ARL1_HUMAN - dbPTM
ARL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARL1_HUMAN
UniProt AC P40616
Protein Name ADP-ribosylation factor-like protein 1
Gene Name ARL1
Organism Homo sapiens (Human).
Sequence Length 181
Subcellular Localization Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side . Membrane
Lipid-anchor .
Protein Description GTP-binding protein that has very low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Can activate phospholipase D with very low efficiency. Important for normal function of the Golgi apparatus..
Protein Sequence MGGFFSSIFSSLFGTREMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAVIYVVDSCDRDRIGISKSELVAMLEEEELRKAILVVFANKQDMEQAMTSSEMANSLGLPALKDRKWQIFKTSATKGTGLDEAMEWLVETLKSRQ
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
2Myristoylation------MGGFFSSIF
------CCCHHHHHH
41.4325255805
6Phosphorylation--MGGFFSSIFSSLF
--CCCHHHHHHHHHH
21.9124043423
7Phosphorylation-MGGFFSSIFSSLFG
-CCCHHHHHHHHHHC
23.6124043423
10PhosphorylationGFFSSIFSSLFGTRE
CHHHHHHHHHHCCCC
25.1824043423
11PhosphorylationFFSSIFSSLFGTREM
HHHHHHHHHHCCCCE
19.5724043423
15PhosphorylationIFSSLFGTREMRILI
HHHHHHCCCCEEEEE
19.0024043423
44PhosphorylationLQVGEVVTTIPTIGF
EECCCEEEECCCCCE
24.96-
45O-linked_GlycosylationQVGEVVTTIPTIGFN
ECCCEEEECCCCCEE
17.22OGP
45UbiquitinationQVGEVVTTIPTIGFN
ECCCEEEECCCCCEE
17.22-
48O-linked_GlycosylationEVVTTIPTIGFNVET
CEEEECCCCCEEEEE
29.86OGP
58PhosphorylationFNVETVTYKNLKFQV
EEEEEEEEECCEEEE
8.11-
59UbiquitinationNVETVTYKNLKFQVW
EEEEEEEECCEEEEE
46.57-
62UbiquitinationTVTYKNLKFQVWDLG
EEEEECCEEEEEECC
43.0521890473
62UbiquitinationTVTYKNLKFQVWDLG
EEEEECCEEEEEECC
43.0521890473
62UbiquitinationTVTYKNLKFQVWDLG
EEEEECCEEEEEECC
43.0521890473
72PhosphorylationVWDLGGQTSIRPYWR
EEECCCCCCCCCEEE
29.4227251275
73PhosphorylationWDLGGQTSIRPYWRC
EECCCCCCCCCEEEE
14.5427251275
87UbiquitinationCYYSNTDAVIYVVDS
EEECCCCEEEEEEEC
6.38-
104UbiquitinationRDRIGISKSELVAML
CCCCCCCHHHHHHHH
46.1321890473
110SulfoxidationSKSELVAMLEEEELR
CHHHHHHHHCHHHHH
3.6430846556
135UbiquitinationQDMEQAMTSSEMANS
HHHHHHHCHHHHHHH
31.92-
140UbiquitinationAMTSSEMANSLGLPA
HHCHHHHHHHCCCHH
9.82-
145UbiquitinationEMANSLGLPALKDRK
HHHHHCCCHHHCCCC
2.45-
149UbiquitinationSLGLPALKDRKWQIF
HCCCHHHCCCCEEEE
58.56-
152UbiquitinationLPALKDRKWQIFKTS
CHHHCCCCEEEEECC
54.29-
157UbiquitinationDRKWQIFKTSATKGT
CCCEEEEECCCCCCC
43.1021890473
157AcetylationDRKWQIFKTSATKGT
CCCEEEEECCCCCCC
43.1025953088
157UbiquitinationDRKWQIFKTSATKGT
CCCEEEEECCCCCCC
43.1021890473
157UbiquitinationDRKWQIFKTSATKGT
CCCEEEEECCCCCCC
43.1021890473
162UbiquitinationIFKTSATKGTGLDEA
EEECCCCCCCCHHHH
54.94-
178UbiquitinationEWLVETLKSRQ----
HHHHHHHHHCC----
51.52-

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 ARL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARL1_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 ARL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOGA1_HUMANGOLGA1physical
12972563
GCC1_HUMANGCC1physical
12972563
GCC2_HUMANGCC2physical
12972563
ARFP2_HUMANARFIP2physical
12972563
GOGA4_HUMANGOLGA4physical
12972563
ARFP2_HUMANARFIP2physical
11792819

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARL1_HUMAN

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Related Literatures of Post-Translational Modification

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