dbPTM

LIPA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LIPA1_HUMAN
UniProt AC	Q13136
Protein Name	Liprin-alpha-1
Gene Name	PPFIA1
Organism	Homo sapiens (Human).
Sequence Length	1202
Subcellular Localization	Cytoplasm . Colocalizes with PTPRF at the ends of focal adhesions most proximal to the cell nucleus.
Protein Description	May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates..
Protein Sequence	MMCEVMPTISEAEGPPGGGGGHGSGSPSQPDADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDADVSDGEDDRDTLLSSVDLLSPSGQADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRVGSGSLDNLGRFRSMSSIPPYPASSLASSSPPGSGRSTPRRIPHSPAREVDRLGVMTLLPPSREEVRDDKTTIKCETSPPSSPRALRLDRLHKGALHTVSHEDIRDIRNSTGSQDGPVSNPSSSNSSQDSLHKAPKKKGIKSSIGRLFGKKEKGRPGQTGKEALGQAGVSETDNSSQDALGLSKLGGQAEKNRKLQKKHELLEEARRQGLPFAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLTSPSAPPTSRTTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRLNYDRKELERKREESQSEIKDVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLLVMGTDRRFDEDDDKSFRRAPSWRKKFRPKDIRGLAAGSAETLPANFRVTSSMSSPSMQPKKMQMDGNVSGTQRLDSATVRTYSC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MMCEVMPTISEAEGP CCCEECCCEECCCCC	21.02	28348404
10	Phosphorylation	CEVMPTISEAEGPPG CEECCCEECCCCCCC	32.98	28348404
24	Phosphorylation	GGGGGHGSGSPSQPD CCCCCCCCCCCCCCC	30.35	26074081
26	Phosphorylation	GGGHGSGSPSQPDAD CCCCCCCCCCCCCCC	24.07	26074081
28	Phosphorylation	GHGSGSPSQPDADSH CCCCCCCCCCCCCHH	56.92	26074081
34	Phosphorylation	PSQPDADSHFEQLMV CCCCCCCHHHHHHHH	31.62	26074081
77	Phosphorylation	EVGHERDSLQRQLNT HHHCCHHHHHHHHHH	32.40	29496963
95	Ubiquitination	QEFAALTKELNVCRE HHHHHHHHHHHHHHH	62.14	-
138	Phosphorylation	LVSRHERSLRMTVVK HHHHCHHHHHEEEEH	19.83	-
150	Phosphorylation	VVKRQAQSPAGVSSE EEHHHCCCCCCCCHH	21.52	25159151
150 (in isoform 2)	Phosphorylation	-	21.52	-
155	Phosphorylation	AQSPAGVSSEVEVLK CCCCCCCCHHHHHHH	21.62	29978859
156	Phosphorylation	QSPAGVSSEVEVLKA CCCCCCCHHHHHHHH	43.16	29396449
156 (in isoform 2)	Phosphorylation	-	43.16	-
172	Ubiquitination	KSLFEHHKALDEKVR HHHHHHHHHHHHHHH	53.18	-
190	Phosphorylation	RVALERCSLLEEELG HHHHHHHHHHHHHHC	42.06	22210691
199	Phosphorylation	LEEELGATHKELMIL HHHHHCCCHHHHHHH	31.51	22210691
215	Phosphorylation	EQNNQKKTLTDGVLD HHCCCCCCCCCCCCC	41.76	21406692
217	Phosphorylation	NNQKKTLTDGVLDIN CCCCCCCCCCCCCCC	35.62	21406692
230	Phosphorylation	INHEQENTPSTSGKR CCCCCCCCCCCCCCC	20.19	23927012
230 (in isoform 2)	Phosphorylation	-	20.19	-
232 (in isoform 2)	Phosphorylation	-	32.92	21406692
