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E3 ubiquitin-protein ligase LRSAM1 (EC 2.3.2.27) (Leucine-rich repeat and sterile alpha motif-containing protein 1) (RING-type E3 ubiquitin transferase LRSAM1) (Tsg101-associated ligase) (hTAL)

 LRSM1_HUMAN             Reviewed;         723 AA.
Q6UWE0; Q5VVV0; Q8NB40; Q96GT5; Q96MX5; Q96MZ7;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 145.
RecName: Full=E3 ubiquitin-protein ligase LRSAM1 {ECO:0000305};
EC=2.3.2.27 {ECO:0000269|PubMed:15256501, ECO:0000269|PubMed:23245322};
AltName: Full=Leucine-rich repeat and sterile alpha motif-containing protein 1 {ECO:0000303|PubMed:20865121};
AltName: Full=RING-type E3 ubiquitin transferase LRSAM1 {ECO:0000305};
AltName: Full=Tsg101-associated ligase {ECO:0000303|PubMed:15256501};
Short=hTAL {ECO:0000303|PubMed:15256501};
Name=LRSAM1 {ECO:0000303|PubMed:20865121};
Synonyms=TAL {ECO:0000303|PubMed:15256501}; ORFNames=UNQ6496/PRO21356;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASP-318.
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF CYS-675;
HIS-692 AND 649-PRO--PRO-664.
PubMed=15256501; DOI=10.1101/gad.294904;
Amit I., Yakir L., Katz M., Zwang Y., Marmor M.D., Citri A.,
Shtiegman K., Alroy I., Tuvia S., Reiss Y., Roubini E., Cohen M.,
Wides R., Bacharach E., Schubert U., Yarden Y.;
"Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor
endocytosis and retrovirus budding.";
Genes Dev. 18:1737-1752(2004).
[6]
INTERACTION WITH TSG101.
PubMed=17556548; DOI=10.1126/science.1143422;
Carlton J.G., Martin-Serrano J.;
"Parallels between cytokinesis and retroviral budding: a role for the
ESCRT machinery.";
Science 316:1908-1912(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-604, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
INVOLVEMENT IN CMT2P.
PubMed=20865121; DOI=10.1371/journal.pgen.1001081;
Guernsey D.L., Jiang H., Bedard K., Evans S.C., Ferguson M.,
Matsuoka M., Macgillivray C., Nightingale M., Perry S., Rideout A.L.,
Orr A., Ludman M., Skidmore D.L., Benstead T., Samuels M.E.;
"Mutation in the gene encoding ubiquitin ligase LRSAM1 in patients
with Charcot-Marie-Tooth disease.";
PLoS Genet. 6:E1001081-E1001081(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23245322; DOI=10.1016/j.chom.2012.10.019;
Huett A., Heath R.J., Begun J., Sassi S.O., Baxt L.A., Vyas J.M.,
Goldberg M.B., Xavier R.J.;
"The LRR and RING domain protein LRSAM1 is an E3 ligase crucial for
ubiquitin-dependent autophagy of intracellular Salmonella
Typhimurium.";
Cell Host Microbe 12:778-790(2012).
[12]
TISSUE SPECIFICITY, AND INVOLVEMENT IN CMT2P.
PubMed=22012984; DOI=10.1093/hmg/ddr471;
Weterman M.A., Sorrentino V., Kasher P.R., Jakobs M.E.,
van Engelen B.G., Fluiter K., de Wissel M.B., Sizarov A., Nurnberg G.,
Nurnberg P., Zelcer N., Schelhaas H.J., Baas F.;
"A frameshift mutation in LRSAM1 is responsible for a dominant
hereditary polyneuropathy.";
Hum. Mol. Genet. 21:358-370(2012).
[13]
INTERACTION WITH PHF23, FUNCTION, AND UBIQUITINATION.
PubMed=25484098; DOI=10.4161/auto.36439;
Wang Z., Hu J., Li G., Qu L., He Q., Lou Y., Song Q., Ma D., Chen Y.;
"PHF23 (plant homeodomain finger protein 23) negatively regulates cell
autophagy by promoting ubiquitination and degradation of E3 ligase
LRSAM1.";
Autophagy 10:2158-2170(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
VARIANT CMT2P ARG-694, CHARACTERIZATION OF VARIANT CMT2P ARG-694,
INTERACTION WITH FUS, AND SUBCELLULAR LOCATION.
