dbPTM

PTTG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTTG1_HUMAN
UniProt AC	O95997
Protein Name	Securin
Gene Name	PTTG1
Organism	Homo sapiens (Human).
Sequence Length	202
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of TP53. The negative regulation of TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation..
Protein Sequence	MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPFNPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQSPSSILSTLDVELPPVCCDIDI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATLIYVDK ------CCEEEEEEC	15.89	22814378
3	Phosphorylation	-----MATLIYVDKE -----CCEEEEEECC	16.64	25106551
6	Phosphorylation	--MATLIYVDKENGE --CCEEEEEECCCCC	13.00	25106551
9	Ubiquitination	ATLIYVDKENGEPGT CEEEEEECCCCCCCC	42.93	11179223
16	Phosphorylation	KENGEPGTRVVAKDG CCCCCCCCEEEECCC	30.88	20068231
21	Ubiquitination	PGTRVVAKDGLKLGS CCCEEEECCCCCCCC	40.49	-
21	Acetylation	PGTRVVAKDGLKLGS CCCEEEECCCCCCCC	40.49	25953088
25	Ubiquitination	VVAKDGLKLGSGPSI EEECCCCCCCCCCCC	57.22	21906983
25	Acetylation	VVAKDGLKLGSGPSI EEECCCCCCCCCCCC	57.22	25953088
28	Phosphorylation	KDGLKLGSGPSIKAL CCCCCCCCCCCCEEC	58.95	25159151
31	Phosphorylation	LKLGSGPSIKALDGR CCCCCCCCCEECCCC	40.00	25159151
33	Ubiquitination	LGSGPSIKALDGRSQ CCCCCCCEECCCCCC	47.43	21906983
33	Acetylation	LGSGPSIKALDGRSQ CCCCCCCEECCCCCC	47.43	25953088
39	Phosphorylation	IKALDGRSQVSTPRF CEECCCCCCCCCCCC	40.23	-
42	Phosphorylation	LDGRSQVSTPRFGKT CCCCCCCCCCCCCCC	25.67	-
43	Phosphorylation	DGRSQVSTPRFGKTF CCCCCCCCCCCCCCC	21.45	-
48	Ubiquitination	VSTPRFGKTFDAPPA CCCCCCCCCCCCCCC	43.22	20080579
48	Acetylation	VSTPRFGKTFDAPPA CCCCCCCCCCCCCCC	43.22	26051181
60	Phosphorylation	PPALPKATRKALGTV CCCCCHHHHHHHHCC	38.54	-
62	Ubiquitination	ALPKATRKALGTVNR CCCHHHHHHHHCCCH	43.54	-
66	Phosphorylation	ATRKALGTVNRATEK HHHHHHHCCCHHHHH	18.56	-
87	Phosphorylation	PLKQKQPSFSAKKMT CCCCCCCCCCCCCCC	29.37	23917254
89	Phosphorylation	KQKQPSFSAKKMTEK CCCCCCCCCCCCCCC	43.44	21815630
91	Acetylation	KQPSFSAKKMTEKTV CCCCCCCCCCCCCCH	41.71	25953088
101	Ubiquitination	TEKTVKAKSSVPASD CCCCHHHHCCCCCCC	37.23	2190698
103	Phosphorylation	KTVKAKSSVPASDDA CCHHHHCCCCCCCCC	31.26	28555341
107	Phosphorylation	AKSSVPASDDAYPEI HHCCCCCCCCCCHHH	29.92	28102081
111	Phosphorylation	VPASDDAYPEIEKFF CCCCCCCCHHHHHHC	14.37	29978859
165	Phosphorylation	LFQLGPPSPVKMPSP HHCCCCCCCCCCCCC	45.52	19664994
171	Phosphorylation	PSPVKMPSPPWESNL CCCCCCCCCCCHHHC	39.84	20068231
176	Phosphorylation	MPSPPWESNLLQSPS CCCCCCHHHCCCCHH	28.98	20068231
181	Phosphorylation	WESNLLQSPSSILST CHHHCCCCHHHHHHH	27.07	20068231
183	Phosphorylation	SNLLQSPSSILSTLD HHCCCCHHHHHHHCC	34.95	20068231
184	Phosphorylation	NLLQSPSSILSTLDV HCCCCHHHHHHHCCC	30.82	20068231
187	Phosphorylation	QSPSSILSTLDVELP CCHHHHHHHCCCCCC	25.84	20068231
188	Phosphorylation	SPSSILSTLDVELPP CHHHHHHHCCCCCCC	24.43	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
31	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
66	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
87	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
89	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
165	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
165	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
183	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
184	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	ANAPC2	Q9UJX6	PMID:12956947
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:18485873
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	CDC20	Q12834	PMID:11553328
-	K	Ubiquitination	E3 ubiquitin ligase	ANAPC11	Q9NYG5	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	UBE4B	O95155	PMID:15611659

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
11	K	ubiquitylation	18485873
Ubiquitinated through 'Lys-11' linkage of ubiquitin moieties by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation.
165	S	Phosphorylation	10656688
Phosphorylated at Ser-165 by CDK1 during mitosis.

