LPIN3_HUMAN - dbPTM
LPIN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LPIN3_HUMAN
UniProt AC Q9BQK8
Protein Name Phosphatidate phosphatase LPIN3
Gene Name LPIN3
Organism Homo sapiens (Human).
Sequence Length 851
Subcellular Localization Nucleus .
Protein Description Regulates fatty acid metabolism. Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis (By similarity)..
Protein Sequence MNYVGQLAETVFGTVKELYRGLNPATLSGGIDVLVVKQVDGSFRCSPFHVRFGKLGVLRSREKVVDIELNGEPVDLHMKLGDSGEAFFVQELESDDEHVPPGLCTSPIPWGGLSGFPSDSQLGTASEPEGLVMAGTASTGRRKRRRRRKPKQKEDAVATDSSPEELEAGAESELSLPEKLRPEPPGVQLEEKSSLQPKDIYPYSDGEWPPQASLSAGELTSPKSDSELEVRTPEPSPLRAESHMQWAWGRLPKVARAERPESSVVLEGRAGATSPPRGGPSTPSTSVAGGVDPLGLPIQQTEAGADLQPDTEDPTLVGPPLHTPETEESKTQSSGDMGLPPASKSWSWATLEVPVPTGQPERVSRGKGSPKRSQHLGPSDIYLDDLPSLDSENAALYFPQSDSGLGARRWSEPSSQKSLRDPNPEHEPEPTLDTVDTIALSLCGGLADSRDISLEKFNQHSVSYQDLTKNPGLLDDPNLVVKINGKHYNWAVAAPMILSLQAFQKNLPKSTMDKLEREKMPRKGGRWWFSWRRRDFLAEERSAQKEKTAAKEQQGEKTEVLSSDDDAPDSPVILEIPSLPPSTPPSTPTYKKSLRLSSDQIRRLNLQEGANDVVFSVTTQYQGTCRCKATIYLWKWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGITSLYHKIQLNGYKFLYCSARAIGMADLTKGYLQWVSEGGCSLPKGPILLSPSSLFSALHREVIEKKPEVFKVACLSDIQQLFLPHGQPFYAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQELIKNHKSTYERLGEVVELLFPPVARGPSTDLANPEYSNFCYWREPLPAVDLDTLD
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 Orthologous
Protein Cluster
3Phosphorylation-----MNYVGQLAET
-----CCHHHHHHHH		12.5022210691
14PhosphorylationLAETVFGTVKELYRG
HHHHHHHHHHHHHCC		19.5526074081
19PhosphorylationFGTVKELYRGLNPAT
HHHHHHHHCCCCHHH		12.0626074081
26PhosphorylationYRGLNPATLSGGIDV
HCCCCHHHHCCCEEE		23.7826074081
159PhosphorylationQKEDAVATDSSPEEL
HHHCCCCCCCCHHHH		29.8028102081
161PhosphorylationEDAVATDSSPEELEA
HCCCCCCCCHHHHHH		43.3628102081
162PhosphorylationDAVATDSSPEELEAG
CCCCCCCCHHHHHHH		38.8628102081
172PhosphorylationELEAGAESELSLPEK
HHHHHCCCCCCCCHH		43.2229802988
175PhosphorylationAGAESELSLPEKLRP
HHCCCCCCCCHHHCC		37.5128102081
179AcetylationSELSLPEKLRPEPPG
CCCCCCHHHCCCCCC		48.107494215
187 (in isoform 2)Phosphorylation-7.8725849741
201PhosphorylationSLQPKDIYPYSDGEW
CCCCCCCCCCCCCCC		13.2723090842
203PhosphorylationQPKDIYPYSDGEWPP
CCCCCCCCCCCCCCC		11.4822617229
204PhosphorylationPKDIYPYSDGEWPPQ
CCCCCCCCCCCCCCC		34.3429116813
213PhosphorylationGEWPPQASLSAGELT
CCCCCCCCCCCCCCC		20.0128348404
215PhosphorylationWPPQASLSAGELTSP
CCCCCCCCCCCCCCC		31.5628348404
220PhosphorylationSLSAGELTSPKSDSE
CCCCCCCCCCCCCCC		38.3923090842
221PhosphorylationLSAGELTSPKSDSEL
CCCCCCCCCCCCCCC		42.8523090842
224PhosphorylationGELTSPKSDSELEVR
CCCCCCCCCCCCEEC		50.1530266825
226PhosphorylationLTSPKSDSELEVRTP
CCCCCCCCCCEECCC		51.6930266825
232PhosphorylationDSELEVRTPEPSPLR
CCCCEECCCCCCCCC		36.8623312004
236PhosphorylationEVRTPEPSPLRAESH
EECCCCCCCCCCHHH		34.6023312004
262PhosphorylationARAERPESSVVLEGR
CCCCCCCCCEEEEEC		30.9928555341
263PhosphorylationRAERPESSVVLEGRA
CCCCCCCCEEEEECC		18.0028555341
273PhosphorylationLEGRAGATSPPRGGP
EEECCCCCCCCCCCC		40.6326699800
274PhosphorylationEGRAGATSPPRGGPS
EECCCCCCCCCCCCC		32.1625849741
