LSAMP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LSAMP_HUMAN
• UniProt AC: Q13449
• Protein Name: Limbic system-associated membrane protein
• Gene Name: LSAMP
• Organism: Homo sapiens (Human).
• Sequence Length: 338
• Subcellular Localization: Cell membrane; Lipid-anchor, GPI-anchor.
• Protein Description: Mediates selective neuronal growth and axon targeting. Contributes to the guidance of developing axons and remodeling of mature circuits in the limbic system. Essential for normal growth of the hyppocampal mossy fiber projection (By similarity)..
• Protein Sequence: MVRRVQPDRKQLPLVLLRLLCLLPTGLPVRSVDFNRGTDNITVRQGDTAILRCVVEDKNSKVAWLNRSGIIFAGHDKWSLDPRVELEKRHSLEYSLRIQKVDVYDEGSYTCSVQTQHEPKTSQVYLIVQVPPKISNISSDVTVNEGSNVTLVCMANGRPEPVITWRHLTPTGREFEGEEEYLEILGITREQSGKYECKAANEVSSADVKQVKVTVNYPPTITESKSNEATTGRQASLKCEASAVPAPDFEWYRDDTRINSANGLEIKSTEGQSSLTVTNVTEEHYGNYTCVAANKLGVTNASLVLFRPGSVRGINGSISLAVPLWLLAASLLCLLSKC

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
40	N-linked_Glycosylation	DFNRGTDNITVRQGD ECCCCCCCEEEECCC	31.50	UniProtKB CARBOHYD
40	N-linked_Glycosylation	DFNRGTDNITVRQGD ECCCCCCCEEEECCC	31.50	19349973
66	N-linked_Glycosylation	NSKVAWLNRSGIIFA CCCEEEEECCCEEEE	25.93	UniProtKB CARBOHYD
91	Phosphorylation	VELEKRHSLEYSLRI HHHHHHHCCEEEEEE	27.25	25332170
94	Phosphorylation	EKRHSLEYSLRIQKV HHHHCCEEEEEEEEE	20.49	21082442
95	Phosphorylation	KRHSLEYSLRIQKVD HHHCCEEEEEEEEEE	11.20	24719451
136	N-linked_Glycosylation	QVPPKISNISSDVTV ECCCCCCCCCCCEEE	41.45	UniProtKB CARBOHYD
148	N-linked_Glycosylation	VTVNEGSNVTLVCMA EEECCCCCEEEEEEE	41.47	UniProtKB CARBOHYD
195	Phosphorylation	TREQSGKYECKAANE CHHHCCCEEEECCCC	30.04	-
204	Phosphorylation	CKAANEVSSADVKQV EECCCCCCCCCCCEE	17.40	25307156
205	Phosphorylation	KAANEVSSADVKQVK ECCCCCCCCCCCEEE	33.39	25307156
214	Phosphorylation	DVKQVKVTVNYPPTI CCCEEEEEEECCCCC	9.41	22798277
222	Phosphorylation	VNYPPTITESKSNEA EECCCCCCCCCCCCC	36.36	22798277
224	Phosphorylation	YPPTITESKSNEATT CCCCCCCCCCCCCCC	32.50	22798277
279	N-linked_Glycosylation	QSSLTVTNVTEEHYG CCCEEEEECCEEHHC	34.08	UniProtKB CARBOHYD
287	N-linked_Glycosylation	VTEEHYGNYTCVAAN CCEEHHCCEEEEEEC	23.05	UniProtKB CARBOHYD
299	O-linked_Glycosylation	AANKLGVTNASLVLF EECCCCCCCEEEEEE	24.22	28657654
300	N-linked_Glycosylation	ANKLGVTNASLVLFR ECCCCCCCEEEEEEC	25.73	19349973
300	N-linked_Glycosylation	ANKLGVTNASLVLFR ECCCCCCCEEEEEEC	25.73	19349973
315	N-linked_Glycosylation	PGSVRGINGSISLAV CCCCCCCCCCCHHHH	40.77	UniProtKB CARBOHYD
315	GPI-anchor	PGSVRGINGSISLAV CCCCCCCCCCCHHHH	40.77	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LSAMP_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of LSAMP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NTRI_HUMAN	NTM	physical	21982860
LSAMP_HUMAN	LSAMP	physical	21982860
NEGR1_HUMAN	NEGR1	physical	21982860

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300, AND MASSSPECTROMETRY.
PubMed: 19349973