dbPTM

LAMP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LAMP1_HUMAN
UniProt AC	P11279
Protein Name	Lysosome-associated membrane glycoprotein 1
Gene Name	LAMP1
Organism	Homo sapiens (Human).
Sequence Length	417
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 . Late endosome . This protein shuttles between lysosomes, endosomes, and the plasm
Protein Description	Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.; Acts as a receptor for Lassa virus protein..
Protein Sequence	MAAPGSARRPLLLLLLLLLLGLMHCASAAMFMVKNGNGTACIMANFSAAFSVNYDTKSGPKNMTFDLPSDATVVLNRSSCGKENTSDPSLVIAFGRGHTLTLNFTRNATRYSVQLMSFVYNLSDTHLFPNASSKEIKTVESITDIRADIDKKYRCVSGTQVHMNNVTVTLHDATIQAYLSNSSFSRGETRCEQDRPSPTTAPPAPPSPSPSPVPKSPSVDKYNVSGTNGTCLLASMGLQLNLTYERKDNTTVTRLLNINPNKTSASGSCGAHLVTLELHSEGTTVLLFQFGMNASSSRFFLQGIQLNTILPDARDPAFKAANGSLRALQATVGNSYKCNAEEHVRVTKAFSVNIFKVWVQAFKVEGGQFGSVEECLLDENSMLIPIAVGGALAGLVLIVLIAYLVGRKRSHAGYQTI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
27	Phosphorylation	LGLMHCASAAMFMVK HHHHHHHHHHHHHEE	23.19	-
37	N-linked_Glycosylation	MFMVKNGNGTACIMA HHHEECCCCEEEEEE	54.78	2584229
37	N-linked_Glycosylation	MFMVKNGNGTACIMA HHHEECCCCEEEEEE	54.78	8323299
45	N-linked_Glycosylation	GTACIMANFSAAFSV CEEEEEEECCEEEEC	17.64	2584229
45	N-linked_Glycosylation	GTACIMANFSAAFSV CEEEEEEECCEEEEC	17.64	8323299
62	N-linked_Glycosylation	DTKSGPKNMTFDLPS CCCCCCCCEEEECCC	37.55	12754519
62	N-linked_Glycosylation	DTKSGPKNMTFDLPS CCCCCCCCEEEECCC	37.55	12754519
69	Phosphorylation	NMTFDLPSDATVVLN CEEEECCCCCEEEEE	47.37	21659604
72	Phosphorylation	FDLPSDATVVLNRSS EECCCCCEEEEEHHH	19.01	21659604
76	N-linked_Glycosylation	SDATVVLNRSSCGKE CCCEEEEEHHHCCCC	30.13	2584229
76	N-linked_Glycosylation	SDATVVLNRSSCGKE CCCEEEEEHHHCCCC	30.13	2243102
78	Phosphorylation	ATVVLNRSSCGKENT CEEEEEHHHCCCCCC	28.98	21659604
79	Phosphorylation	TVVLNRSSCGKENTS EEEEEHHHCCCCCCC	24.53	21659604
84	N-linked_Glycosylation	RSSCGKENTSDPSLV HHHCCCCCCCCCCEE	48.66	2584229
84	N-linked_Glycosylation	RSSCGKENTSDPSLV HHHCCCCCCCCCCEE	48.66	2584229
85	Phosphorylation	SSCGKENTSDPSLVI HHCCCCCCCCCCEEE	35.28	21659604
85	O-linked_Glycosylation	SSCGKENTSDPSLVI HHCCCCCCCCCCEEE	35.28	23301498
89	Phosphorylation	KENTSDPSLVIAFGR CCCCCCCCEEEEECC	40.01	24173317
103	N-linked_Glycosylation	RGHTLTLNFTRNATR CCCEEEEEECCCCHH	30.89	19522481
103	N-linked_Glycosylation	RGHTLTLNFTRNATR CCCEEEEEECCCCHH	30.89	19522481
107	N-linked_Glycosylation	LTLNFTRNATRYSVQ EEEEECCCCHHHEEE	42.48	8323299
107	N-linked_Glycosylation	LTLNFTRNATRYSVQ EEEEECCCCHHHEEE	42.48	2584229
121	N-linked_Glycosylation	QLMSFVYNLSDTHLF EEEEEECCCCCCCCC	27.97	2584229
121	N-linked_Glycosylation	QLMSFVYNLSDTHLF EEEEEECCCCCCCCC	27.97	2584229
130	N-linked_Glycosylation	SDTHLFPNASSKEIK CCCCCCCCCCCCCEE	45.15	2584229
130	N-linked_Glycosylation	SDTHLFPNASSKEIK CCCCCCCCCCCCCEE	45.15	2584229
137	Ubiquitination	NASSKEIKTVESITD CCCCCCEEEEEHHHH	47.84	-
137	Succinylation	NASSKEIKTVESITD CCCCCCEEEEEHHHH	47.84	23954790
164	N-linked_Glycosylation	SGTQVHMNNVTVTLH ECCEEEECCEEEEEE	25.58	8323299
165	N-linked_Glycosylation	GTQVHMNNVTVTLHD CCEEEECCEEEEEEH	24.22	2243102
165	N-linked_Glycosylation	GTQVHMNNVTVTLHD CCEEEECCEEEEEEH	24.22	8323299
181	N-linked_Glycosylation	TIQAYLSNSSFSRGE HHHHHHHCCCCCCCC	38.79	2243102
181	N-linked_Glycosylation	TIQAYLSNSSFSRGE HHHHHHHCCCCCCCC	38.79	8323299
197	O-linked_Glycosylation	RCEQDRPSPTTAPPA CCCCCCCCCCCCCCC	35.45	8323299
197	O-linked_Glycosylation	RCEQDRPSPTTAPPA CCCCCCCCCCCCCCC	35.45	8323299
198 (in isoform 2)	O-linked_Glycosylation	-	36.13	OGP
199	O-linked_Glycosylation	EQDRPSPTTAPPAPP CCCCCCCCCCCCCCC	39.67	8323299
199	O-linked_Glycosylation	EQDRPSPTTAPPAPP CCCCCCCCCCCCCCC	39.67	55830123
200	O-linked_Glycosylation	QDRPSPTTAPPAPPS CCCCCCCCCCCCCCC	40.32	8323299
200	O-linked_Glycosylation	QDRPSPTTAPPAPPS CCCCCCCCCCCCCCC	40.32	8323299
207	Phosphorylation	TAPPAPPSPSPSPVP CCCCCCCCCCCCCCC	36.63	20068231
207	O-linked_Glycosylation	TAPPAPPSPSPSPVP CCCCCCCCCCCCCCC	36.63	8323299
207	O-linked_Glycosylation	TAPPAPPSPSPSPVP CCCCCCCCCCCCCCC	36.63	8323299
209	Phosphorylation	PPAPPSPSPSPVPKS CCCCCCCCCCCCCCC	42.20	20068231
209	O-linked_Glycosylation	PPAPPSPSPSPVPKS CCCCCCCCCCCCCCC	42.20	8323299
209	O-linked_Glycosylation	PPAPPSPSPSPVPKS CCCCCCCCCCCCCCC	42.20	8323299
210 (in isoform 2)	O-linked_Glycosylation	-	46.14	OGP
211	O-linked_Glycosylation	APPSPSPSPVPKSPS CCCCCCCCCCCCCCC	42.75	8323299
211	O-linked_Glycosylation	APPSPSPSPVPKSPS CCCCCCCCCCCCCCC	42.75	8323299
211	Phosphorylation	APPSPSPSPVPKSPS CCCCCCCCCCCCCCC	42.75	20068231
223	N-linked_Glycosylation	SPSVDKYNVSGTNGT CCCCCCCCCCCCCCC	27.50	2584229
223	N-linked_Glycosylation	SPSVDKYNVSGTNGT CCCCCCCCCCCCCCC	27.50	8323299
228	N-linked_Glycosylation	KYNVSGTNGTCLLAS CCCCCCCCCCEEEEE	47.50	2584229
228	N-linked_Glycosylation	KYNVSGTNGTCLLAS CCCCCCCCCCEEEEE	47.50	8323299
230	Phosphorylation	NVSGTNGTCLLASMG CCCCCCCCEEEEECC	11.31	-
241	N-linked_Glycosylation	ASMGLQLNLTYERKD EECCEEEEEEEECCC	19.85	2584229
241	N-linked_Glycosylation	ASMGLQLNLTYERKD EECCEEEEEEEECCC	19.85	8323299
249	N-linked_Glycosylation	LTYERKDNTTVTRLL EEEECCCCCEEEEEE	40.46	16335952
249	N-linked_Glycosylation	LTYERKDNTTVTRLL EEEECCCCCEEEEEE	40.46	2584229
261	N-linked_Glycosylation	RLLNINPNKTSASGS EEEECCCCCCCCCCC	56.61	8323299
261	N-linked_Glycosylation	RLLNINPNKTSASGS EEEECCCCCCCCCCC	56.61	2243102
266	Ubiquitination	NPNKTSASGSCGAHL CCCCCCCCCCCCCEE	30.89	-
284	Ubiquitination	ELHSEGTTVLLFQFG EEECCCCEEEEEEEC	21.73	-
293	N-linked_Glycosylation	LLFQFGMNASSSRFF EEEEECCCCCCCCEE	36.73	2584229
