Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P11279

- LAMP1_HUMAN

UniProt

P11279 - LAMP1_HUMAN

Protein

Lysosome-associated membrane glycoprotein 1

Gene

LAMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (23 Sep 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.

    GO - Molecular functioni

    1. enzyme binding Source: UniProt
    2. protein binding Source: IntAct

    GO - Biological processi

    1. autophagic cell death Source: Ensembl
    2. autophagy Source: Ensembl
    3. establishment of protein localization to organelle Source: UniProt
    4. Golgi to lysosome transport Source: UniProt
    5. granzyme-mediated apoptotic signaling pathway Source: UniProt
    6. positive regulation of natural killer cell degranulation Source: UniProt
    7. positive regulation of natural killer cell mediated cytotoxicity Source: UniProt
    8. protein stabilization Source: UniProt
    9. regulation of organelle transport along microtubule Source: UniProt

    Protein family/group databases

    TCDBi9.A.16.1.1. the lysosomal protein import (lpi) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysosome-associated membrane glycoprotein 1
    Short name:
    LAMP-1
    Short name:
    Lysosome-associated membrane protein 1
    Alternative name(s):
    CD107 antigen-like family member A
    CD_antigen: CD107a
    Gene namesi
    Name:LAMP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:6499. LAMP1.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Late endosome
    Note: This protein shuttles between lysosomes, endosomes, and the plasma membrane. Colocalizes with OSBPL1A at the late endosome.

    GO - Cellular componenti

    1. alveolar lamellar body Source: Ensembl
    2. cytolytic granule Source: Ensembl
    3. cytoplasm Source: MGI
    4. dendrite Source: Ensembl
    5. endosome membrane Source: UniProtKB-SubCell
    6. external side of plasma membrane Source: Ensembl
    7. extracellular vesicular exosome Source: UniProt
    8. integral component of plasma membrane Source: ProtInc
    9. late endosome Source: UniProtKB
    10. lysosomal membrane Source: UniProtKB-SubCell
    11. lysosome Source: UniProtKB
    12. melanosome Source: Ensembl
    13. membrane Source: UniProtKB
    14. multivesicular body Source: Ensembl
    15. neuronal cell body Source: Ensembl
    16. sarcolemma Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Endosome, Lysosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30283.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28282 PublicationsAdd
    BLAST
    Chaini29 – 417389Lysosome-associated membrane glycoprotein 1PRO_0000017104Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi37 – 371N-linked (GlcNAc...)1 Publication
    Disulfide bondi41 ↔ 801 PublicationPROSITE-ProRule annotation
    Glycosylationi45 – 451N-linked (GlcNAc...)1 Publication
    Glycosylationi62 – 621N-linked (GlcNAc...) (polylactosaminoglycan)3 Publications
    Glycosylationi76 – 761N-linked (GlcNAc...)3 Publications
    Glycosylationi84 – 841N-linked (GlcNAc...)2 Publications
    Glycosylationi103 – 1031N-linked (GlcNAc...)4 Publications
    Glycosylationi107 – 1071N-linked (GlcNAc...)1 Publication
    Glycosylationi121 – 1211N-linked (GlcNAc...) (polylactosaminoglycan)2 Publications
    Glycosylationi130 – 1301N-linked (GlcNAc...) (polylactosaminoglycan)2 Publications
    Disulfide bondi155 ↔ 1911 PublicationPROSITE-ProRule annotation
    Glycosylationi165 – 1651N-linked (GlcNAc...)2 Publications
    Glycosylationi181 – 1811N-linked (GlcNAc...)2 Publications
    Glycosylationi197 – 1971O-linked (GalNAc...); partial1 Publication
    Glycosylationi199 – 1991O-linked (GalNAc...)1 Publication
    Glycosylationi200 – 2001O-linked (GalNAc...)1 Publication
    Glycosylationi207 – 2071O-linked (GalNAc...)1 Publication
    Glycosylationi209 – 2091O-linked (GalNAc...)1 Publication
    Glycosylationi211 – 2111O-linked (GalNAc...)1 Publication
    Glycosylationi223 – 2231N-linked (GlcNAc...) (polylactosaminoglycan)1 Publication
    Glycosylationi228 – 2281N-linked (GlcNAc...) (polylactosaminoglycan)1 Publication
    Disulfide bondi231 ↔ 2691 PublicationPROSITE-ProRule annotation
    Glycosylationi241 – 2411N-linked (GlcNAc...)1 Publication
    Glycosylationi249 – 2491N-linked (GlcNAc...)3 Publications
    Glycosylationi261 – 2611N-linked (GlcNAc...)2 Publications
    Glycosylationi293 – 2931N-linked (GlcNAc...)2 Publications
    Glycosylationi322 – 3221N-linked (GlcNAc...)1 Publication
    Disulfide bondi338 ↔ 3751 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    O- and N-glycosylated; some of the 18 N-linked glycans are polylactosaminoglycans.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP11279.
    PaxDbiP11279.
    PRIDEiP11279.

