PAPS1_HUMAN - dbPTM
PAPS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAPS1_HUMAN
UniProt AC O43252
Protein Name Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
Gene Name PAPSS1
Organism Homo sapiens (Human).
Sequence Length 624
Subcellular Localization
Protein Description Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. [PubMed: 9576487]
Protein Sequence MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEKA
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
1Acetylation-------MEIPGSLC
-------CCCCCCCC		10.7222223895
6Phosphorylation--MEIPGSLCKKVKL
--CCCCCCCCCEEEC		25.8225159151
9AcetylationEIPGSLCKKVKLSNN
CCCCCCCCEEECCCC		66.9325953088
9UbiquitinationEIPGSLCKKVKLSNN
CCCCCCCCEEECCCC		66.9323000965
10UbiquitinationIPGSLCKKVKLSNNA
CCCCCCCEEECCCCH		43.5423000965
12AcetylationGSLCKKVKLSNNAQN
CCCCCEEECCCCHHH		55.8925953088
12UbiquitinationGSLCKKVKLSNNAQN
CCCCCEEECCCCHHH		55.8923000965
14PhosphorylationLCKKVKLSNNAQNWG
CCCEEECCCCHHHCC		23.4827251275
26PhosphorylationNWGMQRATNVTYQAH
HCCCHHHHCEEEEEE		32.2021945579
29PhosphorylationMQRATNVTYQAHHVS
CHHHHCEEEEEEECC		16.4021945579
30PhosphorylationQRATNVTYQAHHVSR
HHHHCEEEEEEECCC		10.2221945579
36PhosphorylationTYQAHHVSRNKRGQV
EEEEEECCCCCCCCE		26.2721945579
47MethylationRGQVVGTRGGFRGCT
CCCEEECCCCCCCCE		36.99-
75PhosphorylationVSMALEEYLVCHGIP
HHHHHHHHHHHCCCC		8.6126074081
84PhosphorylationVCHGIPCYTLDGDNI
HHCCCCEEECCCCCH		12.6526074081
85PhosphorylationCHGIPCYTLDGDNIR
HCCCCEEECCCCCHH		25.7026074081
97UbiquitinationNIRQGLNKNLGFSPE
CHHHHHHHCCCCCHH		59.6029967540
102PhosphorylationLNKNLGFSPEDREEN
HHHCCCCCHHHHHHH		26.1121815630
129PhosphorylationDAGLVCITSFISPYT
HCCCEEEEECCCCCC		16.6828348404
130PhosphorylationAGLVCITSFISPYTQ
CCCEEEEECCCCCCC		10.7328348404
133PhosphorylationVCITSFISPYTQDRN
EEEEECCCCCCCCCC		15.1628348404
150UbiquitinationRQIHEGASLPFFEVF
CCCCCCCCCCCEEEE		47.6427667366
154UbiquitinationEGASLPFFEVFVDAP
CCCCCCCEEEEECCC		8.0624816145
162UbiquitinationEVFVDAPLHVCEQRD
EEEECCCHHHHHCCC		5.1823000965
171UbiquitinationVCEQRDVKGLYKKAR
HHHCCCHHHHHHHHH		47.7027667366
175UbiquitinationRDVKGLYKKARAGEI
CCHHHHHHHHHHCCC		45.0324816145
183NeddylationKARAGEIKGFTGIDS
HHHHCCCCCCCCCCC		43.6032015554
183UbiquitinationKARAGEIKGFTGIDS
HHHHCCCCCCCCCCC		43.6023000965
183AcetylationKARAGEIKGFTGIDS
HHHHCCCCCCCCCCC		43.6026051181
190PhosphorylationKGFTGIDSEYEKPEA
CCCCCCCCCCCCCCC		39.9128796482
192PhosphorylationFTGIDSEYEKPEAPE
CCCCCCCCCCCCCCC		32.9528796482
194UbiquitinationGIDSEYEKPEAPELV
CCCCCCCCCCCCCEE		47.4529967540
231PhosphorylationDIVPVDASYEVKELY
CCCCCCCCCEEEEEE		19.8428152594
232PhosphorylationIVPVDASYEVKELYV
CCCCCCCCEEEEEEC		26.8528152594
235UbiquitinationVDASYEVKELYVPEN
CCCCCEEEEEECCCC		30.0229967540
