dbPTM

LPP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LPP_HUMAN
UniProt AC	Q93052
Protein Name	Lipoma-preferred partner
Gene Name	LPP
Organism	Homo sapiens (Human).
Sequence Length	612
Subcellular Localization	Nucleus. Cytoplasm. Cell junction. Cell membrane. Found in the nucleus, in the cytoplasm and at cell adhesion sites. Shuttles between the cytoplasm and the nucleus. It has been found in sites of cell adhesion such as cell-to-cell contact and focal ad
Protein Description	May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus..
Protein Sequence	MSHPSWLPPKSTGEPLGHVPARMETTHSFGNPSISVSTQQPPKKFAPVVAPKPKYNPYKQPGGEGDFLPPPPPPLDDSSALPSISGNFPPPPPLDEEAFKVQGNPGGKTLEERRSSLDAEIDSLTSILADLECSSPYKPRPPQSSTGSTASPPVSTPVTGHKRMVIPNQPPLTATKKSTLKPQPAPQAGPIPVAPIGTLKPQPQPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAAPSSGQIYGSGPQGYNTQPVPVSGQCPPPSTRGGMDYAYIPPPGLQPEPGYGYAPNQGRYYEGYYAAGPGYGGRNDSDPTYGQQGHPNTWKREPGYTPPGAGNQNPPGMYPVTGPKKTYITDPVSAPCAPPLQPKGGHSGQLGPSSVAPSFRPEDELEHLTKKMLYDMENPPADEYFGRCARCGENVVGEGTGCTAMDQVFHVDCFTCIICNNKLRGQPFYAVEKKAYCEPCYINTLEQCNVCSKPIMERILRATGKAYHPHCFTCVMCHRSLDGIPFTVDAGGLIHCIEDFHKKFAPRCSVCKEPIMPAPGQEETVRIVALDRDFHVHCYRCEDCGGLLSEGDNQGCYPLDGHILCKTCNSARIRVLTAKASTDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MSHPSWLPPKST ---CCCCCCCCCCCC	35.50	27251275
11	Phosphorylation	PSWLPPKSTGEPLGH CCCCCCCCCCCCCCC	47.63	25159151
11	O-linked_Glycosylation	PSWLPPKSTGEPLGH CCCCCCCCCCCCCCC	47.63	30059200
12	Phosphorylation	SWLPPKSTGEPLGHV CCCCCCCCCCCCCCC	52.25	25159151
12	O-linked_Glycosylation	SWLPPKSTGEPLGHV CCCCCCCCCCCCCCC	52.25	30059200
25	Phosphorylation	HVPARMETTHSFGNP CCCCEEEEECCCCCC	22.07	28555341
25	O-linked_Glycosylation	HVPARMETTHSFGNP CCCCEEEEECCCCCC	22.07	30059200
26	O-linked_Glycosylation	VPARMETTHSFGNPS CCCEEEEECCCCCCC	11.38	30059200
26	Phosphorylation	VPARMETTHSFGNPS CCCEEEEECCCCCCC	11.38	28857561
28	Phosphorylation	ARMETTHSFGNPSIS CEEEEECCCCCCCEE	32.53	28857561
28	O-linked_Glycosylation	ARMETTHSFGNPSIS CEEEEECCCCCCCEE	32.53	30059200
33	Phosphorylation	THSFGNPSISVSTQQ ECCCCCCCEEEECCC	31.34	28857561
33	O-linked_Glycosylation	THSFGNPSISVSTQQ ECCCCCCCEEEECCC	31.34	30059200
35	Phosphorylation	SFGNPSISVSTQQPP CCCCCCEEEECCCCC	17.85	28857561
35	O-linked_Glycosylation	SFGNPSISVSTQQPP CCCCCCEEEECCCCC	17.85	30059200
43	Acetylation	VSTQQPPKKFAPVVA EECCCCCCCCCCCCC	68.18	26051181
44	Ubiquitination	STQQPPKKFAPVVAP ECCCCCCCCCCCCCC	53.16	-
44	Acetylation	STQQPPKKFAPVVAP ECCCCCCCCCCCCCC	53.16	25953088
52	Malonylation	FAPVVAPKPKYNPYK CCCCCCCCCCCCCCC	44.39	26320211
83	Phosphorylation	DDSSALPSISGNFPP CCCCCCCCCCCCCCC	30.18	27251275
85	Phosphorylation	SSALPSISGNFPPPP CCCCCCCCCCCCCCC	31.83	27251275
108	Acetylation	VQGNPGGKTLEERRS HCCCCCCCCHHHHHH	56.71	27452117
