dbPTM

ARPC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARPC3_HUMAN
UniProt AC	O15145
Protein Name	Actin-related protein 2/3 complex subunit 3
Gene Name	ARPC3
Organism	Homo sapiens (Human).
Sequence Length	178
Subcellular Localization	Cytoplasm, cytoskeleton. Cell projection.
Protein Description	Functions 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	MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKPANKQEDEVMRAYLQQLRQETGLRLCEKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPAYHSSLMDP ----CCCCCCCCCCC	9.07	21406692
6	Phosphorylation	--MPAYHSSLMDPDT --CCCCCCCCCCCCC	16.70	21406692
7	Phosphorylation	-MPAYHSSLMDPDTK -CCCCCCCCCCCCCC	17.88	21406692
13	Phosphorylation	SSLMDPDTKLIGNMA CCCCCCCCCEECCEE	32.89	20068231
14	Ubiquitination	SLMDPDTKLIGNMAL CCCCCCCCEECCEEC	45.55	21906983
14	Sumoylation	SLMDPDTKLIGNMAL CCCCCCCCEECCEEC	45.55	28112733
29	Methylation	LPIRSQFKGPAPRET EECHHCCCCCCCCCC	57.24	-
29	Ubiquitination	LPIRSQFKGPAPRET EECHHCCCCCCCCCC	57.24	21906983
29	Acetylation	LPIRSQFKGPAPRET EECHHCCCCCCCCCC	57.24	25953088
37	Acetylation	GPAPRETKDTDIVDE CCCCCCCCCCCHHHH	54.61	20167786
37	Ubiquitination	GPAPRETKDTDIVDE CCCCCCCCCCCHHHH	54.61	21906983
47	Phosphorylation	DIVDEAIYYFKANVF CHHHHHHHHHHHCEE	15.19	22115753
48	Phosphorylation	IVDEAIYYFKANVFF HHHHHHHHHHHCEEE	7.78	28450419
50	Ubiquitination	DEAIYYFKANVFFKN HHHHHHHHHCEEEEC	23.95	23000965
50	Acetylation	DEAIYYFKANVFFKN HHHHHHHHHCEEEEC	23.95	20167786
56	Ubiquitination	FKANVFFKNYEIKNE HHHCEEEECCEECCH	47.34	23000965
56	Acetylation	FKANVFFKNYEIKNE HHHCEEEECCEECCH	47.34	19608861
56	2-Hydroxyisobutyrylation	FKANVFFKNYEIKNE HHHCEEEECCEECCH	47.34	-
61	Acetylation	FFKNYEIKNEADRTL EEECCEECCHHHHHH	36.47	19608861
61	Malonylation	FFKNYEIKNEADRTL EEECCEECCHHHHHH	36.47	26320211
61	Ubiquitination	FFKNYEIKNEADRTL EEECCEECCHHHHHH	36.47	23000965
81	Ubiquitination	YISECLKKLQKCNSK HHHHHHHHHHHCCCC	43.11	29967540
88	Ubiquitination	KLQKCNSKSQGEKEM HHHHCCCCCCCCCEE	32.57	23503661
93	Ubiquitination	NSKSQGEKEMYTLGI CCCCCCCCEEEEEEE	55.39	33845483
123	Ubiquitination	IYAKPANKQEDEVMR EEEECCCHHHHHHHH	58.11	33845483
132	Phosphorylation	EDEVMRAYLQQLRQE HHHHHHHHHHHHHHH	8.48	28152594
146	Ubiquitination	ETGLRLCEKVFDPQN HHCCHHHHHHCCCCC	57.77	21963094
147	Ubiquitination	TGLRLCEKVFDPQND HCCHHHHHHCCCCCC	47.40	21963094
147	Acetylation	TGLRLCEKVFDPQND HCCHHHHHHCCCCCC	47.40	26822725
154	Ubiquitination	KVFDPQNDKPSKWWT HHCCCCCCCCCHHEE	60.02	32015554
155	2-Hydroxyisobutyrylation	VFDPQNDKPSKWWTC HCCCCCCCCCHHEEE	59.76	-
155	Ubiquitination	VFDPQNDKPSKWWTC HCCCCCCCCCHHEEE	59.76	32015554
155	Acetylation	VFDPQNDKPSKWWTC HCCCCCCCCCHHEEE	59.76	23749302
157	Ubiquitination	DPQNDKPSKWWTCFV CCCCCCCCHHEEEEH	46.80	21963094
158	Acetylation	PQNDKPSKWWTCFVK CCCCCCCHHEEEEHH	56.10	25953088
158	Ubiquitination	PQNDKPSKWWTCFVK CCCCCCCHHEEEEHH	56.10	21963094
164	Ubiquitination	SKWWTCFVKRQFMNK CHHEEEEHHHHHHCH	5.63	23000965
165	Ubiquitination	KWWTCFVKRQFMNKS HHEEEEHHHHHHCHH	21.89	23000965
165	Acetylation	KWWTCFVKRQFMNKS HHEEEEHHHHHHCHH	21.89	26051181
170	Ubiquitination	FVKRQFMNKSLSGPG EHHHHHHCHHCCCCC	31.86	23000965
171	Ubiquitination	VKRQFMNKSLSGPGQ HHHHHHCHHCCCCCC	40.77	23000965
171	Acetylation	VKRQFMNKSLSGPGQ HHHHHHCHHCCCCCC	40.77	25953088
172	Phosphorylation	KRQFMNKSLSGPGQ- HHHHHCHHCCCCCC-	23.82	28102081
174	Phosphorylation	QFMNKSLSGPGQ--- HHHCHHCCCCCC---	50.46	24719451

