MGRN1_MOUSE
ID MGRN1_MOUSE Reviewed; 532 AA.
AC Q9D074; Q3U5V9; Q3UDA1; Q6ZQ97; Q8BZM9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=E3 ubiquitin-protein ligase MGRN1;
DE EC=2.3.2.27;
DE AltName: Full=Mahogunin RING finger protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase MGRN1 {ECO:0000305};
GN Name=Mgrn1; Synonyms=Kiaa0544;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 318-532 (ISOFORM 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Diencephalon, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-532 (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12438443; DOI=10.1172/jci16131;
RA Phan L.K., Lin F., LeDuc C.A., Chung W.K., Leibel R.L.;
RT "The mouse mahoganoid coat color mutation disrupts a novel C3HC4 RING
RT domain protein.";
RL J. Clin. Invest. 110:1449-1459(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, UBIQUITINATION, AND TISSUE SPECIFICITY.
RX PubMed=12560552; DOI=10.1126/science.1079694;
RA He L., Lu X.-Y., Jolly A.F., Eldridge A.G., Watson S.J., Jackson P.K.,
RA Barsh G.S., Gunn T.M.;
RT "Spongiform degeneration in mahoganoid mutant mice.";
RL Science 299:710-712(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-389, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17075880; DOI=10.1002/dvdy.20992;
RA Cota C.D., Bagher P., Pelc P., Smith C.O., Bodner C.R., Gunn T.M.;
RT "Mice with mutations in Mahogunin ring finger-1 (Mgrn1) exhibit abnormal
RT patterning of the left-right axis.";
RL Dev. Dyn. 235:3438-3447(2006).
RN [8]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=17083490; DOI=10.1111/j.1600-0749.2006.00340.x;
RA Bagher P., Jiao J., Owen Smith C., Cota C.D., Gunn T.M.;
RT "Characterization of Mahogunin Ring Finger-1 expression in mice.";
RL Pigment Cell Res. 19:635-643(2006).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=17720281; DOI=10.1016/j.neurobiolaging.2007.07.012;
RA Sun K., Johnson B.S., Gunn T.M.;
RT "Mitochondrial dysfunction precedes neurodegeneration in mahogunin (Mgrn1)
RT mutant mice.";
RL Neurobiol. Aging 28:1840-1852(2007).
RN [10]
RP FUNCTION, INTERACTION WITH TSG101, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 278-CYS--CYS-281 AND 384-PRO--PRO-387.
RX PubMed=19703557; DOI=10.1016/j.bbadis.2009.08.009;
RA Jiao J., Sun K., Walker W.P., Bagher P., Cota C.D., Gunn T.M.;
RT "Abnormal regulation of TSG101 in mice with spongiform neurodegeneration.";
RL Biochim. Biophys. Acta 1792:1027-1035(2009).
RN [11]
RP INTERACTION WITH PRNP, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19524515; DOI=10.1016/j.cell.2009.03.042;
RA Chakrabarti O., Hegde R.S.;
RT "Functional depletion of mahogunin by cytosolically exposed prion protein
RT contributes to neurodegeneration.";
RL Cell 137:1136-1147(2009).
RN [12]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19422019; DOI=10.1002/dvg.20529;
RA Jiao J., Kim H.Y., Liu R.R., Hogan C.A., Sun K., Tam L.M., Gunn T.M.;
RT "Transgenic analysis of the physiological functions of Mahogunin Ring
RT Finger-1 isoforms.";
RL Genesis 47:524-534(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; SER-449 AND SER-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP FUNCTION.
RX PubMed=29290584; DOI=10.1016/j.devcel.2017.12.003;
RA Pusapati G.V., Kong J.H., Patel B.B., Krishnan A., Sagner A., Kinnebrew M.,
RA Briscoe J., Aravind L., Rohatgi R.;
RT "CRISPR screens uncover genes that regulate target cell sensitivity to the
RT morphogen sonic hedgehog.";
RL Dev. Cell 44:113-129(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Mediates TSG101
CC monoubiquitination at multiple sites. Plays a role in the regulation of
CC endosome-to-lysosome trafficking. Impairs MC1R- and MC4R-signaling by
CC competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP
CC production. Does not inhibit ADRB2-signaling. Does not promote MC1R
CC ubiquitination (By similarity). Acts also as a negative regulator of
CC hedgehog signaling (PubMed:29290584). {ECO:0000250,
CC ECO:0000269|PubMed:12560552, ECO:0000269|PubMed:19703557,
CC ECO:0000269|PubMed:29290584}.
