5NTD_HUMAN - dbPTM
5NTD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 5NTD_HUMAN
UniProt AC P21589
Protein Name 5'-nucleotidase
Gene Name NT5E
Organism Homo sapiens (Human).
Sequence Length 574
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor.
Protein Description Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities..
Protein Sequence MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGGVARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYKGAEVAHFMNALRYDAMALGNHEFDNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKETPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVVGGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNVISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNMGNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGTFDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCRVPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYPAVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ
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 Orthologous
Protein Cluster
50UbiquitinationQTSEDSSKCVNASRC
HCCCCHHHHHCHHHH		46.27-
53N-linked_GlycosylationEDSSKCVNASRCMGG
CCHHHHHCHHHHHHH		41.49UniProtKB CARBOHYD
672-HydroxyisobutyrylationGVARLFTKVQQIRRA
HHHHHHHHHHHHHHC		30.61-
133UbiquitinationGLIEPLLKEAKFPIL
CHHHHHHHHCCCCEE		64.4121906983
152PhosphorylationKAKGPLASQISGLYL
EECCCHHHHCCCEEC		35.4125867546
155PhosphorylationGPLASQISGLYLPYK
CCHHHHCCCEECCCE		18.3325867546
158PhosphorylationASQISGLYLPYKVLP
HHHCCCEECCCEEEE		14.7925867546
161PhosphorylationISGLYLPYKVLPVGD
CCCEECCCEEEECCC		15.9025867546
181PhosphorylationVGYTSKETPFLSNPG
EEEECCCCCCCCCCC		24.0730576142
185PhosphorylationSKETPFLSNPGTNLV
CCCCCCCCCCCCCEE		41.1630576142
189PhosphorylationPFLSNPGTNLVFEDE
CCCCCCCCCEEECCC		27.0030576142
198PhosphorylationLVFEDEITALQPEVD
EEECCCCHHCCCCCC		21.1930243723
206UbiquitinationALQPEVDKLKTLNVN
HCCCCCCCCCCCCHH		57.99-
208UbiquitinationQPEVDKLKTLNVNKI
CCCCCCCCCCCHHHE		57.62-
262UbiquitinationSKEVPAGKYPFIVTS
CCCCCCCCCCEEEEC		52.4321906983
311N-linked_GlycosylationHGNPILLNSSIPEDP
CCCCEEECCCCCCCC		30.2023142347
319PhosphorylationSSIPEDPSIKADINK
CCCCCCCCCCCCHHE		49.39-
321UbiquitinationIPEDPSIKADINKWR
CCCCCCCCCCHHEEE		44.322190698
333N-linked_GlycosylationKWRIKLDNYSTQELG
EEEEEECCCCCCCCC		42.9919349973
333N-linked_GlycosylationKWRIKLDNYSTQELG
EEEEEECCCCCCCCC		42.9919159218
403N-linked_GlycosylationSPIDERNNGTITWEN
CCCCCCCCCCEEEEC		56.0319159218
520PhosphorylationDELLRHDSGDQDINV
HHHHCCCCCCCCHHH		37.84-
549GPI-anchorVEGRIKFSTGSHCHG
ECCEEEEECCCCCCC		27.192129526
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 5NTD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 5NTD_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 5NTD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZNT5_HUMANSLC30A5physical
22939629
NDUA2_HUMANNDUFA2physical
22939629
SYJ2B_HUMANSYNJ2BPphysical
22939629
PCDH7_HUMANPCDH7physical
22939629
TM177_HUMANTMEM177physical
22939629
XPO7_HUMANXPO7physical
26186194
CHD1L_HUMANCHD1Lphysical
26186194
FLVC1_HUMANFLVCR1physical
26186194
ATR_HUMANATRphysical
26186194
RPTOR_HUMANRPTORphysical
26186194
GLMN_HUMANGLMNphysical
26186194
RDH13_HUMANRDH13physical