243AcetylationELYVPENKLHLAKTD
EEECCCCCEEECCCC		35.3026822725
243UbiquitinationELYVPENKLHLAKTD
EEECCCCCEEECCCC		35.3032015554
258UbiquitinationAETLPALKINKVDMQ
HHHCCCCCCCCCCHH		46.4732142685
258AcetylationAETLPALKINKVDMQ
HHHCCCCCCCCCCHH		46.4725953088
354MethylationRKEERCARQWGTTCK
HHHHHHHHHHCCCCC		36.09115383527
361UbiquitinationRQWGTTCKNHPYIKM
HHHCCCCCCCHHEEE		57.0829967540
383UbiquitinationLIGGDLQVLDRVYWN
EECCCEEEEEEEECC		8.5827667366
404UbiquitinationRLTPTELKQKFKDMN
ECCHHHHHHHHHHCC		45.2533845483
406UbiquitinationTPTELKQKFKDMNAD
CHHHHHHHHHHCCCC		53.44-
466SulfoxidationKDDDVPLMWRMKQHA
CCCCCCCHHHHHHHH		1.4230846556
518PhosphorylationMVAGANFYIVGRDPA
EECCCCEEEEECCCC		8.4320068231
532PhosphorylationAGMPHPETGKDLYEP
CCCCCCCCCCCCCCC		54.7224719451
537PhosphorylationPETGKDLYEPSHGAK
CCCCCCCCCCCCCCE		35.6127642862
537NitrationPETGKDLYEPSHGAK
CCCCCCCCCCCCCCE		35.61-
547UbiquitinationSHGAKVLTMAPGLIT
CCCCEEEEECCCEEE		17.8024816145
5672-HydroxyisobutyrylationFRVAAYNKKKKRMDY
EEHHHCCCCCCCCCC		53.98-
568UbiquitinationRVAAYNKKKKRMDYY
EHHHCCCCCCCCCCC		60.9524816145
574PhosphorylationKKKKRMDYYDSEHHE
CCCCCCCCCCCCCCC		10.3826846344
575PhosphorylationKKKRMDYYDSEHHED
CCCCCCCCCCCCCCC		14.5526846344
577PhosphorylationKRMDYYDSEHHEDFE
CCCCCCCCCCCCCCC		23.7826846344
587PhosphorylationHEDFEFISGTRMRKL
CCCCCCCCCHHHHHH		39.1626846344
589PhosphorylationDFEFISGTRMRKLAR
CCCCCCCHHHHHHHH		17.9426846344
598UbiquitinationMRKLAREGQKPPEGF
HHHHHHCCCCCCCCC		34.9521890473
600AcetylationKLAREGQKPPEGFMA
HHHHCCCCCCCCCCC		73.6919829777
602UbiquitinationAREGQKPPEGFMAPK
HHCCCCCCCCCCCCH		62.4721890473
609AcetylationPEGFMAPKAWTVLTE
CCCCCCCHHHHHHHH		47.2019829785
619UbiquitinationTVLTEYYKSLEKA--
HHHHHHHHHHHCC--		47.8923000965
619UbiquitinationTVLTEYYKSLEKA--
HHHHHHHHHHHCC--		47.8921890473
623UbiquitinationEYYKSLEKA------
HHHHHHHCC------		65.7723000965
623UbiquitinationEYYKSLEKA------
HHHHHHHCC------		65.7721890473
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 PAPS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAPS1_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 PAPS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1A1_HUMANEEF1A1physical
16169070
U119A_HUMANUNC119physical
16169070
PUR9_HUMANATICphysical
22863883
HMGB3_HUMANHMGB3physical
22863883
MTRR_HUMANMTRRphysical
22863883
LIS1_HUMANPAFAH1B1physical
22863883
PTMA_HUMANPTMAphysical
22863883
PAPS2_HUMANPAPSS2physical
28514442
TFCP2_HUMANTFCP2physical
28514442
GNL1_HUMANGNL1physical
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 PAPS1_HUMAN

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Related Literatures of Post-Translational Modification

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