ENPP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ENPP1_HUMAN
• UniProt AC: P22413
• Protein Name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
• Gene Name: ENPP1
• Organism: Homo sapiens (Human).
• Sequence Length: 925
• Subcellular Localization: Cell membrane ; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Secreted. The proteolytically processed form is secreted (By similarity). Targeted to the basolateral membrane in polarized epithel
• Protein Description: By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity and function..
• Protein Sequence: MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPLEKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNCRCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINYSSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLPKDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSCREPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNVFSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVYTPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYGRPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPLSPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTLLRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKDTSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSFYQQRKEPVSDILKLKTHLPTFSQED

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	DGCAGGGSRGGEGGR CCCCCCCCCCCCCCC	30.90	22777824
34	Phosphorylation	NGRDRGRSHAAEAPG CCCCCCCCCCCCCCC	21.94	28857561
48	Phosphorylation	GDPQAAASLLAPMDV CCHHHHHHHHCCCCC	21.13	28348404
62	Acetylation	VGEEPLEKAARARTA CCCCHHHHHHHHHCC	55.84	7691977
65	Methylation	EPLEKAARARTAKDP CHHHHHHHHHCCCCC	29.48	-
68	Phosphorylation	EKAARARTAKDPNTY HHHHHHHCCCCCCHH	36.75	-
179	N-linked_Glycosylation	DKGDCCINYSSVCQG CCCCEEEEHHHCCCC	19.40	UniProtKB CARBOHYD
227	Phosphorylation	FRAEYLHTWGGLLPV CHHHHHHHHCCHHHH	24.18	25690035
236	Phosphorylation	GGLLPVISKLKKCGT CCHHHHHHHHHHCCC	31.97	25690035
252	Phosphorylation	TKNMRPVYPTKTFPN CCCCCCCCCCCCCCC	14.10	28857561
254	Phosphorylation	NMRPVYPTKTFPNHY CCCCCCCCCCCCCCE	25.65	28857561
256	Phosphorylation	RPVYPTKTFPNHYSI CCCCCCCCCCCCEEE	46.96	25849741
261	Phosphorylation	TKTFPNHYSIVTGLY CCCCCCCEEECCCCC	13.51	29691806
262	Phosphorylation	KTFPNHYSIVTGLYP CCCCCCEEECCCCCC	11.75	29691806
265	Phosphorylation	PNHYSIVTGLYPESH CCCEEECCCCCCCCC	21.57	28857561
280	Phosphorylation	GIIDNKMYDPKMNAS CCCCCCCCCCCCCCC	30.61	18083107
285	N-linked_Glycosylation	KMYDPKMNASFSLKS CCCCCCCCCCEECCC	38.26	19349973
285	N-linked_Glycosylation	KMYDPKMNASFSLKS CCCCCCCCCCEECCC	38.26	UniProtKB CARBOHYD
287	Phosphorylation	YDPKMNASFSLKSKE CCCCCCCCEECCCCC	15.46	24719451
289	Phosphorylation	PKMNASFSLKSKEKF CCCCCCEECCCCCCC	32.18	24719451
341	N-linked_Glycosylation	PDIYKMYNGSVPFEE CHHHHHHCCCCCHHH	32.53	19349973
341	N-linked_Glycosylation	PDIYKMYNGSVPFEE CHHHHHHCCCCCHHH	32.53	19159218
440	Phosphorylation	KYIYLNKYLGDVKNI EEEEHHHHCCCCCCC	18.16	18083107
477	N-linked_Glycosylation	NYEGIARNLSCREPN CHHHHHHHCCCCCCC	27.55	UniProtKB CARBOHYD
585	N-linked_Glycosylation	NLTPAPNNGTHGSLN CCCCCCCCCCCCCHH	56.53	UniProtKB CARBOHYD
643	N-linked_Glycosylation	EDFQTQFNLTVAEEK HHHHHHCCCEEEHHH	25.61	19349973
643	N-linked_Glycosylation	EDFQTQFNLTVAEEK HHHHHHCCCEEEHHH	25.61	19349973
675	Phosphorylation	ENTICLLSQHQFMSG CCEEEEECCCCCCCC	16.81	26074081
681	Phosphorylation	LSQHQFMSGYSQDIL ECCCCCCCCCCCCCC	35.55	26074081
683	Phosphorylation	QHQFMSGYSQDILMP CCCCCCCCCCCCCCC	8.89	26074081
684	Phosphorylation	HQFMSGYSQDILMPL CCCCCCCCCCCCCCH	25.54	26074081
693	Phosphorylation	DILMPLWTSYTVDRN CCCCCHHEEEEECCC	21.38	26503514
694	Phosphorylation	ILMPLWTSYTVDRND CCCCHHEEEEECCCC	13.76	26503514
696	Phosphorylation	MPLWTSYTVDRNDSF CCHHEEEEECCCCCC	18.72	26503514
700	N-linked_Glycosylation	TSYTVDRNDSFSTED EEEEECCCCCCCHHH	44.83	UniProtKB CARBOHYD
731	N-linked_Glycosylation	HKCSFYKNNTKVSYG CCCEECCCCEEEEEE	50.45	UniProtKB CARBOHYD
748	N-linked_Glycosylation	SPPQLNKNSSGIYSE CCCCCCCCCCCCCCH	40.09	19349973
748	N-linked_Glycosylation	SPPQLNKNSSGIYSE CCCCCCCCCCCCCCH	40.09	19349973
779	Phosphorylation	IWRYFHDTLLRKYAE HHHHHHHHHHHHHHH	21.08	24260401
784	Phosphorylation	HDTLLRKYAEERNGV HHHHHHHHHHHHCCC	16.89	25690035

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ENPP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ENPP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ENPP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSD12_HUMAN	PSMD12	physical	27226596
PSA1_HUMAN	PSMA1	physical	27226596
PSB1_HUMAN	PSMB1	physical	27226596

Drug and Disease Associations

• Kegg Disease
• H00214: Hypophosphatemic rickets, including: X-Linked dominant hypophosphatemia (XLH); X-Linked recessive hy
• H00409: Type II diabetes mellitus
• H00431: Ossification of the posterior longitudinal ligament of spine (OPLL)
• H01002: Generalized arterial calcification of infancy
• OMIM Disease
• 602475: Ossification of the posterior longitudinal ligament of the spine (OPLL)
• 208000: Arterial calcification of infancy, generalized, 1 (GACI1)
• 125853: Diabetes mellitus, non-insulin-dependent (NIDDM)
• 613312: Hypophosphatemic rickets, autosomal recessive, 2 (ARHR2)
• 615522: Cole disease (COLED)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-341; ASN-643 AND ASN-748,AND MASS SPECTROMETRY.
PubMed: 19349973

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-341, AND MASSSPECTROMETRY.
PubMed: 19159218