RMD5B_HUMAN
ID RMD5B_HUMAN Reviewed; 393 AA.
AC Q96G75; Q1HE27; Q6UVY7; Q9H6F6;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=E3 ubiquitin-protein transferase RMND5B;
DE EC=2.3.2.27 {ECO:0000269|PubMed:29911972};
DE AltName: Full=Protein RMD5 homolog B;
GN Name=RMND5B; ORFNames=UNQ2508/PRO5996;
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] (ISOFORM 1).
RA Tang W., Yuan W., Wu X.;
RT "A novel human gene RMND5B.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary cancer;
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=25793641; DOI=10.1371/journal.pone.0120342;
RA Pfirrmann T., Villavicencio-Lorini P., Subudhi A.K., Menssen R., Wolf D.H.,
RA Hollemann T.;
RT "RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early
RT embryonic forebrain development.";
RL PLoS ONE 10:E0120342-E0120342(2015).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE CTLH COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29911972; DOI=10.7554/elife.35528;
RA Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA Picotti P., Stoffel M., Peter M.;
RT "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT the transcription factor Hbp1 for degradation.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase
CC complex that selectively accepts ubiquitin from UBE2H and mediates
CC ubiquitination and subsequent proteasomal degradation of the
CC transcription factor HBP1. MAEA and RMND5A are both required for
CC catalytic activity of the CTLH E3 ubiquitin-protein ligase complex
CC (PubMed:29911972). Catalytic activity of the complex is required for
CC normal cell proliferation (PubMed:29911972). The CTLH E3 ubiquitin-
CC protein ligase complex is not required for the degradation of enzymes
CC involved in gluconeogenesis, such as FBP1 (PubMed:29911972).
CC {ECO:0000269|PubMed:29911972}.
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:0000269|PubMed:29911972};
CC -!- SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9
CC and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC RMND5B), GID8, ARMC8, WDR26 and YPEL5 (PubMed:29911972). Within this
CC complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8,
CC WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4,
CC MKLN1, ARMC8 and YPEL5 have ancillary roles (PubMed:29911972).
CC {ECO:0000269|PubMed:29911972}.
CC -!- INTERACTION:
CC Q96G75; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-745055, EBI-5235340;
CC Q96G75; Q13148: TARDBP; NbExp=3; IntAct=EBI-745055, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25793641}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96G75-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96G75-2; Sequence=VSP_013174;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15303.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ494789; ABF50942.1; -; mRNA.
DR EMBL; AY359092; AAQ89450.1; -; mRNA.
DR EMBL; AK025971; BAB15303.1; ALT_INIT; mRNA.
DR EMBL; AK125337; BAG54186.1; -; mRNA.
DR EMBL; AL713670; CAD28476.1; -; mRNA.
DR EMBL; CH471165; EAW53849.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53850.1; -; Genomic_DNA.
DR EMBL; BC009911; AAH09911.1; -; mRNA.
DR CCDS; CCDS4431.1; -. [Q96G75-1]
DR RefSeq; NP_001275723.1; NM_001288794.1. [Q96G75-1]
DR RefSeq; NP_001275724.1; NM_001288795.1.
DR RefSeq; NP_073599.2; NM_022762.4. [Q96G75-1]
DR RefSeq; XP_005266026.1; XM_005265969.3. [Q96G75-1]
DR RefSeq; XP_005266028.1; XM_005265971.4. [Q96G75-2]
DR RefSeq; XP_005266029.1; XM_005265972.3. [Q96G75-2]
DR RefSeq; XP_016865216.1; XM_017009727.1.
DR RefSeq; XP_016865217.1; XM_017009728.1. [Q96G75-2]
DR AlphaFoldDB; Q96G75; -.
DR SMR; Q96G75; -.
DR BioGRID; 122287; 49.
DR IntAct; Q96G75; 29.
DR MINT; Q96G75; -.
DR STRING; 9606.ENSP00000420875; -.
DR iPTMnet; Q96G75; -.
DR PhosphoSitePlus; Q96G75; -.
