Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Argininosuccinate synthase  

UniProtKB / Swiss-Prot ID :  ASSY_HUMAN

Gene Name (Synonyms) : 
ASS1, ASS  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSREFVE...
Predicted Secondary Structure CCCCCEEEEEECCCHHHHHHHHHHHHCCCCEEEEEEECCCCCCHHHHHHHHHHCCCCCEEEHHHHHHHHH...
Protein Variant
LocationDescription
14G -> S (in CTLN1). VAR_000681
18S -> L (in CTLN1). VAR_000682
19C -> R (in CTLN1). VAR_015891
40Q -> L (in CTLN1). VAR_058337
65S -> I (in dbSNP:rs2229556). VAR_050427
69V -> A (in CTLN1). VAR_016013
79S -> P (in CTLN1). VAR_058338
86R -> C (in CTLN1). VAR_000683
86R -> H (in CTLN1). VAR_015892
95R -> S (in CTLN1). VAR_015893
96P -> H (in CTLN1). VAR_058339
96P -> S (in CTLN1). VAR_015894
108R -> L (in CTLN1; dbSNP:rs35269064). VAR_016014
117G -> D (in CTLN1). VAR_015896
117G -> S (in CTLN1). VAR_015895
118A -> T (in CTLN1). VAR_000684
119T -> I (in CTLN1). VAR_016015
124D -> N (in CTLN1). VAR_058340
127R -> Q (in CTLN1). VAR_058341
127R -> W (in CTLN1; severe clinicalcourse).
157R -> C (in CTLN1). VAR_015897
157R -> H (in CTLN1). VAR_000685
160L -> P (in CTLN1). VAR_058343
179W -> R (in CTLN1; mild). VAR_015898
180S -> N (in CTLN1). VAR_000686
190Y -> D (in CTLN1). VAR_058344
191E -> K (in CTLN1). VAR_015899
191E -> Q (in CTLN1). VAR_058345
192A -> V (in CTLN1). VAR_000687
202A -> E (in CTLN1). VAR_058346
206L -> P (in CTLN1). VAR_058347
263V -> M (in CTLN1; mild clinical course). VAR_058348
265R -> C (in CTLN1; severe clinicalcourse).
265R -> H (in CTLN1). VAR_015900
269V -> M (in CTLN1). VAR_015901
270E -> Q (in CTLN1). VAR_016007
272R -> C (in CTLN1). VAR_000688
277K -> T (in CTLN1). VAR_058350
279R -> Q (in CTLN1). VAR_016008
280G -> R (in CTLN1). VAR_000689
283E -> K (in CTLN1). VAR_015902
284T -> I (in CTLN1; mild clinical course). VAR_058351
291Y -> S (in CTLN1). VAR_058352
296D -> G (in CTLN1). VAR_058353
302M -> V (in CTLN1). VAR_058354
304R -> W (in CTLN1). VAR_000690
307R -> C (in CTLN1). VAR_058355
310K -> Q (in CTLN1). VAR_016009
310K -> R (in CTLN1). VAR_015903
324G -> S (in CTLN1). VAR_000691
324G -> V (in CTLN1). VAR_058356
341S -> F (in CTLN1). VAR_058357
345V -> G (in CTLN1). VAR_058358
347G -> R (in CTLN1; severe clinicalcourse).
359Y -> D (in CTLN1; mild clinical course). VAR_058360
362G -> V (in CTLN1; mild). VAR_015904
363R -> G (in CTLN1). VAR_016010
363R -> L (in CTLN1). VAR_000692
363R -> Q (in CTLN1). VAR_016011
363R -> W (in CTLN1). VAR_000693
389T -> I (in CTLN1). VAR_016012
390G -> R (in CTLN1). VAR_000694
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
83PhosphotyrosineSSALYEDRY
CCCEECCCC
18.59Phosphositeplus
Link
87PhosphotyrosineYEDRYLLGT
ECCCCCCCC
20.71HPRD
Link
87PhosphotyrosineYEDRYLLGT
ECCCCCCCC
20.71Phosphositeplus
Link
91PhosphothreonineYLLGTSLAR
CCCCCHHHH
22.12HPRD
Link
92PhosphoserineLLGTSLARP
CCCCHHHHH
20.45HPRD
Link
132S-nitrosocysteineFELSCYSLA
HHHHHHHHC
4.12dbSNO
Link
132S-nitrosocysteineFELSCYSLA
HHHHHHHHC
4.12HPRD
Link
133PhosphotyrosineELSCYSLAP
HHHHHHHCC
11.89Phosphositeplus
Link
165N6-acetyllysineMEYAKQHGI
HHHHHHCCC
41.76HPRD
Link
165N6-acetyllysineMEYAKQHGI
HHHHHHCCC
41.76Phosphositeplus
Link
165N6-acetyllysine.MEYAKQHGI
HHHHHHCCC
41.76UniProtKB
Link
174PhosphothreoninePIPVTPKNP
CCCCCCCCC
24.16HPRD
Link
174PhosphothreoninePIPVTPKNP
CCCCCCCCC
24.16Phosphositeplus
Link
180PhosphoserineKNPWSMDEN
CCCCCCCHH
20.01HPRD
Link
180PhosphoserineKNPWSMDEN
CCCCCCCHH
20.01Phosphositeplus
Link
209Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLYTKTQDP
HHEEEECCH
30.54Phosphositeplus
Link
219PhosphothreonineKAPNTPDIL
HCCCCCEEE
22.68HPRD
Link
219PhosphothreonineKAPNTPDIL
HCCCCCEEE
22.68Phosphositeplus
Link
282PhosphotyrosineSRGIYETPA
ECCCCCCHH
19.30HPRD
Link
322PhosphotyrosineAELVYTGFW
HHHHHCCCC
17.48Phosphositeplus
Link
352PhosphoserineKVQVSVLKG
EEEEEEECC
12.49Phosphositeplus
Link
352Phosphoserine.KVQVSVLKG
EEEEEEECC
12.49UniProtKB
Link
383PhosphotyrosineVQGDYEPTD
CCCCCCHHH
30.54Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-3319181MINT15161933
ASSY_HUMANphysical interactionEBI-758662
intact16189514
CDR2_HUMANphysical interactionEBI-1183372
intact11988016
ASSY_HUMANyeast 2-hybridHPRD:04590HPRD16189514
ASCC2_HUMANyeast 2-hybridHPRD:04590HPRD16169070
ELN_HUMANin vivoHPRD:04590HPRD1372742
ARAF_HUMANyeast 2-hybridHPRD:04590HPRD12620389
AKTIP_HUMANyeast 2-hybridHPRD:04590HPRD16169070
OTC_HUMANENSP00000253004STRING
AATM_HUMANENSP00000253004STRING
AATM_HUMANENSP00000253004STRING
ACY3_HUMANENSP00000253004STRING
DCE2_HUMANENSP00000253004STRING
ACY2_HUMANENSP00000253004STRING
SYDC_HUMANENSP00000253004STRING
PYR1_HUMANENSP00000253004STRING
CMC2_HUMANENSP00000253004STRING
NOS3_HUMANENSP00000253004STRING
NOS2A_HUMANENSP00000253004STRING
DCE1_HUMANENSP00000253004STRING
ARLY_HUMANENSP00000253004STRING
SYDM_HUMANENSP00000253004STRING
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Disease Reference
Kegg disease
OMIM disease
215700Citrullinemia 1 (CTLN1)
Drug Reference
DrugBank
DB00171Adenosine triphosphate
DB00125L-Arginine
DB00128L-Aspartic Acid
DB00155L-Citrulline
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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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures