PUR8_HUMAN - dbPTM
PUR8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUR8_HUMAN
UniProt AC P30566
Protein Name Adenylosuccinate lyase {ECO:0000303|PubMed:8404037}
Gene Name ADSL
Organism Homo sapiens (Human).
Sequence Length 484
Subcellular Localization
Protein Description Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate..
Protein Sequence MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKAELCL
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------MAAGGDHGS
------CCCCCCCCC		18.14-
9PhosphorylationAAGGDHGSPDSYRSP
CCCCCCCCCCCCCCC		23.3229255136
12PhosphorylationGDHGSPDSYRSPLAS
CCCCCCCCCCCCHHH		26.3222167270
13PhosphorylationDHGSPDSYRSPLASR
CCCCCCCCCCCHHHH		23.6125850435
15PhosphorylationGSPDSYRSPLASRYA
CCCCCCCCCHHHHCC		18.9425159151
19PhosphorylationSYRSPLASRYASPEM
CCCCCHHHHCCCHHH		33.2422199227
21PhosphorylationRSPLASRYASPEMCF
CCCHHHHCCCHHHEE		14.6728152594
23PhosphorylationPLASRYASPEMCFVF
CHHHHCCCHHHEEEE		16.6828442448
27GlutathionylationRYASPEMCFVFSDRY
HCCCHHHEEEEECCC		2.2222555962
75AcetylationNLENIDFKMAAEEEK
HHCCCCHHHHHHHHH		24.7123236377
75 (in isoform 2)Ubiquitination-24.7121890473
75UbiquitinationNLENIDFKMAAEEEK
HHCCCCHHHHHHHHH		24.7121906983
82AcetylationKMAAEEEKRLRHDVM
HHHHHHHHHHHHHHH		61.0723749302
94PhosphorylationDVMAHVHTFGHCCPK
HHHHHHHHCCCCCCC		30.17310709025
111PhosphorylationGIIHLGATSCYVGDN
CEEEECCCEEECCCC		19.9668997745
112PhosphorylationIIHLGATSCYVGDNT
EEEECCCEEECCCCC		11.6928857561
114PhosphorylationHLGATSCYVGDNTDL
EECCCEEECCCCCCE		13.7727251275
134UbiquitinationALDLLLPKLARVISR
HHHHHHHHHHHHHHH		55.54-
1342-HydroxyisobutyrylationALDLLLPKLARVISR
HHHHHHHHHHHHHHH		55.54-
147AcetylationSRLADFAKERASLPT
HHHHHHHHHHCCCCC		47.9619608861
147UbiquitinationSRLADFAKERASLPT
HHHHHHHHHHCCCCC		47.9619608861
151PhosphorylationDFAKERASLPTLGFT
HHHHHHCCCCCCCCC		40.8926437602
1702-HydroxyisobutyrylationAQLTTVGKRCCLWIQ
HHEEEHHHHHHHHHH		37.62-
170AcetylationAQLTTVGKRCCLWIQ
HHEEEHHHHHHHHHH		37.6225953088
170UbiquitinationAQLTTVGKRCCLWIQ
HHEEEHHHHHHHHHH		37.6221890473
170 (in isoform 2)Ubiquitination-37.6221890473
170 (in isoform 1)Ubiquitination-37.6221890473
199UbiquitinationDLRFRGVKGTTGTQA
HHHHCCCCCCCCCCH		54.05-
218UbiquitinationLFEGDDHKVEQLDKM
HHCCCCHHHHHHHHH		55.23-
224UbiquitinationHKVEQLDKMVTEKAG
HHHHHHHHHHHHHCC		43.81-
224AcetylationHKVEQLDKMVTEKAG
HHHHHHHHHHHHHCC		43.8123236377
229UbiquitinationLDKMVTEKAGFKRAF
HHHHHHHHCCCCEEE		44.4321906983
229 (in isoform 2)Ubiquitination-44.4321890473
239PhosphorylationFKRAFIITGQTYTRK
CCEEEEEECCCCCCC		20.5820068231
242PhosphorylationAFIITGQTYTRKVDI
EEEEECCCCCCCCCH		28.3628152594
243PhosphorylationFIITGQTYTRKVDIE
EEEECCCCCCCCCHH		9.1728152594
244PhosphorylationIITGQTYTRKVDIEV
EEECCCCCCCCCHHH		27.6628152594
276UbiquitinationIRLLANLKEMEEPFE
HHHHHHHHHCCCCHH		55.6221906983
276 (in isoform 2)Ubiquitination-55.6221890473
284UbiquitinationEMEEPFEKQQIGSSA
HCCCCHHHCCCCCCC		48.1321906983
284 (in isoform 2)Ubiquitination-48.1321890473
284AcetylationEMEEPFEKQQIGSSA
HCCCCHHHCCCCCCC		48.1326822725
289PhosphorylationFEKQQIGSSAMPYKR
HHHCCCCCCCCCCCC		19.2926437602
294PhosphorylationIGSSAMPYKRNPMRS
CCCCCCCCCCCCCHH		14.97119525
295UbiquitinationGSSAMPYKRNPMRSE
CCCCCCCCCCCCHHH		39.5719608861
295AcetylationGSSAMPYKRNPMRSE
CCCCCCCCCCCCHHH		39.5719608861
330PhosphorylationSVQWFERTLDDSANR
CHHHHHHCCCCHHHH		27.6026437602
334PhosphorylationFERTLDDSANRRICL
HHHCCCCHHHHHHHH		27.4026437602
391UbiquitinationNIIMAMVKAGGSRQD
HHHHHHHHCCCCCHH		28.38-
402UbiquitinationSRQDCHEKIRVLSQQ
CCHHHHHHHHHHHHH		16.49-
407PhosphorylationHEKIRVLSQQAASVV
HHHHHHHHHHHHHHH		19.8646159937
412PhosphorylationVLSQQAASVVKQEGG
HHHHHHHHHHHHCCC		30.3821712546
415SumoylationQQAASVVKQEGGDND
HHHHHHHHHCCCCCC		40.2425114211
415AcetylationQQAASVVKQEGGDND
HHHHHHHHHCCCCCC		40.2426051181
415UbiquitinationQQAASVVKQEGGDND
HHHHHHHHHCCCCCC		40.2421906983
432PhosphorylationERIQVDAYFSPIHSQ
HHHHCCEEECCHHHH		10.5028450419
434PhosphorylationIQVDAYFSPIHSQLD
HHCCEEECCHHHHHH		15.4028450419
438PhosphorylationAYFSPIHSQLDHLLD
EEECCHHHHHHHHCC		32.9146159943
447PhosphorylationLDHLLDPSSFTGRAS
HHHHCCCCCCCCCHH		37.4428122231
448PhosphorylationDHLLDPSSFTGRASQ
HHHCCCCCCCCCHHH		32.0128122231
450PhosphorylationLLDPSSFTGRASQQV
HCCCCCCCCCHHHHH		27.9228122231
466PhosphorylationRFLEEEVYPLLKPYE
HHHHHCHHHHCCCHH		7.4611200505
470UbiquitinationEEVYPLLKPYESVMK
HCHHHHCCCHHHHHH		53.92-
472PhosphorylationVYPLLKPYESVMKVK
HHHHCCCHHHHHHHH		21.1729496907
479UbiquitinationYESVMKVKAELCL--
HHHHHHHHHHHCC--		30.53-
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 PUR8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUR8_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 PUR8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TYSY_HUMANTYMSphysical
22939629
NOV_HUMANNOVphysical
21988832
API5_HUMANAPI5physical
22863883
BT3L4_HUMANBTF3L4physical
22863883
5NTC_HUMANNT5C2physical
22863883
OXSR1_HUMANOXSR1physical
22863883
PAIP1_HUMANPAIP1physical
22863883
TWF1_HUMANTWF1physical
22863883
SYWC_HUMANWARSphysical
22863883
WDR4_HUMANWDR4physical
22863883
CACO2_HUMANCALCOCO2physical
24722188
REL_HUMANRELphysical
24722188
AL8A1_HUMANALDH8A1physical
26344197
PUR9_HUMANATICphysical
26344197
PUR6_HUMANPAICSphysical
26344197
TPIS_HUMANTPI1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
103050Adenylosuccinase deficiency (ADSLD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUR8_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, 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-147 AND LYS-295, AND MASSSPECTROMETRY.
Phosphorylation
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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.

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