ID RNF13_HUMAN Reviewed; 381 AA. AC O43567; A6NC87; B3KR12; Q05D66; Q6IBJ9; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 13-FEB-2019, entry version 145. DE RecName: Full=E3 ubiquitin-protein ligase RNF13; DE EC=2.3.2.27; DE AltName: Full=RING finger protein 13; DE AltName: Full=RING-type E3 ubiquitin transferase RNF13 {ECO:0000305}; DE Flags: Precursor; GN Name=RNF13; Synonyms=RZF; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Lomax M.I., Warner S.J., Bersirli C.G., Gong T.-W.L.; RT "The gene for a RING zinc finger protein is expressed in the inner RT chick ear after noise exposure."; RL Prim. Sens. Neuron 2:305-316(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, Glial tumor, and Spleen; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [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]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Skeletal muscle, and Urinary bladder; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Placenta; RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x; RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., RA Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.; RT "Integral and associated lysosomal membrane proteins."; RL Traffic 8:1676-1686(2007). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AUTOUBIQUITINATION, GLYCOSYLATION AT ASN-88, AND MUTAGENESIS OF RP ASN-43; ASN-88; CYS-258; HIS-260 AND TRP-270. RX PubMed=18794910; DOI=10.1038/cr.2008.285; RA Zhang Q., Meng Y., Zhang L., Chen J., Zhu D.; RT "RNF13: a novel RING-type ubiquitin ligase over-expressed in RT pancreatic cancer."; RL Cell Res. 19:348-357(2009). CC -!- FUNCTION: E3 ubiquitin-protein ligase that may play a role in CC controlling cell proliferation. {ECO:0000269|PubMed:18794910}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- CC cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor CC protein]-L-lysine.; EC=2.3.2.27; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- INTERACTION: CC P61088:UBE2N; NbExp=2; IntAct=EBI-2129183, EBI-1052908; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Golgi CC apparatus membrane. Late endosome membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}. Lysosome membrane. Nucleus CC inner membrane {ECO:0000250}. Note=Under certain conditions, CC relocalizes to recycling endosomes and to the inner nuclear CC membrane. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O43567-1; Sequence=Displayed; CC Name=2; CC IsoId=O43567-2; Sequence=VSP_055430, VSP_055431; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). In normal CC pancreas, expressed in islets, but not in ducts, nor in acini (at CC protein level). {ECO:0000269|PubMed:18794910}. CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase CC activity. CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:18794910}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH17878.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF037204; AAC03769.1; -; mRNA. DR EMBL; AF070558; AAC28641.1; -; mRNA. DR EMBL; AK313304; BAG36109.1; -; mRNA. DR EMBL; AK090638; BAG52202.1; -; mRNA. DR EMBL; AK090771; BAG52224.1; -; mRNA. DR EMBL; CR456804; CAG33085.1; -; mRNA. DR EMBL; AC069216; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC117395; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78858.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78859.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78860.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78861.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78862.