RN149_HUMAN
ID RN149_HUMAN Reviewed; 400 AA.
AC Q8NC42; Q53S14; Q8N5I8; Q8NBY5; Q8WUU3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=E3 ubiquitin-protein ligase RNF149;
DE EC=2.3.2.27;
DE AltName: Full=DNA polymerase-transactivated protein 2;
DE AltName: Full=RING finger protein 149;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF149 {ECO:0000305};
DE Flags: Precursor;
GN Name=RNF149; Synonyms=DNAPTP2;
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], AND VARIANT GLU-356.
RA Wang C., Cheng J., Lang Z., Ji D., Yang Y., Zhang L., Wu Y.;
RT "Screening and cloning of the target genes transactivated by hepatitis B
RT virus DNA polymerase using suppression subtractive hybridization (SSH)
RT technique.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-9 AND GLU-356.
RC TISSUE=Placenta, and Teratocarcinoma;
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], AND VARIANT GLU-356.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-9; PHE-344 AND
RP GLU-356.
RC TISSUE=Brain, Cervix, and Placenta;
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 [6]
RP FUNCTION.
RX PubMed=22628551; DOI=10.1074/jbc.m111.319822;
RA Hong S.W., Jin D.H., Shin J.S., Moon J.H., Na Y.S., Jung K.A., Kim S.M.,
RA Kim J.C., Kim K.P., Hong Y.S., Lee J.L., Choi E.K., Lee J.S., Kim T.W.;
RT "Ring finger protein 149 is an E3 ubiquitin ligase active on wild-type v-
RT Raf murine sarcoma viral oncogene homolog B1 (BRAF).";
RL J. Biol. Chem. 287:24017-24025(2012).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-7.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its
CC proteasomal degradation. {ECO:0000269|PubMed:22628551}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
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DR EMBL; AY450390; AAR21083.1; -; mRNA.
DR EMBL; AK074985; BAC11334.1; -; mRNA.
DR EMBL; AK075141; BAC11430.1; -; mRNA.
DR EMBL; AM392566; CAL37444.1; -; mRNA.
DR EMBL; AC013722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073643; AAY14775.1; -; Genomic_DNA.
DR EMBL; BC019355; AAH19355.2; -; mRNA.
DR EMBL; BC032328; AAH32328.2; -; mRNA.
DR EMBL; BC045743; AAH45743.1; -; mRNA.
DR CCDS; CCDS2051.1; -.
DR RefSeq; NP_775918.2; NM_173647.3.
DR AlphaFoldDB; Q8NC42; -.
DR SMR; Q8NC42; -.
DR BioGRID; 129991; 208.
DR IntAct; Q8NC42; 35.
DR MINT; Q8NC42; -.
DR STRING; 9606.ENSP00000295317; -.
DR GlyGen; Q8NC42; 3 sites.
DR iPTMnet; Q8NC42; -.
DR PhosphoSitePlus; Q8NC42; -.
DR BioMuta; RNF149; -.
DR DMDM; 160332298; -.
DR EPD; Q8NC42; -.
DR jPOST; Q8NC42; -.
DR MassIVE; Q8NC42; -.
DR MaxQB; Q8NC42; -.
DR PaxDb; Q8NC42; -.
DR PeptideAtlas; Q8NC42; -.
DR PRIDE; Q8NC42; -.
DR ProteomicsDB; 72848; -.
DR Antibodypedia; 2559; 181 antibodies from 23 providers.
DR DNASU; 284996; -.
DR Ensembl; ENST00000295317.4; ENSP00000295317.3; ENSG00000163162.9.
DR GeneID; 284996; -.
DR KEGG; hsa:284996; -.
DR MANE-Select; ENST00000295317.4; ENSP00000295317.3; NM_173647.4; NP_775918.2.
DR UCSC; uc002taz.3; human.
DR CTD; 284996; -.
DR DisGeNET; 284996; -.
DR GeneCards; RNF149; -.
DR HGNC; HGNC:23137; RNF149.
DR HPA; ENSG00000163162; Low tissue specificity.
DR neXtProt; NX_Q8NC42; -.
DR OpenTargets; ENSG00000163162; -.
DR PharmGKB; PA134895641; -.
DR VEuPathDB; HostDB:ENSG00000163162; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000161020; -.
DR HOGENOM; CLU_049885_1_0_1; -.
DR InParanoid; Q8NC42; -.
DR OMA; NEEHYGN; -.
DR PhylomeDB; Q8NC42; -.
DR TreeFam; TF317486; -.
DR PathwayCommons; Q8NC42; -.
DR SignaLink; Q8NC42; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 284996; 10 hits in 1116 CRISPR screens.
DR ChiTaRS; RNF149; human.
DR GenomeRNAi; 284996; -.
DR Pharos; Q8NC42; Tdark.
DR PRO; PR:Q8NC42; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NC42; protein.
DR Bgee; ENSG00000163162; Expressed in blood and 181 other tissues.
DR ExpressionAtlas; Q8NC42; baseline and differential.
DR Genevisible; Q8NC42; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16804; RING-H2_RNF149; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR042712; RNF149_RING-H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..400
FT /note="E3 ubiquitin-protein ligase RNF149"
FT /id="PRO_0000261611"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 67..175
FT /note="PA"
FT ZN_FING 269..310
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 325..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U2C5"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 7
FT /note="E -> K (in a breast cancer sample; somatic mutation;
FT dbSNP:rs763258401)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035958"
FT VARIANT 9
FT /note="S -> G (in dbSNP:rs11123868)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_029455"
FT VARIANT 344
FT /note="L -> F (in dbSNP:rs17856945)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029456"
FT VARIANT 356
FT /note="D -> E (in dbSNP:rs13151)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.1"
FT /id="VAR_029457"
SQ SEQUENCE 400 AA; 43165 MW; DC03309E0E17DCDE CRC64;
MAWRRREASV GARGVLALAL LALALCVPGA RGRALEWFSA VVNIEYVDPQ TNLTVWSVSE
SGRFGDSSPK EGAHGLVGVP WAPGGDLEGC APDTRFFVPE PGGRGAAPWV ALVARGGCTF
KDKVLVAARR NASAVVLYNE ERYGNITLPM SHAGTGNIVV IMISYPKGRE ILELVQKGIP
VTMTIGVGTR HVQEFISGQS VVFVAIAFIT MMIISLAWLI FYYIQRFLYT GSQIGSQSHR
KETKKVIGQL LLHTVKHGEK GIDVDAENCA VCIENFKVKD IIRILPCKHI FHRICIDPWL
LDHRTCPMCK LDVIKALGYW GEPGDVQEMP APESPPGRDP AANLSLALPD DDGSDDSSPP
SASPAESEPQ CDPSFKGDAG ENTALLEAGR SDSRHGGPIS
