dbPTM

COPB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COPB2_HUMAN
UniProt AC	P35606
Protein Name	Coatomer subunit beta'
Gene Name	COPB2
Organism	Homo sapiens (Human).
Sequence Length	906
Subcellular Localization	Cytoplasm, cytosol. Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane Peripheral membrane protein Cytoplasmic side. The coatomer is cytoplasmic or polymerized on the cytoplasm
Protein Description	The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).; This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner (By similarity). Interacts with JAGN1..
Protein Sequence	MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWDNTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIISYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLATASGNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEGKDFQPSRSTAQQELDGKPASPTPVIVASHTANKEEKSLLELEVDLDNLELEDIDTTDINLDEDILDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	LDIKRKLTARSDRVK CHHHHHHHCCCCCEE	24.06	23828894
15	Phosphorylation	KRKLTARSDRVKSVD HHHHHCCCCCEEEEE	27.57	22817900
20	Phosphorylation	ARSDRVKSVDLHPTE CCCCCEEEEECCCCC	20.29	22817900
26	Phosphorylation	KSVDLHPTEPWMLAS EEEECCCCCHHHHHH	43.88	22817900
40	Ubiquitination	SLYNGSVCVWNHETQ HHHCCCEEEEECCCC	2.92	-
59	Ubiquitination	TFEVCDLPVRAAKFV EEEECCCCHHHHHHH	10.57	22817900
64	2-Hydroxyisobutyrylation	DLPVRAAKFVARKNW CCCHHHHHHHHCCCE	39.11	-
64	Acetylation	DLPVRAAKFVARKNW CCCHHHHHHHHCCCE	39.11	27452117
64	Ubiquitination	DLPVRAAKFVARKNW CCCHHHHHHHHCCCE	39.11	21890473
69	Ubiquitination	AAKFVARKNWVVTGA HHHHHHCCCEEEECC	45.48	-
74	Ubiquitination	ARKNWVVTGADDMQI HCCCEEEECCCCCEE	19.62	21890473
79	Sulfoxidation	VVTGADDMQIRVFNY EEECCCCCEEEEECC	3.52	30846556
86	Phosphorylation	MQIRVFNYNTLERVH CEEEEECCCCCCEEE	9.69	28152594
88	Phosphorylation	IRVFNYNTLERVHMF EEEECCCCCCEEEEC	21.45	28152594
92	Ubiquitination	NYNTLERVHMFEAHS CCCCCCEEEECCCCC	2.54	23000965
94	Sulfoxidation	NTLERVHMFEAHSDY CCCCEEEECCCCCCE	2.72	30846556
99	Phosphorylation	VHMFEAHSDYIRCIA EEECCCCCCEEEEEE	38.87	24719451
101	Phosphorylation	MFEAHSDYIRCIAVH ECCCCCCEEEEEEEC	8.03	28064214
116	Phosphorylation	PTQPFILTSSDDMLI CCCCEEEECCCCEEE	22.74	-
132	Ubiquitination	LWDWDKKWSCSQVFE HHCCCCCCCHHEEEC	15.43	21890473
139	Ubiquitination	WSCSQVFEGHTHYVM CCHHEEECCCCEEEE	51.73	-
139	Ubiquitination	WSCSQVFEGHTHYVM CCHHEEECCCCEEEE	51.73	21890473
165	Methylation	FASASLDRTIKVWQL CCCEECCCEEEEEEC	43.58	-
168	Ubiquitination	ASLDRTIKVWQLGSS EECCCEEEEEECCCC	36.49	21890473
168	Ubiquitination	ASLDRTIKVWQLGSS EECCCEEEEEECCCC	36.49	23000965
170	Ubiquitination	LDRTIKVWQLGSSSP CCCEEEEEECCCCCC	5.23	-
174	Phosphorylation	IKVWQLGSSSPNFTL EEEEECCCCCCCCEE	35.91	25627689
