ARGI1_HUMAN - dbPTM
ARGI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARGI1_HUMAN
UniProt AC P05089
Protein Name Arginase-1
Gene Name ARG1
Organism Homo sapiens (Human).
Sequence Length 322
Subcellular Localization Cytoplasm . Cytoplasmic granule . Localized in azurophil granules of neutrophils (PubMed:15546957).
Protein Description Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.; Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion. [PubMed: 15546957]
Protein Sequence MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK
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
7Phosphorylation-MSAKSRTIGIIGAP
-CCCCCCEEEEECCC
30.5521406692
16 (in isoform 2)Phosphorylation-34.5121406692
16PhosphorylationGIIGAPFSKGQPRGG
EEECCCCCCCCCCCC
34.5121406692
17SuccinylationIIGAPFSKGQPRGGV
EECCCCCCCCCCCCC
63.04-
17SuccinylationIIGAPFSKGQPRGGV
EECCCCCCCCCCCCC
63.04-
29PhosphorylationGGVEEGPTVLRKAGL
CCCCCCHHHHHHHCH
42.92-
332-HydroxyisobutyrylationEGPTVLRKAGLLEKL
CCHHHHHHHCHHHHH
42.52-
33UbiquitinationEGPTVLRKAGLLEKL
CCHHHHHHHCHHHHH
42.5229967540
33MalonylationEGPTVLRKAGLLEKL
CCHHHHHHHCHHHHH
42.5226320211
50PhosphorylationQECDVKDYGDLPFAD
CCCCCCCCCCCCCCC
13.5628192239
62PhosphorylationFADIPNDSPFQIVKN
CCCCCCCCCCEEECC
33.9628192239
72PhosphorylationQIVKNPRSVGKASEQ
EEECCHHHHHHHHHH
36.16-
75SuccinylationKNPRSVGKASEQLAG
CCHHHHHHHHHHHCC
46.73-
75SuccinylationKNPRSVGKASEQLAG
CCHHHHHHHHHHHCC
46.73-
94PhosphorylationVKKNGRISLVLGGDH
EEECCEEEEEECCCC
15.86-
102PhosphorylationLVLGGDHSLAIGSIS
EEECCCCEEEEEEEC
25.00-
107PhosphorylationDHSLAIGSISGHARV
CCEEEEEEECCCCEE
13.89-
109PhosphorylationSLAIGSISGHARVHP
EEEEEEECCCCEECC
26.65-
163PhosphorylationIPDVPGFSWVTPCIS
CCCCCCCCCCCCCCC
26.9320166139
166PhosphorylationVPGFSWVTPCISAKD
CCCCCCCCCCCCHHH
13.2420166139
168S-nitrosocysteineGFSWVTPCISAKDIV
CCCCCCCCCCHHHEE
2.54-
168S-nitrosylationGFSWVTPCISAKDIV
CCCCCCCCCCHHHEE
2.5422178444
170PhosphorylationSWVTPCISAKDIVYI
CCCCCCCCHHHEEEE
35.6626270265
176PhosphorylationISAKDIVYIGLRDVD
CCHHHEEEEEECCCC
6.9326270265
191AcetylationPGEHYILKTLGIKYF
CCCCEEEEECCCCEE
31.9520167786
217PhosphorylationKVMEETLSYLLGRKK
HHHHHHHHHHHCCCC
22.581598908
265PhosphorylationLYITEEIYKTGLLSG
EEEEHHHHHCCCCCC
13.04-
267PhosphorylationITEEIYKTGLLSGLD
EEHHHHHCCCCCCCC
18.9821406692
271PhosphorylationIYKTGLLSGLDIMEV
HHHCCCCCCCCEEEC
42.2121406692
281PhosphorylationDIMEVNPSLGKTPEE
CEEECCCHHCCCHHH
44.5422210691
303S-nitrosocysteineAVAITLACFGLAREG
HHHHHHHHHHHHHCC
2.90-
303S-nitrosylationAVAITLACFGLAREG
HHHHHHHHHHHHHCC
2.9022178444

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 ARGI1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARGI1_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 ARGI1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARGI2_HUMANARG2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
207800Argininemia (ARGIN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00129L-Ornithine
Regulatory Network of ARGI1_HUMAN

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Related Literatures of Post-Translational Modification

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