    PTM databases

    PhosphoSiteiP11279.
    UniCarbKBiP11279.

    Expressioni

    Gene expression databases

    ArrayExpressiP11279.
    BgeeiP11279.
    CleanExiHS_LAMP1.
    GenevestigatoriP11279.

    Organism-specific databases

    HPAiCAB004260.
    HPA014750.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RRAGBQ5VZM22EBI-2805407,EBI-993049

    Protein-protein interaction databases

    BioGridi110110. 19 interactions.
    IntActiP11279. 16 interactions.
    MINTiMINT-3007678.
    STRINGi9606.ENSP00000333298.

    Structurei

    3D structure databases

    ProteinModelPortaliP11279.
    SMRiP11279. Positions 216-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 382354LumenalSequence AnalysisAdd
    BLAST
    Topological domaini406 – 41712CytoplasmicPROSITE-ProRule annotationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei383 – 40523HelicalPROSITE-ProRule annotationAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni29 – 194166First lumenal domainAdd
    BLAST
    Regioni195 – 22733HingeAdd
    BLAST
    Regioni228 – 382155Second lumenal domainAdd
    BLAST

    Sequence similaritiesi

    Belongs to the LAMP family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG301998.
    HOGENOMiHOG000230942.
    HOVERGENiHBG052303.
    InParanoidiP11279.
    KOiK06528.
    OMAiENNMLIP.
    OrthoDBiEOG7ZD1VH.
    PhylomeDBiP11279.
    TreeFamiTF316339.

    Family and domain databases

    InterProiIPR018134. LAMP_CS.
    IPR002000. Lysosome-assoc_membr_glycop.
    [Graphical view]
    PANTHERiPTHR11506. PTHR11506. 1 hit.
    PfamiPF01299. Lamp. 1 hit.
    [Graphical view]
    PRINTSiPR00336. LYSASSOCTDMP.
    PROSITEiPS00310. LAMP_1. 2 hits.
    PS00311. LAMP_2. 1 hit.
    PS51407. LAMP_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11279-1) [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

