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Protein

Lysosome-associated membrane glycoprotein 1

Gene

LAMP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

GO - Biological processi

  • autophagic cell death Source: Ensembl
  • autophagy Source: Ensembl
  • establishment of protein localization to organelle Source: UniProtKB
  • Golgi to lysosome transport Source: UniProtKB
  • granzyme-mediated apoptotic signaling pathway Source: UniProtKB
  • positive regulation of natural killer cell degranulation Source: UniProtKB
  • positive regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of organelle transport along microtubule Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

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 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:6499. LAMP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 382354LumenalSequence AnalysisAdd
BLAST
Transmembranei383 – 40523HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini406 – 41712CytoplasmicPROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

  • alveolar lamellar body Source: Ensembl
  • cytolytic granule Source: Ensembl
  • cytoplasm Source: MGI
  • dendrite Source: Ensembl
  • endosome membrane Source: UniProtKB-SubCell
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • late endosome Source: UniProtKB
  • lysosome Source: UniProtKB
  • melanosome Source: Ensembl
  • membrane Source: UniProtKB
  • multivesicular body Source: Ensembl
  • neuronal cell body Source: Ensembl
  • perinuclear region of cytoplasm Source: AgBase
  • phagolysosome membrane Source: Ensembl
  • plasma membrane Source: UniProtKB
  • sarcolemma Source: Ensembl
  • synaptic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761N → S: Complete loss of interaction with Lassa virus protein GPC. 1 Publication

Organism-specific databases

PharmGKBiPA30283.

Polymorphism and mutation databases

BioMutaiLAMP1.
DMDMi206729915.

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 ↔ 80PROSITE-ProRule annotation1 Publication
Glycosylationi45 – 451N-linked (GlcNAc...)1 Publication
Glycosylationi62 – 621N-linked (GlcNAc...) (polylactosaminoglycan)2 Publications
Glycosylationi76 – 761N-linked (GlcNAc...)2 Publications
Glycosylationi84 – 841N-linked (GlcNAc...)1 Publication
Glycosylationi103 – 1031N-linked (GlcNAc...)3 Publications
Glycosylationi107 – 1071N-linked (GlcNAc...)1 Publication
Glycosylationi121 – 1211N-linked (GlcNAc...) (polylactosaminoglycan)1 Publication
Glycosylationi130 – 1301N-linked (GlcNAc...) (polylactosaminoglycan)1 Publication
Disulfide bondi155 ↔ 191PROSITE-ProRule annotation1 Publication
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 ↔ 269PROSITE-ProRule annotation1 Publication
Glycosylationi241 – 2411N-linked (GlcNAc...)1 Publication
Glycosylationi249 – 2491N-linked (GlcNAc...)2 Publications
Glycosylationi261 – 2611N-linked (GlcNAc...)2 Publications
Glycosylationi293 – 2931N-linked (GlcNAc...)1 Publication
Glycosylationi322 – 3221N-linked (GlcNAc...)1 Publication
Disulfide bondi338 ↔ 375PROSITE-ProRule annotation1 Publication

Post-translational modificationi

O- and N-glycosylated; some of the 18 N-linked glycans are polylactosaminoglycans. The glycosylation of N-76 is essential for Lassa virus entry into cells.5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP11279.
PaxDbiP11279.
PRIDEiP11279.

PTM databases

PhosphoSiteiP11279.
UniCarbKBiP11279.

Expressioni

Gene expression databases

BgeeiP11279.
CleanExiHS_LAMP1.
ExpressionAtlasiP11279. baseline and differential.
GenevisibleiP11279. HS.

Organism-specific databases

HPAiCAB004260.
HPA014750.

Interactioni

Subunit structurei

Interacts with Lassa virus protein GPC; this interaction allows virus entry.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GPCP086694EBI-2805407,EBI-8411266From a different organism.
RRAGBQ5VZM22EBI-2805407,EBI-993049

Protein-protein interaction databases

BioGridi110110. 19 interactions.
IntActiP11279. 17 interactions.
MINTiMINT-3007678.
STRINGi9606.ENSP00000333298.

Structurei

3D structure databases

ProteinModelPortaliP11279.
SMRiP11279. Positions 378-415.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00530000063068.
HOGENOMiHOG000230942.
HOVERGENiHBG052303.
InParanoidiP11279.
KOiK06528.
OMAiNGTACIM.
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. AlignAdd to basket

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

        10         20         30         40         50
MAAPGSARRP LLLLLLLLLL GLMHCASAAM FMVKNGNGTA CIMANFSAAF
60 70 80 90 100
SVNYDTKSGP KNMTFDLPSD ATVVLNRSSC GKENTSDPSL VIAFGRGHTL
110 120 130 140 150
TLNFTRNATR YSVQLMSFVY NLSDTHLFPN ASSKEIKTVE SITDIRADID
160 170 180 190 200
KKYRCVSGTQ VHMNNVTVTL HDATIQAYLS NSSFSRGETR CEQDRPSPTT
210 220 230 240 250
APPAPPSPSP SPVPKSPSVD KYNVSGTNGT CLLASMGLQL NLTYERKDNT
260 270 280 290 300
TVTRLLNINP NKTSASGSCG AHLVTLELHS EGTTVLLFQF GMNASSSRFF
310 320 330 340 350
LQGIQLNTIL PDARDPAFKA ANGSLRALQA TVGNSYKCNA EEHVRVTKAF
360 370 380 390 400
SVNIFKVWVQ AFKVEGGQFG SVEECLLDEN SMLIPIAVGG ALAGLVLIVL
410
IAYLVGRKRS HAGYQTI
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:
EMBLi
GenBanki
DDBJi
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. [P11279-1]
PIRiA31959.
RefSeqiNP_005552.3. NM_005561.3. [P11279-1]
XP_011535797.1. XM_011537495.1. [P11279-2]
UniGeneiHs.494419.

Genome annotation databases

EnsembliENST00000332556; ENSP00000333298; ENSG00000185896.
GeneIDi3916.
KEGGihsa:3916.
UCSCiuc001vtm.1. human. [P11279-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P11279-1]
PIRiA31959.
RefSeqiNP_005552.3. NM_005561.3. [P11279-1]
XP_011535797.1. XM_011537495.1. [P11279-2]
UniGeneiHs.494419.

3D structure databases

ProteinModelPortaliP11279.
SMRiP11279. Positions 378-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110110. 19 interactions.
IntActiP11279. 17 interactions.
MINTiMINT-3007678.
STRINGi9606.ENSP00000333298.

Protein family/group databases

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

PTM databases

PhosphoSiteiP11279.
UniCarbKBiP11279.

Polymorphism and mutation databases

BioMutaiLAMP1.
DMDMi206729915.

Proteomic databases

MaxQBiP11279.
PaxDbiP11279.
PRIDEiP11279.

Protocols and materials databases

DNASUi3916.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332556; ENSP00000333298; ENSG00000185896.
GeneIDi3916.
KEGGihsa:3916.
UCSCiuc001vtm.1. human. [P11279-1]

Organism-specific databases

CTDi3916.
GeneCardsiGC13P113951.
H-InvDBHIX0030831.
HGNCiHGNC:6499. LAMP1.
HPAiCAB004260.
HPA014750.
MIMi153330. gene.
neXtProtiNX_P11279.
PharmGKBiPA30283.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG301998.
GeneTreeiENSGT00530000063068.
HOGENOMiHOG000230942.
HOVERGENiHBG052303.
InParanoidiP11279.
KOiK06528.
OMAiNGTACIM.
OrthoDBiEOG7ZD1VH.
PhylomeDBiP11279.
TreeFamiTF316339.

Miscellaneous databases

ChiTaRSiLAMP1. human.
GeneWikiiLAMP1.
GenomeRNAii3916.
NextBioi15385.
PROiP11279.
SOURCEiSearch...

Gene expression databases

BgeeiP11279.
CleanExiHS_LAMP1.
ExpressionAtlasiP11279. baseline and differential.
GenevisibleiP11279. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. Cited for: INTERACTION WITH LASSA VIRUS PROTEIN GPC, MUTAGENESIS OF ASN-76.

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: July 22, 2015
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.