ARLY_HUMAN - dbPTM
ARLY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARLY_HUMAN
UniProt AC P04424
Protein Name Argininosuccinate lyase
Gene Name ASL
Organism Homo sapiens (Human).
Sequence Length 464
Subcellular Localization
Protein Description
Protein Sequence MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA
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------MASESGKLW
------CCCCCCCCC
23.23-
3Phosphorylation-----MASESGKLWG
-----CCCCCCCCCC
30.8828857561
5Phosphorylation---MASESGKLWGGR
---CCCCCCCCCCCC
38.4424719451
7Acetylation-MASESGKLWGGRFV
-CCCCCCCCCCCCCC
50.8025953088
7Ubiquitination-MASESGKLWGGRFV
-CCCCCCCCCCCCCC
50.80-
23UbiquitinationAVDPIMEKFNASIAY
CCHHHHHHHCHHHCC
26.9121906983
43UbiquitinationEVDVQGSKAYSRGLE
EEECCCCHHHHCHHH
59.1621906983
51UbiquitinationAYSRGLEKAGLLTKA
HHHCHHHHCCCCCHH
53.4421906983
57UbiquitinationEKAGLLTKAEMDQIL
HHCCCCCHHHHHHHH
42.1721906983
69AcetylationQILHGLDKVAEEWAQ
HHHHHHHHHHHHHHH
48.6820167786
80UbiquitinationEWAQGTFKLNSNDED
HHHHCCEECCCCCCC
46.7421906983
83PhosphorylationQGTFKLNSNDEDIHT
HCCEECCCCCCCHHH
56.9723312004
90PhosphorylationSNDEDIHTANERRLK
CCCCCHHHHHHHHHH
31.3524275569
97MalonylationTANERRLKELIGATA
HHHHHHHHHHHHCCC
48.9726320211
97UbiquitinationTANERRLKELIGATA
HHHHHHHHHHHHCCC
48.9721906983
103PhosphorylationLKELIGATAGKLHTG
HHHHHHCCCCCCCCC
30.6322210691
106UbiquitinationLIGATAGKLHTGRSR
HHHCCCCCCCCCCCC
34.3321906983
106MethylationLIGATAGKLHTGRSR
HHHCCCCCCCCCCCC
34.33-
142PhosphorylationLLWELIRTMVDRAEA
HHHHHHHHHHHHHHH
17.9824043423
287UbiquitinationGSSLMPQKKNPDSLE
CCCCCCCCCCCCHHH
48.9621906983
288AcetylationSSLMPQKKNPDSLEL
CCCCCCCCCCCHHHH
69.3520167786
288UbiquitinationSSLMPQKKNPDSLEL
CCCCCCCCCCCHHHH
69.3520167786
323UbiquitinationGLPSTYNKDLQEDKE
CCCCCCCCCHHHCHH
49.7721906983
376PhosphorylationLATDLAYYLVRKGMP
HHHHHHHHHHHCCCC
7.97-
397SulfoxidationASGKAVFMAETKGVA
HCCCEEEEEECHHHH
2.3730846556
446PhosphorylationALGGTARSSVDWQIR
CCCCCCHHCHHHHHH
32.0524275569

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 ARLY_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
288KAcetylation

20167786

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 ARLY_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYQ_HUMANQARSphysical
16189514
ARLY_HUMANASLphysical
9256435
F16P1_HUMANFBP1physical
21988832
HMOX1_HUMANHMOX1physical
21988832
ARLY_HUMANASLphysical
21988832
CSK22_HUMANCSNK2A2physical
21988832
OVGP1_HUMANOVGP1physical
21988832
EFTU_HUMANTUFMphysical
22863883
ARLY_HUMANASLphysical
25416956
NTAQ1_HUMANWDYHV1physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
207900Argininosuccinic aciduria (ARGINSA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00125L-Arginine
Regulatory Network of ARLY_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Regulation of cellular metabolism by protein lysine acetylation.";
Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L.,Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L.,Chin J., Yang P., Chen X., Lei Q., Xiong Y., Guan K.L.;
Science 327:1000-1004(2010).
Cited for: ACETYLATION AT LYS-69 AND LYS-288, ENZYME REGULATION, MASSSPECTROMETRY, AND MUTAGENESIS OF LYS-288.

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