281PhosphorylationSPPRGGPSTPSTSVA
CCCCCCCCCCCCCCC		57.1122468782
282PhosphorylationPPRGGPSTPSTSVAG
CCCCCCCCCCCCCCC		25.1327251275
284PhosphorylationRGGPSTPSTSVAGGV
CCCCCCCCCCCCCCC		33.1427251275
285PhosphorylationGGPSTPSTSVAGGVD
CCCCCCCCCCCCCCC		28.5527251275
286PhosphorylationGPSTPSTSVAGGVDP
CCCCCCCCCCCCCCC		17.8227251275
345PhosphorylationGLPPASKSWSWATLE
CCCCCCCCCEEEEEE		24.6928857561
347PhosphorylationPPASKSWSWATLEVP
CCCCCCCEEEEEEEE		17.5828857561
364PhosphorylationTGQPERVSRGKGSPK
CCCCHHHCCCCCCCC		41.35-
369PhosphorylationRVSRGKGSPKRSQHL
HHCCCCCCCCHHCCC		30.63-
398 (in isoform 2)Phosphorylation-4.6427642862
411PhosphorylationGLGARRWSEPSSQKS
CCCCCCCCCCCCCCC		37.5122617229
412PhosphorylationLGARRWSEPSSQKSL
CCCCCCCCCCCCCCC		42.0932142685
414PhosphorylationARRWSEPSSQKSLRD
CCCCCCCCCCCCCCC		41.1527794612
415PhosphorylationRRWSEPSSQKSLRDP
CCCCCCCCCCCCCCC		52.9527794612
461PhosphorylationLEKFNQHSVSYQDLT
HHHHHHCCCCHHHHC		11.7323312004
463PhosphorylationKFNQHSVSYQDLTKN
HHHHCCCCHHHHCCC		21.7925849741
464PhosphorylationFNQHSVSYQDLTKNP
HHHCCCCHHHHCCCC		12.1423186163
542PhosphorylationDFLAEERSAQKEKTA
HHHHHHHHHHHHHHH		38.0328555341
563PhosphorylationEKTEVLSSDDDAPDS
CCEEECCCCCCCCCC		40.6828961369
582PhosphorylationEIPSLPPSTPPSTPT
ECCCCCCCCCCCCCC		52.1627251275
583PhosphorylationIPSLPPSTPPSTPTY
CCCCCCCCCCCCCCC		45.0227251275
586PhosphorylationLPPSTPPSTPTYKKS
CCCCCCCCCCCCHHH		48.5027251275
587PhosphorylationPPSTPPSTPTYKKSL
CCCCCCCCCCCHHHH		25.9827251275
597PhosphorylationYKKSLRLSSDQIRRL
CHHHHCCCHHHHHHC		25.9922617229
598PhosphorylationKKSLRLSSDQIRRLN
HHHHCCCHHHHHHCH		37.8222617229
736UbiquitinationLHREVIEKKPEVFKV
HHHHHHHHCCCCEEE		63.60-
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 LPIN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LPIN3_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 LPIN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LPIN2_HUMANLPIN2physical
28514442
LPIN1_HUMANLPIN1physical
28514442
KKCC1_HUMANCAMKK1physical
28514442
BIRC2_HUMANBIRC2physical
28514442
HDAC6_HUMANHDAC6physical
28514442
EST1A_HUMANSMG6physical
28514442
CSK22_HUMANCSNK2A2physical
28514442
CSK21_HUMANCSNK2A1physical
28514442
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CING_HUMANCGNphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
MAST3_HUMANMAST3physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
TANC2_HUMANTANC2physical
27173435
RGPS2_HUMANRALGPS2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
NF1_HUMANNF1physical
27173435
CBY1_HUMANCBY1physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
HDAC4_HUMANHDAC4physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
NADK_HUMANNADKphysical
27173435
CWC25_HUMANCWC25physical
27173435
INP5E_HUMANINPP5Ephysical
27173435
RPTOR_HUMANRPTORphysical
27173435
NGAP_HUMANRASAL2physical
27173435
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 LPIN3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159; SER-161 ANDSER-162, AND MASS SPECTROMETRY.

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