175	Phosphorylation	KVWQLGSSSPNFTLE EEEECCCCCCCCEEE	48.28	25627689
176	Phosphorylation	VWQLGSSSPNFTLEG EEECCCCCCCCEEEC	26.09	25159151
183	Ubiquitination	SPNFTLEGHEKGVNC CCCCEEECCCCCCCE	37.05	-
186	Ubiquitination	FTLEGHEKGVNCIDY CEEECCCCCCCEEEE	63.59	29967540
193	Phosphorylation	KGVNCIDYYSGGDKP CCCCEEEECCCCCCC	4.61	21406692
194	Phosphorylation	GVNCIDYYSGGDKPY CCCEEEECCCCCCCE	9.33	21406692
195	Phosphorylation	VNCIDYYSGGDKPYL CCEEEECCCCCCCEE	30.03	21406692
199	Acetylation	DYYSGGDKPYLISGA EECCCCCCCEEEECC	38.55	26051181
199	Ubiquitination	DYYSGGDKPYLISGA EECCCCCCCEEEECC	38.55	29967540
201	Phosphorylation	YSGGDKPYLISGADD CCCCCCCEEEECCCC	23.55	21406692
204	Phosphorylation	GDKPYLISGADDRLV CCCCEEEECCCCCEE	25.90	21406692
212	Ubiquitination	GADDRLVKIWDYQNK CCCCCEEEEEECCCC	42.54	29967540
271	Sulfoxidation	ESTLNYGMERVWCVA EEEECCCCCEEEEEE	1.78	30846556
284	Ubiquitination	VASLRGSNNVALGYD EEEECCCCCEEEECC	50.23	22817900
289	Acetylation	GSNNVALGYDEGSII CCCCEEEECCCCCEE	20.36	-
289	Ubiquitination	GSNNVALGYDEGSII CCCCEEEECCCCCEE	20.36	-
289	Ubiquitination	GSNNVALGYDEGSII CCCCEEEECCCCCEE	20.36	21890473
299	Ubiquitination	EGSIIVKLGREEPAM CCCEEEEECCCCCCC	5.61	-
299	Ubiquitination	EGSIIVKLGREEPAM CCCEEEEECCCCCCC	5.61	21890473
313	Ubiquitination	MSMDANGKIIWAKHS CCCCCCCCEEEECCH	30.72	22817900
317	Ubiquitination	ANGKIIWAKHSEVQQ CCCCEEEECCHHHHH	6.83	-
317	Ubiquitination	ANGKIIWAKHSEVQQ CCCCEEEECCHHHHH	6.83	23000965
318	Ubiquitination	NGKIIWAKHSEVQQA CCCEEEECCHHHHHH	32.44	21890473
318	Acetylation	NGKIIWAKHSEVQQA CCCEEEECCHHHHHH	32.44	21466224
318	Ubiquitination	NGKIIWAKHSEVQQA CCCEEEECCHHHHHH	32.44	22817900
328	Ubiquitination	EVQQANLKAMGDAEI HHHHHCHHHHCCCCC	35.81	21890473
328	Malonylation	EVQQANLKAMGDAEI HHHHHCHHHHCCCCC	35.81	26320211
328	Ubiquitination	EVQQANLKAMGDAEI HHHHHCHHHHCCCCC	35.81	22817900
336	Ubiquitination	AMGDAEIKDGERLPL HHCCCCCCCCCCCCE	51.70	33845483
346	Ubiquitination	ERLPLAVKDMGSCEI CCCCEEEEECCCCEE	36.07	21890473
346	Acetylation	ERLPLAVKDMGSCEI CCCCEEEEECCCCEE	36.07	25953088
346	Malonylation	ERLPLAVKDMGSCEI CCCCEEEEECCCCEE	36.07	26320211
346	Ubiquitination	ERLPLAVKDMGSCEI CCCCEEEEECCCCEE	36.07	23000965
350	Phosphorylation	LAVKDMGSCEIYPQT EEEEECCCCEEECCE	11.26	28348404
354	Phosphorylation	DMGSCEIYPQTIQHN ECCCCEEECCEEEEC	2.72	19658100
354	Ubiquitination	DMGSCEIYPQTIQHN ECCCCEEECCEEEEC	2.72	21890473
357	Acetylation	SCEIYPQTIQHNPNG CCEEECCEEEECCCC	20.35	-
357	Ubiquitination	SCEIYPQTIQHNPNG CCEEECCEEEECCCC	20.35	-
357	Ubiquitination	SCEIYPQTIQHNPNG CCEEECCEEEECCCC	20.35	21890473
361	Ubiquitination	YPQTIQHNPNGRFVV ECCEEEECCCCCEEE	18.50	24816145
379	Phosphorylation	DGEYIIYTAMALRNK CCCEEEEEEEHHCCC	10.27	22210691
386	Ubiquitination	TAMALRNKSFGSAQE EEEHHCCCCCCCHHH	40.50	21890473
386	Acetylation	TAMALRNKSFGSAQE EEEHHCCCCCCCHHH	40.50	23236377
386	Malonylation	TAMALRNKSFGSAQE EEEHHCCCCCCCHHH	40.50	26320211
386	Ubiquitination	TAMALRNKSFGSAQE EEEHHCCCCCCCHHH	40.50	21890473
387	Phosphorylation	AMALRNKSFGSAQEF EEHHCCCCCCCHHHH	38.09	22210691
390	Phosphorylation	LRNKSFGSAQEFAWA HCCCCCCCHHHHHHC	25.43	22210691
401	Phosphorylation	FAWAHDSSEYAIRES HHHCCCCCHHHHHHC	40.46	21601212
403	Phosphorylation	WAHDSSEYAIRESNS HCCCCCHHHHHHCCC	14.85	-
413	Ubiquitination	RESNSIVKIFKNFKE HHCCCHHHHHHCHHC	40.53	33845483
415	Ubiquitination	SNSIVKIFKNFKEKK CCCHHHHHHCHHCCC	4.36	16196087
423	O-linked_Glycosylation	KNFKEKKSFKPDFGA HCHHCCCCCCCCCCC	49.96	29485866
425	Ubiquitination	FKEKKSFKPDFGAES HHCCCCCCCCCCCCC	51.25	-
432	O-linked_Glycosylation	KPDFGAESIYGGFLL CCCCCCCCHHCCCCC	22.15	29485866
443	Phosphorylation	GFLLGVRSVNGLAFY CCCCEEEEECCEEEE	19.96	27050516
470	Ubiquitination	IQPKHIFWSDSGELV ECCCEEEECCCCCEE	10.71	23000965
525	Ubiquitination	GEIQEIVKTGLWVGD HHHHHHHHHCCEECC	42.40	22817900
526	Phosphorylation	EIQEIVKTGLWVGDC HHHHHHHHCCEECCE	26.98	26846344
529	Ubiquitination	EIVKTGLWVGDCFIY HHHHHCCEECCEEEE	8.06	22817900
536	Phosphorylation	WVGDCFIYTSSVNRL EECCEEEEECCCCCE	4.74	26846344
537	Phosphorylation	VGDCFIYTSSVNRLN ECCEEEEECCCCCEE	15.09	26846344
538	Phosphorylation	GDCFIYTSSVNRLNY CCEEEEECCCCCEEE	18.47	26846344
539	Phosphorylation	DCFIYTSSVNRLNYY CEEEEECCCCCEEEE	18.66	26846344
560	Phosphorylation	TIAHLDRTMYLLGYI EEEECCCCCHHEEEE	15.16	24043423
562	Phosphorylation	AHLDRTMYLLGYIPK EECCCCCHHEEEECC	9.73	28509920
566	Phosphorylation	RTMYLLGYIPKDNRL CCCHHEEEECCCCEE	17.64	24043423
568	Ubiquitination	MYLLGYIPKDNRLYL CHHEEEECCCCEEEC	29.48	22817900
569	Acetylation	YLLGYIPKDNRLYLG HHEEEECCCCEEECC	59.06	26051181
574	Phosphorylation	IPKDNRLYLGDKELN ECCCCEEECCCCEEE	12.85	22210691
579	Ubiquitination	RLYLGDKELNIISYS EEECCCCEEEEEEHH	52.36	-
579	Ubiquitination	RLYLGDKELNIISYS EEECCCCEEEEEEHH	52.36	21890473
586	Ubiquitination	ELNIISYSLLVSVLE EEEEEEHHHHHHHHH	14.40	24816145
594	Phosphorylation	LLVSVLEYQTAVMRR HHHHHHHHHHHHHHC	13.65	22210691
596	Phosphorylation	VSVLEYQTAVMRRDF HHHHHHHHHHHHCCC	21.96	22210691
598	Acetylation	VLEYQTAVMRRDFSM HHHHHHHHHHCCCCC	3.30	-
598	Ubiquitination	VLEYQTAVMRRDFSM HHHHHHHHHHCCCCC	3.30	-
604	Phosphorylation	AVMRRDFSMADKVLP HHHHCCCCCHHHCCC	19.83	27499020
608	Ubiquitination	RDFSMADKVLPTIPK CCCCCHHHCCCCCCH	35.81	21890473
608	Ubiquitination	RDFSMADKVLPTIPK CCCCCHHHCCCCCCH	35.81	23000965
612	Phosphorylation	MADKVLPTIPKEQRT CHHHCCCCCCHHHHH	45.83	20068231
615	Malonylation	KVLPTIPKEQRTRVA HCCCCCCHHHHHHHH	63.73	26320211
615	Ubiquitination	KVLPTIPKEQRTRVA HCCCCCCHHHHHHHH	63.73	33845483
627	2-Hydroxyisobutyrylation	RVAHFLEKQGFKQQA HHHHHHHHCCCCEEE	58.84	-
627	Acetylation	RVAHFLEKQGFKQQA HHHHHHHHCCCCEEE	58.84	19608861
627	Malonylation	RVAHFLEKQGFKQQA HHHHHHHHCCCCEEE	58.84	26320211
627	Ubiquitination	RVAHFLEKQGFKQQA HHHHHHHHCCCCEEE	58.84	19608861
640	Ubiquitination	QALTVSTDPEHRFEL EEEEEECCHHHHHHH	38.80	16196087
658	Phosphorylation	LGELKIAYQLAVEAE HCCHHHHHHHHHHHC	13.92	28152594
669	Ubiquitination	VEAESEQKWKQLAEL HHHCCHHHHHHHHHH	52.92	16196087
679	Phosphorylation	QLAELAISKCQFGLA HHHHHHHHHCHHHCH	23.05	21406692
695	Ubiquitination	ECLHHAQDYGGLLLL HHHHHCHHCCCEEEE	44.84	-
695	Ubiquitination	ECLHHAQDYGGLLLL HHHHHCHHCCCEEEE	44.84	23000965
696	Phosphorylation	CLHHAQDYGGLLLLA HHHHCHHCCCEEEEE	10.87	-
724	Ubiquitination	EGAERDGKNNVAFMS HHHHHCCCCCEEHHH	50.03	23000965
730	Sulfoxidation	GKNNVAFMSYFLQGK CCCCEEHHHHHHCCH	1.98	28183972
731	Phosphorylation	KNNVAFMSYFLQGKV CCCEEHHHHHHCCHH	13.28	-
732	Phosphorylation	NNVAFMSYFLQGKVD CCEEHHHHHHCCHHH	9.12	-
742	Ubiquitination	QGKVDACLELLIRTG CCHHHHHHHHHHHHC	5.79	-
750	Ubiquitination	ELLIRTGRLPEAAFL HHHHHHCCCCHHHHH	46.59	22817900
754	Ubiquitination	RTGRLPEAAFLARTY HHCCCCHHHHHHHHC	11.11	-
754	Ubiquitination	RTGRLPEAAFLARTY HHCCCCHHHHHHHHC	11.11	22817900
760	Phosphorylation	EAAFLARTYLPSQVS HHHHHHHHCCHHHHH	24.65	20860994
761	Phosphorylation	AAFLARTYLPSQVSR HHHHHHHCCHHHHHH	15.86	28152594
767	Phosphorylation	TYLPSQVSRVVKLWR HCCHHHHHHHHHHHH	16.24	20860994
771	Ubiquitination	SQVSRVVKLWRENLS HHHHHHHHHHHHHHH	39.20	-
778	Phosphorylation	KLWRENLSKVNQKAA HHHHHHHHHHHHHHH	46.25	25849741
779	Ubiquitination	LWRENLSKVNQKAAE HHHHHHHHHHHHHHH	48.66	22817900
783	Ubiquitination	NLSKVNQKAAESLAD HHHHHHHHHHHHHCC	44.34	21906983
787	Phosphorylation	VNQKAAESLADPTEY HHHHHHHHHCCCHHH	24.91	20068231
792	Phosphorylation	AESLADPTEYENLFP HHHHCCCHHHHHCCC	52.31	27251275
793	Ubiquitination	ESLADPTEYENLFPG HHHCCCHHHHHCCCH	57.12	-
793	Ubiquitination	ESLADPTEYENLFPG HHHCCCHHHHHCCCH	57.12	22817900
794	Nitration	SLADPTEYENLFPGL HHCCCHHHHHCCCHH	16.76	-
794	Phosphorylation	SLADPTEYENLFPGL HHCCCHHHHHCCCHH	16.76	28796482
811	Ubiquitination	AFVVEEWVKETHADL HHHHHHHHHHHCCCC	4.55	24816145
822	Ubiquitination	HADLWPAKQYPLVTP CCCCCCHHHCCCCCC	46.41	22817900
828	Phosphorylation	AKQYPLVTPNEERNV HHHCCCCCCCHHCCC	28.25	26657352
833	Methylation	LVTPNEERNVMEEGK CCCCCHHCCCHHCCC	34.56	-
836	Sulfoxidation	PNEERNVMEEGKDFQ CCHHCCCHHCCCCCC	4.42	21406390
840	Ubiquitination	RNVMEEGKDFQPSRS CCCHHCCCCCCCCCC	59.66	24816145
845	Phosphorylation	EGKDFQPSRSTAQQE CCCCCCCCCCCHHHH	28.25	20860994
847	Phosphorylation	KDFQPSRSTAQQELD CCCCCCCCCHHHHHC	32.22	29209046
848	Phosphorylation	DFQPSRSTAQQELDG CCCCCCCCHHHHHCC	27.63	29209046
859	Phosphorylation	ELDGKPASPTPVIVA HHCCCCCCCCCEEEE	37.52	29255136
861	Phosphorylation	DGKPASPTPVIVASH CCCCCCCCCEEEEEC	27.91	22167270
867	Phosphorylation	PTPVIVASHTANKEE CCCEEEEECCCCHHH	15.52	20201521
869	Phosphorylation	PVIVASHTANKEEKS CEEEEECCCCHHHHH	29.45	29209046
872	Ubiquitination	VASHTANKEEKSLLE EEECCCCHHHHHEEE	65.86	33845483
876	Phosphorylation	TANKEEKSLLELEVD CCCHHHHHEEEEEEE	41.27	26074081

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
Oops, there are no upstream regulatory protein records of COPB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of COPB2_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 COPB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
COPA_HUMAN	COPA	physical	10921873
COPE_HUMAN	COPE	physical	10921873
COPG1_HUMAN	COPG1	physical	10921873
RGS4_HUMAN	RGS4	physical	10982407
RGS2_HUMAN	RGS2	physical	10982407
TMEDA_HUMAN	TMED10	physical	9751720
COPA_HUMAN	COPA	physical	9482852
COPB2_HUMAN	COPB2	physical	9482852
COPE_HUMAN	COPE	physical	9482852
COPA_HUMAN	COPA	physical	14729954
COPB_HUMAN	COPB1	physical	14729954
COPG1_HUMAN	COPG1	physical	14729954
COPG2_HUMAN	COPG2	physical	14729954
COPD_HUMAN	ARCN1	physical	14729954
COPB2_HUMAN	COPB2	physical	14729954
COPG1_HUMAN	COPG1	physical	22939629
COPD_HUMAN	ARCN1	physical	22939629
COPB_HUMAN	COPB1	physical	22939629
COPE_HUMAN	COPE	physical	22939629
COPG2_HUMAN	COPG2	physical	22939629
COPZ1_HUMAN	COPZ1	physical	22939629
NFKB1_HUMAN	NFKB1	physical	21988832
COPA_HUMAN	COPA	physical	22863883
COPZ1_HUMAN	COPZ1	physical	22863883
KLC4_HUMAN	KLC4	physical	22863883
RUFY1_HUMAN	RUFY1	physical	22863883
TELO2_HUMAN	TELO2	physical	22863883
TTI1_HUMAN	TTI1	physical	22863883
COPA_HUMAN	COPA	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
COPG1_HUMAN	COPG1	physical	26344197
COPZ1_HUMAN	COPZ1	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197
TBB4B_HUMAN	TUBB4B	physical	26344197

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 COPB2_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-318 AND LYS-627, AND MASSSPECTROMETRY.	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-859, 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-859 AND THR-861, ANDMASS 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-859, AND MASSSPECTROMETRY.	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-859, AND MASSSPECTROMETRY.	18691976 [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-859, 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-859, AND MASSSPECTROMETRY.	17081983 [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-354, AND MASSSPECTROMETRY.	18083107 [Abstract]