dbPTM

LAP2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LAP2A_HUMAN
UniProt AC	P42166
Protein Name	Lamina-associated polypeptide 2, isoform alpha
Gene Name	TMPO
Organism	Homo sapiens (Human).
Sequence Length	694
Subcellular Localization	Nucleus. Chromosome. Expressed diffusely throughout the nucleus.
Protein Description	May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1.; TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide..
Protein Sequence	MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLPAGTNSKGPPDFSSDEEREPTPVLGSGAAAAGRSRAAVGRKATKKTDKPRQEDKDDLDVTELTNEDLLDQLVKYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTISSSAENTRQNGSNDSDRYSDNEEGKKKEHKKVKSTRDIVPFSELGTTPSGGGFFQGISFPEISTRPPLGSTELQAAKKVHTSKGDLPREPLVATNLPGRGQLQKLASERNLFISCKSSHDRCLEKSSSSSSQPEHSAMLVSTAASPSLIKETTTGYYKDIVENICGREKSGIQPLCPERSHISDQSPLSSKRKALEESESSQLISPPLAQAIRDYVNSLLVQGGVGSLPGTSNSMPPLDVENIQKRIDQSKFQETEFLSPPRKVPRLSEKSVEERDSGSFVAFQNIPGSELMSSFAKTVVSHSLTTLGLEVAKQSQHDKIDASELSFPFHESILKVIEEEWQQVDRQLPSLACKYPVSSREATQILSVPKVDDEILGFISEATPLGGIQAASTESCNQQLDLALCRAYEAAASALQIATHTAFVAKAMQADISQAAQILSSDPSRTHQALGILSKTYDAASYICEAAFDEVKMAAHTMGNATVGRRYLWLKDCKINLASKNKLASTPFKGGTLFGGEVCKVIKKRGNKH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	PEFLEDPSVLTKDKL CCCCCCCCCCCHHHH	41.92	20068231
12	Phosphorylation	LEDPSVLTKDKLKSE CCCCCCCCHHHHHHH	34.73	20068231
13	Sumoylation	EDPSVLTKDKLKSEL CCCCCCCHHHHHHHH	49.02	-
13	Ubiquitination	EDPSVLTKDKLKSEL CCCCCCCHHHHHHHH	49.02	-
13	2-Hydroxyisobutyrylation	EDPSVLTKDKLKSEL CCCCCCCHHHHHHHH	49.02	-
13	Malonylation	EDPSVLTKDKLKSEL CCCCCCCHHHHHHHH	49.02	26320211
13	Acetylation	EDPSVLTKDKLKSEL CCCCCCCHHHHHHHH	49.02	27452117
13	Succinylation	EDPSVLTKDKLKSEL CCCCCCCHHHHHHHH	49.02	23954790
17	Sumoylation	VLTKDKLKSELVANN CCCHHHHHHHHHHCC	47.85	-
17	Ubiquitination	VLTKDKLKSELVANN CCCHHHHHHHHHHCC	47.85	-
18	Phosphorylation	LTKDKLKSELVANNV CCHHHHHHHHHHCCC	46.75	27050516
26	Phosphorylation	ELVANNVTLPAGEQR HHHHCCCEECCCCCH	29.19	25159151
37	Phosphorylation	GEQRKDVYVQLYLQH CCCHHHHHHHHHHHH	7.81	28152594
46	Phosphorylation	QLYLQHLTARNRPPL HHHHHHHHHCCCCCC	22.80	22210691
50	Methylation	QHLTARNRPPLPAGT HHHHHCCCCCCCCCC	28.76	-
57	Phosphorylation	RPPLPAGTNSKGPPD CCCCCCCCCCCCCCC	38.12	23927012
59	Phosphorylation	PLPAGTNSKGPPDFS CCCCCCCCCCCCCCC	38.54	25159151
60	Ubiquitination	LPAGTNSKGPPDFSS CCCCCCCCCCCCCCC	76.99	21906983
60	Acetylation	LPAGTNSKGPPDFSS CCCCCCCCCCCCCCC	76.99	26051181
66	Phosphorylation	SKGPPDFSSDEEREP CCCCCCCCCCCCCCC	44.23	19664994
67	Phosphorylation	KGPPDFSSDEEREPT CCCCCCCCCCCCCCC	49.38	19664994
