dbPTM

PKHO2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PKHO2_HUMAN
UniProt AC	Q8TD55
Protein Name	Pleckstrin homology domain-containing family O member 2
Gene Name	PLEKHO2
Organism	Homo sapiens (Human).
Sequence Length	490
Subcellular Localization
Protein Description
Protein Sequence	MEEEGVKEAGEKPRGAQMVDKAGWIKKSSGGLLGFWKDRYLLLCQAQLLVYENEDDQKCVETVELGSYEKCQDLRALLKRKHRFILLRSPGNKVSDIKFQAPTGEEKESWIKALNEGINRGKNKAFDEVKVDKSCALEHVTRDRVRGGQRRRPPTRVHLKEVASAASDGLLRLDLDVPDSGPPVFAPSNHVSEAQPRETPRPLMPPTKPFLAPETTSPGDRVETPVGERAPTPVSASSEVSPESQEDSETPAEEDSGSEQPPNSVLPDKLKVSWENPSPQEAPAAESAEPSQAPCSETSEAAPREGGKPPTPPPKILSEKLKASMGEMQASGPPAPGTVQVSVNGMDDSPEPAKPSQAEGTPGTPPKDATTSTALPPWDLPPQFHPRCSSLGDLLGEGPRHPLQPRERLYRAQLEVKVASEQTEKLLNKVLGSEPAPVSAETLLSQAVEQLRQATQVLQEMRDLGELSQEAPGLREKRKELVTLYRRSAP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Ubiquitination	-MEEEGVKEAGEKPR -CCCCHHHHCCCCCC	53.34	24816145
20	Ubiquitination	PRGAQMVDKAGWIKK CCCCCCCCCCCEEEC	29.73	29967540
28	Phosphorylation	KAGWIKKSSGGLLGF CCCEEECCCCCCCCC	29.25	21406692
29	Phosphorylation	AGWIKKSSGGLLGFW CCEEECCCCCCCCCH	45.84	21406692
37 (in isoform 1)	Ubiquitination	-	30.02	21890473
37	Ubiquitination	GGLLGFWKDRYLLLC CCCCCCHHHHHHHHH	30.02	23000965
48	Ubiquitination	LLLCQAQLLVYENED HHHHHHEEEEEECCC	3.81	30230243
57	Ubiquitination	VYENEDDQKCVETVE EEECCCCCCEEEEEE	54.06	29967540
70	Ubiquitination	VELGSYEKCQDLRAL EECCCHHHHHHHHHH	29.03	29967540
89	Phosphorylation	HRFILLRSPGNKVSD CEEEEEECCCCCHHE	36.81	29396449
95	Phosphorylation	RSPGNKVSDIKFQAP ECCCCCHHEEEEECC	34.92	29970186
98	Ubiquitination	GNKVSDIKFQAPTGE CCCHHEEEEECCCCC	36.09	30230243
107	Ubiquitination	QAPTGEEKESWIKAL ECCCCCCHHHHHHHH	53.39	29967540
112	Acetylation	EEKESWIKALNEGIN CCHHHHHHHHHHHHH	40.33	7681843
164	Phosphorylation	VHLKEVASAASDGLL CCHHHHHHHHCCCEE	29.55	23911959
167	Phosphorylation	KEVASAASDGLLRLD HHHHHHHCCCEEEEE	31.74	26699800
182	Phosphorylation	LDVPDSGPPVFAPSN CCCCCCCCCCCCCCC	26.32	32142685
199	Phosphorylation	SEAQPRETPRPLMPP CCCCCCCCCCCCCCC	26.36	30206219
207	Phosphorylation	PRPLMPPTKPFLAPE CCCCCCCCCCCCCCC	45.54	30206219
215	Phosphorylation	KPFLAPETTSPGDRV CCCCCCCCCCCCCCC	31.36	26657352
216	Phosphorylation	PFLAPETTSPGDRVE CCCCCCCCCCCCCCC	31.12	25850435
217	Phosphorylation	FLAPETTSPGDRVET CCCCCCCCCCCCCCC	34.01	25850435
224	Phosphorylation	SPGDRVETPVGERAP CCCCCCCCCCCCCCC	22.03	29255136
