PURA_HUMAN - dbPTM
PURA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PURA_HUMAN
UniProt AC Q00577
Protein Name Transcriptional activator protein Pur-alpha
Gene Name PURA
Organism Homo sapiens (Human).
Sequence Length 322
Subcellular Localization Nucleus.
Protein Description This is a probable transcription activator that specifically binds the purine-rich single strand of the PUR element located upstream of the MYC gene. May play a role in the initiation of DNA replication and in recombination..
Protein Sequence MADRDSGSEQGGAALGSGGSLGHPGSGSGSGGGGGGGGGGGGSGGGGGGAPGGLQHETQELASKRVDIQNKRFYLDVKQNAKGRFLKIAEVGAGGNKSRLTLSMSVAVEFRDYLGDFIEHYAQLGPSQPPDLAQAQDEPRRALKSEFLVRENRKYYMDLKENQRGRFLRIRQTVNRGPGLGSTQGQTIALPAQGLIEFRDALAKLIDDYGVEEEPAELPEGTSLTVDNKRFFFDVGSNKYGVFMRVSEVKPTYRNSITVPYKVWAKFGHTFCKYSEEMKKIQEKQREKRAACEQLHQQQQQQQEETAAATLLLQGEEEGEED
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------MADRDSGSE
------CCCCCCCCC		22.1221406692
6Phosphorylation--MADRDSGSEQGGA
--CCCCCCCCCCCCC		45.1517081983
8PhosphorylationMADRDSGSEQGGAAL
CCCCCCCCCCCCCCC		30.6017081983
17PhosphorylationQGGAALGSGGSLGHP
CCCCCCCCCCCCCCC		40.6127251275
20PhosphorylationAALGSGGSLGHPGSG
CCCCCCCCCCCCCCC		34.4027251275
26PhosphorylationGSLGHPGSGSGSGGG
CCCCCCCCCCCCCCC		33.9520068231
28PhosphorylationLGHPGSGSGSGGGGG
CCCCCCCCCCCCCCC		31.3320068231
30PhosphorylationHPGSGSGSGGGGGGG
CCCCCCCCCCCCCCC		35.6420068231
43PhosphorylationGGGGGGGSGGGGGGA
CCCCCCCCCCCCCCC		37.2220363803
58PhosphorylationPGGLQHETQELASKR
CCCHHHHHHHHHHCC		25.8120363803
63PhosphorylationHETQELASKRVDIQN
HHHHHHHHCCCCCCC		33.3520363803
71UbiquitinationKRVDIQNKRFYLDVK
CCCCCCCCEEEEECH		27.7524816145
74PhosphorylationDIQNKRFYLDVKQNA
CCCCCEEEEECHHHC		13.16-
78AcetylationKRFYLDVKQNAKGRF
CEEEEECHHHCCCCE		37.1925953088
87AcetylationNAKGRFLKIAEVGAG
HCCCCEEEEEEECCC		36.8425953088
87MalonylationNAKGRFLKIAEVGAG
HCCCCEEEEEEECCC		36.8426320211
87UbiquitinationNAKGRFLKIAEVGAG
HCCCCEEEEEEECCC		36.8429967540
97UbiquitinationEVGAGGNKSRLTLSM
EECCCCCHHHEEEEE		39.9830230243
98PhosphorylationVGAGGNKSRLTLSMS
ECCCCCHHHEEEEEE		36.20-
103PhosphorylationNKSRLTLSMSVAVEF
CHHHEEEEEEEEHHH		12.0824275569
113PhosphorylationVAVEFRDYLGDFIEH
EEHHHHHHHHHHHHH		14.3427642862
127PhosphorylationHYAQLGPSQPPDLAQ
HHHHHCCCCCCCHHH		54.2224043423
144UbiquitinationDEPRRALKSEFLVRE
CHHHHHHHHHHHHCC		47.13-
145PhosphorylationEPRRALKSEFLVREN
HHHHHHHHHHHHCCC		34.1428857561
154MethylationFLVRENRKYYMDLKE
HHHCCCCCEECCCCC		52.92116252573
155PhosphorylationLVRENRKYYMDLKEN
HHCCCCCEECCCCCC		10.7729341593
156PhosphorylationVRENRKYYMDLKENQ
HCCCCCEECCCCCCC		6.2829341593
160MethylationRKYYMDLKENQRGRF
CCEECCCCCCCCCCE		50.8166701411
173PhosphorylationRFLRIRQTVNRGPGL
CEEEEEEEHHCCCCC		15.2029978859
182PhosphorylationNRGPGLGSTQGQTIA
HCCCCCCCCCCCEEE		23.7021712546
183PhosphorylationRGPGLGSTQGQTIAL
CCCCCCCCCCCEEEE		34.6121712546
187PhosphorylationLGSTQGQTIALPAQG
CCCCCCCEEEEECCH		18.2921712546
204UbiquitinationEFRDALAKLIDDYGV
HHHHHHHHHHHHCCC		46.9924816145
222PhosphorylationPAELPEGTSLTVDNK
CCCCCCCCEEEECCE		20.9218452278
223PhosphorylationAELPEGTSLTVDNKR
CCCCCCCEEEECCEE		32.6618452278
229AcetylationTSLTVDNKRFFFDVG
CEEEECCEEEEEECC		46.2326051181
229UbiquitinationTSLTVDNKRFFFDVG
CEEEECCEEEEEECC		46.2329967540
239UbiquitinationFFDVGSNKYGVFMRV
EEECCCCCEEEEEEE		45.1123000965
240PhosphorylationFDVGSNKYGVFMRVS
EECCCCCEEEEEEEE		23.83-
247PhosphorylationYGVFMRVSEVKPTYR
EEEEEEEEECCCCCC		26.7223312004
250UbiquitinationFMRVSEVKPTYRNSI
EEEEEECCCCCCCCC		27.8224816145
252PhosphorylationRVSEVKPTYRNSITV
EEEECCCCCCCCCCC		29.4223403867
253PhosphorylationVSEVKPTYRNSITVP
EEECCCCCCCCCCCC		19.1423403867
256PhosphorylationVKPTYRNSITVPYKV
CCCCCCCCCCCCHHH		15.6122617229
258PhosphorylationPTYRNSITVPYKVWA
CCCCCCCCCCHHHHH		18.4329691806
261PhosphorylationRNSITVPYKVWAKFG
CCCCCCCHHHHHHHC		17.5320090780
262UbiquitinationNSITVPYKVWAKFGH
CCCCCCHHHHHHHCC		25.8223000965
262AcetylationNSITVPYKVWAKFGH
CCCCCCHHHHHHHCC		25.8225953088
266UbiquitinationVPYKVWAKFGHTFCK
CCHHHHHHHCCHHHH		35.8523000965
266AcetylationVPYKVWAKFGHTFCK
CCHHHHHHHCCHHHH		35.8525953088
273UbiquitinationKFGHTFCKYSEEMKK
HHCCHHHHHHHHHHH		47.8519608861
273MalonylationKFGHTFCKYSEEMKK
HHCCHHHHHHHHHHH		47.8526320211
273AcetylationKFGHTFCKYSEEMKK
HHCCHHHHHHHHHHH		47.8519608861
274PhosphorylationFGHTFCKYSEEMKKI
HCCHHHHHHHHHHHH		23.61-
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 PURA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PURA_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 PURA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
E2F1_HUMANE2F1physical
10597240
PURB_HUMANPURBphysical
22939629
ZN638_HUMANZNF638physical
22939629
RFC3_HUMANRFC3physical
22939629
RFC2_HUMANRFC2physical
22939629
RB_HUMANRB1physical
7592647
IL7RA_HUMANIL7Rphysical
23151878
E2F1_HUMANE2F1physical
15517862
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616158Mental retardation, autosomal dominant 31 (MRD31)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PURA_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-273, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-8, AND MASSSPECTROMETRY.

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