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
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:17142834

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARPC3_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 ARPC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARAP1_HUMAN	ARAP1	physical	16169070
ANM1_HUMAN	PRMT1	physical	16169070
CDN2B_HUMAN	CDKN2B	physical	16169070
BAG6_HUMAN	BAG6	physical	16169070
RS4X_HUMAN	RPS4X	physical	9889097
WASP_HUMAN	WAS	physical	9889097
ARPC4_HUMAN	ARPC4	physical	11162547
ARPC4_HUMAN	ARPC4	physical	22939629
ARPC5_HUMAN	ARPC5	physical	22939629
EZRI_HUMAN	EZR	physical	22939629
WASP_HUMAN	WAS	physical	23148219
ARPC2_HUMAN	ARPC2	physical	23148219
ARPC4_HUMAN	ARPC4	physical	23148219
ARPC5_HUMAN	ARPC5	physical	23148219
ARPC5_HUMAN	ARPC5	physical	22863883
KAPCA_HUMAN	PRKACA	physical	22863883
KAP0_HUMAN	PRKAR1A	physical	22863883
ARPC2_HUMAN	ARPC2	physical	26186194
ARC1A_HUMAN	ARPC1A	physical	26186194
ARP5L_HUMAN	ARPC5L	physical	26186194
ARPC5_HUMAN	ARPC5	physical	26186194
CLU_HUMAN	CLUH	physical	26186194
ARP2_HUMAN	ACTR2	physical	26186194
DOCK7_HUMAN	DOCK7	physical	26186194
DOCK8_HUMAN	DOCK8	physical	26186194
ARP3B_HUMAN	ACTR3B	physical	26186194
ARP3_HUMAN	ACTR3	physical	26186194
LRCH2_HUMAN	LRCH2	physical	26186194
GALT_HUMAN	GALT	physical	26186194
ARP3_HUMAN	ACTR3	physical	26344197
ARPC5_HUMAN	ARPC5	physical	26344197
ARP5L_HUMAN	ARPC5L	physical	26344197
CAZA1_HUMAN	CAPZA1	physical	26344197
CAZA2_HUMAN	CAPZA2	physical	26344197
PTPRF_HUMAN	PTPRF	physical	26344197
STXB1_HUMAN	STXBP1	physical	26344197
GALT_HUMAN	GALT	physical	28514442
ARP3B_HUMAN	ACTR3B	physical	28514442
DOCK8_HUMAN	DOCK8	physical	28514442
LRCH2_HUMAN	LRCH2	physical	28514442
DOCK7_HUMAN	DOCK7	physical	28514442
CLU_HUMAN	CLUH	physical	28514442
ARP3_HUMAN	ACTR3	physical	28514442
ARPC2_HUMAN	ARPC2	physical	28514442
ARP2_HUMAN	ACTR2	physical	28514442
ARP5L_HUMAN	ARPC5L	physical	28514442
ARC1A_HUMAN	ARPC1A	physical	28514442
PREP_HUMAN	PITRM1	physical	27173435
UFM1_HUMAN	UFM1	physical	27173435
CB071_HUMAN	C2orf71	physical	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 ARPC3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-56 AND LYS-61, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, AND MASSSPECTROMETRY.	18083107 [Abstract]