dbPTM

ARP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARP2_HUMAN
UniProt AC	P61160
Protein Name	Actin-related protein 2
Gene Name	ACTR2
Organism	Homo sapiens (Human).
Sequence Length	394
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection .
Protein Description	Functions as ATP-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 pointed end of the daughter actin filament..
Protein Sequence	MDSQGRKVVVCDNGTGFVKCGYAGSNFPEHIFPALVGRPIIRSTTKVGNIEIKDLMVGDEASELRSMLEVNYPMENGIVRNWDDMKHLWDYTFGPEKLNIDTRNCKILLTEPPMNPTKNREKIVEVMFETYQFSGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHICPVYEGFSLPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRMIKEKLCYVGYNIEQEQKLALETTVLVESYTLPDGRIIKVGGERFEAPEALFQPHLINVEGVGVAELLFNTIQAADIDTRSEFYKHIVLSGGSTMYPGLPSRLERELKQLYLERVLKGDVEKLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDNFWMTRQEYQEKGVRVLEKLGVTVR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDSQGRKV -------CCCCCCEE	11.46	25944712
3	Phosphorylation	-----MDSQGRKVVV -----CCCCCCEEEE	32.98	27251275
7	Malonylation	-MDSQGRKVVVCDNG -CCCCCCEEEEECCC	46.32	26320211
7	Acetylation	-MDSQGRKVVVCDNG -CCCCCCEEEEECCC	46.32	27452117
7	Ubiquitination	-MDSQGRKVVVCDNG -CCCCCCEEEEECCC	46.32	33845483
11	S-palmitoylation	QGRKVVVCDNGTGFV CCCEEEEECCCCCEE	1.96	29575903
19	Methylation	DNGTGFVKCGYAGSN CCCCCEEECCCCCCC	21.49	-
19	Ubiquitination	DNGTGFVKCGYAGSN CCCCCEEECCCCCCC	21.49	21963094
22	Phosphorylation	TGFVKCGYAGSNFPE CCEEECCCCCCCCCH	19.77	20090780
43	Phosphorylation	VGRPIIRSTTKVGNI CCCCEEECCCEECCE	29.98	23312004
44	Phosphorylation	GRPIIRSTTKVGNIE CCCEEECCCEECCEE	22.31	23312004
45	Phosphorylation	RPIIRSTTKVGNIEI CCEEECCCEECCEEE	25.61	23312004
46	Ubiquitination	PIIRSTTKVGNIEIK CEEECCCEECCEEEE	48.51	23000965
53	Ubiquitination	KVGNIEIKDLMVGDE EECCEEEEEEECCCH	31.83	21906983
56	Sulfoxidation	NIEIKDLMVGDEASE CEEEEEEECCCHHHH	4.55	21406390
62	Phosphorylation	LMVGDEASELRSMLE EECCCHHHHHHHHHH	34.81	28674151
66	Phosphorylation	DEASELRSMLEVNYP CHHHHHHHHHHCCCC	40.10	21406692
67 (in isoform 2)	Phosphorylation	-	2.75	-
72	Phosphorylation	RSMLEVNYPMENGIV HHHHHCCCCCCCCCC	14.77	21406692
86	Ubiquitination	VRNWDDMKHLWDYTF CCCHHHCHHHHHHCC	42.41	21906983
86	Acetylation	VRNWDDMKHLWDYTF CCCHHHCHHHHHHCC	42.41	26822725
91	Ubiquitination	DMKHLWDYTFGPEKL HCHHHHHHCCCHHHC	7.74	21963094
91	Phosphorylation	DMKHLWDYTFGPEKL HCHHHHHHCCCHHHC	7.74	28152594
92	Phosphorylation	MKHLWDYTFGPEKLN CHHHHHHCCCHHHCC	21.46	28152594
