dbPTM

PESC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PESC_HUMAN
UniProt AC	O00541
Protein Name	Pescadillo homolog {ECO:0000255\|HAMAP-Rule:MF_03028}
Gene Name	PES1 {ECO:0000255\|HAMAP-Rule:MF_03028}
Organism	Homo sapiens (Human).
Sequence Length	588
Subcellular Localization	Nucleus, nucleolus. Nucleus, nucleoplasm. Chromosome. Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli.
Protein Description	Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome..
Protein Sequence	MGGLEKKKYERGSATNYITRNKARKKLQLSLADFRRLCILKGIYPHEPKHKKKVNKGSTAARTFYLIKDIRFLLHEPIVNKFREYKVFVRKLRKAYGKSEWNTVERLKDNKPNYKLDHIIKERYPTFIDALRDLDDALSMCFLFSTFPRTGKCHVQTIQLCRRLTVEFMHYIIAARALRKVFLSIKGIYYQAEVLGQPIVWITPYAFSHDHPTDVDYRVMATFTEFYTTLLGFVNFRLYQLLNLHYPPKLEGQAQAEAKAGEGTYALDSESCMEKLAALSASLARVVVPATEEEAEVDEFPTDGEMSAQEEDRRKELEAQEKHKKLFEGLKFFLNREVPREALAFIIRSFGGEVSWDKSLCIGATYDVTDSRITHQIVDRPGQQTSVIGRCYVQPQWVFDSVNARLLLPVAEYFSGVQLPPHLSPFVTEKEGDYVPPEKLKLLALQRGEDPGNLNESEEEEEEDDNNEGDGDEEGENEEEEEDAEAGSEKEEEARLAALEEQRMEGKKPRVMAGTLKLEDKQRLAQEEESEAKRLAIMMMKKREKYLYQKIMFGKRRKIREANKLAEKRKAHDEAVRSEKKAKKARPE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	GGLEKKKYERGSATN CCCCCCCCCCCCCCC	21.53	29214152
11	Methylation	LEKKKYERGSATNYI CCCCCCCCCCCCCHH	41.08	115487023
13	Phosphorylation	KKKYERGSATNYITR CCCCCCCCCCCHHCH	37.83	19691289
15	Phosphorylation	KYERGSATNYITRNK CCCCCCCCCHHCHHH	30.19	28152594
17	Phosphorylation	ERGSATNYITRNKAR CCCCCCCHHCHHHHH	10.18	19691289
19	Phosphorylation	GSATNYITRNKARKK CCCCCHHCHHHHHHH	20.16	19691289
26	Ubiquitination	TRNKARKKLQLSLAD CHHHHHHHHHCCHHH	35.59	-
30	Phosphorylation	ARKKLQLSLADFRRL HHHHHHCCHHHHHHH	14.46	20860994
41	Ubiquitination	FRRLCILKGIYPHEP HHHHHHHCCCCCCCC	24.29	-
41	Acetylation	FRRLCILKGIYPHEP HHHHHHHCCCCCCCC	24.29	26051181
44	Phosphorylation	LCILKGIYPHEPKHK HHHHCCCCCCCCCCC	13.75	28152594
49	Ubiquitination	GIYPHEPKHKKKVNK CCCCCCCCCCCCCCC	66.14	-
49	Acetylation	GIYPHEPKHKKKVNK CCCCCCCCCCCCCCC	66.14	25825284
65	Phosphorylation	STAARTFYLIKDIRF CHHHHHHHHHHHHHH	13.60	19835603
68 (in isoform 2)	Ubiquitination	-	44.50	21890473
68	Acetylation	ARTFYLIKDIRFLLH HHHHHHHHHHHHHHC	44.50	25825284
68	Ubiquitination	ARTFYLIKDIRFLLH HHHHHHHHHHHHHHC	44.50	21890473
68 (in isoform 1)	Ubiquitination	-	44.50	21890473
81	Ubiquitination	LHEPIVNKFREYKVF HCCHHHHHHHHHHHH	34.60	21890473
81 (in isoform 2)	Ubiquitination	-	34.60	21890473
81	Acetylation	LHEPIVNKFREYKVF HCCHHHHHHHHHHHH	34.60	25825284
