dbPTM

LANC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LANC1_HUMAN
UniProt AC	O43813
Protein Name	LanC-like protein 1
Gene Name	LANCL1
Organism	Homo sapiens (Human).
Sequence Length	399
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein .
Protein Description	May play a role in EPS8 signaling. Binds glutathione..
Protein Sequence	MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYGLCHGSAGNAYAFLTLYNLTQDMKYLYRACKFAEWCLEYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKARFPAFEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQRAFPNP ------CCCCCCCCC	13.94	19413330
10	Phosphorylation	QRAFPNPYADYNKSL CCCCCCCCCCCCHHH	20.81	-
15	Acetylation	NPYADYNKSLAEGYF CCCCCCCHHHHCCCC	40.39	23954790
15	Ubiquitination	NPYADYNKSLAEGYF CCCCCCCHHHHCCCC	40.39	21906983
21	Phosphorylation	NKSLAEGYFDAAGRL CHHHHCCCCCCCCCC	6.98	27642862
29	Phosphorylation	FDAAGRLTPEFSQRL CCCCCCCCHHHHHHH	21.29	-
29	O-linked_Glycosylation	FDAAGRLTPEFSQRL CCCCCCCCHHHHHHH	21.29	23301498
33	Phosphorylation	GRLTPEFSQRLTNKI CCCCHHHHHHHHHHH	16.84	23532336
52	Ubiquitination	QQMERGLKSADPRDG HHHHHHHHCCCCCCC	46.55	-
95	Phosphorylation	AHGYVKQSLNCLTKR HHHHHHHHHHHCCCC	18.81	21406692
100	Phosphorylation	KQSLNCLTKRSITFL HHHHHHCCCCEEEEE	26.98	21406692
101	Ubiquitination	QSLNCLTKRSITFLC HHHHHCCCCEEEEEC	31.06	-
101	Acetylation	QSLNCLTKRSITFLC HHHHHCCCCEEEEEC	31.06	25953088
123	Acetylation	VAAVLYHKMNNEKQA HHHHHHHHHCCHHHH	29.75	30589831
128	Ubiquitination	YHKMNNEKQAEDCIT HHHHCCHHHHHHHHH	57.86	21906983
128	Acetylation	YHKMNNEKQAEDCIT HHHHCCHHHHHHHHH	57.86	25953088
135	Phosphorylation	KQAEDCITRLIHLNK HHHHHHHHHHHHHHC	26.25	-
142	Acetylation	TRLIHLNKIDPHAPN HHHHHHHCCCCCCCC	55.64	19608861
142	Ubiquitination	TRLIHLNKIDPHAPN HHHHHHHCCCCCCCC	55.64	19608861
153	Phosphorylation	HAPNEMLYGRIGYIY CCCCHHHHHHHHHHH	11.75	23917254
173	Ubiquitination	NKNFGVEKIPQSHIQ CCCCCCCCCCHHHHH	58.23	-
185	Phosphorylation	HIQQICETILTSGEN HHHHHHHHHHHCCHH	19.51	24076635
188	Phosphorylation	QICETILTSGENLAR HHHHHHHHCCHHHHH	30.73	24076635
189	Phosphorylation	ICETILTSGENLARK HHHHHHHCCHHHHHH	40.44	26437602
203	Phosphorylation	KRNFTAKSPLMYEWY HCCCCCCCCCHHHHH	22.32	22210691
207	Phosphorylation	TAKSPLMYEWYQEYY CCCCCCHHHHHHHHH	15.82	22210691
245	Ubiquitination	GKLHSLVKPSVDYVC CCCHHCCCCCCCEEE	36.55	-
245	Acetylation	GKLHSLVKPSVDYVC CCCHHCCCCCCCEEE	36.55	25953088
250	Phosphorylation	LVKPSVDYVCQLKFP CCCCCCCEEEEEECC	10.85	-
319	Phosphorylation	YGLLKKGYGLCHGSA HCHHHCCCCCCCCCC	18.79	-
330	Phosphorylation	HGSAGNAYAFLTLYN CCCCCCHHHHHHHHH	11.24	-
336	Phosphorylation	AYAFLTLYNLTQDMK HHHHHHHHHHHHHHH	11.68	-

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 LANC1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LANC1_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 LANC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SERPH_HUMAN	SERPINH1	physical	22939629
A16A1_HUMAN	ALDH16A1	physical	26186194
DEOC_HUMAN	DERA	physical	26186194
TBCD9_HUMAN	TBC1D9	physical	26186194
TBC9B_HUMAN	TBC1D9B	physical	26186194
FIGN_HUMAN	FIGN	physical	26186194
MYO7A_HUMAN	MYO7A	physical	26186194
IPP_HUMAN	IPP	physical	26186194
OCAD1_HUMAN	OCIAD1	physical	26186194
UBN2_HUMAN	UBN2	physical	26186194
FIGN_HUMAN	FIGN	physical	28514442
DEOC_HUMAN	DERA	physical	28514442
IPP_HUMAN	IPP	physical	28514442
A16A1_HUMAN	ALDH16A1	physical	28514442
UBN2_HUMAN	UBN2	physical	28514442
TBCD9_HUMAN	TBC1D9	physical	28514442
TBC9B_HUMAN	TBC1D9B	physical	28514442
MYO7A_HUMAN	MYO7A	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 LANC1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY.	19608861 [Abstract]