RN133_HUMAN
ID RN133_HUMAN Reviewed; 376 AA.
AC Q8WVZ7; A4D0W2; Q8N7G7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=E3 ubiquitin-protein ligase RNF133;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 133;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF133 {ECO:0000305};
GN Name=RNF133;
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=Testis;
RA Guo J.H., Yu L.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Has E3 ubiquitin-protein ligase activity.
CC {ECO:0000250|UniProtKB:Q14B02}.
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: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q14B02}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q14B02}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q14B02}.
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DR EMBL; AF447589; AAM22872.1; -; mRNA.
DR EMBL; AK098524; BAC05321.1; -; mRNA.
DR EMBL; AC006463; AAQ96858.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24341.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83577.1; -; Genomic_DNA.
DR EMBL; BC022038; AAH22038.1; -; mRNA.
DR CCDS; CCDS5784.1; -.
DR RefSeq; NP_631914.1; NM_139175.1.
DR AlphaFoldDB; Q8WVZ7; -.
DR SMR; Q8WVZ7; -.
DR BioGRID; 127962; 26.
DR IntAct; Q8WVZ7; 2.
DR STRING; 9606.ENSP00000344489; -.
DR iPTMnet; Q8WVZ7; -.
DR PhosphoSitePlus; Q8WVZ7; -.
DR BioMuta; RNF133; -.
DR DMDM; 74730905; -.
DR MassIVE; Q8WVZ7; -.
DR PaxDb; Q8WVZ7; -.
DR PeptideAtlas; Q8WVZ7; -.
DR PRIDE; Q8WVZ7; -.
DR Antibodypedia; 2716; 201 antibodies from 24 providers.
DR DNASU; 168433; -.
DR Ensembl; ENST00000340112.3; ENSP00000344489.2; ENSG00000188050.3.
DR GeneID; 168433; -.
DR KEGG; hsa:168433; -.
DR MANE-Select; ENST00000340112.3; ENSP00000344489.2; NM_139175.2; NP_631914.1.
DR UCSC; uc003vkj.2; human.
DR CTD; 168433; -.
DR GeneCards; RNF133; -.
DR HGNC; HGNC:21154; RNF133.
DR HPA; ENSG00000188050; Tissue enriched (testis).
DR neXtProt; NX_Q8WVZ7; -.
DR OpenTargets; ENSG00000188050; -.
DR PharmGKB; PA134991267; -.
DR VEuPathDB; HostDB:ENSG00000188050; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000163928; -.
DR HOGENOM; CLU_049885_1_2_1; -.
DR InParanoid; Q8WVZ7; -.
DR OMA; IIWMNHY; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q8WVZ7; -.
DR TreeFam; TF317486; -.
DR PathwayCommons; Q8WVZ7; -.
DR SignaLink; Q8WVZ7; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 168433; 7 hits in 1106 CRISPR screens.
DR GenomeRNAi; 168433; -.
DR Pharos; Q8WVZ7; Tdark.
DR PRO; PR:Q8WVZ7; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8WVZ7; protein.
DR Bgee; ENSG00000188050; Expressed in sperm and 82 other tissues.
DR Genevisible; Q8WVZ7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
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:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
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 Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..376
FT /note="E3 ubiquitin-protein ligase RNF133"
FT /id="PRO_0000247837"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 65..167
FT /note="PA"
FT ZN_FING 256..297
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 327..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 10
FT /note="R -> G (in Ref. 2; BAC05321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42294 MW; 7C0446D1FB0981F1 CRC64;
MHLLKVGTWR NNTASSWLMK FSVLWLVSQN CCRASVVWMA YMNISFHVGN HVLSELGETG
VFGRSSTLKR VAGVIVPPEG KIQNACNPNT IFSRSKYSET WLALIERGGC TFTQKIKVAT
EKGASGVIIY NVPGTGNQVF PMFHQAFEDV VVVMIGNLKG TEIFHLIKKG VLITAVVEVG
RKHIIWMNHY LVSFVIVTTA TLAYFIFYHI HRLCLARIQN RRWQRLTTDL QNTFGQLQLR
VVKEGDEEIN PNGDSCVICF ERYKPNDIVR ILTCKHFFHK NCIDPWILPH GTCPICKCDI
LKVLGIQVVV ENGTEPLQVL MSNELPETLS PSEEETNNEV SPAGTSDKVI HVEENPTSQN
NDIQPHSVVE DVHPSP