81 (in isoform 1)	Ubiquitination	-	34.60	21890473
86	Acetylation	VNKFREYKVFVRKLR HHHHHHHHHHHHHHH	25.17	26051181
86	Ubiquitination	VNKFREYKVFVRKLR HHHHHHHHHHHHHHH	25.17	-
94	Ubiquitination	VFVRKLRKAYGKSEW HHHHHHHHHHCCCCC	57.29	-
98 (in isoform 1)	Ubiquitination	-	32.31	21890473
98	Ubiquitination	KLRKAYGKSEWNTVE HHHHHHCCCCCCHHH	32.31	19608861
98	Acetylation	KLRKAYGKSEWNTVE HHHHHHCCCCCCHHH	32.31	19608861
98 (in isoform 2)	Ubiquitination	-	32.31	21890473
108	Ubiquitination	WNTVERLKDNKPNYK CCHHHHHHCCCCCCC	66.53	-
115	Ubiquitination	KDNKPNYKLDHIIKE HCCCCCCCHHHHHHH	54.82	-
121	Ubiquitination	YKLDHIIKERYPTFI CCHHHHHHHHCHHHH	35.22	-
152	Acetylation	STFPRTGKCHVQTIQ CCCCCCCCCCHHHHH	22.13	25953088
249	Acetylation	LNLHYPPKLEGQAQA HCCCCCCCCCCHHHH	55.45	26051181
259	Acetylation	GQAQAEAKAGEGTYA CHHHHHHHCCCCEEE	48.72	26051181
264	Phosphorylation	EAKAGEGTYALDSES HHHCCCCEEEECCHH	11.00	28796482
265	Phosphorylation	AKAGEGTYALDSESC HHCCCCEEEECCHHH	18.94	28796482
269	Phosphorylation	EGTYALDSESCMEKL CCEEEECCHHHHHHH	32.06	20873877
271	Phosphorylation	TYALDSESCMEKLAA EEEECCHHHHHHHHH	23.79	20873877
272	Glutathionylation	YALDSESCMEKLAAL EEECCHHHHHHHHHH	3.42	22555962
275	Acetylation	DSESCMEKLAALSAS CCHHHHHHHHHHHHH	19.28	26051181
275	Ubiquitination	DSESCMEKLAALSAS CCHHHHHHHHHHHHH	19.28	-
280	Phosphorylation	MEKLAALSASLARVV HHHHHHHHHHHHEEE	15.87	22985185
282	Phosphorylation	KLAALSASLARVVVP HHHHHHHHHHEEEEE	21.13	29214152
291	Phosphorylation	ARVVVPATEEEAEVD HEEEEECCHHHHCCC	37.55	29978859
302	Phosphorylation	AEVDEFPTDGEMSAQ HCCCCCCCCCCCCCC	63.05	30576142
307	Phosphorylation	FPTDGEMSAQEEDRR CCCCCCCCCCHHHHH	23.62	25849741
315	2-Hydroxyisobutyrylation	AQEEDRRKELEAQEK CCHHHHHHHHHHHHH	68.49	-
325	Ubiquitination	EAQEKHKKLFEGLKF HHHHHHHHHHHHHHH	59.12	-
326 (in isoform 2)	Ubiquitination	-	5.87	21890473
331 (in isoform 1)	Ubiquitination	-	44.95	21890473
331	Acetylation	KKLFEGLKFFLNREV HHHHHHHHHHHCCCC	44.95	26051181
331	Ubiquitination	KKLFEGLKFFLNREV HHHHHHHHHHHCCCC	44.95	21906983
359	Phosphorylation	GEVSWDKSLCIGATY CCCEECCEEEEECEE	26.46	-
365	Phosphorylation	KSLCIGATYDVTDSR CEEEEECEEECCCCC	18.29	28387310
380	Methylation	ITHQIVDRPGQQTSV CEEEEECCCCCEEEE	26.76	115487015
424	Phosphorylation	VQLPPHLSPFVTEKE CCCCCCCCCCCCCCC	17.17	-
428	Phosphorylation	PHLSPFVTEKEGDYV CCCCCCCCCCCCCCC	41.54	-
434	Phosphorylation	VTEKEGDYVPPEKLK CCCCCCCCCCHHHHH	26.22	25159151
