PURA2_HUMAN - dbPTM
PURA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PURA2_HUMAN
UniProt AC P30520
Protein Name Adenylosuccinate synthetase isozyme 2 {ECO:0000255|HAMAP-Rule:MF_03127}
Gene Name ADSS {ECO:0000255|HAMAP-Rule:MF_03127}
Organism Homo sapiens (Human).
Sequence Length 456
Subcellular Localization Cytoplasm. Partially associated with particulate fractions.
Protein Description Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP..
Protein Sequence MAFAETYPAASSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRCQGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGLEGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLRMCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMEKIKPMVRDGVYFLYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAYTTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALALTKLDILDMFTEIKVGVAYKLDGEIIPHIPANQEVLNKVEVQYKTLPGWNTDISNARAFKELPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
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------MAFAETYPA
------CCCCCCCCC		16.62-
6Phosphorylation--MAFAETYPAASSL
--CCCCCCCCCCCCC		31.2325394399
7Phosphorylation-MAFAETYPAASSLP
-CCCCCCCCCCCCCC		5.1625850435
11PhosphorylationAETYPAASSLPNGDC
CCCCCCCCCCCCCCC		34.2225850435
12PhosphorylationETYPAASSLPNGDCG
CCCCCCCCCCCCCCC		43.0227251275
43AcetylationAQWGDEGKGKVVDLL
CEECCCCCCEEEEEE		54.2126051181
45AcetylationWGDEGKGKVVDLLAQ
ECCCCCCEEEEEEEC		42.4426051181
45UbiquitinationWGDEGKGKVVDLLAQ
ECCCCCCEEEEEEEC		42.44-
58GlutathionylationAQDADIVCRCQGGNN
ECCCCEEEEECCCCC		3.5322555962
118UbiquitinationEKNVQKGKGLEGWEK
HHHHHCCCCCCHHHE		68.32-
125UbiquitinationKGLEGWEKRLIISDR
CCCCHHHEEEEEECC		46.10-
130PhosphorylationWEKRLIISDRAHIVF
HHEEEEEECCCEEEE		17.6625106551
157UbiquitinationQRQEQAGKNLGTTKK
HHHHHHHHHCCCCCC		52.60-
164UbiquitinationKNLGTTKKGIGPVYS
HHCCCCCCCCCHHCC		54.38-
170PhosphorylationKKGIGPVYSSKAARS
CCCCCHHCCHHHHHH		15.4528152594
171PhosphorylationKGIGPVYSSKAARSG
CCCCHHCCHHHHHHC		26.1228152594
172PhosphorylationGIGPVYSSKAARSGL
CCCHHCCHHHHHHCC		14.5028152594
173UbiquitinationIGPVYSSKAARSGLR
CCHHCCHHHHHHCCC		39.87-
173AcetylationIGPVYSSKAARSGLR
CCHHCCHHHHHHCCC		39.8726051181
181SulfoxidationAARSGLRMCDLVSDF
HHHHCCCHHCCCCCC		2.2221406390
196UbiquitinationDGFSERFKVLANQYK
CCHHHHHHHHHHHHH		42.43-
203UbiquitinationKVLANQYKSIYPTLE
HHHHHHHHHHCCEEE		22.1821890473
223PhosphorylationELQKLKGYMEKIKPM
HHHHHHHHHHHHHHH		10.667144273
226UbiquitinationKLKGYMEKIKPMVRD
HHHHHHHHHHHHHHH		39.23-
236PhosphorylationPMVRDGVYFLYEALH
HHHHHHHHHHHHHHH		8.0675195
239PhosphorylationRDGVYFLYEALHGPP
HHHHHHHHHHHHCCC		6.8375199
248UbiquitinationALHGPPKKILVEGAN
HHHCCCCEEEEECCC		47.23-
331PhosphorylationRGREFGVTTGRKRRC
HCCCCCCCCCCCCCC		24.7421406692
332PhosphorylationGREFGVTTGRKRRCG
CCCCCCCCCCCCCCC		32.3621406692
368SulfoxidationTKLDILDMFTEIKVG
HHHHHHHHHCCCEEE		3.9221406390
397UbiquitinationANQEVLNKVEVQYKT
CCHHHHHHCEEEEEC		35.29-
402PhosphorylationLNKVEVQYKTLPGWN
HHHCEEEEECCCCCC		15.898227809
403UbiquitinationNKVEVQYKTLPGWNT
HHCEEEEECCCCCCC		26.8821890473
403UbiquitinationNKVEVQYKTLPGWNT
HHCEEEEECCCCCCC		26.8821890473
404O-linked_GlycosylationKVEVQYKTLPGWNTD
HCEEEEECCCCCCCC		33.0028510447
413O-linked_GlycosylationPGWNTDISNARAFKE
CCCCCCCCCCCCHHC		27.5228510447
419UbiquitinationISNARAFKELPVNAQ
CCCCCCHHCCCCCHH		58.3121890473
419AcetylationISNARAFKELPVNAQ
CCCCCCHHCCCCCHH		58.3123749302
419UbiquitinationISNARAFKELPVNAQ
CCCCCCHHCCCCCHH		58.3121890473
441UbiquitinationDELQIPVKWIGVGKS
HHHCCCEEEEECCCC		27.9521890473
441UbiquitinationDELQIPVKWIGVGKS
HHHCCCEEEEECCCC		27.9521890473
447AcetylationVKWIGVGKSRESMIQ
EEEEECCCCHHHHHH		43.8925953088
447UbiquitinationVKWIGVGKSRESMIQ
EEEEECCCCHHHHHH		43.89-
448PhosphorylationKWIGVGKSRESMIQL
EEEECCCCHHHHHHC		35.0423403867
451PhosphorylationGVGKSRESMIQLF--
ECCCCHHHHHHCC--		21.789414821
452SulfoxidationVGKSRESMIQLF---
CCCCHHHHHHCC---		1.6230846556
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 PURA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PURA2_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 PURA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RINI_HUMANRNH1physical
22939629
SGTA_HUMANSGTAphysical
22939629
SMYD1_HUMANSMYD1physical
23455924
FPPS_HUMANFDPSphysical
22863883
CH10_HUMANHSPE1physical
22863883
KYNU_HUMANKYNUphysical
22863883
PDIA3_HUMANPDIA3physical
22863883
PTMS_HUMANPTMSphysical
22863883
RBBP7_HUMANRBBP7physical
22863883
TALDO_HUMANTALDO1physical
22863883
WDR1_HUMANWDR1physical
22863883
ADPPT_HUMANAASDHPPTphysical
26344197
GDE_HUMANAGLphysical
26344197
ARFP1_HUMANARFIP1physical
26344197
ARMT1_HUMANC6orf211physical
26344197
PUR2_HUMANGARTphysical
26344197
GNA1_HUMANGNPNAT1physical
26344197
HCD2_HUMANHSD17B10physical
26344197
IMPA2_HUMANIMPA2physical
26344197
NDKB_HUMANNME2physical
26344197
PHS_HUMANPCBD1physical
26344197
PFKAL_HUMANPFKLphysical
26344197
RPE_HUMANRPEphysical
26344197
TNG2_HUMANTANGO2physical
26344197
UMPS_HUMANUMPSphysical
26344197
PURA1_HUMANADSSL1physical
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
DB00128L-Aspartic Acid
Regulatory Network of PURA2_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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