293	N-linked_Glycosylation	LLFQFGMNASSSRFF EEEEECCCCCCCCEE	36.73	2584229
319	Ubiquitination	DARDPAFKAANGSLR CCCCHHHHHHCCHHH	49.01	21906983
322	N-linked_Glycosylation	DPAFKAANGSLRALQ CHHHHHHCCHHHHHH	45.50	20068230
322	N-linked_Glycosylation	DPAFKAANGSLRALQ CHHHHHHCCHHHHHH	45.50	8323299
331	Phosphorylation	SLRALQATVGNSYKC HHHHHHHHCCCCCCC	18.91	-
331	O-linked_Glycosylation	SLRALQATVGNSYKC HHHHHHHHCCCCCCC	18.91	55831339
336	Phosphorylation	QATVGNSYKCNAEEH HHHCCCCCCCCHHHE	24.45	19060867
337	Methylation	ATVGNSYKCNAEEHV HHCCCCCCCCHHHEE	22.34	115972321
337	2-Hydroxyisobutyrylation	ATVGNSYKCNAEEHV HHCCCCCCCCHHHEE	22.34	-
337	Ubiquitination	ATVGNSYKCNAEEHV HHCCCCCCCCHHHEE	22.34	-
351	Phosphorylation	VRVTKAFSVNIFKVW EEEEEEEEEEEEEEE	21.08	20068231
381	O-linked_Glycosylation	ECLLDENSMLIPIAV EEEECCCCCEEEHHH	16.96	23301498
410	Phosphorylation	YLVGRKRSHAGYQTI HHHCCCCCCCCCCCC	22.26	28152594
414	Phosphorylation	RKRSHAGYQTI---- CCCCCCCCCCC----	11.85	28796482
416	Phosphorylation	RSHAGYQTI------ CCCCCCCCC------	21.85	28152594

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
Oops, there are no upstream regulatory protein records of LAMP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LAMP1_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 LAMP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TP4A1_HUMAN	PTP4A1	physical	22939629
TM9S4_HUMAN	TM9SF4	physical	22939629
SDA1_HUMAN	SDAD1	physical	22939629
ZFPL1_HUMAN	ZFPL1	physical	26344197
ST17B_HUMAN	STK17B	physical	28514442
S38A7_HUMAN	SLC38A7	physical	28514442
FZD7_HUMAN	FZD7	physical	28514442
RAB4A_HUMAN	RAB4A	physical	28514442
FZD2_HUMAN	FZD2	physical	28514442
PLAP_HUMAN	PLAA	physical	28514442
CO4A_HUMAN	C4A	physical	28514442
MAN1_HUMAN	LEMD3	physical	28514442
LEG1_HUMAN	LGALS1	physical	28514442
ELP6_HUMAN	ELP6	physical	28514442
SYRC_HUMAN	RARS	physical	28514442
ORC4_HUMAN	ORC4	physical	28514442
DYN3_HUMAN	DNM3	physical	28514442
CUX1_HUMAN	CUX1	physical	28514442
CASP_HUMAN	CUX1	physical	28514442
FAM3C_HUMAN	FAM3C	physical	28514442
APC7_HUMAN	ANAPC7	physical	28514442
F207A_HUMAN	FAM207A	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LAMP1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-62; ASN-76; ASN-84;ASN-103; ASN-121; ASN-130; ASN-249 AND ASN-293, AND MASS SPECTROMETRY.	19159218 [Abstract]
"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-103 AND ASN-249, AND MASSSPECTROMETRY.	16335952 [Abstract]
"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-62 AND ASN-103.	12754519 [Abstract]
"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.	2243102 [Abstract]
O-linked Glycosylation
Reference	PubMed
"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 191-215.	8323299 [Abstract]