    MAAPGSARRP LLLLLLLLLL GLMHCASAAM FMVKNGNGTA CIMANFSAAF    50
    SVNYDTKSGP KNMTFDLPSD ATVVLNRSSC GKENTSDPSL VIAFGRGHTL 100
    TLNFTRNATR YSVQLMSFVY NLSDTHLFPN ASSKEIKTVE SITDIRADID 150
    KKYRCVSGTQ VHMNNVTVTL HDATIQAYLS NSSFSRGETR CEQDRPSPTT 200
    APPAPPSPSP SPVPKSPSVD KYNVSGTNGT CLLASMGLQL NLTYERKDNT 250
    TVTRLLNINP NKTSASGSCG AHLVTLELHS EGTTVLLFQF GMNASSSRFF 300
    LQGIQLNTIL PDARDPAFKA ANGSLRALQA TVGNSYKCNA EEHVRVTKAF 350
    SVNIFKVWVQ AFKVEGGQFG SVEECLLDEN SMLIPIAVGG ALAGLVLIVL 400
    IAYLVGRKRS HAGYQTI 417
    Length:417
    Mass (Da):44,882
    Last modified:September 23, 2008 - v3
    Checksum:i3E0A285744DD6588
    GO
    Isoform 2 (identifier: P11279-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         135-187: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:364
    Mass (Da):38,986
    Checksum:iD61B19312DC62CF1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → M in AAA60382. (PubMed:3198605)Curated
    Sequence conflicti5 – 51G → R in AAA60382. (PubMed:3198605)Curated
    Sequence conflicti16 – 2611LLLLLGLMHCA → PVAAARPHALS in AAA60382. (PubMed:3198605)CuratedAdd
    BLAST
    Sequence conflicti33 – 408VKNGNGTA → MARGGRVR in AAA59524. (PubMed:3131762)Curated
    Sequence conflicti262 – 2621K → T in AAF66141. (PubMed:8517882)Curated
    Sequence conflicti377 – 3771Missing in AAF66141. (PubMed:8517882)Curated
    Sequence conflicti382 – 3821M → T in AAA60382. (PubMed:3198605)Curated
    Sequence conflicti382 – 3821M → T in AAA59524. (PubMed:3131762)Curated
    Sequence conflicti382 – 3821M → T in AAF66141. (PubMed:8517882)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti309 – 3091I → T.
    Corresponds to variant rs9577230 [ dbSNP | Ensembl ].
    VAR_046450

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei135 – 18753Missing in isoform 2. 1 PublicationVSP_056032Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04182 mRNA. Translation: AAA60382.1.
    AK301584 mRNA. Translation: BAG63075.1.
    AL136221 Genomic DNA. Translation: CAI13797.1.
    CH471085 Genomic DNA. Translation: EAX09202.1.
    BC006345 mRNA. Translation: AAH06345.2.
    BC007845 mRNA. Translation: AAH07845.2.
    BC021288 mRNA. Translation: AAH21288.1.
    BC093044 mRNA. Translation: AAH93044.1.
    J03263 mRNA. Translation: AAA59524.1.
    AH003113 Genomic DNA. Translation: AAF66141.1.
    CCDSiCCDS41909.1.
    PIRiA31959.
    RefSeqiNP_005552.3. NM_005561.3.
    UniGeneiHs.494419.

    Genome annotation databases

    EnsembliENST00000332556; ENSP00000333298; ENSG00000185896.
    ENST00000397181; ENSP00000415354; ENSG00000185896.
    GeneIDi3916.
    KEGGihsa:3916.
    UCSCiuc001vtm.1. human.

    Polymorphism databases

    DMDMi206729915.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04182 mRNA. Translation: AAA60382.1 .
    AK301584 mRNA. Translation: BAG63075.1 .
    AL136221 Genomic DNA. Translation: CAI13797.1 .
    CH471085 Genomic DNA. Translation: EAX09202.1 .
    BC006345 mRNA. Translation: AAH06345.2 .
    BC007845 mRNA. Translation: AAH07845.2 .
    BC021288 mRNA. Translation: AAH21288.1 .
    BC093044 mRNA. Translation: AAH93044.1 .
    J03263 mRNA. Translation: AAA59524.1 .
    AH003113 Genomic DNA. Translation: AAF66141.1 .
    CCDSi CCDS41909.1.
    PIRi A31959.
    RefSeqi NP_005552.3. NM_005561.3.
    UniGenei Hs.494419.

    3D structure databases

    ProteinModelPortali P11279.
    SMRi P11279. Positions 216-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110110. 19 interactions.
    IntActi P11279. 16 interactions.
    MINTi MINT-3007678.
    STRINGi 9606.ENSP00000333298.

    Protein family/group databases

    TCDBi 9.A.16.1.1. the lysosomal protein import (lpi) family.

    PTM databases

    PhosphoSitei P11279.
    UniCarbKBi P11279.

    Polymorphism databases

    DMDMi 206729915.

    Proteomic databases

    MaxQBi P11279.
    PaxDbi P11279.
    PRIDEi P11279.

