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Q6UWE0

- LRSM1_HUMAN

UniProt

Q6UWE0 - LRSM1_HUMAN

Protein

E3 ubiquitin-protein ligase LRSAM1

Gene

LRSAM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri675 – 71036RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. negative regulation of endocytosis Source: UniProtKB
    3. protein autoubiquitination Source: UniProtKB
    4. protein catabolic process Source: UniProtKB
    5. protein polyubiquitination Source: UniProtKB
    6. ubiquitin-dependent endocytosis Source: UniProtKB
    7. viral budding Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Protein transport, Transport, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:LRSAM1
    Synonyms:TAL
    ORF Names:UNQ6496/PRO21356
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:25135. LRSAM1.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Displays a punctuate distribution and localizes to a submembranal ring.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular region Source: InterPro
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi649 – 66416Missing: Abolishes interaction with TSG101. Add
    BLAST
    Mutagenesisi675 – 6751C → A: Abolishes ubiquitination of TSG101. 1 Publication
    Mutagenesisi692 – 6921H → A: Abolishes ubiquitination of TSG101. 1 Publication

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi614436. phenotype.
    Orphaneti300319. Autosomal dominant Charcot-Marie-Tooth disease type 2P.
    PharmGKBiPA134890010.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 723723E3 ubiquitin-protein ligase LRSAM1PRO_0000055923Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei234 – 2341Phosphoserine1 Publication
    Modified residuei604 – 6041Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6UWE0.
    PaxDbiQ6UWE0.
    PRIDEiQ6UWE0.

    PTM databases

    PhosphoSiteiQ6UWE0.

    Expressioni

    Tissue specificityi

    Highly expressed in adult spinal cord motoneurons as well as in fetal spinal cord and muscle tissue.1 Publication

    Gene expression databases

    BgeeiQ6UWE0.
    CleanExiHS_LRSAM1.
    GenevestigatoriQ6UWE0.

    Organism-specific databases

    HPAiHPA021403.
    HPA021844.

    Interactioni

    Subunit structurei

    Interacts with TSG101.1 Publication

    Protein-protein interaction databases

    BioGridi124754. 47 interactions.
    IntActiQ6UWE0. 33 interactions.
    MINTiMINT-1377718.
    STRINGi9606.ENSP00000300417.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6UWE0.
    SMRiQ6UWE0. Positions 34-177, 675-720.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati30 – 5122LRR 1Add
    BLAST
    Repeati56 – 7722LRR 2Add
    BLAST
    Repeati82 – 10322LRR 3Add
    BLAST
    Repeati105 – 12723LRR 4Add
    BLAST
    Repeati128 – 14922LRR 5Add
    BLAST
    Repeati151 – 17222LRR 6Add
    BLAST
    Domaini569 – 63264SAMPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili254 – 380127Sequence AnalysisAdd
    BLAST
    Coiled coili510 – 56253Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi649 – 6524PTAP motif 1
    Motifi661 – 6644PTAP motif 2

    Domaini

    The coiled coil domains interact with the SB domain of TSG101.1 Publication
    The PTAP motifs mediate the binding to UEV domains.1 Publication

    Sequence similaritiesi

    Contains 6 LRR (leucine-rich) repeats.Curated
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri675 – 71036RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Leucine-rich repeat, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000231972.
    HOVERGENiHBG052363.
    InParanoidiQ6UWE0.
    KOiK10641.
    OMAiIFLNCGH.
    OrthoDBiEOG77T149.
    PhylomeDBiQ6UWE0.
    TreeFamiTF329645.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR016179. 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]
    PfamiPF12799. LRR_4. 2 hits.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    SMARTiSM00078. IlGF. 1 hit.
    SM00184. RING. 1 hit.
    SM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    PROSITEiPS51450. LRR. 4 hits.
    PS50105. SAM_DOMAIN. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6UWE0-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPLFFRKRKP SEEARKRLEY QMCLAKEAGA DDILDISKCE LSEIPFGAFA    50
    TCKVLQKKVL IVHTNHLTSL LPKSCSLLSL ATIKVLDLHD NQLTALPDDL 100
    GQLTALQVLN VERNQLMQLP RSIGNLTQLQ TLNVKDNKLK ELPDTVGELR 150
    SLRTLNISGN EIQRLPQMLA HVRTLEMLSL DASAMVYPPR EVCGAGTAAI 200
    LQFLCKESGL EYYPPSQYLL PILEQDGIEN SRDSPDGPTD RFSREELEWQ 250
    NRFSDYEKRK EQKMLEKLEF ERRLELGQRE HTQLLQQSSS QKDEILQTVK 300
    EEQSRLEQGL SEHQRHLNAE RQRLQEQLKQ TEQNISSRIQ KLLQDNQRQK 350
    KSSEILKSLE NERIRMEQLM SITQEETESL RRRDVASAMQ QMLTESCKNR 400
    LIQMAYESQR QNLVQQACSS MAEMDERFQQ ILSWQQMDQN KAISQILQES 450
    AMQKAAFEAL QVKKDLMHRQ IRSQIKLIET ELLQLTQLEL KRKSLDTESL 500
    QEMISEQRWA LSSLLQQLLK EKQQREEELR EILTELEAKS ETRQENYWLI 550
    QYQRLLNQKP LSLKLQEEGM ERQLVALLEE LSAEHYLPIF AHHRLSLDLL 600
    SQMSPGDLAK VGVSEAGLQH EILRRVQELL DAARIQPELK PPMGEVVTPT 650
    APQEPPESVR PSAPPAELEV QASECVVCLE REAQMIFLNC GHVCCCQQCC 700
    QPLRTCPLCR QDIAQRLRIY HSS 723
    Length:723
    Mass (Da):83,594
    Last modified:July 5, 2004 - v1
    Checksum:i4A59461C92467BB1
    GO
    Isoform 2 (identifier: Q6UWE0-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:696
    Mass (Da):80,428
    Checksum:iFA5BF4FF6584DBA0
    GO
    Isoform 3 (identifier: Q6UWE0-3) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:303
    Mass (Da):35,069
    Checksum:iA92853EEC27F0B12
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti385 – 3851V → F in BAB71119. (PubMed:14702039)Curated
    Sequence conflicti402 – 4021I → V in BAC03703. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti318 – 3181N → D.1 Publication
    Corresponds to variant rs1539567 [ dbSNP | Ensembl ].
    VAR_021051