232	Phosphorylation	HEQENTPSTSGKRSS CCCCCCCCCCCCCCC	32.92	25850435
233 (in isoform 2)	Phosphorylation	-	42.58	21406692
233	Phosphorylation	EQENTPSTSGKRSSD CCCCCCCCCCCCCCC	42.58	25850435
234	Phosphorylation	QENTPSTSGKRSSDG CCCCCCCCCCCCCCC	46.80	25159151
236	Acetylation	NTPSTSGKRSSDGSL CCCCCCCCCCCCCCC	49.20	26051181
238	Phosphorylation	PSTSGKRSSDGSLSH CCCCCCCCCCCCCCC	35.95	29255136
238 (in isoform 2)	Phosphorylation	-	35.95	-
239	Phosphorylation	STSGKRSSDGSLSHE CCCCCCCCCCCCCCH	50.45	29255136
239 (in isoform 2)	Phosphorylation	-	50.45	21406692
242	Phosphorylation	GKRSSDGSLSHEEDL CCCCCCCCCCCHHHH	31.52	29255136
242 (in isoform 2)	Phosphorylation	-	31.52	21406692
244	Phosphorylation	RSSDGSLSHEEDLAK CCCCCCCCCHHHHHH	30.46	29255136
244 (in isoform 2)	Phosphorylation	-	30.46	21406692
275	Phosphorylation	QMKERLASLSSHVTE HHHHHHHHHHHHHHH	33.12	28176443
277	Phosphorylation	KERLASLSSHVTELE HHHHHHHHHHHHHHH	18.86	25106551
278	Phosphorylation	ERLASLSSHVTELEE HHHHHHHHHHHHHHH	27.54	29116813
281	Phosphorylation	ASLSSHVTELEEDLD HHHHHHHHHHHHHHH	29.45	25106551
297	Phosphorylation	ARKDLIKSEEMNTKL HHHHHHHHHHHHHHH	31.62	28464451
302	Phosphorylation	IKSEEMNTKLQRDVR HHHHHHHHHHHHHHH	31.64	-
337	Phosphorylation	LAAQREATSVHDLND HHHHHHCCCHHHHHH	26.91	24719451
338	Phosphorylation	AAQREATSVHDLNDK HHHHHCCCHHHHHHH	25.22	28348404
387	Phosphorylation	QTLRKAETLPEVEAE HHHHHCCCCHHHHHH	53.09	30624053
404	Ubiquitination	QRVAALSKAEERHGN HHHHHHHHHHHHHCC	61.74	-
404	2-Hydroxyisobutyrylation	QRVAALSKAEERHGN HHHHHHHHHHHHHCC	61.74	-
448	Phosphorylation	EEHNKRLSDTVDKLL HHHHHHHHHHHHHHH	34.96	20363803
448 (in isoform 2)	Phosphorylation	-	34.96	21406692
450 (in isoform 2)	Phosphorylation	-	27.51	21406692
450	Phosphorylation	HNKRLSDTVDKLLSE HHHHHHHHHHHHHHH	27.51	20873877
456	Phosphorylation	DTVDKLLSESNERLQ HHHHHHHHHCHHHHH	49.79	28348404
458	Phosphorylation	VDKLLSESNERLQLH HHHHHHHCHHHHHHH	40.38	30624053
467	Ubiquitination	ERLQLHLKERMAALE HHHHHHHHHHHHHHH	32.31	-
476	Acetylation	RMAALEDKNSLLREV HHHHHHCHHHHHHHH	38.78	19829873
476	2-Hydroxyisobutyrylation	RMAALEDKNSLLREV HHHHHHCHHHHHHHH	38.78	-
485	Phosphorylation	SLLREVESAKKQLEE HHHHHHHHHHHHHHH	51.03	-
520	Phosphorylation	HMRLRGASLHHGRPH HHHHCCCCCCCCCCC	30.93	28152594
530	Phosphorylation	HGRPHLGSVPDFRFP CCCCCCCCCCCCCCC	36.52	29255136
535	Methylation	LGSVPDFRFPMADGH CCCCCCCCCCCCCCC	41.98	115482171
543	Phosphorylation	FPMADGHTDSYSTSA CCCCCCCCCCCCCHH	31.97	28674419
545	Phosphorylation	MADGHTDSYSTSAVL CCCCCCCCCCCHHHH	23.34	25106551
