RN180_HUMAN
ID RN180_HUMAN Reviewed; 592 AA.
AC Q86T96; Q0JSU3; Q495A8; Q8NBD1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase RNF180;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 180;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF180 {ECO:0000305};
GN Name=RNF180;
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 2).
RC TISSUE=Cerebellum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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: E3 ubiquitin-protein ligase which promotes polyubiquitination
CC and degradation by the proteasome pathway of ZIC2.
CC {ECO:0000250|UniProtKB:Q3U827}.
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 -!- SUBUNIT: Interacts with ZIC2. {ECO:0000250|UniProtKB:Q3U827}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Nucleus envelope {ECO:0000250|UniProtKB:Q3U827}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86T96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86T96-2; Sequence=VSP_021739, VSP_021740;
CC Name=3;
CC IsoId=Q86T96-3; Sequence=VSP_021738, VSP_021739, VSP_021740;
CC -!- DOMAIN: The RING-type zinc finger domain mediates polyubiquitination of
CC the interacting protein.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD89939.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK090756; BAC03514.1; -; mRNA.
DR EMBL; AL832580; CAD89939.1; ALT_INIT; mRNA.
DR EMBL; BC101277; AAI01278.1; -; mRNA.
DR EMBL; BC101278; AAI01279.1; -; mRNA.
DR EMBL; BC101279; AAI01280.1; -; mRNA.
DR EMBL; BC101397; AAI01398.1; -; mRNA.
DR CCDS; CCDS34169.1; -. [Q86T96-2]
DR CCDS; CCDS47219.1; -. [Q86T96-1]
DR RefSeq; NP_001107033.1; NM_001113561.2. [Q86T96-1]
DR RefSeq; NP_001310220.1; NM_001323291.1. [Q86T96-3]
DR RefSeq; NP_001310221.1; NM_001323292.1.
DR RefSeq; NP_848627.1; NM_178532.4. [Q86T96-2]
DR AlphaFoldDB; Q86T96; -.
DR BioGRID; 130174; 5.
DR STRING; 9606.ENSP00000373752; -.
DR iPTMnet; Q86T96; -.
DR PhosphoSitePlus; Q86T96; -.
DR BioMuta; RNF180; -.
DR DMDM; 118573800; -.
DR MassIVE; Q86T96; -.
DR PaxDb; Q86T96; -.
DR PeptideAtlas; Q86T96; -.
DR PRIDE; Q86T96; -.
DR ProteomicsDB; 69673; -. [Q86T96-1]
DR ProteomicsDB; 69674; -. [Q86T96-2]
DR Antibodypedia; 2028; 129 antibodies from 20 providers.
DR DNASU; 285671; -.
DR Ensembl; ENST00000296615.10; ENSP00000296615.6; ENSG00000164197.12. [Q86T96-2]
DR Ensembl; ENST00000389100.9; ENSP00000373752.4; ENSG00000164197.12. [Q86T96-1]
DR GeneID; 285671; -.
DR KEGG; hsa:285671; -.
DR MANE-Select; ENST00000389100.9; ENSP00000373752.4; NM_001113561.2; NP_001107033.1.
DR UCSC; uc003jth.5; human. [Q86T96-1]
DR CTD; 285671; -.
DR DisGeNET; 285671; -.
DR GeneCards; RNF180; -.
DR HGNC; HGNC:27752; RNF180.
DR HPA; ENSG00000164197; Tissue enhanced (parathyroid).
DR MIM; 616015; gene.
DR neXtProt; NX_Q86T96; -.
DR OpenTargets; ENSG00000164197; -.
DR PharmGKB; PA134980027; -.
DR VEuPathDB; HostDB:ENSG00000164197; -.
DR eggNOG; ENOG502QQJ8; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_039803_0_0_1; -.
DR InParanoid; Q86T96; -.
DR OMA; KNHNQEE; -.
DR OrthoDB; 673463at2759; -.
DR PhylomeDB; Q86T96; -.
DR TreeFam; TF328580; -.
DR PathwayCommons; Q86T96; -.
DR SignaLink; Q86T96; -.
DR SIGNOR; Q86T96; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 285671; 8 hits in 1105 CRISPR screens.
DR ChiTaRS; RNF180; human.
DR GenomeRNAi; 285671; -.
DR Pharos; Q86T96; Tbio.
DR PRO; PR:Q86T96; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86T96; protein.
DR Bgee; ENSG00000164197; Expressed in endothelial cell and 157 other tissues.
DR ExpressionAtlas; Q86T96; baseline and differential.
DR Genevisible; Q86T96; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0042415; P:norepinephrine metabolic process; IBA:GO_Central.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
DR GO; GO:0042428; P:serotonin metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033263; RNF180.
DR InterPro; IPR045790; RNF180_C.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46717; PTHR46717; 1.
DR Pfam; PF19332; RNF180_C; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..592
FT /note="E3 ubiquitin-protein ligase RNF180"
FT /id="PRO_0000261617"
FT TOPO_DOM 1..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..592
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ZN_FING 432..474
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 281..489
FT /note="Interaction with ZIC2"
FT /evidence="ECO:0000250"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U827"
FT VAR_SEQ 78..397
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021738"
FT VAR_SEQ 410..416
FT /note="TLNNEMS -> VSIYLLI (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_021739"
FT VAR_SEQ 417..592
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_021740"
FT CONFLICT 15
FT /note="E -> G (in Ref. 2; CAD89939)"
FT /evidence="ECO:0000305"
FT CONFLICT 18..22
FT /note="SILRC -> GETVFSL (in Ref. 2; CAD89939)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="R -> G (in Ref. 2; CAD89939)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="G -> A (in Ref. 2; CAD89939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 68254 MW; 030AF3FD04ECA57B CRC64;
MKRSKELITK NHSQEETSIL RCWKCRKCIA SSGCFMEYLE NQVIKDKDDS VDAQNICHVW
HMNVEALPEW ISCLIQKAQW TVGKLNCPFC GARLGGFNFV STPKCSCGQL AAVHLSKSRT
DYQPTQAGRL MRPSVKYLSH PRVQSGCDKE ALLTGGGSEN RNHRLLNMAR NNNDPGRLTE
ALCLEVRPTY FEMKNEKLLS KASEPKYQLF VPQLVTGRCA TRAFHRKSHS LDLNISEKLT
LLPTLYEIHS KTTAYSRLNE TQPIDLSGLP LQSSKNSYSF QNPSSFDPSM LLQRFSVAPH
ETQTQRGGEF QCGLEAASVY SDHTNTNNLT FLMDLPSAGR SMPEASDQEE HLSPLDFLHS
ANFSLGSINQ RLNKRERSKL KNLRRKQRRR ERWLQKQGKY SGVGLLDHMT LNNEMSTDED
NEYAEEKDSY ICAVCLDVYF NPYMCYPCHH IFCEPCLRTL AKDNPSSTPC PLCRTIISRV
FFQTELNNAT KTFFTKEYLK IKQSFQKSNS AKWPLPSCRK AFHLFGGFRR HAAPVTRRQF
PHGAHRMDYL HFEDDSRGWW FDMDMVIIYI YSVNWVIGFI VFCFLCYFFF PF
