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Reviewed, UniProtKB/Swiss-Prot P11279 (LAMP1_HUMAN)

Last modified June 16, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lysosome-associated membrane glycoprotein 1
      Short name=LAMP-1
Alternative name(s):
    CD107 antigen-like family member A
    CD_antigen=CD107a
Gene names
Name: LAMP1
OrganismHomo sapiens (Human)
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. Note: This protein shuttles between lysosomes, endosomes, and the plasma membrane.

Post-translational modification

O- and N-glycosylated; some of the 18 N-linked glycans are polylactosaminoglycans. Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the LAMP family.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Lysosome
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentendosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to plasma membrane

Traceable author statement. Source: ProtInc

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane fraction

Traceable author statement. Source: ProtInc

Complete GO annotation...

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 – 40523 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.11 Ref.9
Glycosylation761N-linked (GlcNAc...) Ref.9
Glycosylation841N-linked (GlcNAc...)
Glycosylation1031N-linked (GlcNAc...) Ref.11 Ref.12
Glycosylation1071N-linked (GlcNAc...)
Glycosylation1211N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9
Glycosylation1301N-linked (GlcNAc...) (polylactosaminoglycan) Ref.9
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
Glycosylation2611N-linked (GlcNAc...) Ref.9
Glycosylation2931N-linked (GlcNAc...)
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: dbSNP rs9577230.
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
P11279-1 [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: 3198605] [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: 15057823] [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: 15489334] [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: 2912382] [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: 3131762] [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: 8517882] [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: 2584229] [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: 2243102] [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: 8323299] [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: 12754519] [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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103 AND ASN-249, MASS SPECTROMETRY.
Tissue: Plasma.
[13]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]"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: 19159218] [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, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
L08582 expand/collapse EMBL AC list , L08576, L08577, L08578, L08579, L08580, L08581 Genomic DNA. Translation: AAF66141.1.
IPIIPI00884105.
PIRA31959.
RefSeqNP_005552.3.
UniGeneHs.494419

3D structure databases

ModBaseSearch...

PTM databases

GlycoSuiteDBP11279.
PhosphoSiteP11279.

Proteomic databases

PRIDEP11279.

Genome annotation databases

EnsemblENSG00000185896. Homo sapiens. [Contig view]
GeneID3916.
KEGGhsa:3916.

Organism-specific databases

GeneCardsGC13P112999.
H-InvDBHIX0011475.
HGNCHGNC:6499. LAMP1.
HPAHPA014750.
MIM153330. gene.
PharmGKBPA30283.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP11279.
OMAP11279. ENNMLIP.

Gene expression databases

ArrayExpressP11279.
BgeeP11279.
CleanExHS_LAMP1.
GermOnlineENSG00000185896. Homo sapiens.

Family and domain databases

InterProIPR002000. Lamp.
IPR018133. LAMP/LAMP-like_membrane.
IPR018134. LAMP_CS.
[Graphical view]
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 Resources

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: June 16, 2009
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human cell differentiation molecules

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

Human chromosome 13

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents