dbPTM

TOPK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TOPK_HUMAN
UniProt AC	Q96KB5
Protein Name	Lymphokine-activated killer T-cell-originated protein kinase
Gene Name	PBK
Organism	Homo sapiens (Human).
Sequence Length	322
Subcellular Localization
Protein Description	Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage..
Protein Sequence	MEGISNFKTPSKLSEKKKSVLCSTPTINIPASPFMQKLGFGTGVNVYLMKRSPRGLSHSPWAVKKINPICNDHYRSVYQKRLMDEAKILKSLHHPNIVGYRAFTEANDGSLCLAMEYGGEKSLNDLIEERYKASQDPFPAAIILKVALNMARGLKYLHQEKKLLHGDIKSSNVVIKGDFETIKICDVGVSLPLDENMTVTDPEACYIGTEPWKPKEAVEENGVITDKADIFAFGLTLWEMMTLSIPHINLSNDDDDEDKTFDESDFDDEAYYAALGTRPPINMEELDESYQKVIELFSVCTNEDPKDRPSAAHIVEALETDV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEGISNFK -------CCCCCCCC	10.84	22223895
5	Phosphorylation	---MEGISNFKTPSK ---CCCCCCCCCHHH	47.25	22199227
8	Ubiquitination	MEGISNFKTPSKLSE CCCCCCCCCHHHCCH	64.87	-
8	Sumoylation	MEGISNFKTPSKLSE CCCCCCCCCHHHCCH	64.87	-
8	Acetylation	MEGISNFKTPSKLSE CCCCCCCCCHHHCCH	64.87	25953088
8	Sumoylation	MEGISNFKTPSKLSE CCCCCCCCCHHHCCH	64.87	-
8	Ubiquitination	MEGISNFKTPSKLSE CCCCCCCCCHHHCCH	64.87	-
9	Phosphorylation	EGISNFKTPSKLSEK CCCCCCCCHHHCCHH	28.76	29255136
11	Phosphorylation	ISNFKTPSKLSEKKK CCCCCCHHHCCHHCC	52.00	22617229
12	Acetylation	SNFKTPSKLSEKKKS CCCCCHHHCCHHCCC	58.18	-
12	Acetylation	SNFKTPSKLSEKKKS CCCCCHHHCCHHCCC	58.18	23954790
12	Sumoylation	SNFKTPSKLSEKKKS CCCCCHHHCCHHCCC	58.18	-
12	Sumoylation	SNFKTPSKLSEKKKS CCCCCHHHCCHHCCC	58.18	-
12	Ubiquitination	SNFKTPSKLSEKKKS CCCCCHHHCCHHCCC	58.18	-
14	Phosphorylation	FKTPSKLSEKKKSVL CCCHHHCCHHCCCEE	51.62	25159151
16	Acetylation	TPSKLSEKKKSVLCS CHHHCCHHCCCEEEC	63.22	12435587
17	Acetylation	PSKLSEKKKSVLCST HHHCCHHCCCEEECC	46.35	24471253
19	Phosphorylation	KLSEKKKSVLCSTPT HCCHHCCCEEECCCC	29.24	25463755
23	Phosphorylation	KKKSVLCSTPTINIP HCCCEEECCCCCCCC	33.01	20201521
24	Phosphorylation	KKSVLCSTPTINIPA CCCEEECCCCCCCCC	24.37	30278072
26	Phosphorylation	SVLCSTPTINIPASP CEEECCCCCCCCCCH	27.09	23927012
32	Phosphorylation	PTINIPASPFMQKLG CCCCCCCCHHHHHHC	17.20	20201521
42	Phosphorylation	MQKLGFGTGVNVYLM HHHHCCCCCCEEEEE	35.38	26270265
47	Phosphorylation	FGTGVNVYLMKRSPR CCCCCEEEEEECCCC	8.89	26270265
50	Ubiquitination	GVNVYLMKRSPRGLS CCEEEEEECCCCCCC	47.32	-
52	Phosphorylation	NVYLMKRSPRGLSHS EEEEEECCCCCCCCC	17.27	28985074
57	Phosphorylation	KRSPRGLSHSPWAVK ECCCCCCCCCCCHHH	25.41	30266825
59	Phosphorylation	SPRGLSHSPWAVKKI CCCCCCCCCCHHHHH	20.82	20201521
64	Sumoylation	SHSPWAVKKINPICN CCCCCHHHHHCCCCC	39.94	19608861
64	Ubiquitination	SHSPWAVKKINPICN CCCCCHHHHHCCCCC	39.94	19608861
64	Acetylation	SHSPWAVKKINPICN CCCCCHHHHHCCCCC	39.94	23954790
64	2-Hydroxyisobutyrylation	SHSPWAVKKINPICN CCCCCHHHHHCCCCC	39.94	-
64	Sumoylation	SHSPWAVKKINPICN CCCCCHHHHHCCCCC	39.94	-
65	Ubiquitination	HSPWAVKKINPICND CCCCHHHHHCCCCCH	40.91	-
65	Sumoylation	HSPWAVKKINPICND CCCCHHHHHCCCCCH	40.91	-
65	Ubiquitination	HSPWAVKKINPICND CCCCHHHHHCCCCCH	40.91	-
65	Sumoylation	HSPWAVKKINPICND CCCCHHHHHCCCCCH	40.91	-
74	Phosphorylation	NPICNDHYRSVYQKR CCCCCHHHHHHHHHH	13.88	25394399
76	Phosphorylation	ICNDHYRSVYQKRLM CCCHHHHHHHHHHHH	20.29	25159151
78	Phosphorylation	NDHYRSVYQKRLMDE CHHHHHHHHHHHHHH	15.01	-
80	Ubiquitination	HYRSVYQKRLMDEAK HHHHHHHHHHHHHHH	29.79	-
87	Acetylation	KRLMDEAKILKSLHH HHHHHHHHHHHHCCC	46.66	25953088
87	Ubiquitination	KRLMDEAKILKSLHH HHHHHHHHHHHHCCC	46.66	-
87	Ubiquitination	KRLMDEAKILKSLHH HHHHHHHHHHHHCCC	46.66	-
87	Acetylation	KRLMDEAKILKSLHH HHHHHHHHHHHHCCC	46.66	-
90	Ubiquitination	MDEAKILKSLHHPNI HHHHHHHHHCCCCCC	55.21	21890473
90	Acetylation	MDEAKILKSLHHPNI HHHHHHHHHCCCCCC	55.21	26051181
90	Ubiquitination	MDEAKILKSLHHPNI HHHHHHHHHCCCCCC	55.21	21890473
91	Phosphorylation	DEAKILKSLHHPNIV HHHHHHHHCCCCCCC	29.50	25159151
100	Phosphorylation	HHPNIVGYRAFTEAN CCCCCCCEEEEECCC	6.46	-
104	Phosphorylation	IVGYRAFTEANDGSL CCCEEEEECCCCCCE	32.95	28555341
110	Phosphorylation	FTEANDGSLCLAMEY EECCCCCCEEEEEEE	20.83	28555341
122	Phosphorylation	MEYGGEKSLNDLIEE EEECCCCCHHHHHHH	28.27	20873877
132	Ubiquitination	DLIEERYKASQDPFP HHHHHHHHHCCCCCC	48.02	-
132	Ubiquitination	DLIEERYKASQDPFP HHHHHHHHHCCCCCC	48.02	-
155	Ubiquitination	LNMARGLKYLHQEKK HHHHHHHHHHHHHCC	48.90	-
155	Sumoylation	LNMARGLKYLHQEKK HHHHHHHHHHHHHCC	48.90	-
155	Ubiquitination	LNMARGLKYLHQEKK HHHHHHHHHHHHHCC	48.90	-
155	Sumoylation	LNMARGLKYLHQEKK HHHHHHHHHHHHHCC	48.90	-
161	Ubiquitination	LKYLHQEKKLLHGDI HHHHHHHCCHHHCCC	42.00	-
161	2-Hydroxyisobutyrylation	LKYLHQEKKLLHGDI HHHHHHHCCHHHCCC	42.00	-
162	Ubiquitination	KYLHQEKKLLHGDIK HHHHHHCCHHHCCCC	56.37	-
162	Sumoylation	KYLHQEKKLLHGDIK HHHHHHCCHHHCCCC	56.37	-
162	Sumoylation	KYLHQEKKLLHGDIK HHHHHHCCHHHCCCC	56.37	-
169	Ubiquitination	KLLHGDIKSSNVVIK CHHHCCCCCCCEEEE	53.20	-
169	Sumoylation	KLLHGDIKSSNVVIK CHHHCCCCCCCEEEE	53.20	-
169	Sumoylation	KLLHGDIKSSNVVIK CHHHCCCCCCCEEEE	53.20	28112733
169	Ubiquitination	KLLHGDIKSSNVVIK CHHHCCCCCCCEEEE	53.20	-
171	Phosphorylation	LHGDIKSSNVVIKGD HHCCCCCCCEEEECC	28.74	27362937
176	Sumoylation	KSSNVVIKGDFETIK CCCCEEEECCCCEEE	40.60	-
176	Sumoylation	KSSNVVIKGDFETIK CCCCEEEECCCCEEE	40.60	-
176	Ubiquitination	KSSNVVIKGDFETIK CCCCEEEECCCCEEE	40.60	-
181	Phosphorylation	VIKGDFETIKICDVG EEECCCCEEEECEEE	27.80	27362937
213	Ubiquitination	YIGTEPWKPKEAVEE CCCCCCCCCHHHHHH	57.85	-
251	Phosphorylation	SIPHINLSNDDDDED CCCCCCCCCCCCCCC	33.45	22468782
260	Phosphorylation	DDDDEDKTFDESDFD CCCCCCCCCCHHHCC	48.95	20068231
264	Phosphorylation	EDKTFDESDFDDEAY CCCCCCHHHCCHHHH	45.48	20068231
271	Phosphorylation	SDFDDEAYYAALGTR HHCCHHHHHHHHCCC	7.50	20068231
272	Phosphorylation	DFDDEAYYAALGTRP HCCHHHHHHHHCCCC	7.76	20068231
298	Phosphorylation	QKVIELFSVCTNEDP HHHHHHHHHHCCCCC	28.98	27732954
301	Phosphorylation	IELFSVCTNEDPKDR HHHHHHHCCCCCCCC	39.21	27732954
310	Phosphorylation	EDPKDRPSAAHIVEA CCCCCCCCHHHHHHH	38.69	20068231
320	Phosphorylation	HIVEALETDV----- HHHHHHHCCC-----	42.80	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
9	T	Phosphorylation	Kinase	CDK1	P06493	PSP
74	Y	Phosphorylation	Kinase	MET	P08581	PSP
74	Y	Phosphorylation	Kinase	SRC	P12931	PSP
272	Y	Phosphorylation	Kinase	SRC	P12931	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	LNX1	Q8TBB1	PMID:22889411
-	K	Ubiquitination	E3 ubiquitin ligase	CHFR	Q96EP1	PMID:24012691

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GASP1_HUMAN	GPRASP1	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
GPS2_HUMAN	GPS2	physical	16169070
H2AX_HUMAN	H2AFX	physical	17145805
UBP5_HUMAN	USP5	physical	22939629
ZBT26_HUMAN	ZBTB26	physical	25416956
LEG9B_HUMAN	LGALS9B	physical	26186194
LEG9_HUMAN	LGALS9	physical	26186194
CHFR_HUMAN	CHFR	physical	24012691
PTEN_HUMAN	PTEN	physical	24012691
SRC_HUMAN	SRC	physical	27016416
LEG9_HUMAN	LGALS9	physical	28514442
LEG9B_HUMAN	LGALS9B	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 TOPK_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-9; THR-24 AND SER-32, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-9; THR-24 AND SER-32, 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 THR-24; SER-32 AND SER-59,AND MASS SPECTROMETRY.	18669648 [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-59, 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-59, AND MASSSPECTROMETRY.	17081983 [Abstract]