436 (in isoform 2)	Ubiquitination	-	25.71	21890473
439	Ubiquitination	GDYVPPEKLKLLALQ CCCCCHHHHHHHHHH	57.61	-
441 (in isoform 1)	Ubiquitination	-	53.15	21890473
441	Ubiquitination	YVPPEKLKLLALQRG CCCHHHHHHHHHHCC	53.15	21890473
457	Phosphorylation	DPGNLNESEEEEEED CCCCCCCCHHHHCCC	49.59	21659604
488	Phosphorylation	EEDAEAGSEKEEEAR HHHHHCCCHHHHHHH	53.17	30576142
515	Phosphorylation	KPRVMAGTLKLEDKQ CCCEEEEECCHHHHH	15.92	23403867
517	Sumoylation	RVMAGTLKLEDKQRL CEEEEECCHHHHHHH	50.06	-
517	Sumoylation	RVMAGTLKLEDKQRL CEEEEECCHHHHHHH	50.06	25114211
521	Acetylation	GTLKLEDKQRLAQEE EECCHHHHHHHHHHH	28.13	20167786
521	Ubiquitination	GTLKLEDKQRLAQEE EECCHHHHHHHHHHH	28.13	-
528 (in isoform 2)	Ubiquitination	-	55.53	21890473
530	Phosphorylation	RLAQEEESEAKRLAI HHHHHHHHHHHHHHH	46.24	25159151
533 (in isoform 1)	Ubiquitination	-	43.84	21890473
533	Acetylation	QEEESEAKRLAIMMM HHHHHHHHHHHHHHH	43.84	26051181
533	Ubiquitination	QEEESEAKRLAIMMM HHHHHHHHHHHHHHH	43.84	2190698
546	Phosphorylation	MMKKREKYLYQKIMF HHHHHHHHHHHHHHH	13.09	26552605
548	Phosphorylation	KKREKYLYQKIMFGK HHHHHHHHHHHHHCH	12.50	26552605
550	2-Hydroxyisobutyrylation	REKYLYQKIMFGKRR HHHHHHHHHHHCHHH	23.68	-
578	Phosphorylation	AHDEAVRSEKKAKKA HHHHHHHHHHHHHHH	47.36	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
Oops, there are no upstream regulatory protein records of PESC_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR12_HUMAN	WDR12	physical	16738141
BOP1_HUMAN	BOP1	physical	16738141
WDR12_HUMAN	WDR12	physical	17353269
PESC_HUMAN	PES1	physical	16043514
BOP1_HUMAN	BOP1	physical	16043514
WDR12_HUMAN	WDR12	physical	16043514
ARL2_HUMAN	ARL2	physical	22863883
LZTL1_HUMAN	LZTFL1	physical	22863883
BRX1_HUMAN	BRIX1	physical	26344197
CEBPZ_HUMAN	CEBPZ	physical	26344197
FBRL_HUMAN	FBL	physical	26344197
SPB1_HUMAN	FTSJ3	physical	26344197
GNL1_HUMAN	GNL1	physical	26344197
GNL3_HUMAN	GNL3	physical	26344197
NOG1_HUMAN	GTPBP4	physical	26344197
KRR1_HUMAN	KRR1	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
NIP7_HUMAN	NIP7	physical	26344197
NOC2L_HUMAN	NOC2L	physical	26344197
NOP2_HUMAN	NOP2	physical	26344197
NSA2_HUMAN	NSA2	physical	26344197
PWP1_HUMAN	PWP1	physical	26344197
RPF2_HUMAN	RPF2	physical	26344197
RL23_HUMAN	RPL23	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL40_HUMAN	UBA52	physical	26344197
UT14A_HUMAN	UTP14A	physical	26344197
DDX27_HUMAN	DDX27	physical	25825154
BOP1_HUMAN	BOP1	physical	25825154