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 PTTG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DNJA1_HUMAN	DNAJA1	physical	9915854
RS10_HUMAN	RPS10	physical	9915854
PTTG_HUMAN	PTTG1IP	physical	10781616
XRCC6_HUMAN	XRCC6	physical	11238996
P53_HUMAN	TP53	physical	12355087
FBW1A_HUMAN	BTRC	physical	18460583
NUP98_HUMAN	NUP98	physical	16479161
CDC27_HUMAN	CDC27	physical	16479161
PTTG1_HUMAN	PTTG1	physical	20360068
ESPL1_HUMAN	ESPL1	physical	20360068
DECR_HUMAN	DECR1	physical	20360068
BUB1B_HUMAN	BUB1B	physical	19117984
AURKA_HUMAN	AURKA	physical	19117984
P53_HUMAN	TP53	physical	19117984
CDC20_HUMAN	CDC20	physical	19117984
ESPL1_HUMAN	ESPL1	physical	19117984
CDC27_HUMAN	CDC27	physical	16921029
CUL1_HUMAN	CUL1	physical	20198633
FZR1_HUMAN	FZR1	physical	16479161
ESPL1_HUMAN	ESPL1	physical	26186194
DECR_HUMAN	DECR1	physical	26186194
DYR_HUMAN	DHFR	genetic	24104479
S36A1_HUMAN	SLC36A1	genetic	24104479
RPC10_HUMAN	POLR3K	genetic	24104479
CK5P2_HUMAN	CDK5RAP2	genetic	24104479
CSK2B_HUMAN	CSNK2B	genetic	24104479
XIAP_HUMAN	XIAP	genetic	24104479
IMA7_HUMAN	KPNA6	genetic	24104479
NUMA1_HUMAN	NUMA1	genetic	24104479
GPER1_HUMAN	GPER1	genetic	24104479
CASP3_HUMAN	CASP3	genetic	24104479
TRI15_HUMAN	TRIM15	genetic	24104479
B2MG_HUMAN	B2M	genetic	24104479
WRN_HUMAN	WRN	genetic	24104479
PLM_HUMAN	FXYD1	genetic	24104479
KISSR_HUMAN	KISS1R	genetic	24104479
DPOLM_HUMAN	POLM	genetic	24104479
ZN358_HUMAN	ZNF358	genetic	24104479
DCA17_HUMAN	DCAF17	genetic	24104479
ZN142_HUMAN	ZNF142	genetic	24104479
PCX2_HUMAN	PCNXL2	genetic	24104479
NT5M_HUMAN	NT5M	genetic	24104479
PSA3_HUMAN	PSMA3	genetic	24104479
CEP85_HUMAN	CEP85	genetic	24104479
BMAL2_HUMAN	ARNTL2	genetic	24104479
TZAP_HUMAN	ZBTB48	genetic	24104479
EZRI_HUMAN	EZR	genetic	24104479
CBP_HUMAN	CREBBP	genetic	24104479
LC7L3_HUMAN	LUC7L3	genetic	24104479
CD37L_HUMAN	CDC37L1	genetic	24104479
ROAA_HUMAN	HNRNPAB	physical	26496610
PGBM_HUMAN	HSPG2	physical	26496610
PMS1_HUMAN	PMS1	physical	26496610
ESPL1_HUMAN	ESPL1	physical	26496610
TTLL5_HUMAN	TTLL5	physical	26496610
ZC3H3_HUMAN	ZC3H3	physical	26496610
NO40_HUMAN	ZCCHC17	physical	26496610
2ABD_HUMAN	PPP2R2D	physical	16705156
ESPL1_HUMAN	ESPL1	physical	28514442
DECR_HUMAN	DECR1	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
MK01_HUMAN	MAPK1	physical	15845362
PK3CA_HUMAN	PIK3CA	physical	15845362
P85A_HUMAN	PIK3R1	physical	15845362
UBP44_HUMAN	USP44	physical	28938551

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 PTTG1_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 ALA-2, AND MASS SPECTROMETRY.	19413330 [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-165, AND MASSSPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.	16964243 [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-165, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Cell cycle regulated expression and phosphorylation of hpttg proto-oncogene product."; Ramos-Morales F., Dominguez A., Romero F., Luna R., Multon M.-C.,Pintor-Toro J.A., Tortolero M.; Oncogene 19:403-409(2000). Cited for: PHOSPHORYLATION AT SER-165, AND MUTAGENESIS OF SER-165.	10656688 [Abstract]

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