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 MC1R and MC4R (By similarity). Interacts with
CC TSG101. Interacts with mislocalized cytosolically exposed PRNP; this
CC interaction alters MGRN1 subcellular location and causes lysosomal
CC enlargement. {ECO:0000250, ECO:0000269|PubMed:19524515,
CC ECO:0000269|PubMed:19703557}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:19422019,
CC ECO:0000269|PubMed:19524515}. Note=The endosomal localization is
CC dependent on the interaction with TSG101. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Cell membrane
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm. Nucleus. Note=In the
CC cytoplasm, predominantly localized to the perinuclear region and
CC discrete vesicular structures. In the nucleus, broadly distributed, but
CC excluded from nucleoli.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=I;
CC IsoId=Q9D074-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D074-2; Sequence=VSP_019854;
CC Name=3; Synonyms=III;
CC IsoId=Q9D074-3; Sequence=VSP_019856;
CC Name=4; Synonyms=II;
CC IsoId=Q9D074-4; Sequence=VSP_019855;
CC Name=5; Synonyms=IV;
CC IsoId=Q9D074-5; Sequence=VSP_019855, VSP_019856;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain,
CC heart, kidney and liver. In the CNS, especially prominent in the
CC Purkinje cells of the cerebellum. In the skin, expressed in the basal
CC layer of the epidermis and hair follicles, primarily in the outer root
CC sheath. Isoforms 1, 3, 4 and 5 are equally expressed in the liver.
CC Isoforms 1, 3 and 4 are most abundant in brain, kidney and heart,
CC respectively. {ECO:0000269|PubMed:12438443,
CC ECO:0000269|PubMed:12560552, ECO:0000269|PubMed:17083490,
CC ECO:0000269|PubMed:19524515}.
CC -!- DEVELOPMENTAL STAGE: In presomite and early somite stage embryos, most
CC strongly expressed in the node and more weakly in the neuroepithelium.
CC In 6- to 12-somite embryos, strongest expression in the node,
CC symmetrically in the floor plate of the neural tube and in the
CC developing heart; weaker expression in paraxial mesoderm, somites,
CC neuroepithelium, as well as in hind- and foregut pockets. By 9.5 dpc,
CC virtually ubiquitous. {ECO:0000269|PubMed:17075880}.
CC -!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
CC -!- PTM: Autoubiquitinated in vitro. {ECO:0000269|PubMed:12560552}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice have a pleiotropic phenotype that
CC includes the absence of yellow hair pigment, curly hair and whiskers,
CC abnormal craniofacial patterning, reduced embryonic viability due to
CC mispatterning of the left-right body axis and age-dependent spongiform
CC neurodegeneration. Many months before onset of vacuolation,
CC mitochondrial complex IV expression and activity is significantly
CC reduced in mutant brains and oxidative stress is increased. A global
CC reduction of ubiquitinated proteins in the brain is observed. At 1
CC month of age, null mutant mouse brains have less ubiquitinated TSG101,
CC while adult mutant brains contain more ubiquitinated and insoluble
CC TSG101 than wild type. At 1 month of age, significant increase in EGFR
CC levels in the brains of null mutant mice relative to wild-type mice,
CC suggesting an impaired trafficking to the lysosome for degradation.
CC {ECO:0000269|PubMed:12560552, ECO:0000269|PubMed:17075880,
CC ECO:0000269|PubMed:17720281, ECO:0000269|PubMed:19422019,
CC ECO:0000269|PubMed:19703557}.
CC -!- MISCELLANEOUS: [Isoform 1]: Sufficient for normal development,
CC pigmentation and neuronal integrity.
CC -!- MISCELLANEOUS: [Isoform 3]: Sufficient for normal development,
CC pigmentation and neuronal integrity. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Partial rescue of the phenotype of mutant
CC null mice. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Unable to rescue the phenotype of mutant
CC null mice. This sequence has been deduced from the description in
CC PubMed:19422019. {ECO:0000305}.
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DR EMBL; AK011747; BAB27816.2; -; mRNA.
DR EMBL; AK034100; BAC28587.1; -; mRNA.
DR EMBL; AK088533; BAC40408.1; -; mRNA.
DR EMBL; AK150176; BAE29360.1; -; mRNA.
DR EMBL; AK153407; BAE31967.1; -; mRNA.
DR EMBL; BC046830; AAH46830.1; -; mRNA.
DR EMBL; AK129161; BAC97971.1; -; mRNA.
DR CCDS; CCDS49751.1; -. [Q9D074-1]
DR CCDS; CCDS57016.1; -. [Q9D074-2]
DR CCDS; CCDS88868.1; -. [Q9D074-4]
DR CCDS; CCDS88869.1; -. [Q9D074-3]
DR RefSeq; NP_001239366.1; NM_001252437.1. [Q9D074-2]
DR RefSeq; NP_083933.1; NM_029657.4. [Q9D074-1]
DR RefSeq; XP_006521895.1; XM_006521832.1.
DR RefSeq; XP_006521897.1; XM_006521834.1.
DR RefSeq; XP_017172376.1; XM_017316887.1.
DR AlphaFoldDB; Q9D074; -.
DR BioGRID; 201365; 4.
DR STRING; 10090.ENSMUSP00000023159; -.
DR iPTMnet; Q9D074; -.
DR PhosphoSitePlus; Q9D074; -.
DR EPD; Q9D074; -.
DR jPOST; Q9D074; -.