546	Phosphorylation	ADGHTDSYSTSAVLR CCCCCCCCCCHHHHC	20.83	25394399
547	Phosphorylation	DGHTDSYSTSAVLRR CCCCCCCCCHHHHCC	21.60	25106551
548	Phosphorylation	GHTDSYSTSAVLRRP CCCCCCCCHHHHCCC	16.69	29978859
549	Phosphorylation	HTDSYSTSAVLRRPQ CCCCCCCHHHHCCCC	15.50	25106551
568	Phosphorylation	AALRDEPSKVQTLNE CHHCCCCCCCCCCCH	43.33	30266825
569	Ubiquitination	ALRDEPSKVQTLNEQ HHCCCCCCCCCCCHH	49.42	-
572	Phosphorylation	DEPSKVQTLNEQDWE CCCCCCCCCCHHHHH	34.24	30266825
596	Phosphorylation	NVAQAFESDADVSDG HHHHHHHCCCCCCCC	31.48	27732954
601	Phosphorylation	FESDADVSDGEDDRD HHCCCCCCCCCCCHH	40.21	27362937
618	Phosphorylation	LSSVDLLSPSGQADA HHHHHHCCCCCCCCH	25.07	26074081
620	Phosphorylation	SVDLLSPSGQADAHT HHHHCCCCCCCCHHH	39.91	26074081
666	Phosphorylation	EIESRVGSGSLDNLG HHHHHHCCCCCCCCC	23.50	30266825
668	Phosphorylation	ESRVGSGSLDNLGRF HHHHCCCCCCCCCCC	33.96	29255136
668 (in isoform 2)	Phosphorylation	-	33.96	-
677	Phosphorylation	DNLGRFRSMSSIPPY CCCCCCCCCCCCCCC	21.95	29396449
679	Phosphorylation	LGRFRSMSSIPPYPA CCCCCCCCCCCCCCH	26.77	29396449
680	Phosphorylation	GRFRSMSSIPPYPAS CCCCCCCCCCCCCHH	30.39	29396449
684	Phosphorylation	SMSSIPPYPASSLAS CCCCCCCCCHHHCCC	13.18	30278072
687	Phosphorylation	SIPPYPASSLASSSP CCCCCCHHHCCCCCC	22.75	30278072
688	Phosphorylation	IPPYPASSLASSSPP CCCCCHHHCCCCCCC	30.02	30278072
691	Phosphorylation	YPASSLASSSPPGSG CCHHHCCCCCCCCCC	36.32	30278072
692	Phosphorylation	PASSLASSSPPGSGR CHHHCCCCCCCCCCC	41.06	30278072
693	Phosphorylation	ASSLASSSPPGSGRS HHHCCCCCCCCCCCC	32.39	30278072
693 (in isoform 2)	Phosphorylation	-	32.39	-
697	Phosphorylation	ASSSPPGSGRSTPRR CCCCCCCCCCCCCCC	36.49	26055452
700	Phosphorylation	SPPGSGRSTPRRIPH CCCCCCCCCCCCCCC	46.41	23090842
701	Phosphorylation	PPGSGRSTPRRIPHS CCCCCCCCCCCCCCC	21.32	28985074
708	Phosphorylation	TPRRIPHSPAREVDR CCCCCCCCCCCCCCC	18.20	25159151
725	Phosphorylation	VMTLLPPSREEVRDD EEEECCCCHHHHCCC	50.84	28555341
734	Phosphorylation	EEVRDDKTTIKCETS HHHCCCCCEEEEECC	40.52	23403867
735	Phosphorylation	EVRDDKTTIKCETSP HHCCCCCEEEEECCC	24.95	23403867
740	Phosphorylation	KTTIKCETSPPSSPR CCEEEEECCCCCCCC	56.88	29255136
741	Phosphorylation	TTIKCETSPPSSPRA CEEEEECCCCCCCCH	16.72	29255136
741 (in isoform 2)	Phosphorylation	-	16.72	-
744	Phosphorylation	KCETSPPSSPRALRL EEECCCCCCCCHHCC	57.25	29255136
745	Phosphorylation	CETSPPSSPRALRLD EECCCCCCCCHHCCH	24.95	29255136
745 (in isoform 2)	Phosphorylation	-	24.95	-
756	Ubiquitination	LRLDRLHKGALHTVS HCCHHHCCCCCCCCC	50.93	-
761	Phosphorylation	LHKGALHTVSHEDIR HCCCCCCCCCHHHHH	25.26	30266825
763	Phosphorylation	KGALHTVSHEDIRDI CCCCCCCCHHHHHHH	23.47	29255136
763 (in isoform 2)	Phosphorylation	-	23.47	21406692
773	Phosphorylation	DIRDIRNSTGSQDGP HHHHHHHCCCCCCCC	25.05	28176443
773 (in isoform 2)	Phosphorylation	-	25.05	-
774	Phosphorylation	IRDIRNSTGSQDGPV HHHHHHCCCCCCCCC	44.39	25159151
774 (in isoform 2)	Phosphorylation	-	44.39	-
776	Phosphorylation	DIRNSTGSQDGPVSN HHHHCCCCCCCCCCC	25.78	17525332
776 (in isoform 2)	Phosphorylation	-	25.78	-
782	Phosphorylation	GSQDGPVSNPSSSNS CCCCCCCCCCCCCCC	46.27	22199227
785	Phosphorylation	DGPVSNPSSSNSSQD CCCCCCCCCCCCCCH	51.12	23401153
785 (in isoform 2)	Phosphorylation	-	51.12	-
786	Phosphorylation	GPVSNPSSSNSSQDS CCCCCCCCCCCCCHH	34.49	28450419
787	Phosphorylation	PVSNPSSSNSSQDSL CCCCCCCCCCCCHHH	45.10	21955146
789	Phosphorylation	SNPSSSNSSQDSLHK CCCCCCCCCCHHHHC	31.18	28450419
790	Phosphorylation	NPSSSNSSQDSLHKA CCCCCCCCCHHHHCC	42.11	21955146
790 (in isoform 2)	Phosphorylation	-	42.11	-
793	Phosphorylation	SSNSSQDSLHKAPKK CCCCCCHHHHCCCHH	25.41	23401153
801	Acetylation	LHKAPKKKGIKSSIG HHCCCHHHCCCHHHH	72.50	130745
804	Acetylation	APKKKGIKSSIGRLF CCHHHCCCHHHHHHH	46.98	130747
805	Phosphorylation	PKKKGIKSSIGRLFG CHHHCCCHHHHHHHC	25.85	21712546
806	Phosphorylation	KKKGIKSSIGRLFGK HHHCCCHHHHHHHCC	24.86	21712546
833	Phosphorylation	ALGQAGVSETDNSSQ HHHHCCCCCCCCCCH	33.58	27251275
835	Phosphorylation	GQAGVSETDNSSQDA HHCCCCCCCCCCHHH	32.73	20873877
838	Phosphorylation	GVSETDNSSQDALGL CCCCCCCCCHHHHCH	31.99	25159151
839	Phosphorylation	VSETDNSSQDALGLS CCCCCCCCHHHHCHH	38.03	28985074
847	Ubiquitination	QDALGLSKLGGQAEK HHHHCHHHCCCHHHH	57.08	-
915	Phosphorylation	GAIMSALSDTEIQRE CCHHHHCCCHHHHHH	42.05	-
943	Phosphorylation	LAIQEIMSLTSPSAP HHHHHHHHCCCCCCC	33.87	27251275
945	Phosphorylation	IQEIMSLTSPSAPPT HHHHHHCCCCCCCCC	31.14	28348404
946	Phosphorylation	QEIMSLTSPSAPPTS HHHHHCCCCCCCCCC	23.35	27251275
948	Phosphorylation	IMSLTSPSAPPTSRT HHHCCCCCCCCCCCC	53.85	28348404
952	Phosphorylation	TSPSAPPTSRTTLAY CCCCCCCCCCCEEEE	29.76	24719451
953	Phosphorylation	SPSAPPTSRTTLAYG CCCCCCCCCCEEEEC	33.14	28348404
1011	Phosphorylation	GQLKMVDSFHRNSFQ HHHCCHHCCCCCCHH	16.13	28857561
1120	Sulfoxidation	EFNNLLVMGTDRRFD HHHCEEEEECCCCCC	4.89	21406390
1133	Phosphorylation	FDEDDDKSFRRAPSW CCCCCCHHHHCCCHH	30.86	29255136
1139	Phosphorylation	KSFRRAPSWRKKFRP HHHHCCCHHHHHCCH	38.23	25394399
1156	Phosphorylation	IRGLAAGSAETLPAN CCHHCCCCCCCCCCC	20.43	29255136
1159	Phosphorylation	LAAGSAETLPANFRV HCCCCCCCCCCCEEE	37.45	19664994
