ASSY_HUMAN - dbPTM
ASSY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASSY_HUMAN
UniProt AC P00966
Protein Name Argininosuccinate synthase {ECO:0000305}
Gene Name ASS1 {ECO:0000312|HGNC:HGNC:758}
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization Cytoplasm, cytosol .
Protein Description One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues..
Protein Sequence MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKDGTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYILGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK
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
17PhosphorylationAYSGGLDTSCILVWL
EECCCCCCEEEEHHH		30.4624247654
18PhosphorylationYSGGLDTSCILVWLK
ECCCCCCEEEEHHHH		9.9924247654
25"N6,N6-dimethyllysine"SCILVWLKEQGYDVI
EEEEHHHHHCCCCHH		32.07-
25MethylationSCILVWLKEQGYDVI
EEEEHHHHHCCCCHH		32.07-
29PhosphorylationVWLKEQGYDVIAYLA
HHHHHCCCCHHHHHH		13.51-
34PhosphorylationQGYDVIAYLANIGQK
CCCCHHHHHHCCCCC		8.67-
41UbiquitinationYLANIGQKEDFEEAR
HHHCCCCCHHHHHHH		54.78-
49UbiquitinationEDFEEARKKALKLGA
HHHHHHHHHHHHHCC		49.82-
53UbiquitinationEARKKALKLGAKKVF
HHHHHHHHHCCCEEE		50.13-
53AcetylationEARKKALKLGAKKVF
HHHHHHHHHCCCEEE		50.1325953088
582-HydroxyisobutyrylationALKLGAKKVFIEDVS
HHHHCCCEEEEEHHH		41.67-
58UbiquitinationALKLGAKKVFIEDVS
HHHHCCCEEEEEHHH		41.67-
58AcetylationALKLGAKKVFIEDVS
HHHHCCCEEEEEHHH		41.6726822725
79PhosphorylationFIWPAIQSSALYEDR
HHHHHHHCCCCCCCH		16.0927732954
80PhosphorylationIWPAIQSSALYEDRY
HHHHHHCCCCCCCHH		13.1027732954
83PhosphorylationAIQSSALYEDRYLLG
HHHCCCCCCCHHHHC		18.5921253578
87PhosphorylationSALYEDRYLLGTSLA
CCCCCCHHHHCCCCC		20.7117192257
91PhosphorylationEDRYLLGTSLARPCI
CCHHHHCCCCCCCHH		22.1218691976
92PhosphorylationDRYLLGTSLARPCIA
CHHHHCCCCCCCHHH		20.4520068231
97S-nitrosylationGTSLARPCIARKQVE
CCCCCCCHHHHHHHH		2.9424105792
101UbiquitinationARPCIARKQVEIAQR
CCCHHHHHHHHHHHH		50.07-
1012-HydroxyisobutyrylationARPCIARKQVEIAQR
CCCHHHHHHHHHHHH		50.07-
112UbiquitinationIAQREGAKYVSHGAT
HHHHHCCEEEECCCC		57.97-
112AcetylationIAQREGAKYVSHGAT
HHHHHCCEEEECCCC		57.9725953088
113PhosphorylationAQREGAKYVSHGATG
HHHHCCEEEECCCCC		13.4724275569
115PhosphorylationREGAKYVSHGATGKG
HHCCEEEECCCCCCC		17.0828348404
119PhosphorylationKYVSHGATGKGNDQV
EEEECCCCCCCCCCE		43.9828857561
1212-HydroxyisobutyrylationVSHGATGKGNDQVRF
EECCCCCCCCCCEEE		50.62-
121UbiquitinationVSHGATGKGNDQVRF
EECCCCCCCCCCEEE		50.62-
121AcetylationVSHGATGKGNDQVRF
EECCCCCCCCCCEEE		50.6226051181
131PhosphorylationDQVRFELSCYSLAPQ
CCEEEEEEEEECCCC		12.1028152594
132S-nitrosylationQVRFELSCYSLAPQI
CEEEEEEEEECCCCE		4.1222178444
132S-nitrosocysteineQVRFELSCYSLAPQI
CEEEEEEEEECCCCE		4.12-
133PhosphorylationVRFELSCYSLAPQIK
EEEEEEEEECCCCEE		11.8925884760
134PhosphorylationRFELSCYSLAPQIKV
EEEEEEEECCCCEEE		23.5328152594
140UbiquitinationYSLAPQIKVIAPWRM
EECCCCEEEEECCCC		23.49-
140AcetylationYSLAPQIKVIAPWRM
EECCCCEEEEECCCC		23.4926051181
147SulfoxidationKVIAPWRMPEFYNRF
EEEECCCCHHHHHHC		3.0928465586
153MethylationRMPEFYNRFKGRNDL
CCHHHHHHCCCHHHH		24.23-
157DimethylationFYNRFKGRNDLMEYA
HHHHCCCHHHHHHHH		33.80-
157MethylationFYNRFKGRNDLMEYA
HHHHCCCHHHHHHHH		33.80-
161SulfoxidationFKGRNDLMEYAKQHG
CCCHHHHHHHHHHHC		4.0630846556
163PhosphorylationGRNDLMEYAKQHGIP
CHHHHHHHHHHHCCC		12.7224719451
1652-HydroxyisobutyrylationNDLMEYAKQHGIPIP
HHHHHHHHHHCCCCC		41.76-
165UbiquitinationNDLMEYAKQHGIPIP
HHHHHHHHHHCCCCC		41.7619608861
165SuccinylationNDLMEYAKQHGIPIP
HHHHHHHHHHCCCCC		41.7623954790
165AcetylationNDLMEYAKQHGIPIP
HHHHHHHHHHCCCCC		41.7619608861
174PhosphorylationHGIPIPVTPKNPWSM
HCCCCCCCCCCCCCC		24.1625159151
176AcetylationIPIPVTPKNPWSMDE
CCCCCCCCCCCCCCC		67.3028985504
176UbiquitinationIPIPVTPKNPWSMDE
CCCCCCCCCCCCCCC		67.3028985504
180PhosphorylationVTPKNPWSMDENLMH
CCCCCCCCCCCCCEE		20.0120068231
181SulfoxidationTPKNPWSMDENLMHI
CCCCCCCCCCCCEEE		7.0930846556
186SulfoxidationWSMDENLMHISYEAG
CCCCCCCEEEEHHHC		3.8830846556
190PhosphorylationENLMHISYEAGILEN
CCCEEEEHHHCCCCC		14.8124275569
199UbiquitinationAGILENPKNQAPPGL
HCCCCCCCCCCCCCC		73.59-
208PhosphorylationQAPPGLYTKTQDPAK
CCCCCCCCCCCCCCC		32.4325627689
209UbiquitinationAPPGLYTKTQDPAKA
CCCCCCCCCCCCCCC		30.542190698
209AcetylationAPPGLYTKTQDPAKA
CCCCCCCCCCCCCCC		30.5423954790
215UbiquitinationTKTQDPAKAPNTPDI
CCCCCCCCCCCCCCE		70.53-
219PhosphorylationDPAKAPNTPDILEIE
CCCCCCCCCCEEEEE		22.6825159151
228AcetylationDILEIEFKKGVPVKV
CEEEEEEECCCCEEE		35.5126822725
228SuccinylationDILEIEFKKGVPVKV
CEEEEEEECCCCEEE		35.5123954790
228UbiquitinationDILEIEFKKGVPVKV
CEEEEEEECCCCEEE		35.51-
234UbiquitinationFKKGVPVKVTNVKDG
EECCCCEEEEECCCC		36.95-
2342-HydroxyisobutyrylationFKKGVPVKVTNVKDG
EECCCCEEEEECCCC		36.95-
247UbiquitinationDGTTHQTSLELFMYL
CCCCEECHHHHHHHH		17.1821906983
252SulfoxidationQTSLELFMYLNEVAG
ECHHHHHHHHHHHCC		6.1030846556
260AcetylationYLNEVAGKHGVGRID
HHHHHCCCCCCCCEE		27.7026051181
260UbiquitinationYLNEVAGKHGVGRID
HHHHHCCCCCCCCEE		27.70-
272MethylationRIDIVENRFIGMKSR
CEEEECCCCCCCCCC		15.85-
278PhosphorylationNRFIGMKSRGIYETP
CCCCCCCCCCEEECC		27.1824719451
282PhosphorylationGMKSRGIYETPAGTI
CCCCCCEEECCCCEE		19.3020068231
284PhosphorylationKSRGIYETPAGTILY
CCCCEEECCCCEEEE		11.0620068231
288PhosphorylationIYETPAGTILYHAHL
EEECCCCEEEEEEEC		15.2020068231
291PhosphorylationTPAGTILYHAHLDIE
CCCCEEEEEEECCCE		7.9720068231
301PhosphorylationHLDIEAFTMDREVRK
ECCCEEHHCCHHHHH		25.8020068231
310UbiquitinationDREVRKIKQGLGLKF
CHHHHHHHHCCCCCH		41.15-
322PhosphorylationLKFAELVYTGFWHSP
