ARPC4_HUMAN - dbPTM
ARPC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARPC4_HUMAN
UniProt AC P59998
Protein Name Actin-related protein 2/3 complex subunit 4
Gene Name ARPC4
Organism Homo sapiens (Human).
Sequence Length 168
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection .
Protein Description Functions as actin-binding 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. Seems to contact the mother actin filament..
Protein Sequence MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEKVLIEGSINSVRVSIAVKQADEIEKILCHKFMRFMMMRAENFFILRRKPVEGYDISFLITNFHTEQMYKHKLVDFVIHFMEEIDKEISEMKLSVNARARIVAEEFLKNF
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
2Phosphorylation------MTATLRPYL
------CCCCHHHHH		28.4829255136
2Acetylation------MTATLRPYL
------CCCCHHHHH		28.4819413330
4Phosphorylation----MTATLRPYLSA
----CCCCHHHHHHH		17.7129255136
8PhosphorylationMTATLRPYLSAVRAT
CCCCHHHHHHHHHHH		13.5724117733
10 (in isoform 2)Phosphorylation-20.9024719451
10PhosphorylationATLRPYLSAVRATLQ
CCHHHHHHHHHHHHH		20.9024117733
35AcetylationQVVERHNKPEVEVRS
HHHHHCCCCCEEECC		36.1119608861
35UbiquitinationQVVERHNKPEVEVRS
HHHHHCCCCCEEECC		36.1119608861
42PhosphorylationKPEVEVRSSKELLLQ
CCCEEECCCHHEEEE		51.4423663014
43PhosphorylationPEVEVRSSKELLLQP
CCEEECCCHHEEEEE		21.4223663014
43 (in isoform 2)Phosphorylation-21.4224719451
44UbiquitinationEVEVRSSKELLLQPV
CEEECCCHHEEEEEE		54.3423000965
44AcetylationEVEVRSSKELLLQPV
CEEECCCHHEEEEEE		54.3426051181
52PhosphorylationELLLQPVTISRNEKE
HEEEEEEEECCCCCC		21.6623312004
54AcetylationLLQPVTISRNEKEKV
EEEEEEECCCCCCEE		21.4919608861
54UbiquitinationLLQPVTISRNEKEKV
EEEEEEECCCCCCEE		21.4929967540
54PhosphorylationLLQPVTISRNEKEKV
EEEEEEECCCCCCEE		21.4921712546
63UbiquitinationNEKEKVLIEGSINSV
CCCCEEEEEECCCEE		6.7123000965
63UbiquitinationNEKEKVLIEGSINSV
CCCCEEEEEECCCEE		6.7121890473
76UbiquitinationSVRVSIAVKQADEIE
EEEEEEEEECHHHHH		4.5021963094
77AcetylationVRVSIAVKQADEIEK
EEEEEEEECHHHHHH		30.6526051181
84AcetylationKQADEIEKILCHKFM
ECHHHHHHHHHHHHH		46.7926822725
84UbiquitinationKQADEIEKILCHKFM
ECHHHHHHHHHHHHH		46.7929967540
89UbiquitinationIEKILCHKFMRFMMM
HHHHHHHHHHHHHHH		39.6019608861
89AcetylationIEKILCHKFMRFMMM
HHHHHHHHHHHHHHH		39.6025825284
103UbiquitinationMRAENFFILRRKPVE
HHHHCEEEEECCCCC		2.2729967540
108AcetylationFFILRRKPVEGYDIS
EEEEECCCCCCCCEE		27.8119608861
126SulfoxidationTNFHTEQMYKHKLVD
ECCCHHHHHHHHHHH		3.8130846556
139SulfoxidationVDFVIHFMEEIDKEI
HHHHHHHHHHHHHHH		2.5330846556
149SulfoxidationIDKEISEMKLSVNAR
HHHHHHHCCCCHHHH		4.1730846556
166UbiquitinationIVAEEFLKNF-----
HHHHHHHHCC-----		62.7221963094
166AcetylationIVAEEFLKNF-----
HHHHHHHHCC-----		62.7226822725
185Ubiquitination------------------------
------------------------		21963094
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 ARPC4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARPC4_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 ARPC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARPC5_HUMANARPC5physical
22939629
ARC1B_HUMANARPC1Bphysical
22863883
ARPC3_HUMANARPC3physical
22863883
ARPC5_HUMANARPC5physical
22863883
FUBP1_HUMANFUBP1physical
22863883
GRPE1_HUMANGRPEL1physical
22863883
NIF3L_HUMANNIF3L1physical
22863883
PP2AA_HUMANPPP2CAphysical
22863883
KAPCB_HUMANPRKACBphysical
22863883
RFA1_HUMANRPA1physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
TM1L1_HUMANTOM1L1physical
22863883
PFD3_HUMANVBP1physical
22863883
ZPR1_HUMANZPR1physical
22863883
PNMA5_HUMANPNMA5physical
25416956
ARP3_HUMANACTR3physical
26344197
ARC1A_HUMANARPC1Aphysical
26344197
ARC1B_HUMANARPC1Bphysical
26344197
ARPC2_HUMANARPC2physical
26344197
ARPC3_HUMANARPC3physical
26344197
EIF3K_HUMANEIF3Kphysical
27173435
UBE2N_HUMANUBE2Nphysical
27173435
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 ARPC4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-13, AND ACETYLATION AT THR-2.
"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-35 AND LYS-89, AND MASSSPECTROMETRY.

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