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P13473 (LAMP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 158. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosome-associated membrane glycoprotein 2

Short name=LAMP-2
Short name=Lysosome-associated membrane protein 2
Alternative name(s):
CD107 antigen-like family member B
CD_antigen=CD107b
Gene names
Name:LAMP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Implicated in tumor cell metastasis. May function in protection of the lysosomal membrane from autodigestion, maintenance of the acidic environment of the lysosome, adhesion when expressed on the cell surface (plasma membrane), and inter- and intracellular signal transduction. Protects cells from the toxic effects of methylating mutagens. Ref.3

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. Ref.18

Tissue specificity

Isoform LAMP-2A is highly expressed in placenta, lung and liver, less in kidney and pancreas, low in brain and skeletal muscle. Isoform LAMP-2B is highly expressed in skeletal muscle, less in brain, placenta, lung, kidney and pancreas, very low in liver.

Post-translational modification

O- and N-glycosylated; some of the 16 N-linked glycans are polylactosaminoglycans. Ref.14 Ref.15

Involvement in disease

Danon disease (DAND) [MIM:300257]: DAND is a lysosomal glycogen storage disease characterized by the clinical triad of cardiomyopathy, vacuolar myopathy and mental retardation. It is often associated with an accumulation of glycogen in muscle and lysosomes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.22

Sequence similarities

Belongs to the LAMP family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform LAMP-2A (identifier: P13473-1)

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.
Isoform LAMP-2B (identifier: P13473-2)

The sequence of this isoform differs from the canonical sequence as follows:
     367-410: DCSADDDNFL...KHHHAGYEQF → ECSLDDDTIL...RKSYAGYQTL
Isoform LAMP-2C (identifier: P13473-3)

The sequence of this isoform differs from the canonical sequence as follows:
     366-410: QDCSADDDNF...KHHHAGYEQF → EECSADSDLN...RKSRTGYQSV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.1 Ref.11 Ref.12
Chain29 – 410382Lysosome-associated membrane glycoprotein 2
PRO_0000017110

Regions

Topological domain29 – 375347Lumenal Potential
Transmembrane376 – 39924Helical; Potential
Topological domain400 – 41011Cytoplasmic Potential
Region29 – 192164First lumenal domain
Region193 – 22836Hinge
Region229 – 375147Second lumenal domain

Amino acid modifications

Glycosylation321N-linked (GlcNAc...) (polylactosaminoglycan) Ref.13 Ref.16
Glycosylation381N-linked (GlcNAc...) (polylactosaminoglycan) Ref.13 Ref.16
Glycosylation491N-linked (GlcNAc...) Ref.15 Ref.16
Glycosylation581N-linked (GlcNAc...)
Glycosylation751N-linked (GlcNAc...)
Glycosylation1011N-linked (GlcNAc...) Ref.15 Ref.16 Ref.19
Glycosylation1231N-linked (GlcNAc...) Ref.16 Ref.19
Glycosylation1791N-linked (GlcNAc...)
Glycosylation1951O-linked (GalNAc...) Ref.14
Glycosylation1961O-linked (GalNAc...) Ref.14
Glycosylation2001O-linked (GalNAc...) Ref.14
Glycosylation2031O-linked (GalNAc...) Ref.14
Glycosylation2041O-linked (GalNAc...) Ref.14
Glycosylation2071O-linked (GalNAc...); partial Ref.14
Glycosylation2091O-linked (GalNAc...); partial Ref.14
Glycosylation2101O-linked (GalNAc...) Ref.14
Glycosylation2111O-linked (GalNAc...) Ref.14
Glycosylation2131O-linked (GalNAc...); partial
Glycosylation2291N-linked (GlcNAc...)
Glycosylation2421N-linked (GlcNAc...)
Glycosylation2571N-linked (GlcNAc...) Ref.16 Ref.19
Glycosylation2751N-linked (GlcNAc...)
Glycosylation3001N-linked (GlcNAc...)
Glycosylation3071N-linked (GlcNAc...) (polylactosaminoglycan) Ref.13
Glycosylation3171N-linked (GlcNAc...)
Glycosylation3561N-linked (GlcNAc...) Ref.19
Disulfide bond41 ↔ 79 By similarity
Disulfide bond153 ↔ 189 By similarity
Disulfide bond232 ↔ 265 By similarity
Disulfide bond331 ↔ 368 By similarity

