dbPTM

IPYR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IPYR_HUMAN
UniProt AC	Q15181
Protein Name	Inorganic pyrophosphatase
Gene Name	PPA1
Organism	Homo sapiens (Human).
Sequence Length	289
Subcellular Localization	Cytoplasm.
Protein Description
Protein Sequence	MSGFSTEERAAPFSLEYRVFLKNEKGQYISPFHDIPIYADKDVFHMVVEVPRWSNAKMEIATKDPLNPIKQDVKKGKLRYVANLFPYKGYIWNYGAIPQTWEDPGHNDKHTGCCGDNDPIDVCEIGSKVCARGEIIGVKVLGILAMIDEGETDWKVIAINVDDPDAANYNDINDVKRLKPGYLEATVDWFRRYKVPDGKPENEFAFNAEFKDKDFAIDIIKSTHDHWKALVTKKTNGKGISCMNTTLSESPFKCDPDAARAIVDALPPPCESACTVPTDVDKWFHHQKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGFSTEER ------CCCCCHHHC	48.85	20068231
2	Acetylation	------MSGFSTEER ------CCCCCHHHC	48.85	20068231
5	Phosphorylation	---MSGFSTEERAAP ---CCCCCHHHCCCC	38.13	20068231
6	Phosphorylation	--MSGFSTEERAAPF --CCCCCHHHCCCCC	39.34	20068231
14	Phosphorylation	EERAAPFSLEYRVFL HHCCCCCCEEEEEEE	21.16	23312004
17	Phosphorylation	AAPFSLEYRVFLKNE CCCCCEEEEEEEECC	19.85	-
17	Nitration	AAPFSLEYRVFLKNE CCCCCEEEEEEEECC	19.85	-
22	Ubiquitination	LEYRVFLKNEKGQYI EEEEEEEECCCCCEE	52.15	-
22	Acetylation	LEYRVFLKNEKGQYI EEEEEEEECCCCCEE	52.15	27452117
25	Succinylation	RVFLKNEKGQYISPF EEEEECCCCCEECCC	61.79	23954790
25	Acetylation	RVFLKNEKGQYISPF EEEEECCCCCEECCC	61.79	23954790
25	Ubiquitination	RVFLKNEKGQYISPF EEEEECCCCCEECCC	61.79	21890473
28	Phosphorylation	LKNEKGQYISPFHDI EECCCCCEECCCCCC	16.43	27642862
30	Phosphorylation	NEKGQYISPFHDIPI CCCCCEECCCCCCCE	19.31	25159151
38	Phosphorylation	PFHDIPIYADKDVFH CCCCCCEECCCCEEE	11.91	23917254
57	Succinylation	VPRWSNAKMEIATKD CCCCCCCCEEECCCC	41.12	23954790
57	Acetylation	VPRWSNAKMEIATKD CCCCCCCCEEECCCC	41.12	19608861
58	Sulfoxidation	PRWSNAKMEIATKDP CCCCCCCEEECCCCC	4.12	21406390
62	Phosphorylation	NAKMEIATKDPLNPI CCCEEECCCCCCCCH	41.46	20068231
63	Ubiquitination	AKMEIATKDPLNPIK CCEEECCCCCCCCHH	48.61	-
63	Acetylation	AKMEIATKDPLNPIK CCEEECCCCCCCCHH	48.61	23749302
70	Ubiquitination	KDPLNPIKQDVKKGK CCCCCCHHHHHHCCC	41.52	21906983
70	Acetylation	KDPLNPIKQDVKKGK CCCCCCHHHHHHCCC	41.52	25953088
74	Acetylation	NPIKQDVKKGKLRYV CCHHHHHHCCCCEEE	65.19	25953088
75	Acetylation	PIKQDVKKGKLRYVA CHHHHHHCCCCEEEE	62.21	7674077
80	Phosphorylation	VKKGKLRYVANLFPY HHCCCCEEEEECCCC	17.85	28152594
94	Phosphorylation	YKGYIWNYGAIPQTW CCEEEEECCCCCCCC	7.92	-
109	Ubiquitination	EDPGHNDKHTGCCGD CCCCCCCCCCCCCCC	48.67	-
109	Acetylation	EDPGHNDKHTGCCGD CCCCCCCCCCCCCCC	48.67	21466224
111	Phosphorylation	PGHNDKHTGCCGDND CCCCCCCCCCCCCCC	37.34	29396449
128	Ubiquitination	DVCEIGSKVCARGEI EEEECCCCEECCCCE	35.80	-
128	Acetylation	DVCEIGSKVCARGEI EEEECCCCEECCCCE	35.80	21466224
132	Methylation	IGSKVCARGEIIGVK CCCCEECCCCEEEEE	37.84	115488271
155	Acetylation	DEGETDWKVIAINVD ECCCCCCEEEEEECC	26.94	24468141
169	Nitration	DDPDAANYNDINDVK CCCCCCCCCCHHHHH	14.97	-
169	Phosphorylation	DDPDAANYNDINDVK CCCCCCCCCCHHHHH	14.97	28796482
176	Succinylation	YNDINDVKRLKPGYL CCCHHHHHHCCCCCE	55.68	23954790
