Q6UWE0 (LRSM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase LRSAM1
EC=6.3.2.-

Alternative name(s):
Leucine-rich repeat and sterile alpha motif-containing protein 1
Tsg101-associated ligase
Short name=hTAL

Gene names

Name:	LRSAM1
Synonyms:	TAL
ORF Names:	UNQ6496/PRO21356

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with TSG101. Ref.6
Subcellular location	Cytoplasm. Note: Displays a punctuate distribution and localizes to a submembranal ring. Ref.5
Tissue specificity	Highly expressed in adult spinal cord motoneurons as well as in fetal spinal cord and muscle tissue. Ref.11
Domain	The coiled coil domains interact with the SB domain of TSG101. Ref.5 The PTAP motifs mediate the binding to UEV domains. Ref.5
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.11
Sequence similarities	Contains 6 LRR (leucine-rich) repeats. Contains 1 RING-type zinc finger. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Protein transport Transport Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Charcot-Marie-Tooth disease Neuropathy
Domain	Coiled coil Leucine-rich repeat Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of endocytosis Inferred from mutant phenotype Ref.5. Source: UniProtKB non-lytic virus budding Inferred from mutant phenotype Ref.5. Source: UniProtKB protein autoubiquitination Inferred from direct assay Ref.5. Source: UniProtKB protein catabolic process Inferred from mutant phenotype PubMed 18077552. Source: UniProtKB protein polyubiquitination Inferred from direct assay PubMed 18077552. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-dependent endocytosis Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.5PubMed 18077552. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: InterPro membrane part Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay Ref.5PubMed 18077552. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6UWE0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q6UWE0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     474-500: Missing.