DR BioMuta; RMND5B; -.
DR DMDM; 29840869; -.
DR EPD; Q96G75; -.
DR jPOST; Q96G75; -.
DR MassIVE; Q96G75; -.
DR MaxQB; Q96G75; -.
DR PaxDb; Q96G75; -.
DR PeptideAtlas; Q96G75; -.
DR PRIDE; Q96G75; -.
DR ProteomicsDB; 76601; -. [Q96G75-1]
DR ProteomicsDB; 76602; -. [Q96G75-2]
DR Antibodypedia; 46079; 101 antibodies from 23 providers.
DR DNASU; 64777; -.
DR Ensembl; ENST00000313386.9; ENSP00000320623.4; ENSG00000145916.19. [Q96G75-1]
DR Ensembl; ENST00000515098.5; ENSP00000420875.1; ENSG00000145916.19. [Q96G75-1]
DR GeneID; 64777; -.
DR KEGG; hsa:64777; -.
DR MANE-Select; ENST00000313386.9; ENSP00000320623.4; NM_022762.5; NP_073599.2.
DR UCSC; uc003mim.5; human. [Q96G75-1]
DR CTD; 64777; -.
DR DisGeNET; 64777; -.
DR GeneCards; RMND5B; -.
DR HGNC; HGNC:26181; RMND5B.
DR HPA; ENSG00000145916; Low tissue specificity.
DR MalaCards; RMND5B; -.
DR neXtProt; NX_Q96G75; -.
DR OpenTargets; ENSG00000145916; -.
DR PharmGKB; PA144596389; -.
DR VEuPathDB; HostDB:ENSG00000145916; -.
DR eggNOG; KOG2817; Eukaryota.
DR GeneTree; ENSGT00940000153203; -.
DR HOGENOM; CLU_020227_3_1_1; -.
DR InParanoid; Q96G75; -.
DR OMA; KTHEIVH; -.
DR OrthoDB; 987270at2759; -.
DR PhylomeDB; Q96G75; -.
DR TreeFam; TF315176; -.
DR PathwayCommons; Q96G75; -.
DR SignaLink; Q96G75; -.
DR BioGRID-ORCS; 64777; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; RMND5B; human.
DR GeneWiki; RMND5B; -.
DR GenomeRNAi; 64777; -.
DR Pharos; Q96G75; Tbio.
DR PRO; PR:Q96G75; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96G75; protein.
DR Bgee; ENSG00000145916; Expressed in lower esophagus mucosa and 196 other tissues.
DR ExpressionAtlas; Q96G75; baseline and differential.
DR Genevisible; Q96G75; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16795; dRING_RMD5B; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037681; RMD5B_dRING.
DR InterPro; IPR044063; ZF_RING_GID.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR Pfam; PF10607; CLTH; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..393
FT /note="E3 ubiquitin-protein transferase RMND5B"
FT /id="PRO_0000065709"
FT DOMAIN 116..148
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 155..212
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 338..379
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013174"
SQ SEQUENCE 393 AA; 44414 MW; 8C0C3E67996A5502 CRC64;
MEQCACVERE LDKVLQKFLT YGQHCERSLE ELLHYVGQLR AELASAALQG TPLSATLSLV
MSQCCRKIKD TVQKLASDHK DIHSSVSRVG KAIDRNFDSE ICGVVSDAVW DAREQQQQIL
QMAIVEHLYQ QGMLSVAEEL CQESTLNVDL DFKQPFLELN RILEALHEQD LGPALEWAVS
HRQRLLELNS SLEFKLHRLH FIRLLAGGPA KQLEALSYAR HFQPFARLHQ REIQVMMGSL
VYLRLGLEKS PYCHLLDSSH WAEICETFTR DACSLLGLSV ESPLSVSFAS GCVALPVLMN
IKAVIEQRQC TGVWNHKDEL PIEIELGMKC WYHSVFACPI LRQQTSDSNP PIKLICGHVI
SRDALNKLIN GGKLKCPYCP MEQNPADGKR IIF
