BPNT1_HUMAN - dbPTM
BPNT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BPNT1_HUMAN
UniProt AC O95861
Protein Name 3'(2'),5'-bisphosphate nucleotidase 1
Gene Name BPNT1
Organism Homo sapiens (Human).
Sequence Length 308
Subcellular Localization
Protein Description Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6..
Protein Sequence MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPESIKNALVP
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
2Acetylation------MASSNTVLM
------CCCCHHHHH		22.9722223895
3Phosphorylation-----MASSNTVLMR
-----CCCCHHHHHH		23.8720068231
4Phosphorylation----MASSNTVLMRL
----CCCCHHHHHHH		27.2920068231
6Phosphorylation--MASSNTVLMRLVA
--CCCCHHHHHHHHH		19.5720068231
14PhosphorylationVLMRLVASAYSIAQK
HHHHHHHHHHHHHHH		21.9128152594
16PhosphorylationMRLVASAYSIAQKAG
HHHHHHHHHHHHHHC		9.7128152594
17PhosphorylationRLVASAYSIAQKAGM
HHHHHHHHHHHHHCH		15.9128152594
49MalonylationCATDLQTKADRLAQM
CCHHHHHHHHHHHHH		35.0226320211
49 (in isoform 2)Ubiquitination-35.02-
49UbiquitinationCATDLQTKADRLAQM
CCHHHHHHHHHHHHH		35.02-
49AcetylationCATDLQTKADRLAQM
CCHHHHHHHHHHHHH		35.0223749302
57PhosphorylationADRLAQMSICSSLAR
HHHHHHHHHHHHHHH		14.36-
61PhosphorylationAQMSICSSLARKFPK
HHHHHHHHHHHHCCC		22.95-
122PhosphorylationWVDPLDGTKEYTEGL
EECCCCCCHHHHCCH		21.9929514088
189UbiquitinationLKEVPAGKHIITTTR
EEECCCCCEEEEECC		33.46-
189AcetylationLKEVPAGKHIITTTR
EEECCCCCEEEEECC		33.4625953088
193PhosphorylationPAGKHIITTTRSHSN
CCCCEEEEECCCCCC		22.8526657352
194PhosphorylationAGKHIITTTRSHSNK
CCCEEEEECCCCCCC		15.1426657352
195PhosphorylationGKHIITTTRSHSNKL
CCEEEEECCCCCCCC		22.8626657352
197PhosphorylationHIITTTRSHSNKLVT
EEEEECCCCCCCCHH		29.2230622161
199PhosphorylationITTTRSHSNKLVTDC
EEECCCCCCCCHHHH		36.5930622161
204PhosphorylationSHSNKLVTDCVAAMN
CCCCCCHHHHHHHCC		33.8325693802
210SulfoxidationVTDCVAAMNPDAVLR
HHHHHHHCCCCCEEE		5.5821406390
219UbiquitinationPDAVLRVGGAGNKII
CCCEEEECCCCHHHH		17.50-
236PhosphorylationIEGKASAYVFASPGC
EECCCEEEEEECCCC		8.1327251275
240PhosphorylationASAYVFASPGCKKWD
CEEEEEECCCCCCCC		15.4525159151
243S-nitrosocysteineYVFASPGCKKWDTCA
EEEECCCCCCCCCCC		4.68-
243S-nitrosylationYVFASPGCKKWDTCA
EEEECCCCCCCCCCC		4.6819483679
244SuccinylationVFASPGCKKWDTCAP
EEECCCCCCCCCCCH		63.91-
244AcetylationVFASPGCKKWDTCAP
EEECCCCCCCCCCCH		63.9125953088
244MalonylationVFASPGCKKWDTCAP
EEECCCCCCCCCCCH		63.9126320211
244SuccinylationVFASPGCKKWDTCAP
EEECCCCCCCCCCCH		63.91-
245UbiquitinationFASPGCKKWDTCAPE
EECCCCCCCCCCCHH		55.14-
245AcetylationFASPGCKKWDTCAPE
EECCCCCCCCCCCHH		55.1425953088
248PhosphorylationPGCKKWDTCAPEVIL
CCCCCCCCCCHHHHH		14.95-
274UbiquitinationGNVLQYHKDVKHMNS
CCHHHHCCCCCCCCC		60.32-
289MethylationAGVLATLRNYDYYAS
HHHHHHHHCHHHHHH		34.99-
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 BPNT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BPNT1_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 BPNT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAHD1_HUMANFAHD1physical
26344197
GDPP1_HUMANGDPGP1physical
26344197
MEMO1_HUMANMEMO1physical
26344197
D39U1_HUMANSDR39U1physical
28514442
CHDH_HUMANCHDHphysical
28514442
ADRO_HUMANFDXRphysical
28514442
SYVM_HUMANVARS2physical
28514442
GTPBA_HUMANGTPBP10physical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
MTG1_HUMANMTG1physical
28514442
DPOG1_HUMANPOLGphysical
28514442
ACSF2_HUMANACSF2physical
28514442
RRF2M_HUMANGFM2physical
28514442
TRADD_HUMANTRADDphysical
28514442
MTG2_HUMANMTG2physical
28514442
MOCS1_HUMANMOCS1physical
28514442
ABD18_HUMANC4orf29physical
28514442
MTO1_HUMANMTO1physical
28514442
NUD19_HUMANNUDT19physical
28514442
CPSM_HUMANCPS1physical
28514442
RNH2A_HUMANRNASEH2Aphysical
28514442
PDPR_HUMANPDPRphysical
28514442
MRRP3_HUMANKIAA0391physical
28514442
WDR60_HUMANWDR60physical
28514442
NSUN4_HUMANNSUN4physical
28514442
PYC_HUMANPCphysical
28514442
PPOX_HUMANPPOXphysical
28514442
ACD10_HUMANACAD10physical
28514442
TOP3A_HUMANTOP3Aphysical
28514442
AUHM_HUMANAUHphysical
28514442
IF2M_HUMANMTIF2physical
28514442
MICU2_HUMANMICU2physical
28514442
CDC6_HUMANCDC6physical
28514442
REXO5_HUMANLOC81691physical
28514442
NDUF7_HUMANNDUFAF7physical
28514442
SYLM_HUMANLARS2physical
28514442
MYO9B_HUMANMYO9Bphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
MCM8_HUMANMCM8physical
28514442
RSAD1_HUMANRSAD1physical
28514442
LRCH2_HUMANLRCH2physical
28514442
CATH_HUMANCTSHphysical
28514442
MYO9A_HUMANMYO9Aphysical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
SYSM_HUMANSARS2physical
28514442
NFS1_HUMANNFS1physical
28514442
SYNM_HUMANNARS2physical
28514442
TBC9B_HUMANTBC1D9Bphysical
28514442
PTPM1_HUMANPTPMT1physical
28514442
TBB3_HUMANTUBB3physical
28514442
DEFM_HUMANPDFphysical
28514442
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 BPNT1_HUMAN

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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 ALA-2, AND MASS SPECTROMETRY.

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