2-type and C2HC-type zinc fingers)
CC bind DNA and mediate recruitment to double-strand break sites. They
CC show strong preference for DNA with 5'- or 3'-single-stranded
CC overhangs, while they do not bind blunt-ended double-stranded DNA or
CC poly(ADP-ribose) (PAR) polymers. {ECO:0000269|PubMed:26502055}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:16714285}.
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DR EMBL; AF162680; AAD46623.2; -; mRNA.
DR EMBL; AK023579; BAB14614.1; -; mRNA.
DR EMBL; AK315761; BAG38114.1; -; mRNA.
DR EMBL; BT006878; AAP35524.1; -; mRNA.
DR EMBL; CR457150; CAG33431.1; -; mRNA.
DR EMBL; CH471088; EAX01280.1; -; Genomic_DNA.
DR EMBL; BC018107; AAH18107.1; -; mRNA.
DR EMBL; AL133557; CAB63712.1; -; mRNA.
DR CCDS; CCDS11903.1; -. [Q8WVD3-1]
DR CCDS; CCDS11904.1; -. [Q8WVD3-2]
DR PIR; T43439; T43439.
DR RefSeq; NP_001178253.2; NM_001191324.1. [Q8WVD3-1]
DR RefSeq; NP_057355.2; NM_016271.4. [Q8WVD3-1]
DR RefSeq; NP_937761.1; NM_198128.2. [Q8WVD3-2]
DR RefSeq; XP_005258343.1; XM_005258286.1. [Q8WVD3-2]
DR AlphaFoldDB; Q8WVD3; -.
DR BioGRID; 119545; 89.
DR IntAct; Q8WVD3; 59.
DR STRING; 9606.ENSP00000261593; -.
DR iPTMnet; Q8WVD3; -.
DR PhosphoSitePlus; Q8WVD3; -.
DR BioMuta; RNF138; -.
DR DMDM; 74762632; -.
DR EPD; Q8WVD3; -.
DR jPOST; Q8WVD3; -.
DR MassIVE; Q8WVD3; -.
DR MaxQB; Q8WVD3; -.
DR PaxDb; Q8WVD3; -.
DR PeptideAtlas; Q8WVD3; -.
DR PRIDE; Q8WVD3; -.
DR ProteomicsDB; 74778; -. [Q8WVD3-1]
DR ProteomicsDB; 74779; -. [Q8WVD3-2]
DR Antibodypedia; 22190; 221 antibodies from 26 providers.
DR DNASU; 51444; -.
DR Ensembl; ENST00000257190.9; ENSP00000257190.5; ENSG00000134758.14. [Q8WVD3-2]
DR Ensembl; ENST00000261593.8; ENSP00000261593.3; ENSG00000134758.14. [Q8WVD3-1]
DR GeneID; 51444; -.
DR KEGG; hsa:51444; -.
DR MANE-Select; ENST00000261593.8; ENSP00000261593.3; NM_016271.5; NP_057355.2.
DR UCSC; uc002kxg.3; human. [Q8WVD3-1]
DR CTD; 51444; -.
DR DisGeNET; 51444; -.
DR GeneCards; RNF138; -.
DR HGNC; HGNC:17765; RNF138.
DR HPA; ENSG00000134758; Tissue enhanced (bone marrow, testis).
DR MIM; 616319; gene.
DR neXtProt; NX_Q8WVD3; -.
DR OpenTargets; ENSG00000134758; -.
DR PharmGKB; PA134952071; -.
DR VEuPathDB; HostDB:ENSG00000134758; -.
DR eggNOG; ENOG502RP2G; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_0_0_1; -.
DR InParanoid; Q8WVD3; -.
DR OMA; HHYKTCK; -.
DR PhylomeDB; Q8WVD3; -.
DR TreeFam; TF331012; -.
DR PathwayCommons; Q8WVD3; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q8WVD3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 51444; 16 hits in 1134 CRISPR screens.
DR ChiTaRS; RNF138; human.
DR GenomeRNAi; 51444; -.
DR Pharos; Q8WVD3; Tbio.
DR PRO; PR:Q8WVD3; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q8WVD3; protein.
DR Bgee; ENSG00000134758; Expressed in secondary oocyte and 205 other tissues.
DR ExpressionAtlas; Q8WVD3; baseline and differential.
DR Genevisible; Q8WVD3; HS.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR034734; ZF_C2HC_RNF.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF18574; zf_C2HC_14; 1.
DR SMART; SM00184; RING; 2.
DR PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..245
FT /note="E3 ubiquitin-protein ligase RNF138"
FT /id="PRO_0000261607"
FT DOMAIN 225..243
FT /note="UIM"
FT /evidence="ECO:0000305"
FT ZN_FING 18..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 86..105
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144,
FT ECO:0000305"
FT ZN_FING 157..180
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 187..215
FT /note="C2H2-type 2"
FT /evidence="ECO:0000305"
FT REGION 125..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 38..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021732"
FT VARIANT 81
FT /note="K -> R (in dbSNP:rs7229690)"
FT /id="VAR_052109"
FT MUTAGEN 18..21
FT /note="CPVC->APVA: Catalytic inactive mutant that abolishes
FT ability to promote DNA resection and homologous
FT recombination."
FT /evidence="ECO:0000269|PubMed:26502057"
FT MUTAGEN 18
FT /note="C->A: Catalytic inactive mutant that abolishes
FT ability to promote DNA resection and homologous
FT recombination; when associated with A-54."
FT /evidence="ECO:0000269|PubMed:26502055"
FT MUTAGEN 54
FT /note="C->A: Catalytic inactive mutant that abolishes
FT ability to promote DNA resection and homologous
FT recombination; when associated with A-18."
FT /evidence="ECO:0000269|PubMed:26502055"
FT CONFLICT 118
FT /note="I -> V (in Ref. 1; AAD46623)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="H -> R (in Ref. 1; AAD46623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 28193 MW; 807EE4500BE0919C CRC64;
MAEDLSAATS YTEDDFYCPV CQEVLKTPVR TTACQHVFCR KCFLTAMRES GAHCPLCRGN
VTRRERACPE RALDLENIMR KFSGSCRCCA KQIKFYRMRH HYKSCKKYQD EYGVSSIIPN
FQISQDSVGN SNRSETSTSD NTETYQENTS SSGHPTFKCP LCQESNFTRQ RLLDHCNSNH
LFQIVPVTCP ICVSLPWGDP SQITRNFVSH LNQRHQFDYG EFVNLQLDEE TQYQTAVEES
FQVNI
