dbPTM

CCAR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCAR1_HUMAN
UniProt AC	Q8IX12
Protein Name	Cell division cycle and apoptosis regulator protein 1
Gene Name	CCAR1
Organism	Homo sapiens (Human).
Sequence Length	1150
Subcellular Localization	Cytoplasm, perinuclear region .
Protein Description	Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation (By similarity). May be involved in apoptosis signaling in the presence of the reinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation. [PubMed: 12816952 In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells]
Protein Sequence	MAQFGGQKNPPWATQFTATAVSQPAALGVQQPSLLGASPTIYTQQTALAAAGLTTQTPANYQLTQTAALQQQAAAAAAALQQQYSQPQQALYSVQQQLQQPQQTLLTQPAVALPTSLSLSTPQPTAQITVSYPTPRSSQQQTQPQKQRVFTGVVTKLHDTFGFVDEDVFFQLSAVKGKTPQVGDRVLVEATYNPNMPFKWNAQRIQTLPNQNQSQTQPLLKTPPAVLQPIAPQTTFGVQTQPQPQSLLQAQISAASITPLLQTQPQPLLQQPQQKAGLLQPPVRIVSQPQPARRLDPPSRFSGRNDRGDQVPNRKDDRSRERERERRRSRERSPQRKRSRERSPRRERERSPRRVRRVVPRYTVQFSKFSLDCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKNMAILDPPDADHLYSAKVMLMASPSMEDLYHKSCALAEDPQELRDGFQHPARLVKFLVGMKGKDEAMAIGGHWSPSLDGPDPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRPEETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGERKEADGEQDEEEKDDGEAKEISTPTHWSKLDPKTMKVNDLRKELESRALSSKGLKSQLIARLTKQLKVEEQKEEQKELEKSEKEEDEDDDRKSEDDKEEEERKRQEEIERQRRERRYILPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSLLSLPEKEDKKEKDKKSKKDERKDKKEERDDETDEPKPKRRKSGDDKDKKEDRDERKKEDKRKDDSKDDDETEEDNNQDEYDPMEAEEAEDEEDDRDEEEMTKRDDKRDINRYCKERPSKDKEKEKTQMITINRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQVKKLLNKVVLRESCFYRKLTDTSKDEENHEESESLQEDMLGNRLLLPTPTVKQESKDVEENVGLIVYNGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDEKTILNLENSNKSLSGELREVKKDLSQLQENLKISENMNLQFENQMNKTIRNLSTVMDEIHTVLKKDNVKNEDKDQKSKENGASV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	O-linked_Glycosylation	PPWATQFTATAVSQP CCCCCCCEEEEECCC	17.18	23301498
19	O-linked_Glycosylation	WATQFTATAVSQPAA CCCCCEEEEECCCHH	25.24	23301498
22	O-linked_Glycosylation	QFTATAVSQPAALGV CCEEEEECCCHHHCC	28.16	23301498
33	O-linked_Glycosylation	ALGVQQPSLLGASPT HHCCCCHHHCCCCCC	31.71	23301498
54	O-linked_Glycosylation	ALAAAGLTTQTPANY HHHHCCCCCCCCCHH	18.88	23301498
55	O-linked_Glycosylation	LAAAGLTTQTPANYQ HHHCCCCCCCCCHHH	35.17	23301498
115	O-linked_Glycosylation	QPAVALPTSLSLSTP CCCCCCCCEEECCCC	43.05	23301498
116	O-linked_Glycosylation	PAVALPTSLSLSTPQ CCCCCCCEEECCCCC	17.64	23301498
118	O-linked_Glycosylation	VALPTSLSLSTPQPT CCCCCEEECCCCCCC	21.75	23301498
120	O-linked_Glycosylation	LPTSLSLSTPQPTAQ CCCEEECCCCCCCEE	34.37	23301498
121	O-linked_Glycosylation	PTSLSLSTPQPTAQI CCEEECCCCCCCEEE	31.10	23301498
125	O-linked_Glycosylation	SLSTPQPTAQITVSY ECCCCCCCEEEEEEC	26.41	23301498
129	O-linked_Glycosylation	PQPTAQITVSYPTPR CCCCEEEEEECCCCC	7.42	23301498
131	O-linked_Glycosylation	PTAQITVSYPTPRSS CCEEEEEECCCCCCC	19.42	23301498
134	O-linked_Glycosylation	QITVSYPTPRSSQQQ EEEEECCCCCCCCCC	24.09	23301498
137	O-linked_Glycosylation	VSYPTPRSSQQQTQP EECCCCCCCCCCCCC	33.43	23301498
138	O-linked_Glycosylation	SYPTPRSSQQQTQPQ ECCCCCCCCCCCCCC	33.03	23301498
142	O-linked_Glycosylation	PRSSQQQTQPQKQRV CCCCCCCCCCCHHHH	37.57	23301498
146	Acetylation	QQQTQPQKQRVFTGV CCCCCCCHHHHHHHH	46.91	25953088
151	Phosphorylation	PQKQRVFTGVVTKLH CCHHHHHHHHHHHHH	26.64	23186163
179	O-linked_Glycosylation	LSAVKGKTPQVGDRV HHCCCCCCCCCCCEE	27.85	23301498
192	Phosphorylation	RVLVEATYNPNMPFK EEEEEEECCCCCCCC	35.35	22817900
199	Acetylation	YNPNMPFKWNAQRIQ CCCCCCCCEEHHHHH	33.40	26051181
214	Phosphorylation	TLPNQNQSQTQPLLK CCCCCCCCCCCCCCC	42.62	17525332
216	Phosphorylation	PNQNQSQTQPLLKTP CCCCCCCCCCCCCCC	37.08	28555341
222	O-linked_Glycosylation	QTQPLLKTPPAVLQP CCCCCCCCCCCHHCC	34.18	23301498
222	Phosphorylation	QTQPLLKTPPAVLQP CCCCCCCCCCCHHCC	34.18	26074081
240	O-linked_Glycosylation	QTTFGVQTQPQPQSL CCCCCCCCCCCCHHH	39.55	23301498
246	O-linked_Glycosylation	QTQPQPQSLLQAQIS CCCCCCHHHHHHHHH	37.42	23301498
253	O-linked_Glycosylation	SLLQAQISAASITPL HHHHHHHHHHHHHHH	13.00	23301498
256	O-linked_Glycosylation	QAQISAASITPLLQT HHHHHHHHHHHHHHC	27.06	23301498
258	O-linked_Glycosylation	QISAASITPLLQTQP HHHHHHHHHHHHCCC	12.85	23301498
263	O-linked_Glycosylation	SITPLLQTQPQPLLQ HHHHHHHCCCCCHHC	42.03	23301498
287	O-linked_Glycosylation	QPPVRIVSQPQPARR CCCEEEECCCCCCCC	33.50	23301498
287	Phosphorylation	QPPVRIVSQPQPARR CCCEEEECCCCCCCC	33.50	27732954
302	Phosphorylation	LDPPSRFSGRNDRGD CCCCCCCCCCCCCCC	35.41	23186163
318	Phosphorylation	VPNRKDDRSRERERE CCCCCCHHHHHHHHH	47.98	33259812
319	Phosphorylation	PNRKDDRSRERERER CCCCCHHHHHHHHHH	45.55	17081983
329	Phosphorylation	RERERRRSRERSPQR HHHHHHHHHHHCHHH	36.36	22817900
333	Phosphorylation	RRRSRERSPQRKRSR HHHHHHHCHHHHHHH	22.19	33259812
339	Phosphorylation	RSPQRKRSRERSPRR HCHHHHHHHHCCHHH	41.34	20068231
343	Phosphorylation	RKRSRERSPRRERER HHHHHHCCHHHHHHC	20.29	20068231
351	Phosphorylation	PRRERERSPRRVRRV HHHHHHCCHHHHHHH	20.29	17081983
368	Ubiquitination	RYTVQFSKFSLDCPS EEEEEEEECCCCCCC	40.02	-
378	Sulfoxidation	LDCPSCDMMELRRRY CCCCCCCHHHHHHHH	2.36	21406390
416	Phosphorylation	RPFQLGNYCNFYVMH CCCCCCCCCCEEEEH	6.23	22461510
431	Acetylation	REVESLEKNMAILDP HHHHHHHHHHCCCCC	58.26	26051181
445	Phosphorylation	PPDADHLYSAKVMLM CCCHHHHHHHEEEHH	11.80	20068231
446	Phosphorylation	PDADHLYSAKVMLMA CCHHHHHHHEEEHHC	28.15	20068231
454	Phosphorylation	AKVMLMASPSMEDLY HEEEHHCCCCHHHHH	11.98	22115753
456	Phosphorylation	VMLMASPSMEDLYHK EEHHCCCCHHHHHHH	32.10	25159151
461	Phosphorylation	SPSMEDLYHKSCALA CCCHHHHHHHHHHHC	21.37	28450419
463	Acetylation	SMEDLYHKSCALAED CHHHHHHHHHHHCCC	33.40	26051181
465	Glutathionylation	EDLYHKSCALAEDPQ HHHHHHHHHHCCCHH	4.25	22555962
471	Ubiquitination	SCALAEDPQELRDGF HHHHCCCHHHHHHCC	22.50	21890473
471 (in isoform 2)	Ubiquitination	-	22.50	21890473
477	Ubiquitination	DPQELRDGFQHPARL CHHHHHHCCCCHHHH	20.06	29967540
486	Acetylation	QHPARLVKFLVGMKG CCHHHHHHHHHCCCC	37.26	25953088
486	Ubiquitination	QHPARLVKFLVGMKG CCHHHHHHHHHCCCC	37.26	22817900
486 (in isoform 1)	Ubiquitination	-	37.26	21890473
492	Ubiquitination	VKFLVGMKGKDEAMA HHHHHCCCCCCCCCC	57.80	29967540
505	Phosphorylation	MAIGGHWSPSLDGPD CCCCCCCCCCCCCCC	10.03	-
515	Acetylation	LDGPDPEKDPSVLIK CCCCCCCCCHHHHHH	79.08	26051181
537	Phosphorylation	ALTGIDLSVCTQWYR HHHCCCHHHHHHHHH	16.05	27174698
540	Phosphorylation	GIDLSVCTQWYRFAE CCCHHHHHHHHHHHE	21.71	27174698
543	Phosphorylation	LSVCTQWYRFAEIRY HHHHHHHHHHHEEEE	5.99	27174698
550	Phosphorylation	YRFAEIRYHRPEETH HHHHEEEECCCCCCC	14.08	27174698
585	Ubiquitination	HCLPTRSEWETLSRG HHCCCHHHHHHHHHH	46.14	29967540
594	2-Hydroxyisobutyrylation	ETLSRGYKQQLVEKL HHHHHHHHHHHHHHH	34.10	-
594	Acetylation	ETLSRGYKQQLVEKL HHHHHHHHHHHHHHH	34.10	26051181
594	Ubiquitination	ETLSRGYKQQLVEKL HHHHHHHHHHHHHHH	34.10	-
600	2-Hydroxyisobutyrylation	YKQQLVEKLQGERKE HHHHHHHHHHHHHCC	38.33	-
600	Ubiquitination	YKQQLVEKLQGERKE HHHHHHHHHHHHHCC	38.33	29967540
608	Ubiquitination	LQGERKEADGEQDEE HHHHHCCCCCCCCHH	32.89	29967540
612	Phosphorylation	RKEADGEQDEEEKDD HCCCCCCCCHHHCCC	69.79	32142685
618	Ubiquitination	EQDEEEKDDGEAKEI CCCHHHCCCCCCCCC	72.87	22817900
622	Ubiquitination	EEKDDGEAKEISTPT HHCCCCCCCCCCCCC	21.95	18655026
623	Ubiquitination	EKDDGEAKEISTPTH HCCCCCCCCCCCCCC	51.80	29967540
625	Ubiquitination	DDGEAKEISTPTHWS CCCCCCCCCCCCCHH	5.68	22817900
626	Phosphorylation	DGEAKEISTPTHWSK CCCCCCCCCCCCHHH	29.44	23401153
627	Phosphorylation	GEAKEISTPTHWSKL CCCCCCCCCCCHHHC	37.56	25159151
629	Phosphorylation	AKEISTPTHWSKLDP CCCCCCCCCHHHCCC	35.74	30266825
632	Phosphorylation	ISTPTHWSKLDPKTM CCCCCCHHHCCCCCC	18.75	30266825
633	Ubiquitination	STPTHWSKLDPKTMK CCCCCHHHCCCCCCC	52.28	22817900
637	Ubiquitination	HWSKLDPKTMKVNDL CHHHCCCCCCCHHHH	62.00	18655026
640	2-Hydroxyisobutyrylation	KLDPKTMKVNDLRKE HCCCCCCCHHHHHHH	43.02	-
640	Ubiquitination	KLDPKTMKVNDLRKE HCCCCCCCHHHHHHH	43.02	22817900
650	Phosphorylation	DLRKELESRALSSKG HHHHHHHHHHHHCCC	35.16	-
659	2-Hydroxyisobutyrylation	ALSSKGLKSQLIARL HHHCCCHHHHHHHHH	44.84	-
659	Acetylation	ALSSKGLKSQLIARL HHHCCCHHHHHHHHH	44.84	18530607
667	Phosphorylation	SQLIARLTKQLKVEE HHHHHHHHHHHCHHH	15.93	27422710
685	Phosphorylation	EQKELEKSEKEEDED HHHHHHHHHCCCCCC	44.52	26657352
697	Phosphorylation	DEDDDRKSEDDKEEE CCCCCCCCCCHHHHH	47.34	25159151
738	Acetylation	VHPNWAAKSGKFDCS ECCCHHHHCCCCCEE	52.58	25953088
785	Methylation	LQRDFGVRIYKSLLS HHHHHHHHHHHHHHC	27.22	-
799	Ubiquitination	SLPEKEDKKEKDKKS CCCHHHCHHHHHHHC	65.02	24816145
814	Ubiquitination	KKDERKDKKEERDDE HHHHHHHHHHHCCCC	66.18	24816145
822	Phosphorylation	KEERDDETDEPKPKR HHHCCCCCCCCCCCC	53.29	28985074
823	Ubiquitination	EERDDETDEPKPKRR HHCCCCCCCCCCCCC	69.06	24816145
832	Phosphorylation	PKPKRRKSGDDKDKK CCCCCCCCCCCCCCC	45.72	26657352
838	Ubiquitination	KSGDDKDKKEDRDER CCCCCCCCCCHHHHH	64.90	24816145
855	Phosphorylation	EDKRKDDSKDDDETE HHHCCCCCCCCCCCC	48.39	23186163
861	Phosphorylation	DSKDDDETEEDNNQD CCCCCCCCCCCCCCC	52.23	25218447
870	Phosphorylation	EDNNQDEYDPMEAEE CCCCCCCCCHHHHHH	33.37	21406692
891	Phosphorylation	DRDEEEMTKRDDKRD CCCHHHHHHHHHHHH	26.63	21406692
908	Phosphorylation	RYCKERPSKDKEKEK HHHHHCCCCCCHHHH	60.76	22468782
963	Ubiquitination	LSRAQVKKLLNKVVL CCHHHHHHHHHHHHH	60.39	29967540
978	Malonylation	RESCFYRKLTDTSKD HHHHHHHHCCCCCCC	44.34	32601280
978	Ubiquitination	RESCFYRKLTDTSKD HHHHHHHHCCCCCCC	44.34	29967540
980	Phosphorylation	SCFYRKLTDTSKDEE HHHHHHCCCCCCCCC	40.02	23186163
982	Phosphorylation	FYRKLTDTSKDEENH HHHHCCCCCCCCCCH	32.23	27251275
983	Phosphorylation	YRKLTDTSKDEENHE HHHCCCCCCCCCCHH	40.70	27251275
992	Phosphorylation	DEENHEESESLQEDM CCCCHHHCHHHHHHH	29.51	23403867
994	Phosphorylation	ENHEESESLQEDMLG CCHHHCHHHHHHHHC	44.63	21712546
997	Ubiquitination	EESESLQEDMLGNRL HHCHHHHHHHHCCCC	51.16	33845483
1008	Phosphorylation	GNRLLLPTPTVKQES CCCCCCCCCCCCCCC	31.40	29978859
1010	Phosphorylation	RLLLPTPTVKQESKD CCCCCCCCCCCCCCC	42.70	29978859
1012	Sumoylation	LLPTPTVKQESKDVE CCCCCCCCCCCCCHH	51.32	-
1012	Sumoylation	LLPTPTVKQESKDVE CCCCCCCCCCCCCHH	51.32	25114211
1012	Ubiquitination	LLPTPTVKQESKDVE CCCCCCCCCCCCCHH	51.32	33845483
1015	Phosphorylation	TPTVKQESKDVEENV CCCCCCCCCCHHHCE	31.49	25278378
1027	Phosphorylation	ENVGLIVYNGAMVDV HCEEEEEECCEECCH	10.82	25278378
1036	Phosphorylation	GAMVDVGSLLQKLEK CEECCHHHHHHHHHH	26.25	25278378
1039	Ubiquitination	VDVGSLLQKLEKSEK CCHHHHHHHHHHHHH	54.29	22817900
1039 (in isoform 2)	Ubiquitination	-	54.29	21890473
1054	2-Hydroxyisobutyrylation	VRAEVEQKLQLLEEK HHHHHHHHHHHHHHC	25.37	-
1054	Ubiquitination	VRAEVEQKLQLLEEK HHHHHHHHHHHHHHC	25.37	22817900
1054 (in isoform 1)	Ubiquitination	-	25.37	21890473
1062	Ubiquitination	LQLLEEKTDEDEKTI HHHHHHCCCCCHHHH	48.15	33845483
1067	Sumoylation	EKTDEDEKTILNLEN HCCCCCHHHHHHHHH	53.86	-
1067	Acetylation	EKTDEDEKTILNLEN HCCCCCHHHHHHHHH	53.86	26051181
1067	Sumoylation	EKTDEDEKTILNLEN HCCCCCHHHHHHHHH	53.86	28112733
1072	Ubiquitination	DEKTILNLENSNKSL CHHHHHHHHHCCCCC	6.21	22817900
1073	Ubiquitination	EKTILNLENSNKSLS HHHHHHHHHCCCCCC	58.50	21890473
1073 (in isoform 2)	Ubiquitination	-	58.50	21890473
1075	Phosphorylation	TILNLENSNKSLSGE HHHHHHHCCCCCCHH	35.94	28450419
1077	Ubiquitination	LNLENSNKSLSGELR HHHHHCCCCCCHHHH	53.23	33845483
1078	Phosphorylation	NLENSNKSLSGELRE HHHHCCCCCCHHHHH	31.83	25159151
1080	Phosphorylation	ENSNKSLSGELREVK HHCCCCCCHHHHHHH	36.99	25159151
1087	Ubiquitination	SGELREVKKDLSQLQ CHHHHHHHHHHHHHH	35.50	22817900
1088	Ubiquitination	GELREVKKDLSQLQE HHHHHHHHHHHHHHH	69.91	22817900
1088 (in isoform 1)	Ubiquitination	-	69.91	21890473
1091	Phosphorylation	REVKKDLSQLQENLK HHHHHHHHHHHHHHC	38.69	20873877
1100	Phosphorylation	LQENLKISENMNLQF HHHHHCCCHHHCHHH	22.72	-
1114	Phosphorylation	FENQMNKTIRNLSTV HHHHHHHHHHHHHHH	21.84	-
1130	2-Hydroxyisobutyrylation	DEIHTVLKKDNVKNE HHHHHHHHHCCCCCC	54.46	-
1130	Acetylation	DEIHTVLKKDNVKNE HHHHHHHHHCCCCCC	54.46	25953088
1135	Sumoylation	VLKKDNVKNEDKDQK HHHHCCCCCCCCHHH	61.96	-
1135	Sumoylation	VLKKDNVKNEDKDQK HHHHCCCCCCCCHHH	61.96	25218447
1149	Phosphorylation	KSKENGASV------ HHHHCCCCC------	29.74	15302935

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 CCAR1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CCAR1_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 CCAR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_HUMAN	MDM2	physical	18382127
P53_HUMAN	TP53	physical	18382127
U2AF2_HUMAN	U2AF2	physical	22365833
CHERP_HUMAN	CHERP	physical	22365833
RBM10_HUMAN	RBM10	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
R113A_HUMAN	RNF113A	physical	22365833
PIHD3_HUMAN	PIH1D3	physical	25416956
ACTZ_HUMAN	ACTR1A	physical	26344197
ACTY_HUMAN	ACTR1B	physical	26344197
CAND1_HUMAN	CAND1	physical	26344197
DCTN1_HUMAN	DCTN1	physical	26344197
DCTN2_HUMAN	DCTN2	physical	26344197
DC1I2_HUMAN	DYNC1I2	physical	26344197
PCNA_HUMAN	PCNA	physical	26344197
PRI1_HUMAN	PRIM1	physical	26344197
PSMD4_HUMAN	PSMD4	physical	26344197
SAFB2_HUMAN	SAFB2	physical	26344197
TB182_HUMAN	TNKS1BP1	physical	26344197
TPM2_HUMAN	TPM2	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 CCAR1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-214, 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-329; SER-333; SER-339AND SER-343, AND MASS SPECTROMETRY.	17081983 [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-1149, AND MASSSPECTROMETRY.	15302935 [Abstract]
Ubiquitylation
Reference	PubMed
"Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells."; Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.; Proteomics 8:2885-2896(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-637, AND MASSSPECTROMETRY.	18655026 [Abstract]