CCHHHHHHCCCCCCC		17.4826356563
323PhosphorylationKFAELVYTGFWHSPE
CHHHHHHCCCCCCCH		20.5826356563
340UbiquitinationFVRHCIAKSQERVEG
HHHHHHHHCHHHCCC		32.53-
340AcetylationFVRHCIAKSQERVEG
HHHHHHHHCHHHCCC		32.5326051181
348UbiquitinationSQERVEGKVQVSVLK
CHHHCCCEEEEEEEC		18.91-
3482-HydroxyisobutyrylationSQERVEGKVQVSVLK
CHHHCCCEEEEEEEC		18.91-
352PhosphorylationVEGKVQVSVLKGQVY
CCCEEEEEEECCEEE		12.4922817900
359PhosphorylationSVLKGQVYILGRESP
EEECCEEEEECCCCC		5.2028152594
368PhosphorylationLGRESPLSLYNEELV
ECCCCCCCCCCHHHE		31.9922210691
377SulfoxidationYNEELVSMNVQGDYE
CCHHHEECCCCCCCC		4.4330846556
383PhosphorylationSMNVQGDYEPTDATG
ECCCCCCCCCCCCCC		30.5421253578
396PhosphorylationTGFININSLRLKEYH
CCCEECCCHHHHHHH		15.8622210691
402PhosphorylationNSLRLKEYHRLQSKV
CCHHHHHHHHHHHCC		7.2223898821
407PhosphorylationKEYHRLQSKVTAK--
HHHHHHHHCCCCC--		33.4123898821
408UbiquitinationEYHRLQSKVTAK---
HHHHHHHCCCCC---		30.55-
4082-HydroxyisobutyrylationEYHRLQSKVTAK---
HHHHHHHCCCCC---		30.55-
410PhosphorylationHRLQSKVTAK-----
HHHHHCCCCC-----		32.2523898821
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 ASSY_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASSY_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 ASSY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASSY_HUMANASS1physical
16189514
A4_HUMANAPPphysical
21832049
SPRE_HUMANSPRphysical
22939629
GIT2_HUMANGIT2physical
22939629
ASSY_HUMANASS1physical
21988832
JAK2_HUMANJAK2physical
21988832
MT2_HUMANMT2Aphysical
21988832
PTN1_HUMANPTPN1physical
21988832
DLDH_HUMANDLDphysical
22863883
DPP3_HUMANDPP3physical
22863883
GRP75_HUMANHSPA9physical
22863883
SIAS_HUMANNANSphysical
22863883
NHLC2_HUMANNHLRC2physical
22863883
RL23_HUMANRPL23physical
22863883
TFIP8_HUMANTNFAIP8physical
22863883
ASSY_HUMANASS1physical
25416956
ADK_HUMANADKphysical
26344197
ALDOA_HUMANALDOAphysical
26344197
GDIR1_HUMANARHGDIAphysical
26344197
IMA1_HUMANKPNA2physical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
PFKAL_HUMANPFKLphysical
26344197
PRDX2_HUMANPRDX2physical
26344197
RUVB2_HUMANRUVBL2physical
26344197
STIP1_HUMANSTIP1physical
26344197
TAGL2_HUMANTAGLN2physical
26344197
TKT_HUMANTKTphysical
26344197
THIO_HUMANTXNphysical
26344197
PYC_HUMANPCphysical
28514442
SIR3_HUMANSIRT3physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
215700Citrullinemia 1 (CTLN1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00171Adenosine triphosphate
DB00125L-Arginine
DB00128L-Aspartic Acid
DB00155L-Citrulline
Regulatory Network of ASSY_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-165, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND MASSSPECTROMETRY.

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