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P11279 (LAMP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LAMP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

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. Ref.13 Ref.14

Post-translational modification

O- and N-glycosylated; some of the 18 N-linked glycans are polylactosaminoglycans. Ref.10 Ref.11

Sequence similarities

Belongs to the LAMP family.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Lysosome
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to lysosome transport

Inferred from mutant phenotype PubMed 23632890. Source: UniProt

autophagic cell death

Inferred from electronic annotation. Source: Ensembl

autophagy

Inferred from electronic annotation. Source: Ensembl

establishment of protein localization to organelle

Inferred from mutant phenotype PubMed 23632890. Source: UniProt

granzyme-mediated apoptotic signaling pathway

Inferred from mutant phenotype PubMed 23632890. Source: UniProt

positive regulation of natural killer cell degranulation

Inferred from mutant phenotype PubMed 23632890. Source: UniProt

positive regulation of natural killer cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 23632890. Source: UniProt

protein stabilization

Inferred from sequence or structural similarity. Source: UniProt

regulation of organelle transport along microtubule

Inferred from mutant phenotype PubMed 23632890. Source: UniProt

   Cellular_componentalveolar lamellar body

Inferred from electronic annotation. Source: Ensembl

cytolytic granule

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 21266579. Source: MGI

dendrite

Inferred from electronic annotation. Source: Ensembl

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of plasma membrane

Traceable author statement PubMed 3174652. Source: ProtInc

late endosome

Inferred from direct assay PubMed 15052268PubMed 15792797. Source: UniProtKB

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from direct assay PubMed 15052268PubMed 15613468. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: Ensembl

membrane

Traceable author statement PubMed 3174652. Source: ProtInc

multivesicular body

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 22641697. Source: UniProt

protein binding

Inferred from physical interaction PubMed 23394946. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RRAGBQ5VZM22EBI-2805407,EBI-993049

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.1 Ref.5
Chain29 – 417389Lysosome-associated membrane glycoprotein 1
PRO_0000017104

Regions

Topological domain29 – 382354Lumenal Potential
Transmembrane383 – 40523Helical; Potential
Topological domain406 – 41712Cytoplasmic Potential
Region29 – 194166First lumenal domain
Region195 – 22733Hinge
Region228 – 382155Second lumenal domain

Amino acid modifications

Glycosylation371N-linked (GlcNAc...)
Glycosylation451N-linked (GlcNAc...)
Glycosylation621N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9 Ref.11 Ref.15
Glycosylation761N-linked (GlcNAc...) Ref.9 Ref.15
Glycosylation841N-linked (GlcNAc...) Ref.15
Glycosylation1031N-linked (GlcNAc...) Ref.11 Ref.12 Ref.15
Glycosylation1071N-linked (GlcNAc...)
Glycosylation1211N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9 Ref.15
Glycosylation1301N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9 Ref.15
Glycosylation1651N-linked (GlcNAc...) Ref.9
Glycosylation1811N-linked (GlcNAc...) Ref.9
Glycosylation1971O-linked (GalNAc...); partial Ref.10
Glycosylation1991O-linked (GalNAc...) Ref.10
Glycosylation2001O-linked (GalNAc...) Ref.10
Glycosylation2071O-linked (GalNAc...) Ref.10
Glycosylation2091O-linked (GalNAc...) Ref.10
Glycosylation2111O-linked (GalNAc...) Ref.10
Glycosylation2231N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9
Glycosylation2281N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9
Glycosylation2411N-linked (GlcNAc...)
Glycosylation2491N-linked (GlcNAc...) Ref.12 Ref.15
Glycosylation2611N-linked (GlcNAc...) Ref.9
Glycosylation2931N-linked (GlcNAc...) Ref.15
Glycosylation3221N-linked (GlcNAc...)
Disulfide bond41 ↔ 80 Ref.8
Disulfide bond155 ↔ 191 Ref.8
Disulfide bond231 ↔ 269 Ref.8
Disulfide bond338 ↔ 375 Ref.8

Natural variations

Natural variant3091I → T.
Corresponds to variant rs9577230 [ dbSNP | Ensembl ].
VAR_046450

Experimental info

Sequence conflict21A → M in AAA60382. Ref.1
Sequence conflict51G → R in AAA60382. Ref.1
Sequence conflict16 – 2611LLLLLGLMHCA → PVAAARPHALS in AAA60382. Ref.1
Sequence conflict33 – 408VKNGNGTA → MARGGRVR in AAA59524. Ref.6
Sequence conflict2621K → T in AAF66141. Ref.7
Sequence conflict3771Missing in AAF66141. Ref.7
Sequence conflict3821M → T in AAA60382. Ref.1
Sequence conflict3821M → T in AAA59524. Ref.6
Sequence conflict3821M → T in AAF66141. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P11279 [UniParc].

Last modified September 23, 2008. Version 3.
Checksum: 3E0A285744DD6588

FASTA41744,882
        10         20         30         40         50         60 
MAAPGSARRP LLLLLLLLLL GLMHCASAAM FMVKNGNGTA CIMANFSAAF SVNYDTKSGP 

        70         80         90        100        110        120 
KNMTFDLPSD ATVVLNRSSC GKENTSDPSL VIAFGRGHTL TLNFTRNATR YSVQLMSFVY 

       130        140        150        160        170        180 
NLSDTHLFPN ASSKEIKTVE SITDIRADID KKYRCVSGTQ VHMNNVTVTL HDATIQAYLS 

       190        200        210        220        230        240 
NSSFSRGETR CEQDRPSPTT APPAPPSPSP SPVPKSPSVD KYNVSGTNGT CLLASMGLQL 

       250        260        270        280        290        300 
NLTYERKDNT TVTRLLNINP NKTSASGSCG AHLVTLELHS EGTTVLLFQF GMNASSSRFF 

       310        320        330        340        350        360 
LQGIQLNTIL PDARDPAFKA ANGSLRALQA TVGNSYKCNA EEHVRVTKAF SVNIFKVWVQ 

       370        380        390        400        410 
AFKVEGGQFG SVEECLLDEN SMLIPIAVGG ALAGLVLIVL IAYLVGRKRS HAGYQTI 

« Hide

References

« Hide 'large scale' references
[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], PROTEIN SEQUENCE OF 29-51; 117-131 AND 164-198.
[2]"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. expand/collapse author list , 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].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Brain, Pancreas and Testis.
[5]"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.
[6]"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, PARTIAL PROTEIN SEQUENCE.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"Integral and associated lysosomal membrane proteins."
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.
Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Placenta.
[15]"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.
[16]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04182 mRNA. Translation: AAA60382.1.
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.
CCDSCCDS41909.1.
PIRA31959.
RefSeqNP_005552.3. NM_005561.3.
UniGeneHs.494419.

3D structure databases

ProteinModelPortalP11279.
SMRP11279. Positions 216-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110110. 19 interactions.
IntActP11279. 16 interactions.
MINTMINT-3007678.
STRING9606.ENSP00000333298.

Protein family/group databases

TCDB9.A.16.1.1. the lysosomal protein import (lpi) family.

PTM databases

PhosphoSiteP11279.
UniCarbKBP11279.

Polymorphism databases

DMDM206729915.

Proteomic databases

MaxQBP11279.
PaxDbP11279.
PRIDEP11279.

Protocols and materials databases

DNASU3916.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332556; ENSP00000333298; ENSG00000185896.
GeneID3916.
KEGGhsa:3916.
UCSCuc001vtm.1. human.

Organism-specific databases

CTD3916.
GeneCardsGC13P113951.
H-InvDBHIX0030831.
HGNCHGNC:6499. LAMP1.
HPACAB004260.
HPA014750.
MIM153330. gene.
neXtProtNX_P11279.
PharmGKBPA30283.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301998.
HOGENOMHOG000230942.
HOVERGENHBG052303.
InParanoidP11279.
KOK06528.
OMAENNMLIP.
OrthoDBEOG7ZD1VH.
PhylomeDBP11279.
TreeFamTF316339.

Gene expression databases

ArrayExpressP11279.
BgeeP11279.
CleanExHS_LAMP1.
GenevestigatorP11279.

Family and domain databases

InterProIPR018134. LAMP_CS.
IPR002000. Lysosome-assoc_membr_glycop.
[Graphical view]
PANTHERPTHR11506. PTHR11506. 1 hit.
PfamPF01299. Lamp. 1 hit.
[Graphical view]
PRINTSPR00336. LYSASSOCTDMP.
PROSITEPS00310. LAMP_1. 2 hits.
PS00311. LAMP_2. 1 hit.
PS51407. LAMP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLamp1. human.
GeneWikiLAMP1.
GenomeRNAi3916.
NextBio15385.
PROP11279.
SOURCESearch...

Entry information

Entry nameLAMP1_HUMAN
AccessionPrimary (citable) accession number: P11279
Secondary accession number(s): Q8WU33 expand/collapse secondary AC list , Q96I40, Q9BRD2, Q9NP13
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 142 of the entry and version 3 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

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 13

Human chromosome 13: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries