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P11279

- LAMP1_HUMAN

UniProt

P11279 - LAMP1_HUMAN

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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

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. Golgi to lysosome transport Source: UniProt
  2. autophagic cell death Source: Ensembl
  3. autophagy Source: Ensembl
  4. establishment of protein localization to organelle 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
Complete GO annotation...

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.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 382354Lumenal Reviewed prediction
Add
BLAST
Transmembranei383 – 40523Helical; Reviewed prediction
Add
BLAST
Topological domaini406 – 41712Cytoplasmic Reviewed prediction
Add
BLAST

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: ProtInc
  14. multivesicular body Source: Ensembl
  15. neuronal cell body Source: Ensembl
  16. sarcolemma Source: Ensembl
Complete GO annotation...

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 Publications
Add
BLAST
Chaini29 – 417389Lysosome-associated membrane glycoprotein 1
PRO_0000017104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)
Disulfide bondi41 ↔ 801 Publication
Glycosylationi45 – 451N-linked (GlcNAc...)
Glycosylationi62 – 621N-linked (GlcNAc...) (polylactosaminoglycan)3 Publications
Glycosylationi76 – 761N-linked (GlcNAc...)2 Publications
Glycosylationi84 – 841N-linked (GlcNAc...)1 Publication
Glycosylationi103 – 1031N-linked (GlcNAc...)3 Publications
Glycosylationi107 – 1071N-linked (GlcNAc...)
Glycosylationi121 – 1211N-linked (GlcNAc...) (polylactosaminoglycan)2 Publications
Glycosylationi130 – 1301N-linked (GlcNAc...) (polylactosaminoglycan)2 Publications
Disulfide bondi155 ↔ 1911 Publication
Glycosylationi165 – 1651N-linked (GlcNAc...)1 Publication
Glycosylationi181 – 1811N-linked (GlcNAc...)1 Publication
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 Publication
Glycosylationi241 – 2411N-linked (GlcNAc...)
Glycosylationi249 – 2491N-linked (GlcNAc...)2 Publications
Glycosylationi261 – 2611N-linked (GlcNAc...)1 Publication
Glycosylationi293 – 2931N-linked (GlcNAc...)1 Publication
Glycosylationi322 – 3221N-linked (GlcNAc...)
Disulfide bondi338 ↔ 3751 Publication

Post-translational modificationi

O- and N-glycosylated; some of the 18 N-linked glycans are polylactosaminoglycans.2 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 194166First lumenal domain
Add
BLAST
Regioni195 – 22733Hinge
Add
BLAST
Regioni228 – 382155Second lumenal domain
Add
BLAST

Sequence similaritiesi

Belongs to the LAMP family.

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]

Sequencei

Sequence statusi: Complete.

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

P11279-1 [UniParc]FASTAAdd to Basket

« 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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → M in AAA60382. 1 Publication
Sequence conflicti5 – 51G → R in AAA60382. 1 Publication
Sequence conflicti16 – 2611LLLLLGLMHCA → PVAAARPHALS in AAA60382. 1 Publication
Add
BLAST
Sequence conflicti33 – 408VKNGNGTA → MARGGRVR in AAA59524. 1 Publication
Sequence conflicti262 – 2621K → T in AAF66141. 1 Publication
Sequence conflicti377 – 3771Missing in AAF66141. 1 Publication
Sequence conflicti382 – 3821M → T in AAA60382. 1 Publication
Sequence conflicti382 – 3821M → T in AAA59524. 1 Publication
Sequence conflicti382 – 3821M → T in AAF66141. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41909.1.
PIRiA31959.
RefSeqiNP_005552.3. NM_005561.3.
UniGeneiHs.494419.

Genome annotation databases

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

Polymorphism databases

DMDMi206729915.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
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 .
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

« 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], 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLAMP1_HUMAN
AccessioniPrimary (citable) accession number: P11279
Secondary accession number(s): Q8WU33
, Q96I40, Q9BRD2, Q9NP13
Entry historyi
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 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

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