108	Ubiquitination	VQGNPGGKTLEERRS HCCCCCCCCHHHHHH	56.71	-
109	Phosphorylation	QGNPGGKTLEERRSS CCCCCCCCHHHHHHH	42.55	25159151
115	Phosphorylation	KTLEERRSSLDAEID CCHHHHHHHHHHHHH	41.28	25159151
116	Phosphorylation	TLEERRSSLDAEIDS CHHHHHHHHHHHHHH	28.58	25159151
123	Phosphorylation	SLDAEIDSLTSILAD HHHHHHHHHHHHHHH	38.93	28192239
125	Phosphorylation	DAEIDSLTSILADLE HHHHHHHHHHHHHHC	20.06	20068231
126	Phosphorylation	AEIDSLTSILADLEC HHHHHHHHHHHHHCC	22.39	20068231
134	Phosphorylation	ILADLECSSPYKPRP HHHHHCCCCCCCCCC	25.60	23090842
135	Phosphorylation	LADLECSSPYKPRPP HHHHCCCCCCCCCCC	43.86	18669648
137	Phosphorylation	DLECSSPYKPRPPQS HHCCCCCCCCCCCCC	35.26	23090842
144	Phosphorylation	YKPRPPQSSTGSTAS CCCCCCCCCCCCCCC	35.32	26657352
145	Phosphorylation	KPRPPQSSTGSTASP CCCCCCCCCCCCCCC	31.38	27251275
146	Phosphorylation	PRPPQSSTGSTASPP CCCCCCCCCCCCCCC	40.16	26657352
148	Phosphorylation	PPQSSTGSTASPPVS CCCCCCCCCCCCCCC	22.38	26657352
149	Phosphorylation	PQSSTGSTASPPVST CCCCCCCCCCCCCCC	32.28	25159151
151	Phosphorylation	SSTGSTASPPVSTPV CCCCCCCCCCCCCCC	29.80	25849741
155	Phosphorylation	STASPPVSTPVTGHK CCCCCCCCCCCCCCC	32.54	25627689
156	Phosphorylation	TASPPVSTPVTGHKR CCCCCCCCCCCCCCC	23.24	25849741
162	Acetylation	STPVTGHKRMVIPNQ CCCCCCCCCEECCCC	43.46	30590131
173	Phosphorylation	IPNQPPLTATKKSTL CCCCCCCCCCCCCCC	37.75	28555341
175	Phosphorylation	NQPPLTATKKSTLKP CCCCCCCCCCCCCCC	33.50	25159151
175	O-linked_Glycosylation	NQPPLTATKKSTLKP CCCCCCCCCCCCCCC	33.50	30059200
176	Acetylation	QPPLTATKKSTLKPQ CCCCCCCCCCCCCCC	42.11	26051181
181	Acetylation	ATKKSTLKPQPAPQA CCCCCCCCCCCCCCC	41.52	26051181
198	O-linked_Glycosylation	IPVAPIGTLKPQPQP CCEECCCCCCCCCCC	32.12	30059200
200	Acetylation	VAPIGTLKPQPQPVP EECCCCCCCCCCCCC	41.25	26051181
209	O-linked_Glycosylation	QPQPVPASYTTASTS CCCCCCCCEECCCCC	19.55	30059200
211	O-linked_Glycosylation	QPVPASYTTASTSSR CCCCCCEECCCCCCC	17.25	30059200
212	O-linked_Glycosylation	PVPASYTTASTSSRP CCCCCEECCCCCCCC	15.46	30059200
227	Phosphorylation	TFNVQVKSAQPSPHY EEEEEEECCCCCCCE	33.02	21945579
231	Phosphorylation	QVKSAQPSPHYMAAP EEECCCCCCCEEECC	16.54	21945579
234	Phosphorylation	SAQPSPHYMAAPSSG CCCCCCCEEECCCCC	7.57	21945579
239	Phosphorylation	PHYMAAPSSGQIYGS CCEEECCCCCCCCCC	42.23	21945579
240	Phosphorylation	HYMAAPSSGQIYGSG CEEECCCCCCCCCCC	33.39	21945579
244	Phosphorylation	APSSGQIYGSGPQGY CCCCCCCCCCCCCCC	9.43	21945579
246	Phosphorylation	SSGQIYGSGPQGYNT CCCCCCCCCCCCCCC	30.26	21945579
251	Phosphorylation	YGSGPQGYNTQPVPV CCCCCCCCCCCCCCC	15.13	21945579
253	Phosphorylation	SGPQGYNTQPVPVSG CCCCCCCCCCCCCCC	26.26	21945579
259	Phosphorylation	NTQPVPVSGQCPPPS CCCCCCCCCCCCCCC	19.65	21945579
266	Phosphorylation	SGQCPPPSTRGGMDY CCCCCCCCCCCCCCE	36.19	21945579