PubMed=27615052; DOI=10.1002/ana.24776;
Hu B., Arpag S., Zuchner S., Li J.;
"A novel missense mutation of CMT2P alters transcription machinery.";
Ann. Neurol. 80:834-845(2016).
[16]
VARIANT CMT2P TYR-694, AND CHARACTERIZATION OF VARIANT CMT2P TYR-694.
PubMed=27686364; DOI=10.1002/ana.24775;
Peeters K., Palaima P., Pelayo-Negro A.L., Garcia A., Gallardo E.,
Garcia-Barredo R., Mateiu L., Baets J., Menten B., De Vriendt E.,
De Jonghe P., Timmerman V., Infante J., Berciano J., Jordanova A.;
"Charcot-Marie-Tooth disease type 2G redefined by a novel mutation in
LRSAM1.";
Ann. Neurol. 80:823-833(2016).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates
monoubiquitination of TSG101 at multiple sites, leading to
inactivate the ability of TSG101 to sort endocytic (EGF receptors)
and exocytic (HIV-1 viral proteins) cargos (PubMed:15256501).
Bacterial recognition protein that defends the cytoplasm from
invasive pathogens (PubMed:23245322). Localizes to several
intracellular bacterial pathogens and generates the bacteria-
associated ubiquitin signal leading to autophagy-mediated
intracellular bacteria degradation (xenophagy) (PubMed:23245322,
PubMed:25484098). {ECO:0000269|PubMed:15256501,
ECO:0000269|PubMed:23245322, ECO:0000269|PubMed:25484098}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:15256501,
ECO:0000269|PubMed:23245322}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:15256501, ECO:0000269|PubMed:23245322}.
-!- SUBUNIT: Interacts with TSG101 (PubMed:17556548). Interacts with
PHF23 (PubMed:25484098). Interacts with FUS (PubMed:27615052).
{ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:25484098,
ECO:0000269|PubMed:27615052}.
-!- INTERACTION:
P54274:TERF1; NbExp=2; IntAct=EBI-720984, EBI-710997;
Q99816:TSG101; NbExp=9; IntAct=EBI-720984, EBI-346882;
P61088:UBE2N; NbExp=3; IntAct=EBI-720984, EBI-1052908;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15256501,
ECO:0000269|PubMed:27615052}. Note=Displays a punctuate
distribution and localizes to a submembranal ring
(PubMed:15256501). Localizes to intracellular bacterial pathogens
(PubMed:23245322). {ECO:0000269|PubMed:15256501,
ECO:0000269|PubMed:23245322}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6UWE0-1; Sequence=Displayed;
Name=2;
IsoId=Q6UWE0-2; Sequence=VSP_012661;
Name=3;
IsoId=Q6UWE0-3; Sequence=VSP_012660;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in adult spinal cord
motoneurons as well as in fetal spinal cord and muscle tissue.
{ECO:0000269|PubMed:22012984}.
-!- DOMAIN: The coiled coil domains interact with the SB domain of
TSG101. {ECO:0000269|PubMed:15256501}.
-!- DOMAIN: The PTAP motifs mediate the binding to UEV domains.
{ECO:0000269|PubMed:15256501}.
-!- DOMAIN: The LRR domain is necessary and sufficient for
localization to bacterial targets. {ECO:0000269|PubMed:23245322}.
-!- DOMAIN: The RING domain is required for ubiquitination.
{ECO:0000269|PubMed:23245322}.
-!- PTM: Ubiquitination promoted by PHF23 leads to proteasomal
degradation. {ECO:0000269|PubMed:25484098}.
-!- DISEASE: Charcot-Marie-Tooth disease 2P (CMT2P) [MIM:614436]: An
axonal form of Charcot-Marie-Tooth disease, a disorder of the
peripheral nervous system, characterized by progressive weakness
and atrophy, initially of the peroneal muscles and later of the
distal muscles of the arms. Charcot-Marie-Tooth disease is
classified in two main groups on the basis of electrophysiologic
properties and histopathology: primary peripheral demyelinating
neuropathies (designated CMT1 when they are dominantly inherited)
and primary peripheral axonal neuropathies (CMT2). Neuropathies of
the CMT2 group are characterized by signs of axonal degeneration
in the absence of obvious myelin alterations, normal or slightly
reduced nerve conduction velocities, and progressive distal muscle
weakness and atrophy. Nerve conduction velocities are normal or
slightly reduced. {ECO:0000269|PubMed:20865121,
ECO:0000269|PubMed:22012984, ECO:0000269|PubMed:27615052,
ECO:0000269|PubMed:27686364}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; AY358830; AAQ89189.1; -; mRNA.
EMBL; AK056203; BAB71119.1; -; mRNA.
EMBL; AK056305; BAB71144.1; -; mRNA.
EMBL; AK091589; BAC03703.1; -; mRNA.
EMBL; AL445222; CAH72930.1; -; Genomic_DNA.
EMBL; AL445222; CAH72931.1; -; Genomic_DNA.
EMBL; BC009239; AAH09239.1; -; mRNA.
CCDS; CCDS55347.1; -. [Q6UWE0-2]
CCDS; CCDS6873.1; -. [Q6UWE0-1]
RefSeq; NP_001005373.1; NM_001005373.3. [Q6UWE0-1]
RefSeq; NP_001005374.1; NM_001005374.3. [Q6UWE0-1]
RefSeq; NP_001177652.1; NM_001190723.2. [Q6UWE0-2]
RefSeq; NP_612370.3; NM_138361.5. [Q6UWE0-1]
RefSeq; XP_016870772.1; XM_017015283.1. [Q6UWE0-1]
UniGene; Hs.495188; -.
ProteinModelPortal; Q6UWE0; -.
BioGrid; 124754; 55.
ELM; Q6UWE0; -.
IntAct; Q6UWE0; 39.
MINT; MINT-1377718; -.
STRING; 9606.ENSP00000300417; -.
iPTMnet; Q6UWE0; -.
PhosphoSitePlus; Q6UWE0; -.
BioMuta; LRSAM1; -.
DMDM; 62511890; -.
EPD; Q6UWE0; -.
MaxQB; Q6UWE0; -.
PaxDb; Q6UWE0; -.
PeptideAtlas; Q6UWE0; -.
PRIDE; Q6UWE0; -.
Ensembl; ENST00000300417; ENSP00000300417; ENSG00000148356. [Q6UWE0-1]
Ensembl; ENST00000323301; ENSP00000322937; ENSG00000148356. [Q6UWE0-1]
Ensembl; ENST00000373322; ENSP00000362419; ENSG00000148356. [Q6UWE0-1]
Ensembl; ENST00000373324; ENSP00000362421; ENSG00000148356. [Q6UWE0-2]
GeneID; 90678; -.
KEGG; hsa:90678; -.
UCSC; uc004brb.2; human. [Q6UWE0-1]
CTD; 90678; -.
DisGeNET; 90678; -.
EuPathDB; HostDB:ENSG00000148356.13; -.
GeneCards; LRSAM1; -.
GeneReviews; LRSAM1; -.
HGNC; HGNC:25135; LRSAM1.
HPA; CAB037304; -.
HPA; HPA021403; -.
HPA; HPA021844; -.
MalaCards; LRSAM1; -.
MIM; 610933; gene.
MIM; 614436; phenotype.
neXtProt; NX_Q6UWE0; -.
OpenTargets; ENSG00000148356; -.
Orphanet; 300319; Autosomal dominant Charcot-Marie-Tooth disease type 2P.
PharmGKB; PA134890010; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00900000140805; -.
HOGENOM; HOG000231972; -.
HOVERGEN; HBG052363; -.
InParanoid; Q6UWE0; -.
KO; K10641; -.
OMA; IFLNCGH; -.
OrthoDB; EOG091G02SW; -.
PhylomeDB; Q6UWE0; -.
TreeFam; TF329645; -.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; LRSAM1; human.
GeneWiki; LRSAM1; -.
GenomeRNAi; 90678; -.
PRO; PR:Q6UWE0; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148356; -.
CleanEx; HS_LRSAM1; -.
ExpressionAtlas; Q6UWE0; baseline and differential.
Genevisible; Q6UWE0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0045806; P:negative regulation of endocytosis; IMP:UniProtKB.
GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:GO_Central.
GO; GO:1904417; P:positive regulation of xenophagy; IMP:GO_Central.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0070086; P:ubiquitin-dependent endocytosis; IDA:UniProtKB.
