dbPTM

ITPR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ITPR1_HUMAN
UniProt AC	Q14643
Protein Name	Inositol 1,4,5-trisphosphate receptor type 1
Gene Name	ITPR1
Organism	Homo sapiens (Human).
Sequence Length	2758
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein . Cytoplasmic vesicle, secretory vesicle membrane Multi-pass membrane protein . Cytoplasm, perinuclear region . Endoplasmic reticulum and secretory granules (By similarity).
Protein Description	Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. [PubMed: 27108797 Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (By similarity Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways (By similarity]
Protein Sequence	MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	Phosphorylation	RCVVQPETGDLNNPP EEEECCCCCCCCCCC	42.55	20068231
56	S-palmitoylation	PPKKFRDCLFKLCPM CCHHHHHHHHHHCCC	4.13	-
70	Acetylation	MNRYSAQKQFWKAAK CCCHHHHHHHHHHCC	47.37	26051181
100	Acetylation	HHAADLEKKQNETEN HHHHHHHHHCCHHHH	67.94	26051181
113	Phosphorylation	ENRKLLGTVIQYGNV HHHHHHHHHHHHCCE	17.88	25278378
117	Phosphorylation	LLGTVIQYGNVIQLL HHHHHHHHCCEEEEE	10.27	25278378
131	Phosphorylation	LHLKSNKYLTVNKRL EECCCCCCCEECCCH	16.32	24719451
133	Phosphorylation	LKSNKYLTVNKRLPA CCCCCCCEECCCHHH	20.95	24719451
144	Ubiquitination	RLPALLEKNAMRVTL CHHHHHHHCCEEEEE	50.40	-
230 (in isoform 2)	Ubiquitination	-	62.86	-
258	Acetylation	LTCDEHRKKQHVFLR CCCCHHHHHCEEEEE	59.71	20167786
273	Phosphorylation	TTGRQSATSATSSKA CCCCCCCCCCCCCCC	24.92	23403867
274	Phosphorylation	TGRQSATSATSSKAL CCCCCCCCCCCCCCE	29.30	23403867
276	Phosphorylation	RQSATSATSSKALWE CCCCCCCCCCCCEEE	33.04	23403867
277	Phosphorylation	QSATSATSSKALWEV CCCCCCCCCCCEEEE	29.56	23403867
278	Phosphorylation	SATSATSSKALWEVE CCCCCCCCCCEEEEE	20.00	23403867
301	Phosphorylation	GGAGYWNSLFRFKHL CCCCHHHHHHHHHHH	18.10	24719451
353	Phosphorylation	NAQEKMVYSLVSVPE HHHHHHHEEEEECCC	7.87	14761954
412	Acetylation	PIDKEEEKPVMLKIG CCCCCCCCCCEEEEE	46.31	26051181
420	Phosphorylation	PVMLKIGTSPVKEDK CCEEEEECCCCCCCC	33.07	28450419
421	Phosphorylation	VMLKIGTSPVKEDKE CEEEEECCCCCCCCC	23.60	28450419
424	Methylation	KIGTSPVKEDKEAFA EEECCCCCCCCCEEE	64.68	115971475
436	Phosphorylation	AFAIVPVSPAEVRDL EEEEEECCHHHHCCC	16.60	21815630
462	Acetylation	SIAGKLEKGTITQNE HHHHHCCCCCCCHHH	72.32	25953088
482	Phosphorylation	KLLEDLVYFVTGGTN HHHHHHCHHHHCCCC	10.30	-
517	Acetylation	MREQNILKQIFKLLQ HHHHHHHHHHHHHHH	37.23	25953088
557	Phosphorylation	RHICRLCYRVLRHSQ HHHHHHHHHHHHHHH	14.35	30631047
569	Acetylation	HSQQDYRKNQEYIAK HHHHHHHHCHHHHHH	57.67	7664429
576	Acetylation	KNQEYIAKQFGFMQK HCHHHHHHHHCCCHH	36.28	26051181
608	Acetylation	NNRKLLEKHITAAEI CCHHHHHHHCCHHHH	40.03	26051181
658 (in isoform 2)	Phosphorylation	-	34.45	24719451
673	Phosphorylation	IETKLVLSRFEFEGV EEEEEECCEEEEECC	27.69	24719451
704	Phosphorylation	VWLFWRDSNKEIRSK EEEEEECCCHHHHCH	41.02	17192257
800	Phosphorylation	RDPQEQVTPVKYARL CCHHHCCCCCHHHHH	23.27	16237118
820	Phosphorylation	SEIAIDDYDSSGASK CCEECCCCCCCCCCH	17.61	22468782
822	Phosphorylation	IAIDDYDSSGASKDE EECCCCCCCCCCHHH	25.17	22468782
826	Phosphorylation	DYDSSGASKDEIKER CCCCCCCCHHHHHHH	44.13	-
837	Phosphorylation	IKERFAQTMEFVEEY HHHHHHHHHHHHHHH	18.42	27794612
850	S-palmitoylation	EYLRDVVCQRFPFSD HHHHHHHHHHCCCCH	2.11	-
904 (in isoform 4)	Phosphorylation	-	2.56	26471730
904 (in isoform 5)	Phosphorylation	-	2.56	26471730
904 (in isoform 8)	Phosphorylation	-	2.56	26471730
919 (in isoform 3)	Phosphorylation	-	43.04	26471730
940 (in isoform 2)	Phosphorylation	-	3.56	24719451
955	Phosphorylation	GGGFLPMTPMAAAPE CCCCCCCCCCCCCCC	14.15	21815630
1139	Phosphorylation	LRSIVEKSELWVYKG HHHHHHHHHEEEEEC	25.15	25921289
1144	Phosphorylation	EKSELWVYKGQGPDE HHHHEEEEECCCCCC	9.60	20090780
1152	Phosphorylation	KGQGPDETMDGASGE ECCCCCCCCCCCCCC	28.13	25921289
1157	Phosphorylation	DETMDGASGENEHKK CCCCCCCCCCCCCCC	52.77	25921289
1187	Acetylation	SYNYRVVKEILIRLS CHHHHHHHHHHHHHH	35.86	26051181
1201	Phosphorylation	SKLCVQESASVRKSR HHHHHHHCHHHHHHH	14.57	28270605
1203	Phosphorylation	LCVQESASVRKSRKQ HHHHHCHHHHHHHHH	31.56	28270605
1207	Phosphorylation	ESASVRKSRKQQQRL HCHHHHHHHHHHHHH	33.86	25954137
1238	Phosphorylation	PYEKAEDTKMQEIMR CHHHCCCHHHHHHHH	21.66	-
1327	Acetylation	KFLQTIVKAEGKFIK HHHHHHHHHCCHHHH	36.55	26051181
1347	Phosphorylation	VMAELVNSGEDVLVF HHHHHHCCCCCEEEE	35.76	23403867
1355	Phosphorylation	GEDVLVFYNDRASFQ CCCEEEEECCHHHHH	14.52	23403867
1370	Phosphorylation	TLIQMMRSERDRMDE HHHHHHHHHHHCCCC	21.06	23403867
1401	Phosphorylation	CTEGKNVYTEIKCNS HCCCCCEEEEEECCC	14.19	-
1405	Ubiquitination	KNVYTEIKCNSLLPL CCEEEEEECCCCCCH	22.56	-
1482	Phosphorylation	SDRKHADSILEKYVT CCHHHHHHHHHHHHH	29.83	24719451
1550	Phosphorylation	ESCIRVLSDVAKSRA HHHHHHHHHHHHCCC	27.47	25072903
1554	2-Hydroxyisobutyrylation	RVLSDVAKSRAIAIP HHHHHHHHCCCEEEE	40.08	-
1562 (in isoform 2)	Phosphorylation	-	10.50	24719451
1577	Phosphorylation	NLFLKSHSIVQKTAM HHHHHHCHHHHHHHH	31.39	22115753
1581	Methylation	KSHSIVQKTAMNWRL HHCHHHHHHHHHHHH	27.62	9329285
1583 (in isoform 2)	Phosphorylation	-	9.06	24719451
1598	Phosphorylation	RNAARRDSVLAASRD HHHHHHHHHHHHCHH	19.74	29255136
1603	Phosphorylation	RDSVLAASRDYRNII HHHHHHHCHHHHHHH	21.78	26329039
1606	Phosphorylation	VLAASRDYRNIIERL HHHHCHHHHHHHHHH	12.40	29449344
1687	Phosphorylation	LCIKVLQTLREMMTK HHHHHHHHHHHHHHC	24.50	21406692
1704	Phosphorylation	GYGEKLISIDELDNA CCCCCCEEHHHCCCC	34.13	20068231
1729	Phosphorylation	ATEELEPSPPLRQLE CCCCCCCCCCHHHHC	29.76	20068231
1744 (in isoform 2)	Phosphorylation	-	3.24	27251275
1749 (in isoform 2)	Phosphorylation	-	3.94	24719451
1759	Phosphorylation	YYGNVRPSGRRESLT HCCCCCCCCCCCCCC	34.07	27251275
1764	Phosphorylation	RPSGRRESLTSFGNG CCCCCCCCCCCCCCC	34.83	23401153
1766	Phosphorylation	SGRRESLTSFGNGPL CCCCCCCCCCCCCCC	31.15	23401153