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78863.1; -; Genomic_DNA. DR EMBL; BC009803; AAH09803.1; -; mRNA. DR EMBL; BC009781; AAH09781.1; -; mRNA. DR EMBL; BC017878; AAH17878.1; ALT_SEQ; mRNA. DR CCDS; CCDS3146.1; -. [O43567-1] DR CCDS; CCDS87154.1; -. [O43567-2] DR RefSeq; NP_009213.1; NM_007282.4. [O43567-1] DR RefSeq; NP_899237.1; NM_183381.2. [O43567-1] DR RefSeq; XP_005247149.1; XM_005247092.3. [O43567-2] DR RefSeq; XP_011510675.1; XM_011512373.2. [O43567-1] DR RefSeq; XP_011510676.1; XM_011512374.2. [O43567-1] DR RefSeq; XP_011510678.1; XM_011512376.2. [O43567-2] DR RefSeq; XP_016861143.1; XM_017005654.1. [O43567-1] DR RefSeq; XP_016861144.1; XM_017005655.1. [O43567-1] DR RefSeq; XP_016861145.1; XM_017005656.1. [O43567-2] DR RefSeq; XP_016861146.1; XM_017005657.1. [O43567-2] DR RefSeq; XP_016861147.1; XM_017005658.1. [O43567-2] DR RefSeq; XP_016861148.1; XM_017005659.1. DR UniGene; Hs.12333; -. DR ProteinModelPortal; O43567; -. DR SMR; O43567; -. DR BioGrid; 116470; 37. DR IntAct; O43567; 11. DR STRING; 9606.ENSP00000341361; -. DR iPTMnet; O43567; -. DR PhosphoSitePlus; O43567; -. DR BioMuta; RNF13; -. DR EPD; O43567; -. DR jPOST; O43567; -. DR MaxQB; O43567; -. DR PaxDb; O43567; -. DR PeptideAtlas; O43567; -. DR PRIDE; O43567; -. DR ProteomicsDB; 49058; -. DR DNASU; 11342; -. DR Ensembl; ENST00000344229; ENSP00000341361; ENSG00000082996. [O43567-1] DR Ensembl; ENST00000361785; ENSP00000355268; ENSG00000082996. [O43567-2] DR Ensembl; ENST00000392894; ENSP00000376628; ENSG00000082996. [O43567-1] DR GeneID; 11342; -. DR KEGG; hsa:11342; -. DR UCSC; uc003exn.5; human. [O43567-1] DR CTD; 11342; -. DR DisGeNET; 11342; -. DR EuPathDB; HostDB:ENSG00000082996.19; -. DR GeneCards; RNF13; -. DR HGNC; HGNC:10057; RNF13. DR HPA; HPA064784; -. DR MIM; 609247; gene. DR neXtProt; NX_O43567; -. DR OpenTargets; ENSG00000082996; -. DR PharmGKB; PA34422; -. DR eggNOG; KOG4628; Eukaryota. DR eggNOG; ENOG410Z5DF; LUCA. DR GeneTree; ENSGT00940000154942; -. DR HOGENOM; HOG000234362; -. DR HOVERGEN; HBG063762; -. DR InParanoid; O43567; -. DR KO; K15692; -. DR OMA; NYDVCAI; -. DR OrthoDB; 1487241at2759; -. DR PhylomeDB; O43567; -. DR TreeFam; TF317486; -. DR UniPathway; UPA00143; -. DR ChiTaRS; RNF13; human. DR GeneWiki; RNF13; -. DR GenomeRNAi; 11342; -. DR PRO; PR:O43567; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000082996; Expressed in 239 organ(s), highest expression level in corpus callosum. DR ExpressionAtlas; O43567; baseline and differential. DR Genevisible; O43567; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB. 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 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; KW Endosome; Glycoprotein; Golgi apparatus; Lysosome; Membrane; KW Metal-binding; Nucleus; Reference proteome; Signal; Transferase; KW Transmembrane; Transmembrane helix; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT SIGNAL 1 34 {ECO:0000255}. FT CHAIN 35 381 E3 ubiquitin-protein ligase RNF13. FT /FTId=PRO_0000056054. FT TOPO_DOM 35 182 Lumenal. {ECO:0000255}. FT TRANSMEM 183 203 Helical. {ECO:0000255}. FT TOPO_DOM 204 381 Cytoplasmic. {ECO:0000255}. FT DOMAIN 65 160 PA. FT ZN_FING 240 282 RING-type; atypical. FT {ECO:0000255|PROSITE-ProRule:PRU00175}. FT CARBOHYD 88 88 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18794910}. FT VAR_SEQ 1 18 MLLSIGMLMLSATQVYTI -> MLILMTSLAWDPTTVSTV FT (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055430. FT VAR_SEQ 19 137 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055431. FT MUTAGEN 43 43 N->A: No effect on glycosylation. FT {ECO:0000269|PubMed:18794910}. FT MUTAGEN 88 88 N->A: Loss of glycosylation. FT {ECO:0000269|PubMed:18794910}. FT MUTAGEN 258 258 C->A: Complete loss of E3 ligase FT activity; when associated with A-260. FT {ECO:0000269|PubMed:18794910}. FT MUTAGEN 260 260 H->A: Complete loss of E3 ligase FT activity; when associated with A-258. FT {ECO:0000269|PubMed:18794910}. FT MUTAGEN 270 270 W->A: Drastically reduces E3 ligase FT activity. {ECO:0000269|PubMed:18794910}. SQ SEQUENCE 381 AA; 42814 MW; 4600727D0F197653 CRC64; MLLSIGMLML SATQVYTILT VQLFAFLNLL PVEADILAYN FENASQTFDD LPARFGYRLP AEGLKGFLIN SKPENACEPI VPPPVKDNSS GTFIVLIRRL DCNFDIKVLN AQRAGYKAAI VHNVDSDDLI SMGSNDIEVL KKIDIPSVFI GESSANSLKD EFTYEKGGHL ILVPEFSLPL EYYLIPFLII VGICLILIVI FMITKFVQDR HRARRNRLRK DQLKKLPVHK FKKGDEYDVC AICLDEYEDG DKLRILPCSH AYHCKCVDPW LTKTKKTCPV CKQKVVPSQG DSDSDTDSSQ EENEVTEHTP LLRPLASVSA QSFGALSESR SHQNMTESSD YEEDDNEDTD SSDAENEINE HDVVVQLQPN GERDYNIANT V //