97	Ubiquitination	DYTFGPEKLNIDTRN HHCCCHHHCCCCCCC	50.39	21906983
102	Ubiquitination	PEKLNIDTRNCKILL HHHCCCCCCCCEEEE	21.71	21963094
106	Ubiquitination	NIDTRNCKILLTEPP CCCCCCCEEEEECCC	39.68	27667366
110	Phosphorylation	RNCKILLTEPPMNPT CCCEEEEECCCCCCC	42.89	20068231
111	Ubiquitination	NCKILLTEPPMNPTK CCEEEEECCCCCCCC	47.58	27667366
114	Sulfoxidation	ILLTEPPMNPTKNRE EEEECCCCCCCCCHH	15.98	30846556
117	Phosphorylation	TEPPMNPTKNREKIV ECCCCCCCCCHHHHH	35.63	23401153
118	Acetylation	EPPMNPTKNREKIVE CCCCCCCCCHHHHHH	56.09	25953088
118	Ubiquitination	EPPMNPTKNREKIVE CCCCCCCCCHHHHHH	56.09	23000965
118	Neddylation	EPPMNPTKNREKIVE CCCCCCCCCHHHHHH	56.09	32015554
122	Ubiquitination	NPTKNREKIVEVMFE CCCCCHHHHHHHHHE	49.14	23000965
122 (in isoform 2)	Phosphorylation	-	49.14	27251275
123	Ubiquitination	PTKNREKIVEVMFET CCCCHHHHHHHHHEE	2.47	23000965
123	Neddylation	PTKNREKIVEVMFET CCCCHHHHHHHHHEE	2.47	32015554
127	Ubiquitination	REKIVEVMFETYQFS HHHHHHHHHEECCCC	1.27	23000965
195	Ubiquitination	DITRYLIKLLLLRGY HHHHHHHHHHHHHCC	30.41	21906983
200	Ubiquitination	LIKLLLLRGYAFNHS HHHHHHHHCCCCCCC	35.73	22053931
202	Phosphorylation	KLLLLRGYAFNHSAD HHHHHHCCCCCCCCC	11.11	23312004
207	Phosphorylation	RGYAFNHSADFETVR HCCCCCCCCCHHHHH	30.55	28348404
212	Phosphorylation	NHSADFETVRMIKEK CCCCCHHHHHHHHHH	17.26	23312004
212 (in isoform 2)	Phosphorylation	-	17.26	27251275
217	Ubiquitination	FETVRMIKEKLCYVG HHHHHHHHHHHHCCC	39.18	22817900
219	Acetylation	TVRMIKEKLCYVGYN HHHHHHHHHHCCCCC	38.56	25953088
219	Ubiquitination	TVRMIKEKLCYVGYN HHHHHHHHHHCCCCC	38.56	21906983
222	Ubiquitination	MIKEKLCYVGYNIEQ HHHHHHHCCCCCCHH	13.82	22817900
222	Phosphorylation	MIKEKLCYVGYNIEQ HHHHHHHCCCCCCHH	13.82	28152594
224	Ubiquitination	KEKLCYVGYNIEQEQ HHHHHCCCCCCHHHH	5.36	21963094
225	Phosphorylation	EKLCYVGYNIEQEQK HHHHCCCCCCHHHHH	11.70	28152594
237	Phosphorylation	EQKLALETTVLVESY HHHHHHEEEEEEEEE	24.05	-
238	Phosphorylation	QKLALETTVLVESYT HHHHHEEEEEEEEEE	11.49	-
253	Ubiquitination	LPDGRIIKVGGERFE CCCCCEEEECCEECC	32.24	21906983
253	Acetylation	LPDGRIIKVGGERFE CCCCCEEEECCEECC	32.24	25953088
258	Ubiquitination	IIKVGGERFEAPEAL EEEECCEECCCCHHH	37.67	27667366
298	Phosphorylation	IDTRSEFYKHIVLSG CCCHHHHHHHHEECC	9.52	25332170
299	Malonylation	DTRSEFYKHIVLSGG CCHHHHHHHHEECCC	31.98	26320211
299	Acetylation	DTRSEFYKHIVLSGG CCHHHHHHHHEECCC	31.98	19608861
299	Ubiquitination	DTRSEFYKHIVLSGG CCHHHHHHHHEECCC	31.98	23000965
304	Ubiquitination	FYKHIVLSGGSTMYP HHHHHEECCCCCCCC	30.16	23000965