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 420420Missing in isoform 3. 1 PublicationVSP_012660Add
    BLAST
    Alternative sequencei474 – 50027Missing in isoform 2. 1 PublicationVSP_012661Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS55347.1. [Q6UWE0-2]
    CCDS6873.1. [Q6UWE0-1]
    RefSeqiNP_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]
    UniGeneiHs.495188.

    Genome annotation databases

    EnsembliENST00000300417; ENSP00000300417; ENSG00000148356. [Q6UWE0-1]
    ENST00000323301; ENSP00000322937; ENSG00000148356. [Q6UWE0-1]
    ENST00000373322; ENSP00000362419; ENSG00000148356. [Q6UWE0-1]
    ENST00000373324; ENSP00000362421; ENSG00000148356. [Q6UWE0-2]
    GeneIDi90678.
    KEGGihsa:90678.
    UCSCiuc004brb.2. human. [Q6UWE0-1]
    uc004bre.2. human. [Q6UWE0-3]
    uc010mxk.2. human. [Q6UWE0-2]

    Polymorphism databases

    DMDMi62511890.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS55347.1. [Q6UWE0-2 ]
    CCDS6873.1. [Q6UWE0-1 ]
    RefSeqi NP_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 ]
    UniGenei Hs.495188.

    3D structure databases

    ProteinModelPortali Q6UWE0.
    SMRi Q6UWE0. Positions 34-177, 675-720.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124754. 47 interactions.
    IntActi Q6UWE0. 33 interactions.
    MINTi MINT-1377718.
    STRINGi 9606.ENSP00000300417.

    PTM databases

    PhosphoSitei Q6UWE0.

    Polymorphism databases

    DMDMi 62511890.

    Proteomic databases

    MaxQBi Q6UWE0.
    PaxDbi Q6UWE0.
    PRIDEi Q6UWE0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300417 ; ENSP00000300417 ; ENSG00000148356 . [Q6UWE0-1 ]
    ENST00000323301 ; ENSP00000322937 ; ENSG00000148356 . [Q6UWE0-1 ]
    ENST00000373322 ; ENSP00000362419 ; ENSG00000148356 . [Q6UWE0-1 ]
    ENST00000373324 ; ENSP00000362421 ; ENSG00000148356 . [Q6UWE0-2 ]
    GeneIDi 90678.
    KEGGi hsa:90678.
    UCSCi uc004brb.2. human. [Q6UWE0-1 ]
    uc004bre.2. human. [Q6UWE0-3 ]
    uc010mxk.2. human. [Q6UWE0-2 ]

    Organism-specific databases

    CTDi 90678.
    GeneCardsi GC09P130215.
    GeneReviewsi LRSAM1.
    HGNCi HGNC:25135. LRSAM1.
    HPAi HPA021403.
    HPA021844.
    MIMi 610933. gene.
    614436. phenotype.
    neXtProti NX_Q6UWE0.
    Orphaneti 300319. Autosomal dominant Charcot-Marie-Tooth disease type 2P.
    PharmGKBi PA134890010.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000231972.
    HOVERGENi HBG052363.
    InParanoidi Q6UWE0.
    KOi K10641.
    OMAi IFLNCGH.
    OrthoDBi EOG77T149.
    PhylomeDBi Q6UWE0.
    TreeFami TF329645.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi LRSAM1. human.
    GeneWikii LRSAM1.
    GenomeRNAii 90678.
    NextBioi 76927.
    PROi Q6UWE0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6UWE0.
    CleanExi HS_LRSAM1.
    Genevestigatori Q6UWE0.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    3.30.40.10. 1 hit.
    InterProi 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 ]
    Pfami PF12799. LRR_4. 2 hits.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    SMARTi SM00078. IlGF. 1 hit.
    SM00184. RING. 1 hit.
    SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    PROSITEi PS51450. LRR. 4 hits.
    PS50105. SAM_DOMAIN. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: TISSUE SPECIFICITY, INVOLVEMENT IN CMT2P.

    Entry informationi

    Entry nameiLRSM1_HUMAN
    AccessioniPrimary (citable) accession number: Q6UWE0
    Secondary accession number(s): Q5VVV0
    , Q8NB40, Q96GT5, Q96MX5, Q96MZ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3