GO; GO:0046755; P:viral budding; IMP:UniProtKB.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR001841; Znf_RING.
Pfam; PF13855; LRR_8; 1.
Pfam; PF07647; SAM_2; 1.
SMART; SM00369; LRR_TYP; 4.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF52058; SSF52058; 1.
PROSITE; PS51450; LRR; 4.
PROSITE; PS50105; SAM_DOMAIN; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Autophagy; Charcot-Marie-Tooth disease;
Coiled coil; Complete proteome; Cytoplasm; Disease mutation;
Leucine-rich repeat; Metal-binding; Neurodegeneration; Neuropathy;
Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
Repeat; Transferase; Transport; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 723 E3 ubiquitin-protein ligase LRSAM1.
/FTId=PRO_0000055923.
REPEAT 30 51 LRR 1.
REPEAT 56 77 LRR 2.
REPEAT 82 103 LRR 3.
REPEAT 105 127 LRR 4.
REPEAT 128 149 LRR 5.
REPEAT 151 172 LRR 6.
DOMAIN 569 632 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
ZN_FING 675 710 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
COILED 254 380 {ECO:0000255}.
COILED 510 562 {ECO:0000255}.
MOTIF 649 652 PTAP motif 1.
MOTIF 661 664 PTAP motif 2.
MOD_RES 234 234 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 420 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_012660.
VAR_SEQ 474 500 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_012661.
VARIANT 318 318 N -> D (in dbSNP:rs1539567).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_021051.
VARIANT 694 694 C -> R (in CMT2P; abolishes interaction
with FUS; dbSNP:rs759312530).
{ECO:0000269|PubMed:27615052}.
/FTId=VAR_077460.
VARIANT 694 694 C -> Y (in CMT2P; unknown pathological
significance).
{ECO:0000269|PubMed:27686364}.
/FTId=VAR_077461.
MUTAGEN 649 664 Missing: Abolishes interaction with
TSG101. {ECO:0000269|PubMed:15256501}.
MUTAGEN 675 675 C->A: Abolishes ubiquitination of TSG101.
{ECO:0000269|PubMed:15256501}.
MUTAGEN 692 692 H->A: Abolishes ubiquitination of TSG101.
{ECO:0000269|PubMed:15256501}.
CONFLICT 385 385 V -> F (in Ref. 2; BAB71119).
{ECO:0000305}.
CONFLICT 402 402 I -> V (in Ref. 2; BAC03703).
{ECO:0000305}.
SEQUENCE 723 AA; 83594 MW; 4A59461C92467BB1 CRC64;
MPLFFRKRKP SEEARKRLEY QMCLAKEAGA DDILDISKCE LSEIPFGAFA TCKVLQKKVL
IVHTNHLTSL LPKSCSLLSL ATIKVLDLHD NQLTALPDDL GQLTALQVLN VERNQLMQLP
RSIGNLTQLQ TLNVKDNKLK ELPDTVGELR SLRTLNISGN EIQRLPQMLA HVRTLEMLSL
DASAMVYPPR EVCGAGTAAI LQFLCKESGL EYYPPSQYLL PILEQDGIEN SRDSPDGPTD
RFSREELEWQ NRFSDYEKRK EQKMLEKLEF ERRLELGQRE HTQLLQQSSS QKDEILQTVK
EEQSRLEQGL SEHQRHLNAE RQRLQEQLKQ TEQNISSRIQ KLLQDNQRQK KSSEILKSLE
NERIRMEQLM SITQEETESL RRRDVASAMQ QMLTESCKNR LIQMAYESQR QNLVQQACSS
MAEMDERFQQ ILSWQQMDQN KAISQILQES AMQKAAFEAL QVKKDLMHRQ IRSQIKLIET
ELLQLTQLEL KRKSLDTESL QEMISEQRWA LSSLLQQLLK EKQQREEELR EILTELEAKS
ETRQENYWLI QYQRLLNQKP LSLKLQEEGM ERQLVALLEE LSAEHYLPIF AHHRLSLDLL
SQMSPGDLAK VGVSEAGLQH EILRRVQELL DAARIQPELK PPMGEVVTPT APQEPPESVR
PSAPPAELEV QASECVVCLE REAQMIFLNC GHVCCCQQCC QPLRTCPLCR QDIAQRLRIY
HSS


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