1767	Phosphorylation	GRRESLTSFGNGPLS CCCCCCCCCCCCCCC	36.13	23401153
1774	Phosphorylation	SFGNGPLSAGGPGKP CCCCCCCCCCCCCCC	28.18	30266825
1788	Phosphorylation	PGGGGGGSGSSSMSR CCCCCCCCCCCCCCC	38.48	23927012
1790	Phosphorylation	GGGGGSGSSSMSRGE CCCCCCCCCCCCCCC	22.42	23927012
1791	Phosphorylation	GGGGSGSSSMSRGEM CCCCCCCCCCCCCCC	33.32	20068231
1792	Phosphorylation	GGGSGSSSMSRGEMS CCCCCCCCCCCCCCC	23.60	20068231
1794	Phosphorylation	GSGSSSMSRGEMSLA CCCCCCCCCCCCCHH	38.80	20068231
1866	Acetylation	KKSEKFFKVFYDRMK CCCHHHHHHHHHHHH	34.27	26051181
1882	Phosphorylation	AQQEIKATVTVNTSD HHHHHEEEEEECHHH	16.23	-
1910	Ubiquitination	APSRKKAKEPTTQIT CCCHHHCCCCCHHHC	73.44	-
1913	Phosphorylation	RKKAKEPTTQITEEV HHHCCCCCHHHCHHH	32.21	22210691
1914	Phosphorylation	KKAKEPTTQITEEVR HHCCCCCHHHCHHHH	28.79	22210691
1928	Phosphorylation	RDQLLEASAATRKAF HHHHHHHHHHHHHHH	14.73	28060719
1931	Phosphorylation	LLEASAATRKAFTTF HHHHHHHHHHHHHHH	32.21	22210691
1933	Ubiquitination	EASAATRKAFTTFRR HHHHHHHHHHHHHHH	43.42	-
1937	Phosphorylation	ATRKAFTTFRREADP HHHHHHHHHHHCCCC	14.53	-
1948	Phosphorylation	EADPDDHYQPGEGTQ CCCCCCCCCCCCCCC	24.33	28796482
2097	2-Hydroxyisobutyrylation	MDLVLELKNNASKLL HHHHHHHCCCHHHHH	38.49	-
2228	Phosphorylation	PSICEFLTKESKLRI CHHHHHHCCCCCEEE	37.78	25599653
2231	Phosphorylation	CEFLTKESKLRIYYT HHHHCCCCCEEEEEE	38.25	25599653
2232 (in isoform 2)	Ubiquitination	-	42.76	-
2240 (in isoform 2)	Phosphorylation	-	50.78	24719451
2247	Ubiquitination	ERDEQGSKINDFFLR CCCCCCCCCCCCHHC	52.97	-
2251 (in isoform 2)	Ubiquitination	-	5.55	-
2255	Phosphorylation	INDFFLRSEDLFNEM CCCCHHCCHHHHHHC	37.29	24719451
2275	Phosphorylation	LRAQPVLYWCARNMS HCHHHHHHHHHHCCC	9.93	20068231
2434	Phosphorylation	DLVYREETLLNVIKS HHHHCHHHHHHHHHH	31.62	28258704
2512	N-linked_Glycosylation	CRVESGENCSSPAPR CEECCCCCCCCCCCH	34.20	19159218
2565	Phosphorylation	GDVLRKPSKEEPLFA HHCCCCCCCCCCHHH	56.59	22210691
2649	Phosphorylation	EEHNMWHYLCFIVLV HHHHHHHHEEEEEEE	6.94	-
2661	Phosphorylation	VLVKVKDSTEYTGPE EEEECCCCCCCCCCH	19.88	-
2662	Phosphorylation	LVKVKDSTEYTGPES EEECCCCCCCCCCHH	43.05	-
2664	Phosphorylation	KVKDSTEYTGPESYV ECCCCCCCCCCHHHH	19.65	-
2675 (in isoform 2)	Phosphorylation	-	2.93	24719451
2681 (in isoform 2)	Phosphorylation	-	48.82	24719451
2690	Phosphorylation	FPRMRAMSLVSSDSE HHHHHHHHHHCCCCH	25.32	29214152
2693	Phosphorylation	MRAMSLVSSDSEGEQ HHHHHHHCCCCHHHH	33.45	29214152
2694	Phosphorylation	RAMSLVSSDSEGEQN HHHHHHCCCCHHHHH	37.36	30576142
2696	Phosphorylation	MSLVSSDSEGEQNEL HHHHCCCCHHHHHHH	49.83	29214152
2706 (in isoform 2)	Phosphorylation	-	5.86	27251275
2718	Phosphorylation	ESTMKLVTNLSGQLS HHHHHHHHHHHHHHH	40.66	20068231
2721	Phosphorylation	MKLVTNLSGQLSELK HHHHHHHHHHHHHHH	26.94	20068231
2725	Phosphorylation	TNLSGQLSELKDQMT HHHHHHHHHHHHHHH	32.75	20068231
2732	Phosphorylation	SELKDQMTEQRKQKQ HHHHHHHHHHHHHHH	24.27	20068231