Natural variations

Alternative sequence366 – 41045QDCSA…GYEQF → EECSADSDLNFLIPVAVGVA LGFLIIVVFISYMIGRRKSR TGYQSV in isoform LAMP-2C.
VSP_042519
Alternative sequence367 – 41044DCSAD…GYEQF → ECSLDDDTILIPIIVGAGLS GLIIVIVIAYVIGRRKSYAG YQTL in isoform LAMP-2B.
VSP_003044
Natural variant2561P → H.
Corresponds to variant rs1043878 [ dbSNP | Ensembl ].
VAR_011992
Natural variant3211W → R in DAND. Ref.21 Ref.22
VAR_026230

Experimental info

Sequence conflict8 – 136PVPGSG → RFRSGLR Ref.3
Sequence conflict531R → G Ref.3
Sequence conflict681D → V in AAB41647. Ref.2
Sequence conflict1111I → N in AAB41647. Ref.2
Sequence conflict1431I → Y in AAB41647. Ref.2
Sequence conflict2201A → P in AAB41647. Ref.2
Sequence conflict2341L → R in AAB41647. Ref.2
Sequence conflict263 – 2697GSCRSHT → AAAVSH Ref.3
Sequence conflict322 – 3265DAPLG → MPP in AAA60383. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform LAMP-2A [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 9E08E3B62D58F454

FASTA41044,961
        10         20         30         40         50         60 
MVCFRLFPVP GSGLVLVCLV LGAVRSYALE LNLTDSENAT CLYAKWQMNF TVRYETTNKT 

        70         80         90        100        110        120 
YKTVTISDHG TVTYNGSICG DDQNGPKIAV QFGPGFSWIA NFTKAASTYS IDSVSFSYNT 

       130        140        150        160        170        180 
GDNTTFPDAE DKGILTVDEL LAIRIPLNDL FRCNSLSTLE KNDVVQHYWD VLVQAFVQNG 

       190        200        210        220        230        240 
TVSTNEFLCD KDKTSTVAPT IHTTVPSPTT TPTPKEKPEA GTYSVNNGND TCLLATMGLQ 

       250        260        270        280        290        300 
LNITQDKVAS VININPNTTH STGSCRSHTA LLRLNSSTIK YLDFVFAVKN ENRFYLKEVN 

       310        320        330        340        350        360 
ISMYLVNGSV FSIANNNLSY WDAPLGSSYM CNKEQTVSVS GAFQINTFDL RVQPFNVTQG 

       370        380        390        400        410 
KYSTAQDCSA DDDNFLVPIA VGAALAGVLI LVLLAYFIGL KHHHAGYEQF 

« Hide

Isoform LAMP-2B [UniParc].

Checksum: 70B523369D40DEFA
Show »

FASTA41044,956
Isoform LAMP-2C [UniParc].

Checksum: B37AAC83BA1C3B1B
Show »

