dbPTM

TOIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TOIP1_HUMAN
UniProt AC	Q5JTV8
Protein Name	Torsin-1A-interacting protein 1
Gene Name	TOR1AIP1
Organism	Homo sapiens (Human).
Sequence Length	583
Subcellular Localization	Nucleus inner membrane Single-pass membrane protein .
Protein Description	Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina..
Protein Sequence	MAGDGRRAEAVREGWGVYVTPRAPIREGRGRLAPQNGGSSDAPAYRTPPSRQGRREVRFSDEPPEVYGDFEPLVAKERSPVGKRTRLEEFRSDSAKEEVRESAYYLRSRQRRQPRPQETEEMKTRRTTRLQQQHSEQPPLQPSPVMTRRGLRDSHSSEEDEASSQTDLSQTISKKTVRSIQEAPVSEDLVIRLRRPPLRYPRYEATSVQQKVNFSEEGETEEDDQDSSHSSVTTVKARSRDSDESGDKTTRSSSQYIESFWQSSQSQNFTAHDKQPSVLSSGYQKTPQEWAPQTARIRTRMQNDSILKSELGNQSPSTSSRQVTGQPQNASFVKRNRWWLLPLIAALASGSFWFFSTPEVETTAVQEFQNQMNQLKNKYQGQDEKLWKRSQTFLEKHLNSSHPRSQPAILLLTAARDAEEALRCLSEQIADAYSSFRSVRAIRIDGTDKATQDSDTVKLEVDQELSNGFKNGQNAAVVHRFESFPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLGTSLGLKEVEEKVRDFLKVKFTNSNTPNSYNHMDPDKLNGLWSRISHLVLPVQPENALKRGICL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Sulfoxidation	-------MAGDGRRA -------CCCCCHHH	9.44	30846556
18	Phosphorylation	VREGWGVYVTPRAPI HHCCCEEEECCCCCC	8.48	29396449
20	Phosphorylation	EGWGVYVTPRAPIRE CCCEEEECCCCCCCC	6.86	21815630
39	Phosphorylation	LAPQNGGSSDAPAYR CCCCCCCCCCCCCCC	26.83	27732954
40	Phosphorylation	APQNGGSSDAPAYRT CCCCCCCCCCCCCCC	40.86	27732954
45	Phosphorylation	GSSDAPAYRTPPSRQ CCCCCCCCCCCCCCC	17.60	25002506
47	Phosphorylation	SDAPAYRTPPSRQGR CCCCCCCCCCCCCCC	27.20	26055452
50	Phosphorylation	PAYRTPPSRQGRREV CCCCCCCCCCCCCEE	38.14	26055452
60	Phosphorylation	GRREVRFSDEPPEVY CCCEEECCCCCCCCC	30.42	21712546
67	Phosphorylation	SDEPPEVYGDFEPLV CCCCCCCCCCCHHCC	14.87	24173317
76	Ubiquitination	DFEPLVAKERSPVGK CCHHCCCCCCCCCCC	46.29	29967540
79	Phosphorylation	PLVAKERSPVGKRTR HCCCCCCCCCCCCHH	25.65	25849741
92	Phosphorylation	TRLEEFRSDSAKEEV HHHHHHCCCHHHHHH	41.04	25159151
94	Phosphorylation	LEEFRSDSAKEEVRE HHHHCCCHHHHHHHH	42.35	25159151
102	Phosphorylation	AKEEVRESAYYLRSR HHHHHHHHHHHHHHH	15.82	28555341
115	Methylation	SRQRRQPRPQETEEM HHCCCCCCCCCHHHH	36.88	115386881
127	Phosphorylation	EEMKTRRTTRLQQQH HHHHHHHHHHHHHHH	16.99	29116813
128	Phosphorylation	EMKTRRTTRLQQQHS HHHHHHHHHHHHHHC	27.80	29116813
135	Phosphorylation	TRLQQQHSEQPPLQP HHHHHHHCCCCCCCC	33.32	23401153
143	Phosphorylation	EQPPLQPSPVMTRRG CCCCCCCCCCCCCCC	19.71	22167270
146	Sulfoxidation	PLQPSPVMTRRGLRD CCCCCCCCCCCCCCC	2.47	21406390
147	Phosphorylation	LQPSPVMTRRGLRDS CCCCCCCCCCCCCCC	19.90	22167270