MBB1A_HUMAN	MYBBP1A	physical	25825154
G3BP1_HUMAN	G3BP1	physical	25825154
RRP12_HUMAN	RRP12	physical	25825154
MRT4_HUMAN	MRTO4	physical	25825154
BRX1_HUMAN	BRIX1	physical	25825154
RRBP1_HUMAN	RRBP1	physical	25825154
DKC1_HUMAN	DKC1	physical	25825154
MMTA2_HUMAN	C1orf35	physical	25825154
PR40A_HUMAN	PRPF40A	physical	25825154
NOC2L_HUMAN	NOC2L	physical	25825154
TOP1_HUMAN	TOP1	physical	25825154
NOP2_HUMAN	NOP2	physical	25825154
ZCCHV_HUMAN	ZC3HAV1	physical	25825154
KIF2A_HUMAN	KIF2A	physical	25825154
ELOA1_HUMAN	TCEB3	physical	25825154
PDIA3_HUMAN	PDIA3	physical	25825154
SNUT1_HUMAN	SART1	physical	25825154
MYH9_HUMAN	MYH9	physical	25825154
BUB3_HUMAN	BUB3	physical	25825154
NOC3L_HUMAN	NOC3L	physical	25825154
DDX18_HUMAN	DDX18	physical	25825154
NOG1_HUMAN	GTPBP4	physical	25825154
EBP2_HUMAN	EBNA1BP2	physical	25825154
RL7L_HUMAN	RPL7L1	physical	25825154
RRS1_HUMAN	RRS1	physical	25825154
PESC_HUMAN	PES1	physical	25825154
RRP1B_HUMAN	RRP1B	physical	25825154
POP1_HUMAN	POP1	physical	25825154
WDR12_HUMAN	WDR12	physical	25825154
BRD2_HUMAN	BRD2	physical	28514442
BOP1_HUMAN	BOP1	physical	28514442
WDR12_HUMAN	WDR12	physical	28514442
F263_HUMAN	PFKFB3	physical	28514442
NAF1_HUMAN	NAF1	physical	28514442
CWC22_HUMAN	CWC22	physical	28514442
UBF1_HUMAN	UBTF	physical	28514442
TRI26_HUMAN	TRIM26	physical	28514442
TNC18_HUMAN	TNRC18	physical	28514442
SET1A_HUMAN	SETD1A	physical	28514442
RL7L_HUMAN	RPL7L1	physical	28514442
AFF4_HUMAN	AFF4	physical	28514442
CXXC1_HUMAN	CXXC1	physical	28514442
AF9_HUMAN	MLLT3	physical	28514442
CENPB_HUMAN	CENPB	physical	28514442
KLH23_HUMAN	KLHL23	physical	28514442
PININ_HUMAN	PNN	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
DDX27_HUMAN	DDX27	physical	28514442
NVL_HUMAN	NVL	physical	28514442
PPIL4_HUMAN	PPIL4	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
CR025_HUMAN	C18orf25	physical	28514442
CCD91_HUMAN	CCDC91	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
AP3B1_HUMAN	AP3B1	physical	28514442
NOC3L_HUMAN	NOC3L	physical	28514442
KBTB7_HUMAN	KBTBD7	physical	28514442
RL36_HUMAN	RPL36	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 PESC_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-98, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-457 AND SER-488, ANDMASS SPECTROMETRY.	18669648 [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-548, AND MASSSPECTROMETRY.	18083107 [Abstract]