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
353	Y	Phosphorylation	Kinase	FYN	P06241	PSP
421	S	Phosphorylation	Kinase	CDK1	P06493	PSP
800	T	Phosphorylation	Kinase	CDK1	P06493	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF170	Q96K19	PMID:21610068

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
48	K	ubiquitylation		-
Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked (By similarity).

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 ITPR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAH8_HUMAN	CA8	physical	12611586
CABP1_HUMAN	CABP1	physical	14685260
TRPC1_HUMAN	TRPC1	physical	14505576
TRPC3_HUMAN	TRPC3	physical	14505576
TRPC4_HUMAN	TRPC4	physical	14505576
TRPC5_HUMAN	TRPC5	physical	14505576
TRPC6_HUMAN	TRPC6	physical	14505576
E41L1_HUMAN	EPB41L1	physical	12676536
MRVI1_HUMAN	MRVI1	physical	10724174
KGP1_HUMAN	PRKG1	physical	10724174
SAHH2_HUMAN	AHCYL1	physical	12525476
FKB1A_HUMAN	FKBP1A	physical	16278292
FKB1A_HUMAN	FKBP1A	physical	9346894
CABP1_HUMAN	CABP1	physical	12032348
HOME1_RAT	Homer1	physical	9808459
HOME2_RAT	Homer2	physical	9808459
ITPR3_HUMAN	ITPR3	physical	7559486
ERLN1_HUMAN	ERLIN1	physical	19240031
ERLN2_HUMAN	ERLIN2	physical	19240031
TERA_HUMAN	VCP	physical	19240031
PSMD2_HUMAN	PSMD2	physical	17502376
AMFR_HUMAN	AMFR	physical	17502376
UFD1_HUMAN	UFD1L	physical	17502376
ERLN2_HUMAN	ERLIN2	physical	17502376
AKT1_HUMAN	AKT1	physical	18250332
BCL2_HUMAN	BCL2	physical	19706527
BRCA1_HUMAN	BRCA1	physical	25645916
RN170_HUMAN	RNF170	physical	25882839
ERLN2_HUMAN	ERLIN2	physical	25882839

Drug and Disease Associations

Kegg Disease
H00063	Spinocerebellar ataxia (SCA); Machado-Joseph disease (SCA3)
OMIM Disease
606658	Spinocerebellar ataxia 15 (SCA15)
117360	Spinocerebellar ataxia 29 (SCA29)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00201	Caffeine

Regulatory Network of ITPR1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2512, AND MASSSPECTROMETRY.	19159218 [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-1598, AND MASSSPECTROMETRY.	19690332 [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-1598 AND SER-1764, ANDMASS 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-704, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1598, AND MASSSPECTROMETRY.	19007248 [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-1598, AND MASSSPECTROMETRY.	17081983 [Abstract]

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