1159 (in isoform 2)	Phosphorylation	-	37.45	-
1167	Phosphorylation	LPANFRVTSSMSSPS CCCCEEEEECCCCCC	15.72	22167270
1168	Phosphorylation	PANFRVTSSMSSPSM CCCEEEEECCCCCCC	22.61	30266825
1169	Phosphorylation	ANFRVTSSMSSPSMQ CCEEEEECCCCCCCC	17.20	30266825
1171	Phosphorylation	FRVTSSMSSPSMQPK EEEEECCCCCCCCCC	40.83	30266825
1171 (in isoform 2)	Phosphorylation	-	40.83	29507054
1172	Phosphorylation	RVTSSMSSPSMQPKK EEEECCCCCCCCCCE	16.62	29255136
1172 (in isoform 2)	Phosphorylation	-	16.62	29507054
1174	Phosphorylation	TSSMSSPSMQPKKMQ EECCCCCCCCCCEEC	31.81	30266825
1174 (in isoform 2)	Phosphorylation	-	31.81	29116813
1194	Phosphorylation	SGTQRLDSATVRTYS CCCCCCCCCEEEEEC	30.36	28857561

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
701	T	Phosphorylation	Kinase	CDK5	Q00535	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LIPA1_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 LIPA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GIT1_HUMAN	GIT1	physical	12629171
ERC2_HUMAN	ERC2	physical	12923177
MBIP1_HUMAN	MBIP	physical	16189514
GIT1_HUMAN	GIT1	physical	12923177
GRIP2_HUMAN	GRIP2	physical	12923177
PTPRF_HUMAN	PTPRF	physical	8524829
PTPRS_HUMAN	PTPRS	physical	8524829
NCOA2_HUMAN	NCOA2	physical	11931740
LIPA1_HUMAN	PPFIA1	physical	9624153
LIPA2_HUMAN	PPFIA2	physical	9624153
LIPA1_HUMAN	PPFIA1	physical	22072677
LIPA_CAEEL	syd-2	physical	22072677
MBIP1_HUMAN	MBIP	physical	19060904
CEP70_HUMAN	CEP70	physical	19060904
NEMO_HUMAN	IKBKG	physical	22863883
F161A_HUMAN	FAM161A	physical	25416956
TXLNA_HUMAN	TXLNA	physical	25416956
BRCA1_HUMAN	BRCA1	physical	25184681
LIPA3_HUMAN	PPFIA3	physical	9624153
LIPB1_HUMAN	PPFIBP1	physical	9624153

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 LIPA1_HUMAN

Related Literatures of Post-Translational Modification

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-239; SER-242; SER-244;SER-693 AND THR-1159, AND MASS SPECTROMETRY.	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-668; SER-693 ANDSER-1172, AND MASS SPECTROMETRY.	19413330 [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-230; SER-239; SER-242;SER-244; SER-741 AND SER-745, AND MASS SPECTROMETRY.	18669648 [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-763, AND MASSSPECTROMETRY.	18220336 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776, AND MASSSPECTROMETRY.	17525332 [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-239 AND SER-242, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-684, AND MASSSPECTROMETRY.	17053785 [Abstract]