74	Phosphorylation	SDEEREPTPVLGSGA CCCCCCCCCCCCCHH	22.67	19664994
79	Phosphorylation	EPTPVLGSGAAAAGR CCCCCCCCHHHHHCC	22.54	23927012
86	Methylation	SGAAAAGRSRAAVGR CHHHHHCCCHHHHCC	20.45	-
87	Phosphorylation	GAAAAGRSRAAVGRK HHHHHCCCHHHHCCC	25.92	26074081
88	Methylation	AAAAGRSRAAVGRKA HHHHCCCHHHHCCCC	25.79	-
94	Methylation	SRAAVGRKATKKTDK CHHHHCCCCCCCCCC	55.25	23748837
96	Phosphorylation	AAVGRKATKKTDKPR HHHCCCCCCCCCCCC	35.79	17287340
99	Phosphorylation	GRKATKKTDKPRQED CCCCCCCCCCCCCCC	51.30	17287340
107	Ubiquitination	DKPRQEDKDDLDVTE CCCCCCCCCCCCHHH	53.00	21906983
107	Acetylation	DKPRQEDKDDLDVTE CCCCCCCCCCCCHHH	53.00	26051181
113	Phosphorylation	DKDDLDVTELTNEDL CCCCCCHHHHCCHHH	25.58	24732914
116	Phosphorylation	DLDVTELTNEDLLDQ CCCHHHHCCHHHHHH	30.26	24732914
126	Ubiquitination	DLLDQLVKYGVNPGP HHHHHHHHCCCCCCC	44.90	-
127	Phosphorylation	LLDQLVKYGVNPGPI HHHHHHHCCCCCCCC	20.87	28152594
137	Phosphorylation	NPGPIVGTTRKLYEK CCCCCCCHHHHHHHH	16.72	25159151
138	Phosphorylation	PGPIVGTTRKLYEKK CCCCCCHHHHHHHHH	21.63	30001349
154	Phosphorylation	LKLREQGTESRSSTP HHHHHCCCCCCCCCC	30.40	22167270
156	Phosphorylation	LREQGTESRSSTPLP HHHCCCCCCCCCCCC	36.98	22167270
158	Phosphorylation	EQGTESRSSTPLPTI HCCCCCCCCCCCCCC	48.09	22167270
159	Phosphorylation	QGTESRSSTPLPTIS CCCCCCCCCCCCCCC	32.69	22167270
160	Phosphorylation	GTESRSSTPLPTISS CCCCCCCCCCCCCCC	30.05	29255136
164	Phosphorylation	RSSTPLPTISSSAEN CCCCCCCCCCCCCCC	40.97	22167270
166	Phosphorylation	STPLPTISSSAENTR CCCCCCCCCCCCCCC	22.25	22167270
167	Phosphorylation	TPLPTISSSAENTRQ CCCCCCCCCCCCCCC	29.71	22167270
168	Phosphorylation	PLPTISSSAENTRQN CCCCCCCCCCCCCCC	32.58	22167270
172	Phosphorylation	ISSSAENTRQNGSND CCCCCCCCCCCCCCC	25.74	30278072
177	Phosphorylation	ENTRQNGSNDSDRYS CCCCCCCCCCCCCCC	45.04	26329039
180	Phosphorylation	RQNGSNDSDRYSDNE CCCCCCCCCCCCCCC	28.39	23401153
182	Methylation	NGSNDSDRYSDNEEG CCCCCCCCCCCCCHH	36.49	115918657
183	Phosphorylation	GSNDSDRYSDNEEGK CCCCCCCCCCCCHHH	25.93	26329039
184	Phosphorylation	SNDSDRYSDNEEGKK CCCCCCCCCCCHHHH	34.55	22167270
211	Phosphorylation	VPFSELGTTPSGGGF CCHHHCCCCCCCCCC	48.43	20068231
212	Phosphorylation	PFSELGTTPSGGGFF CHHHCCCCCCCCCCC	17.41	26074081
214	Phosphorylation	SELGTTPSGGGFFQG HHCCCCCCCCCCCCC	48.23	26074081
235	Phosphorylation	STRPPLGSTELQAAK CCCCCCCCHHHHHHH	26.79	20068231
246	Phosphorylation	QAAKKVHTSKGDLPR HHHHHHCCCCCCCCC	34.81	20068231
247	Phosphorylation	AAKKVHTSKGDLPRE HHHHHCCCCCCCCCC	21.55	-
248	Ubiquitination	AKKVHTSKGDLPREP HHHHCCCCCCCCCCC	58.56	-
259	Phosphorylation	PREPLVATNLPGRGQ CCCCEEECCCCCHHH	29.79	28555341
264	Methylation	VATNLPGRGQLQKLA EECCCCCHHHHHHHH	27.95	115918661
269	Sumoylation	PGRGQLQKLASERNL CCHHHHHHHHHHCCC	55.39	-
269	Ubiquitination	PGRGQLQKLASERNL CCHHHHHHHHHHCCC	55.39	-
269	Sumoylation	PGRGQLQKLASERNL CCHHHHHHHHHHCCC	55.39	-
269	Acetylation	PGRGQLQKLASERNL CCHHHHHHHHHHCCC	55.39	26051181
272	Phosphorylation	GQLQKLASERNLFIS HHHHHHHHHCCCEEE	47.74	25159151
279	Phosphorylation	SERNLFISCKSSHDR HHCCCEEEECCHHHH	14.25	23403867
281	Methylation	RNLFISCKSSHDRCL CCCEEEECCHHHHHH	48.48	42373573
281	Sumoylation	RNLFISCKSSHDRCL CCCEEEECCHHHHHH	48.48	-
281	Ubiquitination	RNLFISCKSSHDRCL CCCEEEECCHHHHHH	48.48	21906983
281	Sumoylation	RNLFISCKSSHDRCL CCCEEEECCHHHHHH	48.48	-
281	Acetylation	RNLFISCKSSHDRCL CCCEEEECCHHHHHH	48.48	25953088
283	Phosphorylation	LFISCKSSHDRCLEK CEEEECCHHHHHHHC	18.20	28555341
290	Ubiquitination	SHDRCLEKSSSSSSQ HHHHHHHCCCCCCCC	42.56	-
290	Acetylation	SHDRCLEKSSSSSSQ HHHHHHHCCCCCCCC	42.56	26051181
291	Phosphorylation	HDRCLEKSSSSSSQP HHHHHHCCCCCCCCC	26.52	28787133
292	Phosphorylation	DRCLEKSSSSSSQPE HHHHHCCCCCCCCCC	45.36	28348404
293	Phosphorylation	RCLEKSSSSSSQPEH HHHHCCCCCCCCCCH	41.13	25159151
294	Phosphorylation	CLEKSSSSSSQPEHS HHHCCCCCCCCCCHH	35.64	25159151
295	Phosphorylation	LEKSSSSSSQPEHSA HHCCCCCCCCCCHHH	34.63	25159151
296	Phosphorylation	EKSSSSSSQPEHSAM HCCCCCCCCCCHHHH	52.26	25159151
301	Phosphorylation	SSSQPEHSAMLVSTA CCCCCCHHHHHHHHC	17.45	25159151
303	Sulfoxidation	SQPEHSAMLVSTAAS CCCCHHHHHHHHCCC	4.21	21406390
306	Phosphorylation	EHSAMLVSTAASPSL CHHHHHHHHCCCHHH	14.36	27794612
307	Phosphorylation	HSAMLVSTAASPSLI HHHHHHHHCCCHHHH	20.82	27794612
310	Phosphorylation	MLVSTAASPSLIKET HHHHHCCCHHHHHHC	16.74	25159151
312	Phosphorylation	VSTAASPSLIKETTT HHHCCCHHHHHHCCC	39.99	27794612
315	Ubiquitination	AASPSLIKETTTGYY CCCHHHHHHCCCCHH	55.06	-
318	Phosphorylation	PSLIKETTTGYYKDI HHHHHHCCCCHHHHH	21.22	28796482
319	Phosphorylation	SLIKETTTGYYKDIV HHHHHCCCCHHHHHH	30.52	28796482
321	Phosphorylation	IKETTTGYYKDIVEN HHHCCCCHHHHHHHH	12.78	28796482
322	Phosphorylation	KETTTGYYKDIVENI HHCCCCHHHHHHHHH	11.97	28796482
323	Ubiquitination	ETTTGYYKDIVENIC HCCCCHHHHHHHHHH	32.28	-
323	Acetylation	ETTTGYYKDIVENIC HCCCCHHHHHHHHHH	32.28	26051181
334	Ubiquitination	ENICGREKSGIQPLC HHHHCCCCCCCCCCC	53.25	-
334	2-Hydroxyisobutyrylation	ENICGREKSGIQPLC HHHHCCCCCCCCCCC	53.25	-
334	Acetylation	ENICGREKSGIQPLC HHHHCCCCCCCCCCC	53.25	25953088
335	Phosphorylation	NICGREKSGIQPLCP HHHCCCCCCCCCCCC	36.05	24732914
345	Phosphorylation	QPLCPERSHISDQSP CCCCCCCCCCCCCCC	24.42	22167270
348	Phosphorylation	CPERSHISDQSPLSS CCCCCCCCCCCCCHH	24.95	30266825