Isoform 3 (identifier: Q6UWE0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-420: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 723	723	E3 ubiquitin-protein ligase LRSAM1		PRO_0000055923
Regions
	Repeat	30 – 51	22	LRR 1
	Repeat	56 – 77	22	LRR 2
	Repeat	82 – 103	22	LRR 3
	Repeat	105 – 127	23	LRR 4
	Repeat	128 – 149	22	LRR 5
	Repeat	151 – 172	22	LRR 6
	Domain	569 – 632	64	SAM
	Zinc finger	675 – 710	36	RING-type
	Coiled coil	254 – 380	127	Potential
	Coiled coil	510 – 562	53	Potential
	Motif	649 – 652	4	PTAP motif 1
	Motif	661 – 664	4	PTAP motif 2
Amino acid modifications
	Modified residue	234	1	Phosphoserine Ref.7
	Modified residue	604	1	Phosphoserine Ref.7 Ref.9
Natural variations
	Alternative sequence	1 – 420	420	Missing in isoform 3.		VSP_012660
	Alternative sequence	474 – 500	27	Missing in isoform 2.		VSP_012661
	Natural variant	318	1	N → D. Ref.4 Corresponds to variant rs1539567 [ dbSNP | Ensembl ].		VAR_021051
Experimental info
	Mutagenesis	649 – 664	16	Missing: Abolishes interaction with TSG101. Ref.5
	Mutagenesis	675	1	C → A: Abolishes ubiquitination of TSG101. Ref.5
	Mutagenesis	692	1	H → A: Abolishes ubiquitination of TSG101. Ref.5
	Sequence conflict	385	1	V → F in BAB71119. Ref.2
	Sequence conflict	402	1	I → V in BAC03703. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4A59461C92467BB1	FASTA	723	83,594
	10 20 30 40 50 60 MPLFFRKRKP SEEARKRLEY QMCLAKEAGA DDILDISKCE LSEIPFGAFA TCKVLQKKVL 70 80 90 100 110 120 IVHTNHLTSL LPKSCSLLSL ATIKVLDLHD NQLTALPDDL GQLTALQVLN VERNQLMQLP 130 140 150 160 170 180 RSIGNLTQLQ TLNVKDNKLK ELPDTVGELR SLRTLNISGN EIQRLPQMLA HVRTLEMLSL 190 200 210 220 230 240 DASAMVYPPR EVCGAGTAAI LQFLCKESGL EYYPPSQYLL PILEQDGIEN SRDSPDGPTD 250 260 270 280 290 300 RFSREELEWQ NRFSDYEKRK EQKMLEKLEF ERRLELGQRE HTQLLQQSSS QKDEILQTVK 310 320 330 340 350 360 EEQSRLEQGL SEHQRHLNAE RQRLQEQLKQ TEQNISSRIQ KLLQDNQRQK KSSEILKSLE 370 380 390 400 410 420 NERIRMEQLM SITQEETESL RRRDVASAMQ QMLTESCKNR LIQMAYESQR QNLVQQACSS 430 440 450 460 470 480 MAEMDERFQQ ILSWQQMDQN KAISQILQES AMQKAAFEAL QVKKDLMHRQ IRSQIKLIET 490 500 510 520 530 540 ELLQLTQLEL KRKSLDTESL QEMISEQRWA LSSLLQQLLK EKQQREEELR EILTELEAKS 550 560 570 580 590 600 ETRQENYWLI QYQRLLNQKP LSLKLQEEGM ERQLVALLEE LSAEHYLPIF AHHRLSLDLL 610 620 630 640 650 660 SQMSPGDLAK VGVSEAGLQH EILRRVQELL DAARIQPELK PPMGEVVTPT APQEPPESVR 670 680 690 700 710 720 PSAPPAELEV QASECVVCLE REAQMIFLNC GHVCCCQQCC QPLRTCPLCR QDIAQRLRIY HSS
	Isoform 2 [UniParc]. Checksum: FA5BF4FF6584DBA0	FASTA	696	80,428
	10 20 30 40 50 60 MPLFFRKRKP SEEARKRLEY QMCLAKEAGA DDILDISKCE LSEIPFGAFA TCKVLQKKVL 70 80 90 100 110 120 IVHTNHLTSL LPKSCSLLSL ATIKVLDLHD NQLTALPDDL GQLTALQVLN VERNQLMQLP 130 140 150 160 170 180 RSIGNLTQLQ TLNVKDNKLK ELPDTVGELR SLRTLNISGN EIQRLPQMLA HVRTLEMLSL 190 200 210 220 230 240 DASAMVYPPR EVCGAGTAAI LQFLCKESGL EYYPPSQYLL PILEQDGIEN SRDSPDGPTD 250 260 270 280 290 300 RFSREELEWQ NRFSDYEKRK EQKMLEKLEF ERRLELGQRE HTQLLQQSSS QKDEILQTVK 310 320 330 340 350 360 EEQSRLEQGL SEHQRHLNAE RQRLQEQLKQ TEQNISSRIQ KLLQDNQRQK KSSEILKSLE 370 380 390 400 410 420 NERIRMEQLM SITQEETESL RRRDVASAMQ QMLTESCKNR LIQMAYESQR QNLVQQACSS 430 440 450 460 470 480 MAEMDERFQQ ILSWQQMDQN KAISQILQES AMQKAAFEAL QVKKDLMHRQ IRSQEMISEQ 490 500 510 520 530 540 RWALSSLLQQ LLKEKQQREE ELREILTELE AKSETRQENY WLIQYQRLLN QKPLSLKLQE 550 560 570 580 590 600 EGMERQLVAL LEELSAEHYL PIFAHHRLSL DLLSQMSPGD LAKVGVSEAG LQHEILRRVQ 610 620 630 640 650 660 ELLDAARIQP ELKPPMGEVV TPTAPQEPPE SVRPSAPPAE LEVQASECVV CLEREAQMIF 670 680 690 LNCGHVCCCQ QCCQPLRTCP LCRQDIAQRL RIYHSS
	Isoform 3 [UniParc]. Checksum: A92853EEC27F0B12	FASTA	303	35,069
	10 20 30 40 50 60 MAEMDERFQQ ILSWQQMDQN KAISQILQES AMQKAAFEAL QVKKDLMHRQ IRSQIKLIET 70 80 90 100 110 120 ELLQLTQLEL KRKSLDTESL QEMISEQRWA LSSLLQQLLK EKQQREEELR EILTELEAKS 130 140 150 160 170 180 ETRQENYWLI QYQRLLNQKP LSLKLQEEGM ERQLVALLEE LSAEHYLPIF AHHRLSLDLL 190 200 210 220 230 240 SQMSPGDLAK VGVSEAGLQH EILRRVQELL DAARIQPELK PPMGEVVTPT APQEPPESVR 250 260 270 280 290 300 PSAPPAELEV QASECVVCLE REAQMIFLNC GHVCCCQQCC QPLRTCPLCR QDIAQRLRIY HSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." 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. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Brain and Teratocarcinoma.