    Protocols and materials databases

    DNASUi 3916.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332556 ; ENSP00000333298 ; ENSG00000185896 .
    ENST00000397181 ; ENSP00000415354 ; ENSG00000185896 .
    GeneIDi 3916.
    KEGGi hsa:3916.
    UCSCi uc001vtm.1. human.

    Organism-specific databases

    CTDi 3916.
    GeneCardsi GC13P113951.
    H-InvDB HIX0030831.
    HGNCi HGNC:6499. LAMP1.
    HPAi CAB004260.
    HPA014750.
    MIMi 153330. gene.
    neXtProti NX_P11279.
    PharmGKBi PA30283.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301998.
    HOGENOMi HOG000230942.
    HOVERGENi HBG052303.
    InParanoidi P11279.
    KOi K06528.
    OMAi ENNMLIP.
    OrthoDBi EOG7ZD1VH.
    PhylomeDBi P11279.
    TreeFami TF316339.

    Miscellaneous databases

    ChiTaRSi Lamp1. human.
    GeneWikii LAMP1.
    GenomeRNAii 3916.
    NextBioi 15385.
    PROi P11279.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11279.
    Bgeei P11279.
    CleanExi HS_LAMP1.
    Genevestigatori P11279.

    Family and domain databases

    InterProi IPR018134. LAMP_CS.
    IPR002000. Lysosome-assoc_membr_glycop.
    [Graphical view ]
    PANTHERi PTHR11506. PTHR11506. 1 hit.
    Pfami PF01299. Lamp. 1 hit.
    [Graphical view ]
    PRINTSi PR00336. LYSASSOCTDMP.
    PROSITEi PS00310. LAMP_1. 2 hits.
    PS00311. LAMP_2. 1 hit.
    PS51407. LAMP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences."
      Fukuda M., Viitala J., Matteson J., Carlsson S.R.
      J. Biol. Chem. 263:18920-18928(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 29-51; 117-131 AND 164-198.
    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] (ISOFORM 2).
      Tissue: Mammary gland.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
      Tissue: Brain, Pancreas and Testis.
    6. "Purification and characterization of human lysosomal membrane glycoproteins."
      Mane S.M., Marzella L., Bainton D.F., Holt V.K., Cha Y., Hildreth J.E.K., August J.T.
      Arch. Biochem. Biophys. 268:360-378(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-59.
    7. "Molecular cloning of cDNAs encoding lamp A, a human lysosomal membrane glycoprotein with apparent Mr approximately equal to 120,000."
      Viitala J., Carlsson S.R., Siebert P.D., Fukuda M.
      Proc. Natl. Acad. Sci. U.S.A. 85:3743-3747(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-417 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    8. "The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-2. 5'-flanking sequence of lamp-2 gene and comparison of exon organization in two genes."
      Sawada R., Jardine K.A., Fukuda M.
      J. Biol. Chem. 268:9014-9022(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-417.
      Tissue: Placenta.
    9. "Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement."
      Carlsson S.R., Fukuda M.
      J. Biol. Chem. 264:20526-20531(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    10. "The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones."
      Carlsson S.R., Fukuda M.
      J. Biol. Chem. 265:20488-20495(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYLACTOSAMINOGLYCANS.
    11. "Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2."
      Carlsson S.R., Lycksell P.-O., Fukuda M.
      Arch. Biochem. Biophys. 304:65-73(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION OF HINGE REGION, PROTEIN SEQUENCE OF 191-215.
    12. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-62 AND ASN-103.
    13. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103 AND ASN-249.
      Tissue: Plasma.
    14. "The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments."
      Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.
      Mol. Biol. Cell 16:5480-5492(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Placenta.
    16. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-62; ASN-76; ASN-84; ASN-103; ASN-121; ASN-130; ASN-249 AND ASN-293.
      Tissue: Liver.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLAMP1_HUMAN
    AccessioniPrimary (citable) accession number: P11279
    Secondary accession number(s): B4DWL3
    , Q8WU33, Q96I40, Q9BRD2, Q9NP13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3