154	Phosphorylation	TRRGLRDSHSSEEDE CCCCCCCCCCCHHHH	20.87	29255136
156	Phosphorylation	RGLRDSHSSEEDEAS CCCCCCCCCHHHHHH	43.31	29255136
157	Phosphorylation	GLRDSHSSEEDEASS CCCCCCCCHHHHHHC	39.31	29255136
163	Phosphorylation	SSEEDEASSQTDLSQ CCHHHHHHCCCCHHH	22.41	23927012
164	Phosphorylation	SEEDEASSQTDLSQT CHHHHHHCCCCHHHH	44.11	23927012
166	Phosphorylation	EDEASSQTDLSQTIS HHHHHCCCCHHHHHC	40.64	30278072
169	Phosphorylation	ASSQTDLSQTISKKT HHCCCCHHHHHCHHH	28.25	17525332
171	Phosphorylation	SQTDLSQTISKKTVR CCCCHHHHHCHHHHC	24.68	23927012
173	Phosphorylation	TDLSQTISKKTVRSI CCHHHHHCHHHHCHH	31.33	23927012
174	Ubiquitination	DLSQTISKKTVRSIQ CHHHHHCHHHHCHHH	48.92	21906983
174 (in isoform 1)	Ubiquitination	-	48.92	21890473
174 (in isoform 2)	Ubiquitination	-	48.92	21890473
175	Ubiquitination	LSQTISKKTVRSIQE HHHHHCHHHHCHHHH	45.52	22817900
176	Phosphorylation	SQTISKKTVRSIQEA HHHHCHHHHCHHHHC	25.53	23312004
179	Phosphorylation	ISKKTVRSIQEAPVS HCHHHHCHHHHCCCC	25.04	29255136
179 (in isoform 2)	Phosphorylation	-	25.04	22777824
179 (in isoform 3)	Phosphorylation	-	25.04	22777824
186	O-linked_Glycosylation	SIQEAPVSEDLVIRL HHHHCCCCCCEEEEE	25.08	30059200
186	Phosphorylation	SIQEAPVSEDLVIRL HHHHCCCCCCEEEEE	25.08	21712546
187 (in isoform 2)	Phosphorylation	-	56.45	28122231
187 (in isoform 3)	Phosphorylation	-	56.45	28122231
200	Phosphorylation	LRRPPLRYPRYEATS ECCCCCCCCCCCCCC	10.35	-
203	Nitration	PPLRYPRYEATSVQQ CCCCCCCCCCCCCHH	12.86	-
203	Phosphorylation	PPLRYPRYEATSVQQ CCCCCCCCCCCCCHH	12.86	28796482
206	Phosphorylation	RYPRYEATSVQQKVN CCCCCCCCCCHHCCC	19.93	27422710
211	Ubiquitination	EATSVQQKVNFSEEG CCCCCHHCCCCCCCC	23.27	23503661
212	Ubiquitination	ATSVQQKVNFSEEGE CCCCHHCCCCCCCCC	8.32	23503661
215	Phosphorylation	VQQKVNFSEEGETEE CHHCCCCCCCCCCCC	29.54	29255136
216	Phosphorylation	QQKVNFSEEGETEED HHCCCCCCCCCCCCC	66.92	27251275
220	Phosphorylation	NFSEEGETEEDDQDS CCCCCCCCCCCCCCC	56.37	19664994
221	Phosphorylation	FSEEGETEEDDQDSS CCCCCCCCCCCCCCC	55.94	32645325
227	Phosphorylation	TEEDDQDSSHSSVTT CCCCCCCCCCCCEEE	25.07	30266825
228	Phosphorylation	EEDDQDSSHSSVTTV CCCCCCCCCCCEEEE	35.36	22167270
229	Phosphorylation	EDDQDSSHSSVTTVK CCCCCCCCCCEEEEE	28.22	27251275
230	Phosphorylation	DDQDSSHSSVTTVKA CCCCCCCCCEEEEEE	28.58	22167270
231	Phosphorylation	DQDSSHSSVTTVKAR CCCCCCCCEEEEEEE	20.33	22167270
232	Phosphorylation	QDSSHSSVTTVKARS CCCCCCCEEEEEEEC	6.12	27251275
233	Phosphorylation	DSSHSSVTTVKARSR CCCCCCEEEEEEECC	28.02	22167270
234	Phosphorylation	SSHSSVTTVKARSRD CCCCCEEEEEEECCC	20.18	22167270
236	Ubiquitination	HSSVTTVKARSRDSD CCCEEEEEEECCCCC	35.67	21906983
236 (in isoform 2)	Ubiquitination	-	35.67	21890473
237	Ubiquitination	SSVTTVKARSRDSDE CCEEEEEEECCCCCC	15.45	21963094
237 (in isoform 1)	Ubiquitination	-	15.45	21890473
239	Phosphorylation	VTTVKARSRDSDESG EEEEEEECCCCCCCC	45.35	30242111
242	Phosphorylation	VKARSRDSDESGDKT EEEECCCCCCCCCCC	42.01	28176443
245	Phosphorylation	RSRDSDESGDKTTRS ECCCCCCCCCCCCCC	58.23	28176443
248	Ubiquitination	DSDESGDKTTRSSSQ CCCCCCCCCCCCHHH	56.15	33845483
249	Phosphorylation	SDESGDKTTRSSSQY CCCCCCCCCCCHHHH	31.98	24247654
249	Ubiquitination	SDESGDKTTRSSSQY CCCCCCCCCCCHHHH	31.98	33845483
250	Phosphorylation	DESGDKTTRSSSQYI CCCCCCCCCCHHHHH	34.00	27251275
252	Phosphorylation	SGDKTTRSSSQYIES CCCCCCCCHHHHHHH	32.05	21712546
253	Phosphorylation	GDKTTRSSSQYIESF CCCCCCCHHHHHHHH	20.40	27794612
254	Phosphorylation	DKTTRSSSQYIESFW CCCCCCHHHHHHHHH	28.40	17525332
256	Phosphorylation	TTRSSSQYIESFWQS CCCCHHHHHHHHHHH	14.49	25884760
259	Phosphorylation	SSSQYIESFWQSSQS CHHHHHHHHHHHCCC	23.40	23403867
263	Phosphorylation	YIESFWQSSQSQNFT HHHHHHHHCCCCCCC	22.42	23403867
264	Phosphorylation	IESFWQSSQSQNFTA HHHHHHHCCCCCCCC	20.81	23403867
266	Phosphorylation	SFWQSSQSQNFTAHD HHHHHCCCCCCCCCC	29.10	17525332
270	O-linked_Glycosylation	SSQSQNFTAHDKQPS HCCCCCCCCCCCCCC	30.54	30059200
270	Phosphorylation	SSQSQNFTAHDKQPS HCCCCCCCCCCCCCC	30.54	23403867
274	Ubiquitination	QNFTAHDKQPSVLSS CCCCCCCCCCCHHCC	55.00	22817900
275	Ubiquitination	NFTAHDKQPSVLSSG CCCCCCCCCCHHCCC	41.37	21890473
277	Phosphorylation	TAHDKQPSVLSSGYQ CCCCCCCCHHCCCCC	32.94	25159151
280	Phosphorylation	DKQPSVLSSGYQKTP CCCCCHHCCCCCCCH	21.40	25159151
281	Phosphorylation	KQPSVLSSGYQKTPQ CCCCHHCCCCCCCHH	37.04	25159151
285	Ubiquitination	VLSSGYQKTPQEWAP HHCCCCCCCHHHHCC	54.40	22817900
286	Phosphorylation	LSSGYQKTPQEWAPQ HCCCCCCCHHHHCCC	18.06	25159151
286	Ubiquitination	LSSGYQKTPQEWAPQ HCCCCCCCHHHHCCC	18.06	21890473
287	Phosphorylation	SSGYQKTPQEWAPQT CCCCCCCHHHHCCCH	36.81	27251275
294	Phosphorylation	PQEWAPQTARIRTRM HHHHCCCHHHHHHHH	19.49	25159151
300	Methylation	QTARIRTRMQNDSIL CHHHHHHHHHCCHHH	18.16	115918745
305	Phosphorylation	RTRMQNDSILKSELG HHHHHCCHHHHHHHC	37.05	23401153
308	Sumoylation	MQNDSILKSELGNQS HHCCHHHHHHHCCCC	39.97	28112733
308	Ubiquitination	MQNDSILKSELGNQS HHCCHHHHHHHCCCC	39.97	23000965
309	Phosphorylation	QNDSILKSELGNQSP HCCHHHHHHHCCCCC	34.31	28176443
309	Ubiquitination	QNDSILKSELGNQSP HCCHHHHHHHCCCCC	34.31	23000965
309 (in isoform 1)	Ubiquitination	-	34.31	21890473
315	Phosphorylation	KSELGNQSPSTSSRQ HHHHCCCCCCCCCCC	25.47	29255136
316	Phosphorylation	SELGNQSPSTSSRQV HHHCCCCCCCCCCCC	31.68	27251275
317	Phosphorylation	ELGNQSPSTSSRQVT HHCCCCCCCCCCCCC	46.28	23401153
318	Phosphorylation	LGNQSPSTSSRQVTG HCCCCCCCCCCCCCC	33.82	30266825
319	Phosphorylation	GNQSPSTSSRQVTGQ CCCCCCCCCCCCCCC	28.06	30266825
320	Phosphorylation	NQSPSTSSRQVTGQP CCCCCCCCCCCCCCC	27.16	30266825
324	Phosphorylation	STSSRQVTGQPQNAS CCCCCCCCCCCCCCH	23.04	26074081
331	Phosphorylation	TGQPQNASFVKRNRW CCCCCCCHHHHHCHH	37.81	22210691
334	2-Hydroxyisobutyrylation	PQNASFVKRNRWWLL CCCCHHHHHCHHHHH	41.78	-
334	Acetylation	PQNASFVKRNRWWLL CCCCHHHHHCHHHHH	41.78	26051181
334	Ubiquitination	PQNASFVKRNRWWLL CCCCHHHHHCHHHHH	41.78	27667366
335	Ubiquitination	QNASFVKRNRWWLLP CCCHHHHHCHHHHHH	32.42	21890473
335 (in isoform 1)	Ubiquitination	-	32.42	21890473
349	Ubiquitination	PLIAALASGSFWFFS HHHHHHHHCCEEECC	35.50	21890473
350	Ubiquitination	LIAALASGSFWFFST HHHHHHHCCEEECCC	22.66	21890473
351 (in isoform 2)	Ubiquitination	-	19.46	21890473
379	Phosphorylation	MNQLKNKYQGQDEKL HHHHHHHHCCCCHHH	27.54	-
385	Acetylation	KYQGQDEKLWKRSQT HHCCCCHHHHHHHHH	68.86	26051181
385	Ubiquitination	KYQGQDEKLWKRSQT HHCCCCHHHHHHHHH	68.86	29967540
386	Ubiquitination	YQGQDEKLWKRSQTF HCCCCHHHHHHHHHH	6.49	29967540
399	N-linked_Glycosylation	TFLEKHLNSSHPRSQ HHHHHHHCCCCCCCC	40.98	19159218
399	N-linked_Glycosylation	TFLEKHLNSSHPRSQ HHHHHHHCCCCCCCC	40.98	20068230
400	O-linked_Glycosylation	FLEKHLNSSHPRSQP HHHHHHCCCCCCCCH	36.06	30059200
405	Phosphorylation	LNSSHPRSQPAILLL HCCCCCCCCHHHHHH	44.99	21712546
424	Glutathionylation	DAEEALRCLSEQIAD CHHHHHHHHHHHHHH	5.22	22555962
449	Ubiquitination	IRIDGTDKATQDSDT EEECCCCCCCCCCCC	53.85	24816145
450	Ubiquitination	RIDGTDKATQDSDTV EECCCCCCCCCCCCE	17.19	24816145
464	Ubiquitination	VKLEVDQELSNGFKN EEEEECHHHHHCCCC	50.10	24816145
465	Ubiquitination	KLEVDQELSNGFKNG EEEECHHHHHCCCCC	3.91	24816145
466	Phosphorylation	LEVDQELSNGFKNGQ EEECHHHHHCCCCCC	33.87	27251275
467	Phosphorylation	EVDQELSNGFKNGQN EECHHHHHCCCCCCC	72.97	27251275
488	Phosphorylation	FESFPAGSTLIFYKY EECCCCCCEEEEEEE	23.34	27251275
489	Phosphorylation	ESFPAGSTLIFYKYC ECCCCCCEEEEEEEC	23.97	27251275
539	Ubiquitination	VRDFLKVKFTNSNTP HHHHHEEEECCCCCC	44.90	29967540
540	Ubiquitination	RDFLKVKFTNSNTPN HHHHEEEECCCCCCC	9.77	29967540
543	Phosphorylation	LKVKFTNSNTPNSYN HEEEECCCCCCCCCC	38.74	20068231
556	Acetylation	YNHMDPDKLNGLWSR CCCCCHHHCCCHHHH	49.60	26051181
556	Ubiquitination	YNHMDPDKLNGLWSR CCCCCHHHCCCHHHH	49.60	22817900
557	Ubiquitination	NHMDPDKLNGLWSRI CCCCHHHCCCHHHHH	8.84	21890473
571	Ubiquitination	ISHLVLPVQPENALK HHHHHCCCCCHHHHH	15.04	21890473
572	Ubiquitination	SHLVLPVQPENALKR HHHHCCCCCHHHHHC	37.34	21890473
578	2-Hydroxyisobutyrylation	VQPENALKRGICL-- CCCHHHHHCCCCC--	46.28	-
578	Ubiquitination	VQPENALKRGICL-- CCCHHHHHCCCCC--	46.28	24816145
579	Ubiquitination	QPENALKRGICL--- CCHHHHHCCCCC---	40.33	24816145
593	Ubiquitination	----------------- -----------------		24816145
594	Ubiquitination	------------------ ------------------		24816145

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
143	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TOIP1_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 TOIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LMNA_HUMAN	LMNA	physical	16248985
TOR1A_HUMAN	TOR1A	physical	20861018
TOR1A_HUMAN	TOR1A	physical	15767459
TOR1A_HUMAN	TOR1A	physical	23569223
TOR1A_HUMAN	TOR1A	physical	25352667
IF4G1_HUMAN	EIF4G1	physical	26496610
PPM1A_HUMAN	PPM1A	physical	26496610
THIO_HUMAN	TXN	physical	26496610
UBP1_HUMAN	USP1	physical	26496610
AIFM1_HUMAN	AIFM1	physical	26496610
GT2D1_HUMAN	GTF2IRD1	physical	26496610
NARF_HUMAN	NARF	physical	26496610
CSN7A_HUMAN	COPS7A	physical	26496610
PIGT_HUMAN	PIGT	physical	26496610
MIC19_HUMAN	CHCHD3	physical	26496610
MREG_HUMAN	MREG	physical	26496610
IPO4_HUMAN	IPO4	physical	26496610
PEAK1_HUMAN	PEAK1	physical	26496610
MIA40_HUMAN	CHCHD4	physical	26496610
KLH15_HUMAN	KLHL15	physical	28514442
MD2BP_HUMAN	MAD2L1BP	physical	28514442
AIFM1_HUMAN	AIFM1	physical	28514442

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 TOIP1_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-399, 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-154; SER-156; SER-157;SER-215; THR-220; SER-227 AND SER-305, 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-215; THR-220 ANDSER-315, 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 SER-135; SER-143; SER-154;SER-156; SER-157; SER-186; SER-215; THR-220; SER-305; SER-315 ANDSER-317, 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-143 AND SER-315, ANDMASS SPECTROMETRY.	18691976 [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-154; SER-156; SER-164;SER-169 AND SER-266, AND MASS SPECTROMETRY.	17525332 [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 SER-143, AND MASSSPECTROMETRY.	17924679 [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-143; SER-154; SER-163AND THR-220, AND MASS SPECTROMETRY.	17081983 [Abstract]