dbPTM

ARPC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARPC2_HUMAN
UniProt AC	O15144
Protein Name	Actin-related protein 2/3 complex subunit 2
Gene Name	ARPC2
Organism	Homo sapiens (Human).
Sequence Length	300
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection . Cell junction, synapse, synaptosome.
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	MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSISLKFYKELQAHGADELLKRVYGSFLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNCFASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKVFMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNTINLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Sulfoxidation	-------MILLEVNN -------CEEEEECH	4.37	30846556
27	Ubiquitination	ENAAAGNKPEAVEVT HHHHCCCCCCEEEEE	43.23	-
58	Phosphorylation	DKTKVMVSISLKFYK CCEEEEEEEEHHHHH	6.59	22210691
60	Phosphorylation	TKVMVSISLKFYKEL EEEEEEEEHHHHHHH	20.28	22210691
65	Malonylation	SISLKFYKELQAHGA EEEHHHHHHHHHCCH	55.89	26320211
65	2-Hydroxyisobutyrylation	SISLKFYKELQAHGA EEEHHHHHHHHHCCH	55.89	-
65	Ubiquitination	SISLKFYKELQAHGA EEEHHHHHHHHHCCH	55.89	21890473
65	Acetylation	SISLKFYKELQAHGA EEEHHHHHHHHHCCH	55.89	26822725
77	Ubiquitination	HGADELLKRVYGSFL CCHHHHHHHHHHHCC	53.06	-
77	2-Hydroxyisobutyrylation	HGADELLKRVYGSFL CCHHHHHHHHHHHCC	53.06	-
77	Acetylation	HGADELLKRVYGSFL CCHHHHHHHHHHHCC	53.06	23236377
108	Phosphorylation	NLPASKDSIVHQAGM CCCCCCCHHHHHHHH	30.19	21406692
115	Sulfoxidation	SIVHQAGMLKRNCFA HHHHHHHHHHHHHHH	4.46	21406390
117	Ubiquitination	VHQAGMLKRNCFASV HHHHHHHHHHHHHHH	32.45	21906983
117	Acetylation	VHQAGMLKRNCFASV HHHHHHHHHHHHHHH	32.45	25953088
117	2-Hydroxyisobutyrylation	VHQAGMLKRNCFASV HHHHHHHHHHHHHHH	32.45	-
123	Phosphorylation	LKRNCFASVFEKYFQ HHHHHHHHHHHHHHH	13.69	21712546
127	Acetylation	CFASVFEKYFQFQEE HHHHHHHHHHHHHHC	39.64	7407333
127	Ubiquitination	CFASVFEKYFQFQEE HHHHHHHHHHHHHHC	39.64	-
136	Ubiquitination	FQFQEEGKEGENRAV HHHHHCCCCCCCEEE	66.86	21906983
136	2-Hydroxyisobutyrylation	FQFQEEGKEGENRAV HHHHHCCCCCCCEEE	66.86	-
146	Phosphorylation	ENRAVIHYRDDETMY CCEEEEEEECCCEEE	12.47	30576142
151	Phosphorylation	IHYRDDETMYVESKK EEEECCCEEEEEECC	22.31	25954137
152	Sulfoxidation	HYRDDETMYVESKKD EEECCCEEEEEECCC	3.12	30846556
153	Phosphorylation	YRDDETMYVESKKDR EECCCEEEEEECCCC	14.42	25954137
156	Phosphorylation	DETMYVESKKDRVTV CCEEEEEECCCCEEE	34.65	30576142
157	Malonylation	ETMYVESKKDRVTVV CEEEEEECCCCEEEE	45.23	32601280
157	Ubiquitination	ETMYVESKKDRVTVV CEEEEEECCCCEEEE	45.23	21906983
179	Ubiquitination	DDDVVIGKVFMQEFK CCCEEEEEHHHHHHH	22.60	-
186	2-Hydroxyisobutyrylation	KVFMQEFKEGRRASH EHHHHHHHCCCCCCC	59.51	-
186	Malonylation	KVFMQEFKEGRRASH EHHHHHHHCCCCCCC	59.51	26320211
186	Ubiquitination	KVFMQEFKEGRRASH EHHHHHHHCCCCCCC	59.51	-
186	Acetylation	KVFMQEFKEGRRASH EHHHHHHHCCCCCCC	59.51	23749302
192	Phosphorylation	FKEGRRASHTAPQVL HHCCCCCCCCCCCHH	21.40	26462736
194	Phosphorylation	EGRRASHTAPQVLFS CCCCCCCCCCCHHHC	37.22	28152594