DR MaxQB; Q9D074; -.
DR PaxDb; Q9D074; -.
DR PeptideAtlas; Q9D074; -.
DR PRIDE; Q9D074; -.
DR ProteomicsDB; 293471; -. [Q9D074-1]
DR ProteomicsDB; 293472; -. [Q9D074-2]
DR ProteomicsDB; 293473; -. [Q9D074-3]
DR ProteomicsDB; 293474; -. [Q9D074-4]
DR ProteomicsDB; 293475; -. [Q9D074-5]
DR Antibodypedia; 2013; 263 antibodies from 28 providers.
DR DNASU; 17237; -.
DR Ensembl; ENSMUST00000023159; ENSMUSP00000023159; ENSMUSG00000022517. [Q9D074-3]
DR Ensembl; ENSMUST00000070658; ENSMUSP00000068314; ENSMUSG00000022517. [Q9D074-1]
DR Ensembl; ENSMUST00000229038; ENSMUSP00000155034; ENSMUSG00000022517. [Q9D074-2]
DR Ensembl; ENSMUST00000230990; ENSMUSP00000155425; ENSMUSG00000022517. [Q9D074-4]
DR GeneID; 17237; -.
DR KEGG; mmu:17237; -.
DR UCSC; uc007yap.2; mouse. [Q9D074-1]
DR UCSC; uc007yaq.2; mouse. [Q9D074-2]
DR CTD; 23295; -.
DR MGI; MGI:2447670; Mgrn1.
DR VEuPathDB; HostDB:ENSMUSG00000022517; -.
DR eggNOG; KOG4265; Eukaryota.
DR GeneTree; ENSGT00390000009925; -.
DR HOGENOM; CLU_016631_1_1_1; -.
DR InParanoid; Q9D074; -.
DR OMA; CAQSGPP; -.
DR OrthoDB; 883624at2759; -.
DR PhylomeDB; Q9D074; -.
DR TreeFam; TF314969; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 17237; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Mgrn1; mouse.
DR PRO; PR:Q9D074; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D074; protein.
DR Bgee; ENSMUSG00000022517; Expressed in interventricular septum and 233 other tissues.
DR Genevisible; Q9D074; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16789; mRING-HC-C3HC5_MGRN1_like---blasttree; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR045195; MGRN1/RNF157_mRING_C3HC5.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; PTHR22996; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Endosome; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60291"
FT CHAIN 2..532
FT /note="E3 ubiquitin-protein ligase MGRN1"
FT /id="PRO_0000246688"
FT ZN_FING 277..316
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 419..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 384..387
FT /note="Required for TSG101-binding"
FT COMPBIAS 419..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60291"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 29
FT /note="S -> SA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019854"
FT VAR_SEQ 355
FT /note="S -> SCPFKKSKSHPASLASKKPKRET (in isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019855"
FT VAR_SEQ 520..532
FT /note="ALGPESCSVGIEE -> GWSTSMETPHSLGTTSSPWPLLSGSSPEPGVAELT
FT PF (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_019856"
FT MUTAGEN 278..281
FT /note="CVVC->AVVA: Loss of ubiquitin-protein ligase
FT activity. Increase in TSG101-binding."
FT /evidence="ECO:0000269|PubMed:19703557"
FT MUTAGEN 384..387
FT /note="PSAP->ASAA: Loss of TSG101-binding."
FT /evidence="ECO:0000269|PubMed:19703557"
FT CONFLICT 15
FT /note="I -> F (in Ref. 1; BAE29360)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="N -> D (in Ref. 1; BAE29360)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="H -> R (in Ref. 1; BAE29360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 58477 MW; 89C2C1A28F9417EE CRC64;
MGSILSRRIA GVEDIDIQAN SAYRYPPKSG NYFASHFFMG GEKFDTPHPE GYLFGENMDL
NFLGSRPVQF PYVTPAPHEP VKTLRSLVNI RKDSLRLVRY KEDADSPTED GEKPRVLYSL
EFTFDADARV AITIYCQAVE ELVNGVAVYS CKNPSLQSET VHYKRGVSQQ FSLPSFKIDF
SEWKDDELNF DLDRGVFPVV IQAVVDEGDV VEVTGHAHVL LAAFEKHVDG SFSVKPLKQK
QIVDRVSYLL QEIYGIENKN NQETKPSDDE NSDNSSECVV CLSDLRDTLI LPCRHLCLCT
SCADTLRYQA NNCPICRLPF RALLQIRAVR KKPGALSPIS FSPVLAQSVD HDEHSSSDSI
PPGYEPISLL EALNGLRAVS PAIPSAPLYE EITYSGISDG LSQASCPLAG LDRIMESGLQ
KGKTQSKSPD STLRSPSFPI HEEDEEKLSE DSDAPLPPSG VELVLRESSS PESFGTEEGD
EPSLKQGSRV PSIDDVLQDG SPQHHGCSQP VPPADIYLPA LGPESCSVGI EE
