dbPTM

LPIN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LPIN2_HUMAN
UniProt AC	Q92539
Protein Name	Phosphatidate phosphatase LPIN2
Gene Name	LPIN2
Organism	Homo sapiens (Human).
Sequence Length	896
Subcellular Localization	Nucleus. Cytoplasm, cytosol. Endoplasmic reticulum membrane. Translocates to endoplasmic reticulum membrane with increasing levels of oleate..
Protein Description	Plays important roles in controlling the metabolism of fatty acids at different levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism (By similarity)..
Protein Sequence	MNYVGQLAGQVIVTVKELYKGINQATLSGCIDVIVVQQQDGSYQCSPFHVRFGKLGVLRSKEKVIDIEINGSAVDLHMKLGDNGEAFFVEETEEEYEKLPAYLATSPIPTEDQFFKDIDTPLVKSGGDETPSQSSDISHVLETETIFTPSSVKKKKRRRKKYKQDSKKEEQAASAAAEDTCDVGVSSDDDKGAQAARGSSNASLKEEECKEPLLFHSGDHYPLSDGDWSPLETTYPQTACPKSDSELEVKPAESLLRSESHMEWTWGGFPESTKVSKRERSDHHPRTATITPSENTHFRVIPSEDNLISEVEKDASMEDTVCTIVKPKPRALGTQMSDPTSVAELLEPPLESTQISSMLDADHLPNAALAEAPSESKPAAKVDSPSKKKGVHKRSQHQGPDDIYLDDLKGLEPEVAALYFPKSESEPGSRQWPESDTLSGSQSPQSVGSAAADSGTECLSDSAMDLPDVTLSLCGGLSENGEISKEKFMEHIITYHEFAENPGLIDNPNLVIRIYNRYYNWALAAPMILSLQVFQKSLPKATVESWVKDKMPKKSGRWWFWRKRESMTKQLPESKEGKSEAPPASDLPSSSKEPAGARPAENDSSSDEGSQELEESITVDPIPTEPLSHGSTTSYKKSLRLSSDQIAKLKLHDGPNDVVFSITTQYQGTCRCAGTIYLWNWNDKIIISDIDGTITKSDALGQILPQLGKDWTHQGIAKLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLMLSPSSLFSAFHREVIEKKPEKFKIECLNDIKNLFAPSKQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQERTKGNKSSYHRLSELVEHVFPLLSKEQNSAFPCPEFSSFCYWRDPIPEVDLDDLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
92	Phosphorylation	EAFFVEETEEEYEKL CEEEEEECHHHHHHC	34.88	27251275
102	Phosphorylation	EYEKLPAYLATSPIP HHHHCCHHHCCCCCC	8.57	25850435
105	Phosphorylation	KLPAYLATSPIPTED HCCHHHCCCCCCCHH	32.23	29255136
106	Phosphorylation	LPAYLATSPIPTEDQ CCHHHCCCCCCCHHH	18.41	29255136
110	Phosphorylation	LATSPIPTEDQFFKD HCCCCCCCHHHCHHC	53.57	28102081
120	Phosphorylation	QFFKDIDTPLVKSGG HCHHCCCCCCCCCCC	20.89	21815630
125	Phosphorylation	IDTPLVKSGGDETPS CCCCCCCCCCCCCCC	40.29	28857561
130	Phosphorylation	VKSGGDETPSQSSDI CCCCCCCCCCCCCCC	32.74	28857561
132	Phosphorylation	SGGDETPSQSSDISH CCCCCCCCCCCCCCC	50.55	28270605
134	Phosphorylation	GDETPSQSSDISHVL CCCCCCCCCCCCCCE	34.02	28270605
135	Phosphorylation	DETPSQSSDISHVLE CCCCCCCCCCCCCEE	31.18	28270605
138	Phosphorylation	PSQSSDISHVLETET CCCCCCCCCCEEECC	16.72	28270605
143	Phosphorylation	DISHVLETETIFTPS CCCCCEEECCCCCHH	33.98	26270265
145	Phosphorylation	SHVLETETIFTPSSV CCCEEECCCCCHHHH	28.89	26270265
148	Phosphorylation	LETETIFTPSSVKKK EEECCCCCHHHHHHH	20.57	26270265
150	Phosphorylation	TETIFTPSSVKKKKR ECCCCCHHHHHHHHH	44.71	23186163
151	Phosphorylation	ETIFTPSSVKKKKRR CCCCCHHHHHHHHHH	38.88	23186163
174	Phosphorylation	KKEEQAASAAAEDTC HHHHHHHHHHHHHCC	22.81	28060719
180	Phosphorylation	ASAAAEDTCDVGVSS HHHHHHHCCCCCCCC	11.34	23927012
186	Phosphorylation	DTCDVGVSSDDDKGA HCCCCCCCCCCHHHH	23.32	23927012
187	Phosphorylation	TCDVGVSSDDDKGAQ CCCCCCCCCCHHHHH	42.53	23927012
199	Phosphorylation	GAQAARGSSNASLKE HHHHHCCCCCCCCCH	18.18	25627689
200	Phosphorylation	AQAARGSSNASLKEE HHHHCCCCCCCCCHH	38.96	25627689
203	Phosphorylation	ARGSSNASLKEEECK HCCCCCCCCCHHHHC	44.20	25159151
217	Phosphorylation	KEPLLFHSGDHYPLS CCCEEECCCCCCCCC	38.28	28270605
221	Phosphorylation	LFHSGDHYPLSDGDW EECCCCCCCCCCCCC	15.60	28270605
224	Phosphorylation	SGDHYPLSDGDWSPL CCCCCCCCCCCCCCC	34.73	25159151
229	Phosphorylation	PLSDGDWSPLETTYP CCCCCCCCCCCCCCC	25.09	25159151
233	Phosphorylation	GDWSPLETTYPQTAC CCCCCCCCCCCCCCC	39.03	28270605
234	Phosphorylation	DWSPLETTYPQTACP CCCCCCCCCCCCCCC	24.67	28270605
235	Phosphorylation	WSPLETTYPQTACPK CCCCCCCCCCCCCCC	10.77	28348404
243	Phosphorylation	PQTACPKSDSELEVK CCCCCCCCCCCCEEC	31.35	29255136
245	Phosphorylation	TACPKSDSELEVKPA CCCCCCCCCCEECCH	51.69	30266825
254	Phosphorylation	LEVKPAESLLRSESH CEECCHHHHHHCCCC	34.51	23927012
258	Phosphorylation	PAESLLRSESHMEWT CHHHHHHCCCCCCCC	43.34	27251275
260	Phosphorylation	ESLLRSESHMEWTWG HHHHHCCCCCCCCCC	29.40	27251275
287	Phosphorylation	RSDHHPRTATITPSE CCCCCCCCCEECCCC	32.38	29396449
289	Phosphorylation	DHHPRTATITPSENT CCCCCCCEECCCCCC	25.44	26657352
291	Phosphorylation	HPRTATITPSENTHF CCCCCEECCCCCCCE	19.19	26657352
293	Phosphorylation	RTATITPSENTHFRV CCCEECCCCCCCEEE	34.52	29396449
296	Phosphorylation	TITPSENTHFRVIPS EECCCCCCCEEECCC	20.52	29396449
303	Phosphorylation	THFRVIPSEDNLISE CCEEECCCCCCHHHH	46.59	20058876
309	Phosphorylation	PSEDNLISEVEKDAS CCCCCHHHHHHHCCC	38.46	24972180
384	Phosphorylation	KPAAKVDSPSKKKGV CCCCCCCCCCCCCCC	33.78	22817900
386	Phosphorylation	AAKVDSPSKKKGVHK CCCCCCCCCCCCCCC	62.14	22817900
393	Ubiquitination	SKKKGVHKRSQHQGP CCCCCCCCCCCCCCC	51.87	29967540
395	Phosphorylation	KKGVHKRSQHQGPDD CCCCCCCCCCCCCCC	36.50	27251275
404	Phosphorylation	HQGPDDIYLDDLKGL CCCCCCEEHHHCCCC	15.86	27642862
409	Ubiquitination	DIYLDDLKGLEPEVA CEEHHHCCCCCHHEE	69.33	29967540
419	Phosphorylation	EPEVAALYFPKSESE CHHEEEEECCCCCCC	17.07	27642862
425	Phosphorylation	LYFPKSESEPGSRQW EECCCCCCCCCCCCC	57.07	25072903
566	Phosphorylation	WFWRKRESMTKQLPE CEEEECHHHHCCCCC	35.47	15994876
568	Phosphorylation	WRKRESMTKQLPESK EEECHHHHCCCCCCC	25.56	22798277
574	Phosphorylation	MTKQLPESKEGKSEA HHCCCCCCCCCCCCC	33.78	-
604	Phosphorylation	ARPAENDSSSDEGSQ CCCCCCCCCCCCCCH	43.24	24275569
605	Phosphorylation	RPAENDSSSDEGSQE CCCCCCCCCCCCCHH	44.67	24275569
606	Phosphorylation	PAENDSSSDEGSQEL CCCCCCCCCCCCHHH	43.57	24275569
610	Phosphorylation	DSSSDEGSQELEESI CCCCCCCCHHHHHCE	20.59	24275569
781	Ubiquitination	FHREVIEKKPEKFKI HHHHHHHHCCHHCEE	63.60	-
865	Phosphorylation	EHVFPLLSKEQNSAF HHHHHHCCCCCCCCC	41.66	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:32008742

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LPIN2_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 LPIN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of LPIN2_HUMAN !!

Drug and Disease Associations

Kegg Disease
H01117	Majeed syndrome; Chronic recurrent multifocal osteomyelitis (CRMO)
OMIM Disease
609628	Majeed syndrome (MAJEEDS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LPIN2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASSSPECTROMETRY.	17081983 [Abstract]