LAMP2_HUMAN - dbPTM
LAMP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LAMP2_HUMAN
UniProt AC P13473
Protein Name Lysosome-associated membrane glycoprotein 2
Gene Name LAMP2
Organism Homo sapiens (Human).
Sequence Length 410
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Endosome membrane
Single-pass type I membrane protein . Lysosome membrane
Single-pass type I membrane protein . Cytoplasmic vesicle, autophagosome membrane . This protein shuttles between lyso
Protein Description Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. [PubMed: 8662539]
Protein Sequence MVCFRLFPVPGSGLVLVCLVLGAVRSYALELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSYWDAPLGSSYMCNKEQTVSVSGAFQINTFDLRVQPFNVTQGKYSTAQDCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGYEQF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
32N-linked_GlycosylationRSYALELNLTDSENA
HHHHHHCCCCCCCCC		31.363198605
38N-linked_GlycosylationLNLTDSENATCLYAK
CCCCCCCCCEEEEEE		44.493198605
49N-linked_GlycosylationLYAKWQMNFTVRYET
EEEEEEEEEEEEEEE		17.843198605
54PhosphorylationQMNFTVRYETTNKTY
EEEEEEEEEECCCEE		17.1923663014
56PhosphorylationNFTVRYETTNKTYKT
EEEEEEEECCCEEEE		27.0823663014
57PhosphorylationFTVRYETTNKTYKTV
EEEEEEECCCEEEEE		23.8323663014
58N-linked_GlycosylationTVRYETTNKTYKTVT
EEEEEECCCEEEEEE		41.938323299
592-HydroxyisobutyrylationVRYETTNKTYKTVTI
EEEEECCCEEEEEEE		51.65-
59UbiquitinationVRYETTNKTYKTVTI
EEEEECCCEEEEEEE		51.6527667366
63PhosphorylationTTNKTYKTVTISDHG
ECCCEEEEEEECCCC		16.68-
65PhosphorylationNKTYKTVTISDHGTV
CCEEEEEEECCCCEE		21.72-
67PhosphorylationTYKTVTISDHGTVTY
EEEEEEECCCCEEEE		17.75-
75N-linked_GlycosylationDHGTVTYNGSICGDD
CCCEEEECCEECCCC		28.508323299
101N-linked_GlycosylationPGFSWIANFTKAAST
CCCHHHEEEEECCCC		35.6719522481
123N-linked_GlycosylationFSYNTGDNTTFPDAE
EEEECCCCCCCCCHH		42.2219159218
179N-linked_GlycosylationLVQAFVQNGTVSTNE
HHHHHHHCCCEECCE		42.688323299
194O-linked_GlycosylationFLCDKDKTSTVAPTI
EECCCCCCCCCCCEE		39.50OGP
195O-linked_GlycosylationLCDKDKTSTVAPTIH
ECCCCCCCCCCCEEE		26.998323299
196O-linked_GlycosylationCDKDKTSTVAPTIHT
CCCCCCCCCCCEEEE		26.398323299
200O-linked_GlycosylationKTSTVAPTIHTTVPS
CCCCCCCEEEECCCC		18.698323299
203O-linked_GlycosylationTVAPTIHTTVPSPTT
CCCCEEEECCCCCCC		26.168323299
204PhosphorylationVAPTIHTTVPSPTTT
CCCEEEECCCCCCCC		19.0924719451
204O-linked_GlycosylationVAPTIHTTVPSPTTT
CCCEEEECCCCCCCC		19.0955828521
207O-linked_GlycosylationTIHTTVPSPTTTPTP
EEEECCCCCCCCCCC		30.468323299
209O-linked_GlycosylationHTTVPSPTTTPTPKE
EECCCCCCCCCCCCC		47.878323299
209PhosphorylationHTTVPSPTTTPTPKE
EECCCCCCCCCCCCC		47.8724719451
210O-linked_GlycosylationTTVPSPTTTPTPKEK
ECCCCCCCCCCCCCC		33.888323299
211PhosphorylationTVPSPTTTPTPKEKP
CCCCCCCCCCCCCCC		27.878323299
211O-linked_GlycosylationTVPSPTTTPTPKEKP
CCCCCCCCCCCCCCC		27.87772373011
213O-linked_GlycosylationPSPTTTPTPKEKPEA
CCCCCCCCCCCCCCC		44.928323299
213PhosphorylationPSPTTTPTPKEKPEA
CCCCCCCCCCCCCCC		44.928323299
229N-linked_GlycosylationTYSVNNGNDTCLLAT
EEEECCCCCCEEEEE		43.478323299
242N-linked_GlycosylationATMGLQLNITQDKVA
EEECCEEEECCCCEE		23.468323299
257N-linked_GlycosylationSVININPNTTHSTGS
EEEECCCCCCCCCCC		53.7918638581
267PhosphorylationHSTGSCRSHTALLRL
CCCCCCCCCCEEEEC		29.5320068231
269PhosphorylationTGSCRSHTALLRLNS
CCCCCCCCEEEECCC		21.9020068231
275N-linked_GlycosylationHTALLRLNSSTIKYL
CCEEEECCCCCCEEE		27.728323299
276PhosphorylationTALLRLNSSTIKYLD
CEEEECCCCCCEEEE		33.1920068231
277PhosphorylationALLRLNSSTIKYLDF
EEEECCCCCCEEEEE		32.8320068231
278PhosphorylationLLRLNSSTIKYLDFV
EEECCCCCCEEEEEE		22.7020068231
281PhosphorylationLNSSTIKYLDFVFAV
CCCCCCEEEEEEEEE		13.9820068231
293MethylationFAVKNENRFYLKEVN
EEEECCCCEEEEEEE		18.53115481749
300N-linked_GlycosylationRFYLKEVNISMYLVN
CEEEEEEEEEEEEEC		23.008323299
304PhosphorylationKEVNISMYLVNGSVF
EEEEEEEEEECCEEE		10.74-
307N-linked_GlycosylationNISMYLVNGSVFSIA
EEEEEEECCEEEEEC		34.138323299