267	Phosphorylation	GQCPPPSTRGGMDYA CCCCCCCCCCCCCEE	38.82	21945579
271	Sulfoxidation	PPSTRGGMDYAYIPP CCCCCCCCCEEECCC	3.87	30846556
273	Phosphorylation	STRGGMDYAYIPPPG CCCCCCCEEECCCCC	7.75	21945579
275	Phosphorylation	RGGMDYAYIPPPGLQ CCCCCEEECCCCCCC	14.02	21945579
287	Phosphorylation	GLQPEPGYGYAPNQG CCCCCCCCCCCCCCC	20.06	21945579
289	Phosphorylation	QPEPGYGYAPNQGRY CCCCCCCCCCCCCCC	15.48	21945579
296	Phosphorylation	YAPNQGRYYEGYYAA CCCCCCCCEEEEEEC	16.82	21945579
297	Phosphorylation	APNQGRYYEGYYAAG CCCCCCCEEEEEECC	11.08	21945579
300	Phosphorylation	QGRYYEGYYAAGPGY CCCCEEEEEECCCCC	4.31	21945579
301	Phosphorylation	GRYYEGYYAAGPGYG CCCEEEEEECCCCCC	10.79	21945579
307	Phosphorylation	YYAAGPGYGGRNDSD EEECCCCCCCCCCCC	21.38	21945579
313	Phosphorylation	GYGGRNDSDPTYGQQ CCCCCCCCCCCCCCC	49.38	21945579
316	Phosphorylation	GRNDSDPTYGQQGHP CCCCCCCCCCCCCCC	45.32	21945579
317	Phosphorylation	RNDSDPTYGQQGHPN CCCCCCCCCCCCCCC	20.51	21945579
325	Phosphorylation	GQQGHPNTWKREPGY CCCCCCCCCCCCCCC	36.49	21945579
327	Acetylation	QGHPNTWKREPGYTP CCCCCCCCCCCCCCC	44.86	25953088
327	Sumoylation	QGHPNTWKREPGYTP CCCCCCCCCCCCCCC	44.86	25114211
327	Ubiquitination	QGHPNTWKREPGYTP CCCCCCCCCCCCCCC	44.86	-
332	Phosphorylation	TWKREPGYTPPGAGN CCCCCCCCCCCCCCC	27.13	21945579
333	Phosphorylation	WKREPGYTPPGAGNQ CCCCCCCCCCCCCCC	28.99	21945579
345	Sulfoxidation	GNQNPPGMYPVTGPK CCCCCCCCCCCCCCC	4.16	30846556
346	Phosphorylation	NQNPPGMYPVTGPKK CCCCCCCCCCCCCCC	10.64	21945579
349	Phosphorylation	PPGMYPVTGPKKTYI CCCCCCCCCCCCCEE	43.17	21945579
352	Ubiquitination	MYPVTGPKKTYITDP CCCCCCCCCCEECCC	60.12	-
352	Acetylation	MYPVTGPKKTYITDP CCCCCCCCCCEECCC	60.12	26051181
353	Methylation	YPVTGPKKTYITDPV CCCCCCCCCEECCCC	50.09	115972579
354	Phosphorylation	PVTGPKKTYITDPVS CCCCCCCCEECCCCC	26.70	28152594
355	Phosphorylation	VTGPKKTYITDPVSA CCCCCCCEECCCCCC	15.65	28152594
357	Phosphorylation	GPKKTYITDPVSAPC CCCCCEECCCCCCCC	24.68	28152594
361	Phosphorylation	TYITDPVSAPCAPPL CEECCCCCCCCCCCC	31.70	28152594
371	Ubiquitination	CAPPLQPKGGHSGQL CCCCCCCCCCCCCCC	65.64	-
375	Phosphorylation	LQPKGGHSGQLGPSS CCCCCCCCCCCCCCC	31.35	25159151
381	Phosphorylation	HSGQLGPSSVAPSFR CCCCCCCCCCCCCCC	35.33	28555341
382	Phosphorylation	SGQLGPSSVAPSFRP CCCCCCCCCCCCCCC	25.98	28555341
386	Phosphorylation	GPSSVAPSFRPEDEL CCCCCCCCCCCHHHH	24.93	27251275
397	Phosphorylation	EDELEHLTKKMLYDM HHHHHHHHHHHHHCC	30.44	20873877
398	Ubiquitination	DELEHLTKKMLYDME HHHHHHHHHHHHCCC	42.41	-
400	Sulfoxidation	LEHLTKKMLYDMENP HHHHHHHHHHCCCCC	4.46	30846556
402	Phosphorylation	HLTKKMLYDMENPPA HHHHHHHHCCCCCCH	15.11	28796482
404	Sulfoxidation	TKKMLYDMENPPADE HHHHHHCCCCCCHHH	3.20	30846556
412	Phosphorylation	ENPPADEYFGRCARC CCCCHHHHCCCCCCC	16.33	22817900