351	Phosphorylation	RSHISDQSPLSSKRK CCCCCCCCCCHHHHH	32.57	22167270
354	Phosphorylation	ISDQSPLSSKRKALE CCCCCCCHHHHHHHH	36.88	22167270
355	Phosphorylation	SDQSPLSSKRKALEE CCCCCCHHHHHHHHH	44.13	22167270
356	Acetylation	DQSPLSSKRKALEES CCCCCHHHHHHHHHH	55.32	25953088
356	Sumoylation	DQSPLSSKRKALEES CCCCCHHHHHHHHHH	55.32	-
356	Ubiquitination	DQSPLSSKRKALEES CCCCCHHHHHHHHHH	55.32	-
356	Sumoylation	DQSPLSSKRKALEES CCCCCHHHHHHHHHH	55.32	-
358	Ubiquitination	SPLSSKRKALEESES CCCHHHHHHHHHHHH	62.15	-
363	Phosphorylation	KRKALEESESSQLIS HHHHHHHHHHHCCCC	33.14	24732914
365	Phosphorylation	KALEESESSQLISPP HHHHHHHHHCCCCHH	32.44	24732914
366	Phosphorylation	ALEESESSQLISPPL HHHHHHHHCCCCHHH	25.59	25159151
370	Phosphorylation	SESSQLISPPLAQAI HHHHCCCCHHHHHHH	29.11	25159151
392	Phosphorylation	LVQGGVGSLPGTSNS HHCCCCCCCCCCCCC	29.05	28348404
396	Phosphorylation	GVGSLPGTSNSMPPL CCCCCCCCCCCCCCC	23.85	28348404
397	Phosphorylation	VGSLPGTSNSMPPLD CCCCCCCCCCCCCCC	32.59	28348404
399	Phosphorylation	SLPGTSNSMPPLDVE CCCCCCCCCCCCCHH	32.22	28348404
410	Ubiquitination	LDVENIQKRIDQSKF CCHHHHHHHHHHHHC	47.74	-
415	Phosphorylation	IQKRIDQSKFQETEF HHHHHHHHHCCCCCC	31.52	24732914
416	Ubiquitination	QKRIDQSKFQETEFL HHHHHHHHCCCCCCC	45.49	21906983
416	2-Hydroxyisobutyrylation	QKRIDQSKFQETEFL HHHHHHHHCCCCCCC	45.49	-
416	Acetylation	QKRIDQSKFQETEFL HHHHHHHHCCCCCCC	45.49	26051181
420	Phosphorylation	DQSKFQETEFLSPPR HHHHCCCCCCCCCCC	22.66	23927012
424	Phosphorylation	FQETEFLSPPRKVPR CCCCCCCCCCCCCCC	37.87	19664994
428	Ubiquitination	EFLSPPRKVPRLSEK CCCCCCCCCCCCCCC	63.47	-
433	Phosphorylation	PRKVPRLSEKSVEER CCCCCCCCCCCCCCC	44.23	26055452
435	Acetylation	KVPRLSEKSVEERDS CCCCCCCCCCCCCCC	57.32	23749302
435	Ubiquitination	KVPRLSEKSVEERDS CCCCCCCCCCCCCCC	57.32	21906983
436	Phosphorylation	VPRLSEKSVEERDSG CCCCCCCCCCCCCCC	30.61	23401153
442	Phosphorylation	KSVEERDSGSFVAFQ CCCCCCCCCCEEEEE	42.42	25159151
444	Phosphorylation	VEERDSGSFVAFQNI CCCCCCCCEEEEECC	22.09	25159151
454	Phosphorylation	AFQNIPGSELMSSFA EEECCCHHHHHHHHH	23.39	24719451
457	Sulfoxidation	NIPGSELMSSFAKTV CCCHHHHHHHHHHHH	2.50	21406390
458	Phosphorylation	IPGSELMSSFAKTVV CCHHHHHHHHHHHHH	34.62	20068231
459	Phosphorylation	PGSELMSSFAKTVVS CHHHHHHHHHHHHHH	18.43	20068231
471	Phosphorylation	VVSHSLTTLGLEVAK HHHHHHHHHCHHHHH	24.91	-
478	Ubiquitination	TLGLEVAKQSQHDKI HHCHHHHHHCCCCCC	56.51	-
484	Ubiquitination	AKQSQHDKIDASELS HHHCCCCCCCHHHCC	40.12	-
497	Phosphorylation	LSFPFHESILKVIEE CCCCHHHHHHHHHHH	25.34	25159151
500	Ubiquitination	PFHESILKVIEEEWQ CHHHHHHHHHHHHHH	39.22	-
511	Methylation	EEWQQVDRQLPSLAC HHHHHHHHHCCHHHH	40.87	115918665
