ASSY_MOUSE - dbPTM
ASSY_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASSY_MOUSE
UniProt AC P16460
Protein Name Argininosuccinate synthase {ECO:0000305}
Gene Name Ass1 {ECO:0000312|MGI:MGI:88090}
Organism Mus musculus (Mouse).
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 MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYEDRYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVTNIKDGTTRTTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKEYHRLQSKVTAK
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
29PhosphorylationVWLKEQGYDVIAYLA
HHHHHCCCCHHHHHH
13.5125195567
41AcetylationYLANIGQKEDFEEAR
HHHCCCCCHHHHHHH
54.7822733758
41MalonylationYLANIGQKEDFEEAR
HHHCCCCCHHHHHHH
54.7826073543
41UbiquitinationYLANIGQKEDFEEAR
HHHCCCCCHHHHHHH
54.78-
53AcetylationEARKKALKLGAKKVF
HHHHHHHHHCCCEEE
50.1323864654
53MalonylationEARKKALKLGAKKVF
HHHHHHHHHCCCEEE
50.1326320211
58UbiquitinationALKLGAKKVFIEDVS
HHHHCCCEEEEEHHC
41.67-
58AcetylationALKLGAKKVFIEDVS
HHHHCCCEEEEEHHC
41.6723576753
58GlutarylationALKLGAKKVFIEDVS
HHHHCCCEEEEEHHC
41.6724703693
58MalonylationALKLGAKKVFIEDVS
HHHHCCCEEEEEHHC
41.6726073543
79PhosphorylationFIWPAVQSSALYEDR
HHHHHHHCCCCCCCH
15.8123984901
80PhosphorylationIWPAVQSSALYEDRY
HHHHHHCCCCCCCHH
12.7623984901
83PhosphorylationAVQSSALYEDRYLLG
HHHCCCCCCCHHHHC
18.5923984901
87PhosphorylationSALYEDRYLLGTSLA
CCCCCCHHHHCCCCH
20.7125195567
91PhosphorylationEDRYLLGTSLARPCI
CCHHHHCCCCHHHHH
22.1220469934
92PhosphorylationDRYLLGTSLARPCIA
CHHHHCCCCHHHHHH
20.4523140645
97S-palmitoylationGTSLARPCIARRQVE
CCCCHHHHHHHHHHH
2.9428526873
112UbiquitinationIAQREGAKYVSHGAT
HHHHHCCEEEECCCC
57.97-
112AcetylationIAQREGAKYVSHGAT
HHHHHCCEEEECCCC
57.9723576753
112GlutarylationIAQREGAKYVSHGAT
HHHHHCCEEEECCCC
57.9724703693
112MalonylationIAQREGAKYVSHGAT
HHHHHCCEEEECCCC
57.9726073543
113PhosphorylationAQREGAKYVSHGATG
HHHHCCEEEECCCCC
13.4729899451
115PhosphorylationREGAKYVSHGATGKG
HHCCEEEECCCCCCC
17.0822324799
119PhosphorylationKYVSHGATGKGNDQV
EEEECCCCCCCCCCE
43.9822324799
121GlutarylationVSHGATGKGNDQVRF
EECCCCCCCCCCEEE
50.6224703693
121MalonylationVSHGATGKGNDQVRF
EECCCCCCCCCCEEE
50.6226073543
121UbiquitinationVSHGATGKGNDQVRF
EECCCCCCCCCCEEE
50.62-
121AcetylationVSHGATGKGNDQVRF
EECCCCCCCCCCEEE
50.6223864654
131PhosphorylationDQVRFELTCYSLAPQ
CCEEEEEEEEECCCC
11.3825195567
132S-palmitoylationQVRFELTCYSLAPQI
CEEEEEEEEECCCCE
3.2128526873
133PhosphorylationVRFELTCYSLAPQIK
EEEEEEEEECCCCEE
11.0729472430
134PhosphorylationRFELTCYSLAPQIKV
EEEEEEEECCCCEEE
21.8717242355
140UbiquitinationYSLAPQIKVIAPWRM
EECCCCEEEEECCCC
23.49-
140MalonylationYSLAPQIKVIAPWRM
EECCCCEEEEECCCC
23.4926073543
151PhosphorylationPWRMPEFYNRFKGRN
CCCCHHHHHHCCCHH
12.0817242355
155UbiquitinationPEFYNRFKGRNDLME
HHHHHHCCCHHHHHH
54.4422790023
161SulfoxidationFKGRNDLMEYAKQHG
CCCHHHHHHHHHHHC
4.0621406390
163PhosphorylationGRNDLMEYAKQHGIP
CHHHHHHHHHHHCCC
12.7228576409
165AcetylationNDLMEYAKQHGIPIP
HHHHHHHHHHCCCCC
41.7623864654
165UbiquitinationNDLMEYAKQHGIPIP
HHHHHHHHHHCCCCC
41.76-
165MalonylationNDLMEYAKQHGIPIP
HHHHHHHHHHCCCCC
41.7626320211
174PhosphorylationHGIPIPVTPKSPWSM
HCCCCCCCCCCCCCC
21.4622324799
176UbiquitinationIPIPVTPKSPWSMDE
CCCCCCCCCCCCCCC
60.84-
176AcetylationIPIPVTPKSPWSMDE
CCCCCCCCCCCCCCC
60.84-
176MalonylationIPIPVTPKSPWSMDE
CCCCCCCCCCCCCCC
60.8426320211
177PhosphorylationPIPVTPKSPWSMDEN
CCCCCCCCCCCCCCC
32.5721082442
180PhosphorylationVTPKSPWSMDENLMH