26186194
SCAM1_HUMANSCAMP1physical
26186194
UBP22_HUMANUSP22physical
26186194
HSDL1_HUMANHSDL1physical
26186194
RFC2_HUMANRFC2physical
26186194
RAB9A_HUMANRAB9Aphysical
26186194
DAAF5_HUMANDNAAF5physical
26186194
MTOR_HUMANMTORphysical
26186194
GHITM_HUMANGHITMphysical
26186194
PDS5A_HUMANPDS5Aphysical
26186194
RHOG_HUMANRHOGphysical
26186194
TNPO2_HUMANTNPO2physical
26186194
PLAP_HUMANPLAAphysical
26186194
CTR2_HUMANSLC7A2physical
26186194
ARL2_HUMANARL2physical
26186194
STEA3_HUMANSTEAP3physical
26186194
S41A1_HUMANSLC41A1physical
26186194
PAQR1_HUMANADIPOR1physical
26186194
S47A1_HUMANSLC47A1physical
26186194
ARF5_HUMANARF5physical
26186194
DEGS1_HUMANDEGS1physical
26186194
SAR1B_HUMANSAR1Bphysical
26186194
UBP36_HUMANUSP36physical
26186194
CXA1_HUMANGJA1physical
26186194
CTL1_HUMANSLC44A1physical
26186194
GNL3L_HUMANGNL3Lphysical
26186194
MOT8_HUMANSLC16A2physical
26186194
S26A6_HUMANSLC26A6physical
26186194
ARL8A_HUMANARL8Aphysical
26186194
SC6A8_HUMANSLC6A8physical
26186194
VANG2_HUMANVANGL2physical
26186194
COT2_HUMANNR2F2physical
26186194
CP2S1_HUMANCYP2S1physical
26186194
UBP36_HUMANUSP36physical
28514442
UBP22_HUMANUSP22physical
28514442
SCAM1_HUMANSCAMP1physical
28514442
CTL1_HUMANSLC44A1physical
28514442
GLMN_HUMANGLMNphysical
28514442
SC6A8_HUMANSLC6A8physical
28514442
XPO7_HUMANXPO7physical
28514442
FLVC1_HUMANFLVCR1physical
28514442
ARL2_HUMANARL2physical
28514442
MOT8_HUMANSLC16A2physical
28514442
PAQR1_HUMANADIPOR1physical
28514442
UBP3_HUMANUSP3physical
28514442
PDS5A_HUMANPDS5Aphysical
28514442
RHOG_HUMANRHOGphysical
28514442
HSDL1_HUMANHSDL1physical
28514442
CP2S1_HUMANCYP2S1physical
28514442
RAB9A_HUMANRAB9Aphysical
28514442
MTOR_HUMANMTORphysical
28514442
RDH13_HUMANRDH13physical
28514442
DAAF5_HUMANDNAAF5physical
28514442
CTR2_HUMANSLC7A2physical
28514442
ARF5_HUMANARF5physical
28514442
SAR1B_HUMANSAR1Bphysical
28514442
ARL8A_HUMANARL8Aphysical
28514442
S47A1_HUMANSLC47A1physical
28514442
CXA1_HUMANGJA1physical
28514442
CXCR4_HUMANCXCR4physical
28514442
VANG2_HUMANVANGL2physical
28514442
RPTOR_HUMANRPTORphysical
28514442
COT2_HUMANNR2F2physical
28514442
STEA3_HUMANSTEAP3physical
28514442
TM192_HUMANTMEM192physical
28514442
S26A6_HUMANSLC26A6physical
28514442
Drug and Disease Associations
Kegg Disease
H00824 Calcification of joints and arteries
OMIM Disease
211800Calcification of joints and arteries (CALJA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 5NTD_HUMAN

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Related Literatures of Post-Translational Modification
GPI-anchor
ReferencePubMed
"Primary structure of human placental 5'-nucleotidase andidentification of the glycolipid anchor in the mature form.";
Misumi Y., Ogata S., Ohkubo K., Hirose S., Ikehara Y.;
Eur. J. Biochem. 191:563-569(1990).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, ANDGPI-ANCHOR AT SER-549.
N-linked Glycosylation
ReferencePubMed
"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-333, AND MASSSPECTROMETRY.
"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-311; ASN-333 AND ASN-403,AND MASS SPECTROMETRY.

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