519	Ubiquitination	QLPSLACKYPVSSRE HCCHHHHCCCCCCCC	47.16	-
520	Phosphorylation	LPSLACKYPVSSREA CCHHHHCCCCCCCCH	14.57	29978859
523	Phosphorylation	LACKYPVSSREATQI HHHCCCCCCCCHHHH	21.12	25954137
524	Phosphorylation	ACKYPVSSREATQIL HHCCCCCCCCHHHHC	34.08	25954137
528	Phosphorylation	PVSSREATQILSVPK CCCCCCHHHHCCCCC	16.05	25954137
532	Phosphorylation	REATQILSVPKVDDE CCHHHHCCCCCCCHH	37.69	24719451
573	Phosphorylation	DLALCRAYEAAASAL HHHHHHHHHHHHHHH	6.17	28152594
620	Ubiquitination	QALGILSKTYDAASY HHHHHHHCHHHHHHH	47.89	-
629	Glutathionylation	YDAASYICEAAFDEV HHHHHHHHHHHHHHH	1.90	22555962
642	Phosphorylation	EVKMAAHTMGNATVG HHHHHHHHCCCCCCC	23.27	-
647	Phosphorylation	AHTMGNATVGRRYLW HHHCCCCCCCCCEEE	27.74	25599653
656	Acetylation	GRRYLWLKDCKINLA CCCEEEECCCEEEEC	49.88	19608861
656	Ubiquitination	GRRYLWLKDCKINLA CCCEEEECCCEEEEC	49.88	19608861
659	Ubiquitination	YLWLKDCKINLASKN EEEECCCEEEECCCC	44.77	21906983
659	Acetylation	YLWLKDCKINLASKN EEEECCCEEEECCCC	44.77	25953088
665	Ubiquitination	CKINLASKNKLASTP CEEEECCCCCCCCCC	53.12	-
665	Acetylation	CKINLASKNKLASTP CEEEECCCCCCCCCC	53.12	25953088
667	Sumoylation	INLASKNKLASTPFK EEECCCCCCCCCCCC	49.52	-
667	Ubiquitination	INLASKNKLASTPFK EEECCCCCCCCCCCC	49.52	-
667	Sumoylation	INLASKNKLASTPFK EEECCCCCCCCCCCC	49.52	-
667	Acetylation	INLASKNKLASTPFK EEECCCCCCCCCCCC	49.52	25953088
670	Phosphorylation	ASKNKLASTPFKGGT CCCCCCCCCCCCCCC	47.23	21712546
671	Phosphorylation	SKNKLASTPFKGGTL CCCCCCCCCCCCCCC	27.43	21815630
674	Methylation	KLASTPFKGGTLFGG CCCCCCCCCCCCCCH	58.60	24785253
674	Sumoylation	KLASTPFKGGTLFGG CCCCCCCCCCCCCCH	58.60	-
674	Ubiquitination	KLASTPFKGGTLFGG CCCCCCCCCCCCCCH	58.60	21906983
674	Sumoylation	KLASTPFKGGTLFGG CCCCCCCCCCCCCCH	58.60	-
674	Acetylation	KLASTPFKGGTLFGG CCCCCCCCCCCCCCH	58.60	25953088
677	Phosphorylation	STPFKGGTLFGGEVC CCCCCCCCCCCHHHH	27.81	26552605
685	Ubiquitination	LFGGEVCKVIKKRGN CCCHHHHHHHHHCCC	52.77	21906983
685	Acetylation	LFGGEVCKVIKKRGN CCCHHHHHHHHHCCC	52.77	25953088

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
424	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LAP2A_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 LAP2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB_HUMAN	RB1	physical	12475961
LMNA_HUMAN	LMNA	physical	12475961
LMNA_HUMAN	LMNA	physical	10984438
AKP8L_HUMAN	AKAP8L	physical	12538639
BAF_HUMAN	BANF1	physical	10393804
LMNB1_HUMAN	LMNB1	physical	9490046
LMNB2_HUMAN	LMNB2	physical	9490046
LMNB1_HUMAN	LMNB1	physical	8324822
HDAC3_HUMAN	HDAC3	physical	16129885
MS18B_HUMAN	OIP5	physical	17284516