461	Ubiquitination	QPFYAVEKKAYCEPC CCEEEEECCEECEEC	35.78	-
461	Malonylation	QPFYAVEKKAYCEPC CCEEEEECCEECEEC	35.78	26320211
469	Phosphorylation	KAYCEPCYINTLEQC CEECEECCCCCHHHC	14.12	-
504	Sulfoxidation	PHCFTCVMCHRSLDG CCCEEHHEECCCCCC	1.41	30846556
508	Phosphorylation	TCVMCHRSLDGIPFT EHHEECCCCCCCCEE	13.72	26657352
537	Phosphorylation	KKFAPRCSVCKEPIM HHHCCCCCCCCCCCC	31.65	26657352
544	Sulfoxidation	SVCKEPIMPAPGQEE CCCCCCCCCCCCCCC	3.20	30846556
567	Phosphorylation	RDFHVHCYRCEDCGG CCEEEEEEECCCCCC	11.92	-
577	Phosphorylation	EDCGGLLSEGDNQGC CCCCCCCCCCCCCCC	44.57	27251275
585	Phosphorylation	EGDNQGCYPLDGHIL CCCCCCCEECCCEEE	17.41	22817900
605	Phosphorylation	SARIRVLTAKASTDL CCEEEEEEEECCCCC	24.21	22199227
607	Ubiquitination	RIRVLTAKASTDL-- EEEEEEEECCCCC--	37.32	-
609	Phosphorylation	RVLTAKASTDL---- EEEEEECCCCC----	23.03	26846344
610	Phosphorylation	VLTAKASTDL----- EEEEECCCCC-----	46.29	26846344

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
244	Y	Phosphorylation	Kinase	SRC	P12931	PSP
300	Y	Phosphorylation	Kinase	SRC	P12931	PSP
301	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EGLN2_HUMAN	EGLN2	physical	22286099
VHL_HUMAN	VHL	physical	22286099
PNPO_HUMAN	PNPO	physical	22939629
AGFG1_HUMAN	AGFG1	physical	22863883
HEM2_HUMAN	ALAD	physical	22863883
ARPC3_HUMAN	ARPC3	physical	22863883
ARPC4_HUMAN	ARPC4	physical	22863883
CALR_HUMAN	CALR	physical	22863883
DBNL_HUMAN	DBNL	physical	22863883
HPBP1_HUMAN	HSPBP1	physical	22863883
IPO11_HUMAN	IPO11	physical	22863883
P3H1_HUMAN	P3H1	physical	22863883
NIF3L_HUMAN	NIF3L1	physical	22863883
NPL4_HUMAN	NPLOC4	physical	22863883
OGT1_HUMAN	OGT	physical	22863883
PPME1_HUMAN	PPME1	physical	22863883
2A5D_HUMAN	PPP2R5D	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
RADI_HUMAN	RDX	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
UBE3A_HUMAN	UBE3A	physical	22863883
ZPR1_HUMAN	ZPR1	physical	22863883

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 LPP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND THR-397, ANDMASS SPECTROMETRY.	18187866 [Abstract]
"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-333, AND MASSSPECTROMETRY.	18669648 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300 AND TYR-301, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-317, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301 AND TYR-317, ANDMASS SPECTROMETRY.	16094384 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300; TYR-301 ANDTYR-317, AND MASS SPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND MASSSPECTROMETRY.	15951569 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-297 AND TYR-300, ANDMASS SPECTROMETRY.	15144186 [Abstract]
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND MASSSPECTROMETRY.	12522270 [Abstract]