dbPTM

LANC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LANC2_HUMAN
UniProt AC	Q9NS86
Protein Name	LanC-like protein 2
Gene Name	LANCL2
Organism	Homo sapiens (Human).
Sequence Length	450
Subcellular Localization	Nucleus . Cytoplasm . Cell membrane . Localizes to the juxta-nuclear vesicles (PubMed:16979580). Associates with the cortical actin cytoskeleton (PubMed:16979580). Cholesterol depletion by methyl-beta-cyclodextrin causes partial dissociation from the
Protein Description	Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes..
Protein Sequence	MGETMSKRLKLHLGGEAEMEERAFVNPFPDYEAAAGALLASGAAEETGCVRPPATTDEPGLPFHQDGKIIHNFIRRIQTKIKDLLQQMEEGLKTADPHDCSAYTGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNGRRVTFLCGDAGPLAVGAVIYHKLRSDCESQECVTKLLQLQRSVVCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVCESAIKEVVNAIIESGKTLSREERKTERCPLLYQWHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNETDRLVHWCHGAPGVIHMLMQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAHGCRIPDRPYSLFEGMAGAIHFLSDVLGPETSRFPAFELDSSKRD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGETMSKRL ------CCCCHHHHH	38.80	-
2	Myristoylation	------MGETMSKRL ------CCCCHHHHH	38.80	16979580
4	Phosphorylation	----MGETMSKRLKL ----CCCCHHHHHHH	22.48	27794612
6	Phosphorylation	--MGETMSKRLKLHL --CCCCHHHHHHHHC	23.26	27794612
19	Sulfoxidation	HLGGEAEMEERAFVN HCCCCCHHHHHCCCC	9.27	21406390
82	Ubiquitination	RRIQTKIKDLLQQME HHHHHHHHHHHHHHH	43.83	-
134	2-Hydroxyisobutyrylation	LRSLDYVKRTLRNLN HHHHHHHHHHHHHCC	33.17	-
164	Ubiquitination	VGAVIYHKLRSDCES HHHHHHHHHHCCCCC	28.73	-
167	Phosphorylation	VIYHKLRSDCESQEC HHHHHHHCCCCCHHH	57.98	21406692
171	Phosphorylation	KLRSDCESQECVTKL HHHCCCCCHHHHHHH	37.30	21406692
176	Phosphorylation	CESQECVTKLLQLQR CCCHHHHHHHHHHHH	27.86	21406692
198	Phosphorylation	DLPDELLYGRAGYLY CCCHHHHHHHHHHHH	19.72	19060867
236	Ubiquitination	NAIIESGKTLSREER HHHHHHCCCCCHHHH	56.42	-
239	Phosphorylation	IESGKTLSREERKTE HHHCCCCCHHHHHHC	42.76	-
259	Phosphorylation	YQWHRKQYVGAAHGM HHHHHHHHHHHHHHH	12.13	21082442
288	Sulfoxidation	DQETLTEMVKPSIDY CHHHHHHHHCCCCCH	3.85	28465586
290	Ubiquitination	ETLTEMVKPSIDYVR HHHHHHHCCCCCHHH	31.56	-
295	Phosphorylation	MVKPSIDYVRHKKFR HHCCCCCHHHCCCCC	9.56	24927040
300	Acetylation	IDYVRHKKFRSGNYP CCHHHCCCCCCCCCC	39.63	7663155
303	Phosphorylation	VRHKKFRSGNYPSSL HHCCCCCCCCCCCCC	34.23	28152594
306	Phosphorylation	KKFRSGNYPSSLSNE CCCCCCCCCCCCCCH	14.17	28152594
308	Phosphorylation	FRSGNYPSSLSNETD CCCCCCCCCCCCHHH	33.29	28152594
309	Phosphorylation	RSGNYPSSLSNETDR CCCCCCCCCCCHHHH	31.17	24076635
311	Phosphorylation	GNYPSSLSNETDRLV CCCCCCCCCHHHHHH	34.27	24076635
314	Phosphorylation	PSSLSNETDRLVHWC CCCCCCHHHHHHHHH	30.57	-

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 LANC2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LANC2_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 LANC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049
MON1B_HUMAN	MON1B	physical	22939629

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 LANC2_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"Myristoylation of human LanC-like protein 2 (LANCL2) is essential forthe interaction with the plasma membrane and the increase in cellularsensitivity to adriamycin."; Landlinger C., Salzer U., Prohaska R.; Biochim. Biophys. Acta 1758:1759-1767(2006). Cited for: SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2,AND INTERACTION WITH INOSITOL PHOSPHOLIPIDS.	16979580 [Abstract]