176	Ubiquitination	YNDINDVKRLKPGYL CCCHHHHHHCCCCCE	55.68	21890473
176	Acetylation	YNDINDVKRLKPGYL CCCHHHHHHCCCCCE	55.68	23954790
179	Acetylation	INDVKRLKPGYLEAT HHHHHHCCCCCEEEE	40.19	26051181
179	Ubiquitination	INDVKRLKPGYLEAT HHHHHHCCCCCEEEE	40.19	21890473
182	Phosphorylation	VKRLKPGYLEATVDW HHHCCCCCEEEEEEH	15.19	-
186	Phosphorylation	KPGYLEATVDWFRRY CCCCEEEEEEHHHHC	15.04	-
193	Phosphorylation	TVDWFRRYKVPDGKP EEEHHHHCCCCCCCC	16.45	28152594
194	Acetylation	VDWFRRYKVPDGKPE EEHHHHCCCCCCCCC	45.54	23954790
199	Acetylation	RYKVPDGKPENEFAF HCCCCCCCCCCCCCE	57.44	23749302
213	Ubiquitination	FNAEFKDKDFAIDII EEEEECCCCEEEEEH	56.17	-
221	Acetylation	DFAIDIIKSTHDHWK CEEEEEHHHCHHHHH	50.03	25953088
221	Ubiquitination	DFAIDIIKSTHDHWK CEEEEEHHHCHHHHH	50.03	21890473
228	Ubiquitination	KSTHDHWKALVTKKT HHCHHHHHHHEEECC	28.55	19608861
228	Acetylation	KSTHDHWKALVTKKT HHCHHHHHHHEEECC	28.55	19608861
235	Phosphorylation	KALVTKKTNGKGISC HHHEEECCCCCCEEE	51.24	-
238	Ubiquitination	VTKKTNGKGISCMNT EEECCCCCCEEEEEC	55.96	-
238	Acetylation	VTKKTNGKGISCMNT EEECCCCCCEEEEEC	55.96	26051181
241	Phosphorylation	KTNGKGISCMNTTLS CCCCCCEEEEECCCC	18.91	26270265
242	Glutathionylation	TNGKGISCMNTTLSE CCCCCEEEEECCCCC	2.00	22555962
243	Sulfoxidation	NGKGISCMNTTLSES CCCCEEEEECCCCCC	3.89	21406390
245	Phosphorylation	KGISCMNTTLSESPF CCEEEEECCCCCCCC	11.39	29978859
246	Phosphorylation	GISCMNTTLSESPFK CEEEEECCCCCCCCC	24.23	29978859
248	Phosphorylation	SCMNTTLSESPFKCD EEEECCCCCCCCCCC	33.66	25159151
250	Phosphorylation	MNTTLSESPFKCDPD EECCCCCCCCCCCHH	32.06	25159151
253	Ubiquitination	TLSESPFKCDPDAAR CCCCCCCCCCHHHHH	40.90	21890473
253	Acetylation	TLSESPFKCDPDAAR CCCCCCCCCCHHHHH	40.90	25953088
254	Glutathionylation	LSESPFKCDPDAARA CCCCCCCCCHHHHHH	10.58	22555962
274	Glutathionylation	PPPCESACTVPTDVD CCCCCCCCCCCCCHH	5.69	22555962
282	Ubiquitination	TVPTDVDKWFHHQKN CCCCCHHHHHHCCCC	52.16	-
282	Acetylation	TVPTDVDKWFHHQKN CCCCCHHHHHHCCCC	52.16	26822725
288	Ubiquitination	DKWFHHQKN------ HHHHHCCCC------	61.34	-
288	Acetylation	DKWFHHQKN------ HHHHHCCCC------	61.34	25953088

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 IPYR_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SETB1_HUMAN	SETDB1	physical	16169070
P53_HUMAN	TP53	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
CK054_HUMAN	C11orf54	physical	26344197
DDAH2_HUMAN	DDAH2	physical	26344197
DUT_HUMAN	DUT	physical	26344197
ITPA_HUMAN	ITPA	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
HPRT_HUMAN	HPRT1	physical	27173435
SIAS_HUMAN	NANS	physical	27173435
UBE2N_HUMAN	UBE2N	physical	27173435
G6PI_HUMAN	GPI	physical	27173435
ANXA5_HUMAN	ANXA5	physical	27173435
PA2G4_HUMAN	PA2G4	physical	27173435
PLST_HUMAN	PLS3	physical	27173435

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 IPYR_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-57 AND LYS-228, AND MASSSPECTROMETRY.	19608861 [Abstract]