201	Phosphorylation	TAPQVLFSHREPPLE CCCCHHHCCCCCCCC	19.92	20873877
210	Ubiquitination	REPPLELKDTDAAVG CCCCCCCCCCCCCCC	49.56	-
240	Phosphorylation	NASARDNTINLIHTF CCCCCCCEEEEHHHH	18.61	20068231
246	Phosphorylation	NTINLIHTFRDYLHY CEEEEHHHHHHHHHH	17.24	29523821
250	Phosphorylation	LIHTFRDYLHYHIKC EHHHHHHHHHHHHEE	7.36	29523821
253	Phosphorylation	TFRDYLHYHIKCSKA HHHHHHHHHHEECCC	11.57	29523821
256	Ubiquitination	DYLHYHIKCSKAYIH HHHHHHHEECCCCHH	21.10	-
256	Acetylation	DYLHYHIKCSKAYIH HHHHHHHEECCCCHH	21.10	26051181
259	Ubiquitination	HYHIKCSKAYIHTRM HHHHEECCCCHHHHH	55.46	-
261	Phosphorylation	HIKCSKAYIHTRMRA HHEECCCCHHHHHHH	9.29	-
269	2-Hydroxyisobutyrylation	IHTRMRAKTSDFLKV HHHHHHHCHHHHHHH	37.89	-
269	Ubiquitination	IHTRMRAKTSDFLKV HHHHHHHCHHHHHHH	37.89	-
275	Acetylation	AKTSDFLKVLNRARP HCHHHHHHHHHHHCC	44.67	19608861
275	Malonylation	AKTSDFLKVLNRARP HCHHHHHHHHHHHCC	44.67	26320211
275	Ubiquitination	AKTSDFLKVLNRARP HCHHHHHHHHHHHCC	44.67	21890473
286	2-Hydroxyisobutyrylation	RARPDAEKKEMKTIT HHCCCHHHHHHHHHC	56.61	-
290	Acetylation	DAEKKEMKTITGKTF CHHHHHHHHHCCCCC	37.56	26210075
290	Ubiquitination	DAEKKEMKTITGKTF CHHHHHHHHHCCCCC	37.56	-
291	Phosphorylation	AEKKEMKTITGKTFS HHHHHHHHHCCCCCC	23.59	28857561
293	Phosphorylation	KKEMKTITGKTFSSR HHHHHHHCCCCCCCC	37.55	26074081
295	Ubiquitination	EMKTITGKTFSSR-- HHHHHCCCCCCCC--	37.43	21890473
295	Methylation	EMKTITGKTFSSR-- HHHHHCCCCCCCC--	37.43	19608861
295	Acetylation	EMKTITGKTFSSR-- HHHHHCCCCCCCC--	37.43	19608861
295	Malonylation	EMKTITGKTFSSR-- HHHHHCCCCCCCC--	37.43	26320211
296	Phosphorylation	MKTITGKTFSSR--- HHHHCCCCCCCC---	30.05	26074081
298	Phosphorylation	TITGKTFSSR----- HHCCCCCCCC-----	30.36	26074081
299	Phosphorylation	ITGKTFSSR------ HCCCCCCCC------	37.51	26074081

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 ARPC2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARPC2_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 ARPC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARPC3_HUMAN	ARPC3	physical	9230079
ARPC4_HUMAN	ARPC4	physical	11162547
ARC1B_HUMAN	ARPC1B	physical	20603326
ARPC4_HUMAN	ARPC4	physical	22939629
ARPC3_HUMAN	ARPC3	physical	22939629
ARPC5_HUMAN	ARPC5	physical	22939629
AASD1_HUMAN	AARSD1	physical	22863883
ARP3_HUMAN	ACTR3	physical	22863883
ARPC3_HUMAN	ARPC3	physical	22863883
ARPC4_HUMAN	ARPC4	physical	22863883
ARPC5_HUMAN	ARPC5	physical	22863883
FUBP1_HUMAN	FUBP1	physical	22863883
METH_HUMAN	MTR	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
KAPCA_HUMAN	PRKACA	physical	22863883
KAPCB_HUMAN	PRKACB	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
RFA2_HUMAN	RPA2	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	22863883
THG1_HUMAN	THG1L	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
ARP3_HUMAN	ACTR3	physical	26344197
ARPC3_HUMAN	ARPC3	physical	26344197
EF2_HUMAN	EEF2	physical	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 ARPC2_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-275 AND LYS-295, AND MASSSPECTROMETRY.	19608861 [Abstract]