PCGF2_HUMAN	PCGF2	physical	19727227
LMNA_HUMAN	LMNA	physical	19727227
MRE11_HUMAN	MRE11A	physical	22939629
SYLC_HUMAN	LARS	physical	26344197
ATRX_HUMAN	ATRX	physical	26496610
BST2_HUMAN	BST2	physical	26496610
CHD1_HUMAN	CHD1	physical	26496610
STOM_HUMAN	STOM	physical	26496610
PGBM_HUMAN	HSPG2	physical	26496610
DNLI3_HUMAN	LIG3	physical	26496610
LMNA_HUMAN	LMNA	physical	26496610
LMNB1_HUMAN	LMNB1	physical	26496610
PHB_HUMAN	PHB	physical	26496610
RRBP1_HUMAN	RRBP1	physical	26496610
SDC2_HUMAN	SDC2	physical	26496610
SPT6H_HUMAN	SUPT6H	physical	26496610
TBG1_HUMAN	TUBG1	physical	26496610
UBF1_HUMAN	UBTF	physical	26496610
SYVC_HUMAN	VARS	physical	26496610
AF10_HUMAN	MLLT10	physical	26496610
HIRP3_HUMAN	HIRIP3	physical	26496610
VA0D1_HUMAN	ATP6V0D1	physical	26496610
NOLC1_HUMAN	NOLC1	physical	26496610
KAT7_HUMAN	KAT7	physical	26496610
RL35_HUMAN	RPL35	physical	26496610
PHB2_HUMAN	PHB2	physical	26496610
EXOS8_HUMAN	EXOSC8	physical	26496610
BRD1_HUMAN	BRD1	physical	26496610
NUSAP_HUMAN	NUSAP1	physical	26496610
PHIP_HUMAN	PHIP	physical	26496610
JADE1_HUMAN	JADE1	physical	26496610
CAVN3_HUMAN	PRKCDBP	physical	26496610
SMS2_HUMAN	SGMS2	physical	26496610

Drug and Disease Associations

Kegg Disease
OMIM Disease
613740	Cardiomyopathy, dilated 1T (CMD1T)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LAP2A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-656, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74;SER-79; THR-154; THR-160; THR-164; SER-351 AND SER-424, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-66; SER-67; THR-74;SER-159; THR-160 AND SER-424, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-67, AND MASSSPECTROMETRY.	18318008 [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 SER-351; SER-370 ANDSER-424, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-424, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-424, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-310, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160; SER-351 ANDSER-424, AND MASS SPECTROMETRY.	17924679 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74 ANDTHR-160, AND MASS SPECTROMETRY.	17487921 [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-66; SER-67; SER-79;SER-156; THR-160; SER-184 AND SER-351, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND SER-168,AND MASS SPECTROMETRY.	15302935 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, AND MASSSPECTROMETRY.	19367720 [Abstract]
"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 THR-160, AND MASSSPECTROMETRY.	18187866 [Abstract]