232	Phosphorylation	PVGERAPTPVSASSE CCCCCCCCCCCCCCC	35.02	26657352
235	Phosphorylation	ERAPTPVSASSEVSP CCCCCCCCCCCCCCC	24.52	29970186
237	Phosphorylation	APTPVSASSEVSPES CCCCCCCCCCCCCCC	21.37	26074081
238	Phosphorylation	PTPVSASSEVSPESQ CCCCCCCCCCCCCCC	41.56	26074081
241	Phosphorylation	VSASSEVSPESQEDS CCCCCCCCCCCCCCC	20.92	28857561
244	Phosphorylation	SSEVSPESQEDSETP CCCCCCCCCCCCCCC	42.10	26657352
248	Phosphorylation	SPESQEDSETPAEED CCCCCCCCCCCCCCC	42.49	26657352
250	Phosphorylation	ESQEDSETPAEEDSG CCCCCCCCCCCCCCC	31.58	27251275
256	Phosphorylation	ETPAEEDSGSEQPPN CCCCCCCCCCCCCCC	47.72	20058876
258	Phosphorylation	PAEEDSGSEQPPNSV CCCCCCCCCCCCCCC	36.69	28270605
261	Phosphorylation	EDSGSEQPPNSVLPD CCCCCCCCCCCCCCC	26.45	32142685
264	Phosphorylation	GSEQPPNSVLPDKLK CCCCCCCCCCCCCCE	30.70	27251275
273	Phosphorylation	LPDKLKVSWENPSPQ CCCCCEEEECCCCCC	27.38	28450419
278	Phosphorylation	KVSWENPSPQEAPAA EEEECCCCCCCCCCH	51.28	28450419
287	Phosphorylation	QEAPAAESAEPSQAP CCCCCHHCCCCCCCC	32.95	26074081
291	Phosphorylation	AAESAEPSQAPCSET CHHCCCCCCCCCCCC	30.40	26074081
296	Phosphorylation	EPSQAPCSETSEAAP CCCCCCCCCCCCCCC	42.73	26074081
298	Phosphorylation	SQAPCSETSEAAPRE CCCCCCCCCCCCCCC	18.64	26074081
299	Phosphorylation	QAPCSETSEAAPREG CCCCCCCCCCCCCCC	22.61	26074081
311	Phosphorylation	REGGKPPTPPPKILS CCCCCCCCCCCHHHC	57.88	23401153
318	Phosphorylation	TPPPKILSEKLKASM CCCCHHHCHHHHHHH	35.84	24719451
338	Phosphorylation	SGPPAPGTVQVSVNG CCCCCCCEEEEEECC	13.50	29514088
342	Phosphorylation	APGTVQVSVNGMDDS CCCEEEEEECCCCCC	7.86	29514088
349	Phosphorylation	SVNGMDDSPEPAKPS EECCCCCCCCCCCCC	27.22	29514088
349	O-linked_Glycosylation	SVNGMDDSPEPAKPS EECCCCCCCCCCCCC	27.22	29351928
356	Phosphorylation	SPEPAKPSQAEGTPG CCCCCCCCCCCCCCC	41.12	29514088
361	Phosphorylation	KPSQAEGTPGTPPKD CCCCCCCCCCCCCCC	15.28	25850435
364	Phosphorylation	QAEGTPGTPPKDATT CCCCCCCCCCCCCCC	37.31	29507054
367	Ubiquitination	GTPGTPPKDATTSTA CCCCCCCCCCCCCCC	62.29	33845483
371	Phosphorylation	TPPKDATTSTALPPW CCCCCCCCCCCCCCC	26.29	24275569
372	Phosphorylation	PPKDATTSTALPPWD CCCCCCCCCCCCCCC	13.82	24275569
375	Ubiquitination	DATTSTALPPWDLPP CCCCCCCCCCCCCCC	5.47	29967540
389	Phosphorylation	PQFHPRCSSLGDLLG CCCCCCCCCHHHHCC	29.85	30266825
390	Phosphorylation	QFHPRCSSLGDLLGE CCCCCCCCHHHHCCC	39.74	23401153
400	Methylation	DLLGEGPRHPLQPRE HHCCCCCCCCCCHHH	55.71	115387799
417	Ubiquitination	YRAQLEVKVASEQTE HHHHHHHHHCHHHHH	23.78	33845483
420	Phosphorylation	QLEVKVASEQTEKLL HHHHHHCHHHHHHHH	32.97	-
425	Ubiquitination	VASEQTEKLLNKVLG HCHHHHHHHHHHHHC	62.76	29967540
429	Ubiquitination	QTEKLLNKVLGSEPA HHHHHHHHHHCCCCC	38.51	-
433	Phosphorylation	LLNKVLGSEPAPVSA HHHHHHCCCCCCCCH	35.92	28464451
439	Phosphorylation	GSEPAPVSAETLLSQ CCCCCCCCHHHHHHH	21.23	28674151
442	Phosphorylation	PAPVSAETLLSQAVE CCCCCHHHHHHHHHH	32.49	28464451
445	Phosphorylation	VSAETLLSQAVEQLR CCHHHHHHHHHHHHH	21.14	23403867
468	Phosphorylation	MRDLGELSQEAPGLR HHHHHHHHHHCCCHH	22.98	23401153
483	Phosphorylation	EKRKELVTLYRRSAP HHHHHHHHHHHCCCC	30.60	29514088
485	Phosphorylation	RKELVTLYRRSAP-- HHHHHHHHHCCCC--	8.46	29514088
488	Phosphorylation	LVTLYRRSAP----- HHHHHHCCCC-----	35.57	28985074

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 PKHO2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PKHO2_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 PKHO2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
BRE1A_HUMAN	RNF20	physical	26186194
BRE1B_HUMAN	RNF40	physical	26186194
VEZA_HUMAN	VEZT	physical	26186194
APC7_HUMAN	ANAPC7	physical	26186194
FAD1_HUMAN	FLAD1	physical	26186194
TACC3_HUMAN	TACC3	physical	26186194
ZMYM6_HUMAN	ZMYM6	physical	26186194
2ABD_HUMAN	PPP2R2D	physical	26186194
CAZA1_HUMAN	CAPZA1	physical	26186194
CAPZB_HUMAN	CAPZB	physical	26186194
M3K6_HUMAN	MAP3K6	physical	26186194
F184A_HUMAN	FAM184A	physical	26186194
UBR2_HUMAN	UBR2	physical	26186194
BBS7_HUMAN	BBS7	physical	26186194
CENPJ_HUMAN	CENPJ	physical	26186194
FP100_HUMAN	C17orf70	physical	26186194
CDC20_HUMAN	CDC20	physical	26186194
TACC3_HUMAN	TACC3	physical	28514442
M3K6_HUMAN	MAP3K6	physical	28514442
UBR2_HUMAN	UBR2	physical	28514442
CENPJ_HUMAN	CENPJ	physical	28514442
F184A_HUMAN	FAM184A	physical	28514442
FAD1_HUMAN	FLAD1	physical	28514442
CAPZB_HUMAN	CAPZB	physical	28514442
CAZA1_HUMAN	CAPZA1	physical	28514442
FP100_HUMAN	C17orf70	physical	28514442
VEZA_HUMAN	VEZT	physical	28514442
BRE1A_HUMAN	RNF20	physical	28514442
ZMYM6_HUMAN	ZMYM6	physical	28514442
2ABD_HUMAN	PPP2R2D	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 PKHO2_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-468, AND MASSSPECTROMETRY.	17525332 [Abstract]