FASTA41145,170

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] (ISOFORM LAMP-2A), PROTEIN SEQUENCE OF 29-64; 216-223 AND 238-256.
[2]"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] (ISOFORM LAMP-2A).
Tissue: Placenta.
[3]"Molecular and cellular characterization of Mex-/methylation-resistant phenotype. Gene and cDNA cloning, serum dependence, and tumor suppression of transfectant strains."
Fritz G., Dosch J., Thielmann H.W., Kaina B.
J. Biol. Chem. 268:21102-21112(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2B), FUNCTION.
Tissue: Fibroblast.
[4]"Complete cDNA sequence of human lysosome-associated membrane protein-2."
Konecki D.S., Foetisch K., Schlotter M., Lichter-Konecki U.
Biochem. Biophys. Res. Commun. 205:1-5(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2A).
Tissue: Liver.
[5]"An alternatively spliced form of the human lysosome-associated membrane protein-2 gene is expressed in a tissue-specific manner."
Konecki D.S., Foetisch K., Zimmer K.P., Schlotter M., Lichter-Konecki U.
Biochem. Biophys. Res. Commun. 215:757-767(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2B).
[6]"Lamp-2 isoforms play different roles in lysosomal biogenesis."
Zhou D., Blum J.S.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LAMP-2C).
[7]"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. expand/collapse author list , 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 LAMP-2A).
[8]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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 LAMP-2B).
Tissue: Lymph.
[11]"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 29-66.
[12]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-43.
[13]"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.
[14]"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 187-215.
[15]"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-49 AND ASN-101.
[16]"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-32; ASN-38; ASN-49; ASN-101; ASN-123 AND ASN-257.
Tissue: Plasma.
[17]"Unifying nomenclature for the isoforms of the lysosomal membrane protein LAMP-2."
Eskelinen E.L., Cuervo A.M., Taylor M.R., Nishino I., Blum J.S., Dice J.F., Sandoval I.V., Lippincott-Schwartz J., August J.T., Saftig P.
Traffic 6:1058-1061(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[18]"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.
[19]"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-101; ASN-123; ASN-257 AND ASN-356.
Tissue: Liver.
[20]"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].
[21]"Glycogen storage diseases presenting as hypertrophic cardiomyopathy."
Arad M., Maron B.J., Gorham J.M., Johnson W.H. Jr., Saul J.P., Perez-Atayde A.R., Spirito P., Wright G.B., Kanter R.J., Seidman C.E., Seidman J.G.
N. Engl. J. Med. 352:362-372(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DAND ARG-321.
[22]"Asymptomatic hyperCKemia in a case of Danon disease due to a missense mutation in Lamp-2 gene."
Musumeci O., Rodolico C., Nishino I., Di Guardo G., Migliorato A., Aguennouz M., Mazzeo A., Messina C., Vita G., Toscano A.
Neuromuscul. Disord. 15:409-411(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DAND ARG-321.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04183 mRNA. Translation: AAA60383.1.
L09717 expand/collapse EMBL AC list , L09709, L09710, L09711, L09712, L09713, L09714, L09715, L09716 Genomic DNA. Translation: AAB41647.1.
X77196 mRNA. Translation: CAA54416.1.
S79873 mRNA. Translation: AAB35426.1.
U36336 mRNA. Translation: AAA91149.1.
AY561849 mRNA. Translation: AAS67876.1.
AK291090 mRNA. Translation: BAF83779.1.
AC002476 Genomic DNA. Translation: AAB67313.1.
AC002476 Genomic DNA. Translation: AAB67314.1.
CH471107 Genomic DNA. Translation: EAX11881.1.
CH471107 Genomic DNA. Translation: EAX11882.1.
CH471107 Genomic DNA. Translation: EAX11883.1.
CH471107 Genomic DNA. Translation: EAX11884.1.
BC002965 mRNA. Translation: AAH02965.1.
PIRB31959. JC2414.
JC4317.
RefSeqNP_001116078.1. NM_001122606.1.
NP_002285.1. NM_002294.2.
NP_054701.1. NM_013995.2.
UniGeneHs.496684.

3D structure databases

ProteinModelPortalP13473.
SMRP13473. Positions 219-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110114. 38 interactions.
IntActP13473. 12 interactions.
MINTMINT-5003281.
STRING9606.ENSP00000408411.

Protein family/group databases

TCDB9.A.16.1.2. the lysosomal protein import (lpi) family.

PTM databases

PhosphoSiteP13473.
UniCarbKBP13473.

Polymorphism databases

DMDM1708854.

Proteomic databases

PaxDbP13473.
PRIDEP13473.

Protocols and materials databases

DNASU3920.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000200639; ENSP00000200639; ENSG00000005893. [P13473-1]
ENST00000371335; ENSP00000360386; ENSG00000005893. [P13473-2]
ENST00000434600; ENSP00000408411; ENSG00000005893. [P13473-3]
GeneID3920.
KEGGhsa:3920.
UCSCuc004ess.4. human. [P13473-3]
uc004est.4. human. [P13473-1]
uc010nqp.1. human. [P13473-2]

Organism-specific databases

CTD3920.
GeneCardsGC0XM119560.
HGNCHGNC:6501. LAMP2.
HPACAB005272.
HPA029100.
MIM300257. phenotype.
309060. gene.
neXtProtNX_P13473.
Orphanet34587. Glycogen storage disease due to LAMP-2 deficiency.
PharmGKBPA30285.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301998.
HOGENOMHOG000230942.
HOVERGENHBG052303.
KOK06528.
OMAAEECFAD.
OrthoDBEOG7ZD1VH.
PhylomeDBP13473.
TreeFamTF316339.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP13473.
BgeeP13473.
CleanExHS_LAMP2.
GenevestigatorP13473.

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. 1 hit.
PS00311. LAMP_2. 1 hit.
PS51407. LAMP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMP2. human.
GeneWikiLAMP2.
GenomeRNAi3920.
NextBio15399.
PMAP-CutDBP13473.
PROP13473.
SOURCESearch...

Entry information

Entry nameLAMP2_HUMAN
AccessionPrimary (citable) accession number: P13473
Secondary accession number(s): A8K4X5 expand/collapse secondary AC list , D3DTF0, Q16641, Q6Q3G8, Q96J30, Q99534, Q9UD93
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 158 of the entry and version 2 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 X

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

Human cell differentiation molecules

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