CCCCCCCCCCCCCCC
21.5326643407
189PhosphorylationDENLMHISYEAGILE
CCCCCCEEHHHCCCC
11.4023140645
190PhosphorylationENLMHISYEAGILEN
CCCCCEEHHHCCCCC
14.8123140645
199UbiquitinationAGILENPKNQAPPGL
HCCCCCCCCCCCCCC
73.59-
199MalonylationAGILENPKNQAPPGL
HCCCCCCCCCCCCCC
73.5926320211
207PhosphorylationNQAPPGLYTKTQDPA
CCCCCCCCCCCCCCC
16.4725195567
209UbiquitinationAPPGLYTKTQDPAKA
CCCCCCCCCCCCCCC
30.54-
209MalonylationAPPGLYTKTQDPAKA
CCCCCCCCCCCCCCC
30.5426320211
210PhosphorylationPPGLYTKTQDPAKAP
CCCCCCCCCCCCCCC
30.3321183079
215MalonylationTKTQDPAKAPNSPDV
CCCCCCCCCCCCCCE
70.5326320211
215UbiquitinationTKTQDPAKAPNSPDV
CCCCCCCCCCCCCCE
70.53-
215AcetylationTKTQDPAKAPNSPDV
CCCCCCCCCCCCCCE
70.5323864654
219PhosphorylationDPAKAPNSPDVLEIE
CCCCCCCCCCEEEEE
22.7825521595
228AcetylationDVLEIEFKKGVPVKV
CEEEEEEECCCCEEE
35.5123954790
228UbiquitinationDVLEIEFKKGVPVKV
CEEEEEEECCCCEEE
35.51-
228MalonylationDVLEIEFKKGVPVKV
CEEEEEEECCCCEEE
35.5126320211
229MalonylationVLEIEFKKGVPVKVT
EEEEEEECCCCEEEE
71.1525418362
229AcetylationVLEIEFKKGVPVKVT
EEEEEEECCCCEEEE
71.15156747
234MalonylationFKKGVPVKVTNIKDG
EECCCCEEEEECCCC
36.9526320211
234UbiquitinationFKKGVPVKVTNIKDG
EECCCCEEEEECCCC
36.95-
239MalonylationPVKVTNIKDGTTRTT
CEEEEECCCCCCEEE
52.7726073543
239AcetylationPVKVTNIKDGTTRTT
CEEEEECCCCCCEEE
52.7722733758
239UbiquitinationPVKVTNIKDGTTRTT
CEEEEECCCCCCEEE
52.77-
239GlutarylationPVKVTNIKDGTTRTT
CEEEEECCCCCCEEE
52.7724703693
245PhosphorylationIKDGTTRTTSLELFM
CCCCCCEEEHHHHHH
20.7429899451
246PhosphorylationKDGTTRTTSLELFMY
CCCCCEEEHHHHHHH
28.2029472430
247PhosphorylationDGTTRTTSLELFMYL
CCCCEEEHHHHHHHH
21.1629472430
260UbiquitinationYLNEVAGKHGVGRID
HHHHHCCCCCCCCEE
27.7022790023
260AcetylationYLNEVAGKHGVGRID
HHHHHCCCCCCCCEE
27.7023864654
277UbiquitinationENRFIGMKSRGIYET
CCCCCCCCCCCEEEC
31.61-
277MalonylationENRFIGMKSRGIYET
CCCCCCCCCCCEEEC
31.6126320211
278PhosphorylationNRFIGMKSRGIYETP
CCCCCCCCCCEEECC
27.18-
310SuccinylationDREVRKIKQGLGLKF
CHHHHHHHHCCCCCH
41.1523954790
310UbiquitinationDREVRKIKQGLGLKF
CHHHHHHHHCCCCCH
41.15-
322PhosphorylationLKFAELVYTGFWHSP
CCHHHHHHCCCCCCH
17.4823984901
323PhosphorylationKFAELVYTGFWHSPE
CHHHHHHCCCCCCHH
20.5823984901
331S-palmitoylationGFWHSPECEFVRHCI
CCCCCHHHHHHHHHH
5.8128526873
340UbiquitinationFVRHCIQKSQERVEG
HHHHHHHHHHHHHCC
33.91-
340AcetylationFVRHCIQKSQERVEG
HHHHHHHHHHHHHCC
33.9123864654
340MalonylationFVRHCIQKSQERVEG
HHHHHHHHHHHHHCC
33.9126320211
348SuccinylationSQERVEGKVQVSVFK
HHHHHCCCEEEEEEC
18.9123954790
348MalonylationSQERVEGKVQVSVFK
HHHHHCCCEEEEEEC
18.9126320211
352PhosphorylationVEGKVQVSVFKGQVY
HCCCEEEEEECCEEE
12.5422006019
355SuccinylationKVQVSVFKGQVYILG
CEEEEEECCEEEEEC
46.4023954790
355AcetylationKVQVSVFKGQVYILG
CEEEEEECCEEEEEC
46.4023864654
383PhosphorylationSMNVQGDYEPIDATG
ECCCCCCCCCCCCCC
30.35-
402PhosphorylationNSLRLKEYHRLQSKV
CCCCHHHHHHHHHCC
7.2229514104
408MalonylationEYHRLQSKVTAK---
HHHHHHHCCCCC---
30.5526320211
408UbiquitinationEYHRLQSKVTAK---
HHHHHHHCCCCC---
30.55-

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
219SPhosphorylationKinaseMAPK14P47811
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASSY_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ASSY_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASSY_MOUSE

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Related Literatures of Post-Translational Modification

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