PNPH_HUMAN - dbPTM
PNPH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PNPH_HUMAN
UniProt AC P00491
Protein Name Purine nucleoside phosphorylase
Gene Name PNP
Organism Homo sapiens (Human).
Sequence Length 289
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm .
Protein Description The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate..
Protein Sequence MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
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
1Sulfoxidation-------MENGYTYE
-------CCCCCCHH		9.0028183972
1Acetylation-------MENGYTYE
-------CCCCCCHH		9.0022223895
11UbiquitinationGYTYEDYKNTAEWLL
CCCHHHHCCHHHHHH		61.21-
13PhosphorylationTYEDYKNTAEWLLSH
CHHHHCCHHHHHHHC		23.0825867546
19PhosphorylationNTAEWLLSHTKHRPQ
CHHHHHHHCCCCCCE		27.2625867546
21PhosphorylationAEWLLSHTKHRPQVA
HHHHHHCCCCCCEEE		25.7725867546
22UbiquitinationEWLLSHTKHRPQVAI
HHHHHCCCCCCEEEE		31.9921906983
33PhosphorylationQVAIICGSGLGGLTD
EEEEEECCCCCHHHH		26.8328348404
39PhosphorylationGSGLGGLTDKLTQAQ
CCCCCHHHHCCHHHH		34.0730108239
95UbiquitinationYEGYPLWKVTFPVRV
EECCCCEEEEECHHH		38.8021906983
95AcetylationYEGYPLWKVTFPVRV
EECCCCEEEEECHHH		38.8023954790
163PhosphorylationGDRFPAMSDAYDRTM
HHCCHHHHHHHHHHH		22.6123403867
166PhosphorylationFPAMSDAYDRTMRQR
CHHHHHHHHHHHHHH		15.7923403867
168MethylationAMSDAYDRTMRQRAL
HHHHHHHHHHHHHHH		20.11115485467
169PhosphorylationMSDAYDRTMRQRALS
HHHHHHHHHHHHHHH		17.5123403867
176PhosphorylationTMRQRALSTWKQMGE
HHHHHHHHHHHHHHH		31.1026546556
177PhosphorylationMRQRALSTWKQMGEQ
HHHHHHHHHHHHHHH		37.2220736484
179UbiquitinationQRALSTWKQMGEQRE
HHHHHHHHHHHHHEE		30.4121906983
179AcetylationQRALSTWKQMGEQRE
HHHHHHHHHHHHHEE		30.4125953088
206GlutathionylationSFETVAECRVLQKLG
CHHHHHHHHHHHHHC		2.3522555962
211UbiquitinationAECRVLQKLGADAVG
HHHHHHHHHCCCCCC		44.7321906983
211AcetylationAECRVLQKLGADAVG
HHHHHHHHHCCCCCC		44.7323749302
211MalonylationAECRVLQKLGADAVG
HHHHHHHHHCCCCCC		44.7332601280
2112-HydroxyisobutyrylationAECRVLQKLGADAVG
HHHHHHHHHCCCCCC		44.73-
219SulfoxidationLGADAVGMSTVPEVI
HCCCCCCCCCCCHHH		2.1421406390
220PhosphorylationGADAVGMSTVPEVIV
CCCCCCCCCCCHHHH		21.9627050516
239PhosphorylationGLRVFGFSLITNKVI
CCEEEEEEEECCCEE		21.1723898821
242PhosphorylationVFGFSLITNKVIMDY
EEEEEEECCCEECCH		33.9921712546
247SulfoxidationLITNKVIMDYESLEK
EECCCEECCHHHHHH		5.1321406390
249PhosphorylationTNKVIMDYESLEKAN
CCCEECCHHHHHHCC		7.0521945579
251PhosphorylationKVIMDYESLEKANHE
CEECCHHHHHHCCHH		35.2821945579
254UbiquitinationMDYESLEKANHEEVL
CCHHHHHHCCHHHHH		60.84-
254AcetylationMDYESLEKANHEEVL
CCHHHHHHCCHHHHH		60.8423954790
265MalonylationEEVLAAGKQAAQKLE
HHHHHHHHHHHHHHH		31.8526320211
265UbiquitinationEEVLAAGKQAAQKLE
HHHHHHHHHHHHHHH		31.85-
265AcetylationEEVLAAGKQAAQKLE
HHHHHHHHHHHHHHH		31.8525953088
276PhosphorylationQKLEQFVSILMASIP
HHHHHHHHHHHHCCC		15.9928060719
281PhosphorylationFVSILMASIPLPDKA
HHHHHHHCCCCCCCC		15.6928060719
287UbiquitinationASIPLPDKAS-----
HCCCCCCCCC-----		48.90-
289PhosphorylationIPLPDKAS-------
CCCCCCCC-------		46.6325159151
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 PNPH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PNPH_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 PNPH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM48_HUMANRBM48physical
16169070
CC90B_HUMANCCDC90Bphysical
16169070
P53_HUMANTP53physical
16169070
ZHX1_HUMANZHX1physical
16169070
APLP1_HUMANAPLP1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
TM177_HUMANTMEM177physical
22939629
GUAA_HUMANGMPSphysical
22863883
MTAP_HUMANMTAPphysical
22863883
SERC_HUMANPSAT1physical
22863883
PSMD5_HUMANPSMD5physical
22863883
RAB1A_HUMANRAB1Aphysical
22863883
PNPH_HUMANPNPphysical
25416956
TPPC4_HUMANTRAPPC4physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613179Purine nucleoside phosphorylase deficiency (PNPD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00242Cladribine
DB00900Didanosine
Regulatory Network of PNPH_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 MET-1, AND MASS SPECTROMETRY.
"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-95, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory