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Q6UWE0 (LRSM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processProtein transport
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCharcot-Marie-Tooth disease
Neurodegeneration
Neuropathy
   DomainCoiled coil
Leucine-rich repeat
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of endocytosis

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

viral budding

Inferred from mutant phenotype Ref.5. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.5PubMed 18077552. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: InterPro

membrane

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.5PubMed 18077552. Source: UniProtKB

ubiquitin-protein transferase 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 723723E3 ubiquitin-protein ligase LRSAM1
PRO_0000055923

Regions

Repeat30 – 5122LRR 1
Repeat56 – 7722LRR 2
Repeat82 – 10322LRR 3
Repeat105 – 12723LRR 4
Repeat128 – 14922LRR 5
Repeat151 – 17222LRR 6
Domain569 – 63264SAM
Zinc finger675 – 71036RING-type
Coiled coil254 – 380127 Potential
Coiled coil510 – 56253 Potential
Motif649 – 6524PTAP motif 1
Motif661 – 6644PTAP motif 2

Amino acid modifications

Modified residue2341Phosphoserine Ref.7
Modified residue6041Phosphoserine Ref.7 Ref.9

Natural variations

Alternative sequence1 – 420420Missing in isoform 3.
VSP_012660
Alternative sequence474 – 50027Missing in isoform 2.
VSP_012661
Natural variant3181N → D. Ref.4
Corresponds to variant rs1539567 [ dbSNP | Ensembl ].
VAR_021051

Experimental info

Mutagenesis649 – 66416Missing: Abolishes interaction with TSG101. Ref.5
Mutagenesis6751C → A: Abolishes ubiquitination of TSG101. Ref.5
Mutagenesis6921H → A: Abolishes ubiquitination of TSG101. Ref.5
Sequence conflict3851V → F in BAB71119. Ref.2
Sequence conflict4021I → V in BAC03703. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4A59461C92467BB1

FASTA72383,594
        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 

« Hide

Isoform 2 [UniParc].

Checksum: FA5BF4FF6584DBA0
Show »

FASTA69680,428
Isoform 3 [UniParc].

Checksum: A92853EEC27F0B12
Show »

FASTA30335,069

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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:E1001081-E1001081(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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS55347.1. [Q6UWE0-2]
CCDS6873.1. [Q6UWE0-1]
RefSeqNP_001005373.1. NM_001005373.3. [Q6UWE0-1]
NP_001005374.1. NM_001005374.3. [Q6UWE0-1]
NP_001177652.1. NM_001190723.2. [Q6UWE0-2]
NP_612370.3. NM_138361.5. [Q6UWE0-1]
UniGeneHs.495188.

3D structure databases

ProteinModelPortalQ6UWE0.
SMRQ6UWE0. Positions 34-177, 675-720.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124754. 47 interactions.
IntActQ6UWE0. 33 interactions.
MINTMINT-1377718.
STRING9606.ENSP00000300417.

PTM databases

PhosphoSiteQ6UWE0.

Polymorphism databases

DMDM62511890.

Proteomic databases

MaxQBQ6UWE0.
PaxDbQ6UWE0.
PRIDEQ6UWE0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300417; ENSP00000300417; ENSG00000148356. [Q6UWE0-1]
ENST00000323301; ENSP00000322937; ENSG00000148356. [Q6UWE0-1]
ENST00000373322; ENSP00000362419; ENSG00000148356. [Q6UWE0-1]
ENST00000373324; ENSP00000362421; ENSG00000148356. [Q6UWE0-2]
GeneID90678.
KEGGhsa:90678.
UCSCuc004brb.2. human. [Q6UWE0-1]
uc004bre.2. human. [Q6UWE0-3]
uc010mxk.2. human. [Q6UWE0-2]

Organism-specific databases

CTD90678.
GeneCardsGC09P130215.
GeneReviewsLRSAM1.
HGNCHGNC:25135. LRSAM1.
HPAHPA021403.
HPA021844.
MIM610933. gene.
614436. phenotype.
neXtProtNX_Q6UWE0.
Orphanet300319. Autosomal dominant Charcot-Marie-Tooth disease type 2P.
PharmGKBPA134890010.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000231972.
HOVERGENHBG052363.
InParanoidQ6UWE0.
KOK10641.
OMAIFLNCGH.
OrthoDBEOG77T149.
PhylomeDBQ6UWE0.
TreeFamTF329645.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

BgeeQ6UWE0.
CleanExHS_LRSAM1.
GenevestigatorQ6UWE0.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
3.30.40.10. 1 hit.
InterProIPR016179. 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]
PfamPF12799. LRR_4. 2 hits.
PF07647. SAM_2. 1 hit.
[Graphical view]
SMARTSM00078. IlGF. 1 hit.
SM00184. RING. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
PROSITEPS51450. LRR. 4 hits.
PS50105. SAM_DOMAIN. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLRSAM1. human.
GeneWikiLRSAM1.
GenomeRNAi90678.
NextBio76927.
PROQ6UWE0.
SOURCESearch...

Entry information

Entry nameLRSM1_HUMAN
AccessionPrimary (citable) accession number: Q6UWE0
Secondary accession number(s): Q5VVV0 expand/collapse secondary AC list , Q8NB40, Q96GT5, Q96MX5, Q96MZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM