dbPTM

PSA6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSA6_HUMAN
UniProt AC	P60900
Protein Name	Proteasome subunit alpha type-6
Gene Name	PSMA6
Organism	Homo sapiens (Human).
Sequence Length	246
Subcellular Localization	Cytoplasm . Nucleus . Colocalizes with TRIM5 in cytoplasmic bodies.
Protein Description	Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex)..
Protein Sequence	MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSRGSSAGF ------CCCCCCCCC	45.40	19413330
2	Phosphorylation	------MSRGSSAGF ------CCCCCCCCC	45.40	28450419
3	Methylation	-----MSRGSSAGFD -----CCCCCCCCCC	47.95	115367909
5	O-linked_Glycosylation	---MSRGSSAGFDRH ---CCCCCCCCCCCE	18.86	UniProtKB CARBOHYD
5	Phosphorylation	---MSRGSSAGFDRH ---CCCCCCCCCCCE	18.86	22115753
6	Phosphorylation	--MSRGSSAGFDRHI --CCCCCCCCCCCEE	34.92	21815630
11	Methylation	GSSAGFDRHITIFSP CCCCCCCCEEEEECC	22.35	115489337
14	Phosphorylation	AGFDRHITIFSPEGR CCCCCEEEEECCCCC	15.16	29396449
17	Phosphorylation	DRHITIFSPEGRLYQ CCEEEEECCCCCEEE	20.42	25159151
21	Methylation	TIFSPEGRLYQVEYA EEECCCCCEEEEEEH	28.67	115489345
23	Ubiquitination	FSPEGRLYQVEYAFK ECCCCCEEEEEEHHH	14.78	-
23	Acetylation	FSPEGRLYQVEYAFK ECCCCCEEEEEEHHH	14.78	19608861
23	Phosphorylation	FSPEGRLYQVEYAFK ECCCCCEEEEEEHHH	14.78	28152594
23	Ubiquitination	FSPEGRLYQVEYAFK ECCCCCEEEEEEHHH	14.78	19608861
25	Acetylation	PEGRLYQVEYAFKAI CCCCEEEEEEHHHHH	3.72	-
25	Ubiquitination	PEGRLYQVEYAFKAI CCCCEEEEEEHHHHH	3.72	-
25	Acetylation	PEGRLYQVEYAFKAI CCCCEEEEEEHHHHH	3.72	19608861
25	Ubiquitination	PEGRLYQVEYAFKAI CCCCEEEEEEHHHHH	3.72	19608861
26	Acetylation	EGRLYQVEYAFKAIN CCCEEEEEEHHHHHH	18.67	-
26	Ubiquitination	EGRLYQVEYAFKAIN CCCEEEEEEHHHHHH	18.67	-
27	Phosphorylation	GRLYQVEYAFKAINQ CCEEEEEEHHHHHHC	20.62	28152594
30	Acetylation	YQVEYAFKAINQGGL EEEEEHHHHHHCCCC	39.94	25953088
30	Methylation	YQVEYAFKAINQGGL EEEEEHHHHHHCCCC	39.94	66700553
30	Ubiquitination	YQVEYAFKAINQGGL EEEEEHHHHHHCCCC	39.94	-
35	Ubiquitination	AFKAINQGGLTSVAV HHHHHHCCCCEEEEE	28.70	-
36	Acetylation	FKAINQGGLTSVAVR HHHHHCCCCEEEEEC	18.93	-
36	Ubiquitination	FKAINQGGLTSVAVR HHHHHCCCCEEEEEC	18.93	-
37	Acetylation	KAINQGGLTSVAVRG HHHHCCCCEEEEECC	4.05	-
37	Ubiquitination	KAINQGGLTSVAVRG HHHHCCCCEEEEECC	4.05	-
40	Acetylation	NQGGLTSVAVRGKDC HCCCCEEEEECCCCE	4.87	-
40	Ubiquitination	NQGGLTSVAVRGKDC HCCCCEEEEECCCCE	4.87	-
45	Acetylation	TSVAVRGKDCAVIVT EEEEECCCCEEEEEE	38.78	23749302
45	Ubiquitination	TSVAVRGKDCAVIVT EEEEECCCCEEEEEE	38.78	21906983
52	Ubiquitination	KDCAVIVTQKKVPDK CCEEEEEECCCCCHH	24.44	-
54	2-Hydroxyisobutyrylation	CAVIVTQKKVPDKLL EEEEEECCCCCHHHC	46.50	-
54	Ubiquitination	CAVIVTQKKVPDKLL EEEEEECCCCCHHHC	46.50	-
55	Acetylation	AVIVTQKKVPDKLLD EEEEECCCCCHHHCC	49.54	23749302
55	Sumoylation	AVIVTQKKVPDKLLD EEEEECCCCCHHHCC	49.54	-
55	Ubiquitination	AVIVTQKKVPDKLLD EEEEECCCCCHHHCC	49.54	21906983
59	Ubiquitination	TQKKVPDKLLDSSTV ECCCCCHHHCCCCHH	44.90	21890473
59	Ubiquitination	TQKKVPDKLLDSSTV ECCCCCHHHCCCCHH	44.90	21890473
59	Acetylation	TQKKVPDKLLDSSTV ECCCCCHHHCCCCHH	44.90	23749302
59	Ubiquitination	TQKKVPDKLLDSSTV ECCCCCHHHCCCCHH	44.90	21906983
63	Phosphorylation	VPDKLLDSSTVTHLF CCHHHCCCCHHHHHH	28.07	20068231
64	Phosphorylation	PDKLLDSSTVTHLFK CHHHCCCCHHHHHHH	26.94	20068231
65	Phosphorylation	DKLLDSSTVTHLFKI HHHCCCCHHHHHHHH	33.12	20068231
67	Phosphorylation	LLDSSTVTHLFKITE HCCCCHHHHHHHHHC	16.98	23186163
71	Ubiquitination	STVTHLFKITENIGC CHHHHHHHHHCCCCE	55.89	-
73	Phosphorylation	VTHLFKITENIGCVM HHHHHHHHCCCCEEE	24.46	-
78	Glutathionylation	KITENIGCVMTGMTA HHHCCCCEEEECCCC	1.35	22555962
80	Sulfoxidation	TENIGCVMTGMTADS HCCCCEEEECCCCCC	2.89	30846556
81	Phosphorylation	ENIGCVMTGMTADSR CCCCEEEECCCCCCH	11.91	27251275
83	Acetylation	IGCVMTGMTADSRSQ CCEEEECCCCCCHHH	1.73	19608861
83	Sulfoxidation	IGCVMTGMTADSRSQ CCEEEECCCCCCHHH	1.73	30846556
83	Ubiquitination	IGCVMTGMTADSRSQ CCEEEECCCCCCHHH	1.73	19608861
84	Phosphorylation	GCVMTGMTADSRSQV CEEEECCCCCCHHHH	28.76	27251275
85	Ubiquitination	CVMTGMTADSRSQVQ EEEECCCCCCHHHHH	12.14	-
85	Acetylation	CVMTGMTADSRSQVQ EEEECCCCCCHHHHH	12.14	19608861
85	Ubiquitination	CVMTGMTADSRSQVQ EEEECCCCCCHHHHH	12.14	19608861
92	Ubiquitination	ADSRSQVQRARYEAA CCCHHHHHHHHHHHH	26.19	-
96	Phosphorylation	SQVQRARYEAANWKY HHHHHHHHHHHCCHH	14.67	23917254
102	Acetylation	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	-
102	Ubiquitination	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	21890473
102	Ubiquitination	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	21890473
102	2-Hydroxyisobutyrylation	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	-
102	Acetylation	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	19608861
102	Methylation	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	22648033
102	Succinylation	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	23954790
102	Sumoylation	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	19608861
102	Ubiquitination	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	21890473
103	Ubiquitination	YEAANWKYKYGYEIP HHHHCCHHHCCCCCC	10.89	-
103	Phosphorylation	YEAANWKYKYGYEIP HHHHCCHHHCCCCCC	10.89	28152594
104	Ubiquitination	EAANWKYKYGYEIPV HHHCCHHHCCCCCCH	28.59	21890473
104	Ubiquitination	EAANWKYKYGYEIPV HHHCCHHHCCCCCCH	28.59	21890473
104	2-Hydroxyisobutyrylation	EAANWKYKYGYEIPV HHHCCHHHCCCCCCH	28.59	-
104	Acetylation	EAANWKYKYGYEIPV HHHCCHHHCCCCCCH	28.59	19608861
104	Malonylation	EAANWKYKYGYEIPV HHHCCHHHCCCCCCH	28.59	26320211
104	Ubiquitination	EAANWKYKYGYEIPV HHHCCHHHCCCCCCH	28.59	21890473
105	Phosphorylation	AANWKYKYGYEIPVD HHCCHHHCCCCCCHH	23.11	20090780
107	Phosphorylation	NWKYKYGYEIPVDML CCHHHCCCCCCHHHH	13.95	28152594
113	Sulfoxidation	GYEIPVDMLCKRIAD CCCCCHHHHHHHHHH	4.88	30846556
115	Glutathionylation	EIPVDMLCKRIADIS CCCHHHHHHHHHHHH	1.92	22555962
116	2-Hydroxyisobutyrylation	IPVDMLCKRIADISQ CCHHHHHHHHHHHHH	42.76	-
116	Acetylation	IPVDMLCKRIADISQ CCHHHHHHHHHHHHH	42.76	23749302
116	Ubiquitination	IPVDMLCKRIADISQ CCHHHHHHHHHHHHH	42.76	-
153	Ubiquitination	EQGPQVYKCDPAGYY CCCCCEEEECCCCCC	33.05	-
154	S-nitrosocysteine	QGPQVYKCDPAGYYC CCCCEEEECCCCCCC	4.08	-
154	S-nitrosylation	QGPQVYKCDPAGYYC CCCCEEEECCCCCCC	4.08	19483679
159	Phosphorylation	YKCDPAGYYCGFKAT EEECCCCCCCCEEEE	9.55	20090780
160	Phosphorylation	KCDPAGYYCGFKATA EECCCCCCCCEEEEE	5.79	21082442
161	S-nitrosocysteine	CDPAGYYCGFKATAA ECCCCCCCCEEEEEC	3.78	-
161	S-nitrosylation	CDPAGYYCGFKATAA ECCCCCCCCEEEEEC	3.78	19483679
162	Acetylation	DPAGYYCGFKATAAG CCCCCCCCEEEEECC	15.80	19608861
162	Ubiquitination	DPAGYYCGFKATAAG CCCCCCCCEEEEECC	15.80	19608861
164	Acetylation	AGYYCGFKATAAGVK CCCCCCEEEEECCCC	30.06	25953088
164	Ubiquitination	AGYYCGFKATAAGVK CCCCCCEEEEECCCC	30.06	21906983
171	2-Hydroxyisobutyrylation	KATAAGVKQTESTSF EEEECCCCCCCCCCH	51.05	-
171	Acetylation	KATAAGVKQTESTSF EEEECCCCCCCCCCH	51.05	25953088
171	Malonylation	KATAAGVKQTESTSF EEEECCCCCCCCCCH	51.05	26320211
171	Ubiquitination	KATAAGVKQTESTSF EEEECCCCCCCCCCH	51.05	-
173	Phosphorylation	TAAGVKQTESTSFLE EECCCCCCCCCCHHH	26.62	26437602
175	Phosphorylation	AGVKQTESTSFLEKK CCCCCCCCCCHHHHH	32.51	30622161
176	Phosphorylation	GVKQTESTSFLEKKV CCCCCCCCCHHHHHH	19.77	28348404
177	Phosphorylation	VKQTESTSFLEKKVK CCCCCCCCHHHHHHH	36.79	27050516
181	2-Hydroxyisobutyrylation	ESTSFLEKKVKKKFD CCCCHHHHHHHHHCC	66.08	-
181	Acetylation	ESTSFLEKKVKKKFD CCCCHHHHHHHHHCC	66.08	23954790
181	Ubiquitination	ESTSFLEKKVKKKFD CCCCHHHHHHHHHCC	66.08	21906983
182	Ubiquitination	STSFLEKKVKKKFDW CCCHHHHHHHHHCCC	50.33	-
211	Ubiquitination	TVLSIDFKPSEIEVG HHHCCCCCCCEEEEE	43.84	-
213	Phosphorylation	LSIDFKPSEIEVGVV HCCCCCCCEEEEEEE	52.36	24719451
231	Phosphorylation	NPKFRILTEAEIDAH CCCEEEEEHHHHHHH	30.67	-
245	Methylation	HLVALAERD------ HHHHHHCCC------	49.70	115489353

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 PSA6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSA6_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 PSA6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSA3_HUMAN	PSMA3	physical	16169070
CUL1_HUMAN	CUL1	physical	16759355
RBX1_HUMAN	RBX1	physical	16759355
PSMD4_HUMAN	PSMD4	physical	19781552
PSDE_HUMAN	PSMD14	physical	19781552
ADRM1_HUMAN	ADRM1	physical	19781552
PSMD1_HUMAN	PSMD1	physical	19781552
TXNL1_HUMAN	TXNL1	physical	19781552
PSME1_HUMAN	PSME1	physical	12419264
TAT_HV1H2	tat	physical	12419264
PSA7_HUMAN	PSMA7	physical	15225636
PSA4_HUMAN	PSMA4	physical	15225636
PSA2_HUMAN	PSMA2	physical	14733938
PSA7_HUMAN	PSMA7	physical	14733938
PP2BA_HUMAN	PPP3CA	physical	21420386
CCND1_HUMAN	CCND1	physical	22158041
CCNE1_HUMAN	CCNE1	physical	22158041
CCNA2_HUMAN	CCNA2	physical	22158041
CCNB1_HUMAN	CCNB1	physical	22158041
CDK4_HUMAN	CDK4	physical	22158041
CDK1_HUMAN	CDK1	physical	22158041
CDK2_HUMAN	CDK2	physical	22158041
CCNF_HUMAN	CCNF	physical	22158041
CSN1_HUMAN	GPS1	physical	16045761
CSN5_HUMAN	COPS5	physical	16045761
PSMD6_HUMAN	PSMD6	physical	16045761
PRS4_HUMAN	PSMC1	physical	16045761
POMP_HUMAN	POMP	physical	17948026
PSA4_HUMAN	PSMA4	physical	17948026
PSB5_HUMAN	PSMB5	physical	17948026
PSB8_HUMAN	PSMB8	physical	17948026
PSA7_HUMAN	PSMA7	physical	17948026
PSA7_HUMAN	PSMA7	physical	22939629
PSD13_HUMAN	PSMD13	physical	22939629
PSB1_HUMAN	PSMB1	physical	22939629
PSB2_HUMAN	PSMB2	physical	22939629
PSB3_HUMAN	PSMB3	physical	22939629
PSB4_HUMAN	PSMB4	physical	22939629
PSB5_HUMAN	PSMB5	physical	22939629
PSB6_HUMAN	PSMB6	physical	22939629
PSB7_HUMAN	PSMB7	physical	22939629
PSMD6_HUMAN	PSMD6	physical	22939629
PSMD1_HUMAN	PSMD1	physical	22939629
PSMD2_HUMAN	PSMD2	physical	22939629
PSMD3_HUMAN	PSMD3	physical	22939629
PSMD8_HUMAN	PSMD8	physical	22939629
PSD12_HUMAN	PSMD12	physical	22939629
PSD11_HUMAN	PSMD11	physical	22939629
PSMD4_HUMAN	PSMD4	physical	22939629
PSB8_HUMAN	PSMB8	physical	22939629
PSDE_HUMAN	PSMD14	physical	22939629
PSMD7_HUMAN	PSMD7	physical	22939629
PSMD5_HUMAN	PSMD5	physical	22939629
PSME2_HUMAN	PSME2	physical	22939629
PSME1_HUMAN	PSME1	physical	22939629
PSME3_HUMAN	PSME3	physical	22939629
PSA7L_HUMAN	PSMA8	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
TCPE_HUMAN	CCT5	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
TPM4_HUMAN	TPM4	physical	22939629
TCPD_HUMAN	CCT4	physical	22939629
TCPG_HUMAN	CCT3	physical	22939629
TCPQ_HUMAN	CCT8	physical	22939629
TADBP_HUMAN	TARDBP	physical	22939629
ICAL_HUMAN	CAST	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
PSA1_HUMAN	PSMA1	physical	22863883
PSA2_HUMAN	PSMA2	physical	22863883
PSA3_HUMAN	PSMA3	physical	22863883
PSA4_HUMAN	PSMA4	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSA7_HUMAN	PSMA7	physical	22863883
PSB1_HUMAN	PSMB1	physical	22863883
PSB3_HUMAN	PSMB3	physical	22863883
PSB4_HUMAN	PSMB4	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSB6_HUMAN	PSMB6	physical	22863883
PSB7_HUMAN	PSMB7	physical	22863883
PSB8_HUMAN	PSMB8	physical	22863883
P5CR3_HUMAN	PYCRL	physical	22863883
RPP30_HUMAN	RPP30	physical	22863883
RPP38_HUMAN	RPP38	physical	22863883
PSMG1_HUMAN	PSMG1	physical	17189198
PSMG3_HUMAN	PSMG3	physical	17189198
PSMG2_HUMAN	PSMG2	physical	17189198
PSA3_HUMAN	PSMA3	physical	17189198
PSA5_HUMAN	PSMA5	physical	17189198
CADM1_HUMAN	CADM1	physical	25416956
ZBT44_HUMAN	ZBTB44	physical	25416956
TRI39_HUMAN	TRIM39	physical	25416956
CS057_HUMAN	C19orf57	physical	25416956
LIMD2_HUMAN	LIMD2	physical	25416956
RN170_HUMAN	RNF170	physical	25416956
KRA42_HUMAN	KRTAP4-2	physical	25416956
RTP5_HUMAN	RTP5	physical	25416956
ACTN4_HUMAN	ACTN4	physical	26344197
CAND2_HUMAN	CAND2	physical	26344197
CAZA1_HUMAN	CAPZA1	physical	26344197
ELP6_HUMAN	ELP6	physical	26344197
EXOS4_HUMAN	EXOSC4	physical	26344197
EXOS6_HUMAN	EXOSC6	physical	26344197
EXOS9_HUMAN	EXOSC9	physical	26344197
ISY1_HUMAN	ISY1	physical	26344197
ECM29_HUMAN	KIAA0368	physical	26344197
NELFE_HUMAN	NELFE	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
RPB1_HUMAN	POLR2A	physical	26344197
PSA1_HUMAN	PSMA1	physical	26344197
PSA2_HUMAN	PSMA2	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
PSA5_HUMAN	PSMA5	physical	26344197
PSA7_HUMAN	PSMA7	physical	26344197
PSA7L_HUMAN	PSMA8	physical	26344197
PSB2_HUMAN	PSMB2	physical	26344197
PSB3_HUMAN	PSMB3	physical	26344197
PSB4_HUMAN	PSMB4	physical	26344197
PSB5_HUMAN	PSMB5	physical	26344197
PSB6_HUMAN	PSMB6	physical	26344197
PSB7_HUMAN	PSMB7	physical	26344197
PSB8_HUMAN	PSMB8	physical	26344197
PSB9_HUMAN	PSMB9	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
PRS6A_HUMAN	PSMC3	physical	26344197
PRS8_HUMAN	PSMC5	physical	26344197
PSMD1_HUMAN	PSMD1	physical	26344197
PSD11_HUMAN	PSMD11	physical	26344197
PSD12_HUMAN	PSMD12	physical	26344197
PSD13_HUMAN	PSMD13	physical	26344197
PSDE_HUMAN	PSMD14	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
PSMD3_HUMAN	PSMD3	physical	26344197
PSMD5_HUMAN	PSMD5	physical	26344197
PSMD6_HUMAN	PSMD6	physical	26344197
PSMD7_HUMAN	PSMD7	physical	26344197
TPM3_HUMAN	TPM3	physical	26344197
WDR11_HUMAN	WDR11	physical	26344197
PSA6_HUMAN	PSMA6	physical	26657688
MLP3B_HUMAN	MAP1LC3B	physical	27791183
SQSTM_HUMAN	SQSTM1	physical	27791183

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 PSA6_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-102 AND LYS-104, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-160, AND MASSSPECTROMETRY.	18083107 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-59, AND MASSSPECTROMETRY.	17370265 [Abstract]