309PhosphorylationSMYLVNGSVFSIANN
EEEEECCEEEEECCC		18.13-
317N-linked_GlycosylationVFSIANNNLSYWDAP
EEEECCCCCCCCCCC		30.128323299
356N-linked_GlycosylationDLRVQPFNVTQGKYS
EEEEEEECCCCCCCC		42.4817660510
402UbiquitinationAYFIGLKHHHAGYEQ
HHHHHHHHHHCCCCC		24.0233845483
402 (in isoform 2)Ubiquitination-24.02-
403 (in isoform 2)Phosphorylation-15.7728152594
404 (in isoform 2)Phosphorylation-22.1428152594
407 (in isoform 2)Phosphorylation-13.8228796482
409 (in isoform 2)Phosphorylation-40.6528152594
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
211TPhosphorylationKinaseMAPK14Q16539
GPS
213TPhosphorylationKinaseMAPK14Q16539
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXO27Q8NI29
PMID:28743755
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LAMP2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LAMP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UCHL1_HUMANUCHL1physical
18550537
MCM7_HUMANMCM7physical
22939629
RBBP4_HUMANRBBP4physical
22939629
SF3B3_HUMANSF3B3physical
22939629
PRP19_HUMANPRPF19physical
22939629
SRP14_HUMANSRP14physical
22939629
PDS5B_HUMANPDS5Bphysical
22939629
TBA1B_HUMANTUBA1Bphysical
22939629
RFC1_HUMANRFC1physical
22939629
SYEP_HUMANEPRSphysical
22939629
NPM_HUMANNPM1physical
22939629
PCNA_HUMANPCNAphysical
22939629
SF3B6_HUMANSF3B6physical
22939629
SPF27_HUMANBCAS2physical
22939629
TBB5_HUMANTUBBphysical
22939629
NICA_HUMANNCSTNphysical
22939629
SAFB1_HUMANSAFBphysical
22939629
RU2A_HUMANSNRPA1physical
22939629
THOC6_HUMANTHOC6physical
22939629
TCP4_HUMANSUB1physical
22939629
LAMP2_HUMANLAMP2physical
23880665
HIF1A_HUMANHIF1Aphysical
23880665
HSP7C_HUMANHSPA8physical
23880665
PIAS4_HUMANPIAS4physical
21988832
IMDH1_HUMANIMPDH1physical
22863883
BRF2_HUMANBRF2physical
28514442
MTG2_HUMANMTG2physical
28514442
CDC6_HUMANCDC6physical
28514442
NEK6_HUMANNEK6physical
28514442
STK39_HUMANSTK39physical
28514442
TAM41_HUMANTAMM41physical
28514442
CP2S1_HUMANCYP2S1physical
28514442
GUF1_HUMANGUF1physical
28514442
HS12A_HUMANHSPA12Aphysical
28514442
HELLS_HUMANHELLSphysical
28514442
FOLC_HUMANFPGSphysical
28514442
CHD1L_HUMANCHD1Lphysical
28514442
MSTO1_HUMANMSTO1physical
28514442
BDH_HUMANBDH1physical
28514442
GPD1L_HUMANGPD1Lphysical
28514442
MMSA_HUMANALDH6A1physical
28514442
JAK1_HUMANJAK1physical
28514442
ORC5_HUMANORC5physical
28514442
XRCC3_HUMANXRCC3physical
28514442
GNL3L_HUMANGNL3Lphysical
28514442
PPTC7_HUMANPPTC7physical
28514442
PLCE_HUMANAGPAT5physical
28514442
PDXD1_HUMANPDXDC1physical
28514442
RAB18_HUMANRAB18physical
28514442
COT2_HUMANNR2F2physical
28514442
MTX3_HUMANMTX3physical
28514442
PTPM1_HUMANPTPMT1physical
28514442
TTK_HUMANTTKphysical
28514442
HSP7C_HUMANHSPA8physical
28465257
EP300_HUMANEP300physical
28465257
CBP_HUMANCREBBPphysical
28465257
Drug and Disease Associations
Kegg Disease
H00150 Danon disease; X-linked vacuolar cardiomyopathy and myopathy
OMIM Disease
300257Danon disease (DAND)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LAMP2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101; ASN-123; ASN-257 ANDASN-356, AND MASS SPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-32; ASN-38; ASN-49;ASN-101; ASN-123 AND ASN-257, AND MASS SPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-49 AND ASN-101.
"The polylactosaminoglycans of human lysosomal membrane glycoproteinslamp-1 and lamp-2. Localization on the peptide backbones.";
Carlsson S.R., Fukuda M.;
J. Biol. Chem. 265:20488-20495(1990).
Cited for: POLYLACTOSAMINOGLYCANS.
O-linked Glycosylation
ReferencePubMed
"Assignment of O-glycan attachment sites to the hinge-like regions ofhuman lysosomal membrane glycoproteins lamp-1 and lamp-2.";
Carlsson S.R., Lycksell P.-O., Fukuda M.;
Arch. Biochem. Biophys. 304:65-73(1993).
Cited for: GLYCOSYLATION OF HINGE REGION, AND PROTEIN SEQUENCE OF 187-215.

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