[3]	"DNA sequence and analysis of human chromosome 9." 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. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-318. Tissue: Skin.
[5]	"Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding." 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. Genes Dev. 18:1737-1752(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-675; HIS-692 AND 649-PRO--PRO-664.
[6]	"Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery." Carlton J.G., Martin-Serrano J. Science 316:1908-1912(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TSG101.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-604, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Mutation in the gene encoding ubiquitin ligase LRSAM1 in patients with Charcot-Marie-Tooth disease." 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. PLoS Genet. 6:1-7(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CMT2P.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"A frameshift mutation in LRSAM1 is responsible for a dominant hereditary polyneuropathy." 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. Hum. Mol. Genet. 21:358-370(2012) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INVOLVEMENT IN CMT2P.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY358830 mRNA. Translation: AAQ89189.1. AK056203 mRNA. Translation: BAB71119.1. AK056305 mRNA. Translation: BAB71144.1. AK091589 mRNA. Translation: BAC03703.1. AL445222 Genomic DNA. Translation: CAH72930.1. AL445222 Genomic DNA. Translation: CAH72931.1. BC009239 mRNA. Translation: AAH09239.1.
IPI	IPI00289113. IPI00300805. IPI00550437.
RefSeq	NP_001005373.1. NM_001005373.3. NP_001005374.1. NM_001005374.3. NP_001177652.1. NM_001190723.2. NP_612370.3. NM_138361.5.
UniGene	Hs.495188.
3D structure databases
ProteinModelPortal	Q6UWE0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6UWE0. 33 interactions.
MINT	MINT-1377718.
STRING	9606.ENSP00000300417.
PTM databases
PhosphoSite	Q6UWE0.
Polymorphism databases
DMDM	62511890.
Proteomic databases
PaxDb	Q6UWE0.
PRIDE	Q6UWE0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000300417; ENSP00000300417; ENSG00000148356. ENST00000323301; ENSP00000322937; ENSG00000148356. ENST00000373322; ENSP00000362419; ENSG00000148356. ENST00000373324; ENSP00000362421; ENSG00000148356.
GeneID	90678.
KEGG	hsa:90678.
UCSC	uc004brb.2. human. uc004bre.2. human. uc010mxk.2. human.
Organism-specific databases
CTD	90678.
GeneCards	GC09P130215.
HGNC	HGNC:25135. LRSAM1.
HPA	HPA021403. HPA021844.
MIM	610933. gene. 614436. phenotype.
neXtProt	NX_Q6UWE0.
Orphanet	300319. Autosomal dominant Charcot-Marie-Tooth disease type 2P.
PharmGKB	PA134890010.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4886.
HOGENOM	HOG000231972.
HOVERGEN	HBG052363.
InParanoid	Q6UWE0.
KO	K10641.
OMA	FGAFATC.
PhylomeDB	Q6UWE0.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
Bgee	Q6UWE0.
CleanEx	HS_LRSAM1.
Genevestigator	Q6UWE0.
GermOnline	ENSG00000148356. Homo sapiens.
Family and domain databases
Gene3D	1.10.150.50. 1 hit. 3.30.40.10. 1 hit.
InterPro	IPR016179. Insulin-like. IPR001611. Leu-rich_rpt. IPR025875. Leu-rich_rpt_4. IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF12799. LRR_4. 2 hits. PF07647. SAM_2. 1 hit. [Graphical view]
SMART	SM00078. IlGF. 1 hit. SM00184. RING. 1 hit. SM00454. SAM. 1 hit. [Graphical view]
SUPFAM	SSF47769. SAM_homology. 1 hit.
PROSITE	PS51450. LRR. 4 hits. PS50105. SAM_DOMAIN. 1 hit. PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LRSAM1. human.
GenomeRNAi	90678.
NextBio	76927.
SOURCE	Search...

Entry information

Entry name

LRSM1_HUMAN

Accession

Primary (citable) accession number: Q6UWE0
Secondary accession number(s): Q5VVV0 , Q8NB40, Q96GT5, Q96MX5, Q96MZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.