ARP5L_HUMAN - dbPTM
ARP5L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARP5L_HUMAN
UniProt AC Q9BPX5
Protein Name Actin-related protein 2/3 complex subunit 5-like protein
Gene Name ARPC5L
Organism Homo sapiens (Human).
Sequence Length 153
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks..
Protein Sequence MARNTLSSRFRRVDIDEFDENKFVDEQEEAAAAAAEPGPDPSEVDGLLRQGDMLRAFHAALRNSPVNTKNQAVKERAQGVVLKVLTNFKSSEIEQAVQSLDRNGVDLLMKYIYKGFEKPTENSSAVLLQWHEKALAVGGLGSIIRVLTARKTV
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
3Methylation-----MARNTLSSRF
-----CCCCHHHHHH
35.05-
5Phosphorylation---MARNTLSSRFRR
---CCCCHHHHHHHC
23.5929414761
7Phosphorylation-MARNTLSSRFRRVD
-CCCCHHHHHHHCCC
19.8925056879
7O-linked_Glycosylation-MARNTLSSRFRRVD
-CCCCHHHHHHHCCC
19.8930379171
22UbiquitinationIDEFDENKFVDEQEE
HHHCCCCCCCCHHHH
44.7221906983
64PhosphorylationFHAALRNSPVNTKNQ
HHHHHHCCCCCCCCH
24.6425159151
68PhosphorylationLRNSPVNTKNQAVKE
HHCCCCCCCCHHHHH
31.4423927012
69UbiquitinationRNSPVNTKNQAVKER
HCCCCCCCCHHHHHH
41.6921906983
83UbiquitinationRAQGVVLKVLTNFKS
HHHHHHHHHHHHCCH
24.48-
86PhosphorylationGVVLKVLTNFKSSEI
HHHHHHHHHCCHHHH
41.4127251275
89UbiquitinationLKVLTNFKSSEIEQA
HHHHHHCCHHHHHHH
55.9621906983
90PhosphorylationKVLTNFKSSEIEQAV
HHHHHCCHHHHHHHH
29.1225307156
91PhosphorylationVLTNFKSSEIEQAVQ
HHHHCCHHHHHHHHH
43.0921406692
99PhosphorylationEIEQAVQSLDRNGVD
HHHHHHHHCHHCCHH
26.1621406692
110UbiquitinationNGVDLLMKYIYKGFE
CCHHHHHHHHHHCCC
28.5921906983
114UbiquitinationLLMKYIYKGFEKPTE
HHHHHHHHCCCCCCC
47.79-
118AcetylationYIYKGFEKPTENSSA
HHHHCCCCCCCCCCC
55.7826051181
118UbiquitinationYIYKGFEKPTENSSA
HHHHCCCCCCCCCCC
55.78-
142PhosphorylationLAVGGLGSIIRVLTA
HHHCCHHHHHHHHHH
21.6421712546
148PhosphorylationGSIIRVLTARKTV--
HHHHHHHHHCCCC--
22.8924719451

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 ARP5L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARP5L_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 ARP5L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARPC4_HUMANARPC4physical
16169070
ARPC4_HUMANARPC4physical
22939629
ARPC2_HUMANARPC2physical
22939629
ARPC3_HUMANARPC3physical
22939629
GA45G_HUMANGADD45Gphysical
21988832
ARPC2_HUMANARPC2physical
22863883
ARPC3_HUMANARPC3physical
22863883
ARPC4_HUMANARPC4physical
22863883
ARPC5_HUMANARPC5physical
22863883
KAPCA_HUMANPRKACAphysical
22863883
TM10A_HUMANTRMT10Aphysical
22863883
SH3G1_HUMANSH3GL1physical
22863883
ARP3_HUMANACTR3physical
26344197
ARC1A_HUMANARPC1Aphysical
26344197
ARPC2_HUMANARPC2physical
26344197
ARPC4_HUMANARPC4physical
26344197
CAPZB_HUMANCAPZBphysical
26344197

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 ARP5L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASSSPECTROMETRY.

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