304	Acetylation	FYKHIVLSGGSTMYP HHHHHEECCCCCCCC	30.16	19608861
304	Phosphorylation	FYKHIVLSGGSTMYP HHHHHEECCCCCCCC	30.16	25332170
309	Sulfoxidation	VLSGGSTMYPGLPSR EECCCCCCCCCCCHH	3.99	30846556
315	O-linked_Glycosylation	TMYPGLPSRLERELK CCCCCCCHHHHHHHH	55.32	30379171
315	Phosphorylation	TMYPGLPSRLERELK CCCCCCCHHHHHHHH	55.32	25332170
322	Acetylation	SRLERELKQLYLERV HHHHHHHHHHHHHHH	33.24	19608861
322	Ubiquitination	SRLERELKQLYLERV HHHHHHHHHHHHHHH	33.24	21906983
327	Acetylation	ELKQLYLERVLKGDV HHHHHHHHHHHCCCH	27.47	19608861
327	Ubiquitination	ELKQLYLERVLKGDV HHHHHHHHHHHCCCH	27.47	27667366
331	Sumoylation	LYLERVLKGDVEKLS HHHHHHHCCCHHHHH	50.65	-
331	Ubiquitination	LYLERVLKGDVEKLS HHHHHHHCCCHHHHH	50.65	23000965
331	Succinylation	LYLERVLKGDVEKLS HHHHHHHCCCHHHHH	50.65	23954790
331	Sumoylation	LYLERVLKGDVEKLS HHHHHHHCCCHHHHH	50.65	-
336	Ubiquitination	VLKGDVEKLSKFKIR HHCCCHHHHHCCEEE	58.89	23000965
336	Acetylation	VLKGDVEKLSKFKIR HHCCCHHHHHCCEEE	58.89	25953088
339	Ubiquitination	GDVEKLSKFKIRIED CCHHHHHCCEEEECC	62.20	24816145
341	Ubiquitination	VEKLSKFKIRIEDPP HHHHHCCEEEECCCC	34.51	23000965
344	Ubiquitination	LSKFKIRIEDPPRRK HHCCEEEECCCCCCC	8.85	24816145
366	Ubiquitination	AVLADIMKDKDNFWM HHHHHHHHCCCCCEE	63.06	23000965
368	Ubiquitination	LADIMKDKDNFWMTR HHHHHHCCCCCEECH	49.40	23000965
368	Acetylation	LADIMKDKDNFWMTR HHHHHHCCCCCEECH	49.40	25953088
371	Ubiquitination	IMKDKDNFWMTRQEY HHHCCCCCEECHHHH	7.27	23000965
373	Ubiquitination	KDKDNFWMTRQEYQE HCCCCCEECHHHHHH	1.61	23000965
374	Phosphorylation	DKDNFWMTRQEYQEK CCCCCEECHHHHHHH	21.57	21406692
378	Phosphorylation	FWMTRQEYQEKGVRV CEECHHHHHHHCCHH	17.40	-
381	Neddylation	TRQEYQEKGVRVLEK CHHHHHHHCCHHHHH	47.37	32015554
381	Acetylation	TRQEYQEKGVRVLEK CHHHHHHHCCHHHHH	47.37	25953088
381	Ubiquitination	TRQEYQEKGVRVLEK CHHHHHHHCCHHHHH	47.37	21906983
386	Ubiquitination	QEKGVRVLEKLGVTV HHHCCHHHHHHCCCC	3.17	24816145
386	Neddylation	QEKGVRVLEKLGVTV HHHCCHHHHHHCCCC	3.17	32015554
388	Sumoylation	KGVRVLEKLGVTVR- HCCHHHHHHCCCCC-	46.51	-
388	Acetylation	KGVRVLEKLGVTVR- HCCHHHHHHCCCCC-	46.51	27178108
388	Sumoylation	KGVRVLEKLGVTVR- HCCHHHHHHCCCCC-	46.51	-
388	Ubiquitination	KGVRVLEKLGVTVR- HCCHHHHHHCCCCC-	46.51	23000965
393	Ubiquitination	LEKLGVTVR------ HHHHCCCCC------	6.76	23000965

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
202	Y	Phosphorylation	Kinase	MAP3K14	Q99558	GPS
237	T	Phosphorylation	Kinase	MAP3K14	Q99558	GPS
237	T	Phosphorylation	Kinase	PLK4	O00444	PSP
238	T	Phosphorylation	Kinase	MAP3K14	Q99558	GPS
238	T	Phosphorylation	Kinase	PLK4	O00444	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARP2_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 ARP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARP3_HUMAN	ACTR3	physical	22939629
ARPC4_HUMAN	ARPC4	physical	22939629
ARPC5_HUMAN	ARPC5	physical	22939629
ARPC2_HUMAN	ARPC2	physical	22939629
ARPC3_HUMAN	ARPC3	physical	22939629
ARP5L_HUMAN	ARPC5L	physical	22939629
COR1C_HUMAN	CORO1C	physical	22939629
UBE2N_HUMAN	UBE2N	physical	22939629
ELF5_HUMAN	ELF5	physical	21988832
ARP3_HUMAN	ACTR3	physical	22863883
HEM2_HUMAN	ALAD	physical	22863883
ARPC2_HUMAN	ARPC2	physical	22863883
ARPC4_HUMAN	ARPC4	physical	22863883
CALU_HUMAN	CALU	physical	22863883
CRTAP_HUMAN	CRTAP	physical	22863883
FUBP1_HUMAN	FUBP1	physical	22863883
GRPE1_HUMAN	GRPEL1	physical	22863883
HPBP1_HUMAN	HSPBP1	physical	22863883
KBP_HUMAN	KIAA1279	physical	22863883
TRMB_HUMAN	METTL1	physical	22863883
NIF3L_HUMAN	NIF3L1	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
OGT1_HUMAN	OGT	physical	22863883
PANK4_HUMAN	PANK4	physical	22863883
PPME1_HUMAN	PPME1	physical	22863883
KAPCB_HUMAN	PRKACB	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
RPR1A_HUMAN	RPRD1A	physical	22863883
RPR1B_HUMAN	RPRD1B	physical	22863883
SH3G1_HUMAN	SH3GL1	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	22863883
SRP09_HUMAN	SRP9	physical	22863883
SURF2_HUMAN	SURF2	physical	22863883
TM1L1_HUMAN	TOM1L1	physical	22863883
PRPK_HUMAN	TP53RK	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
UFM1_HUMAN	UFM1	physical	22863883
WDR4_HUMAN	WDR4	physical	22863883
ZPR1_HUMAN	ZPR1	physical	22863883
ARP3_HUMAN	ACTR3	physical	26344197
ARPC2_HUMAN	ARPC2	physical	26344197
ARPC3_HUMAN	ARPC3	physical	26344197
ARPC4_HUMAN	ARPC4	physical	26344197
ARPC5_HUMAN	ARPC5	physical	26344197
ARP5L_HUMAN	ARPC5L	physical	26344197
CAZA2_HUMAN	CAPZA2	physical	26344197
COR1B_HUMAN	CORO1B	physical	26344197
FA98B_HUMAN	FAM98B	physical	26344197
TCPZ_HUMAN	CCT6A	physical	26496610
COF1_HUMAN	CFL1	physical	26496610
CLCA_HUMAN	CLTA	physical	26496610
CLCB_HUMAN	CLTB	physical	26496610
DAB2_HUMAN	DAB2	physical	26496610
DREB_HUMAN	DBN1	physical	26496610
DSG2_HUMAN	DSG2	physical	26496610
SRC8_HUMAN	CTTN	physical	26496610
GELS_HUMAN	GSN	physical	26496610
ITPR3_HUMAN	ITPR3	physical	26496610
MYO6_HUMAN	MYO6	physical	26496610
MYPT1_HUMAN	PPP1R12A	physical	26496610
SVIL_HUMAN	SVIL	physical	26496610
TCPA_HUMAN	TCP1	physical	26496610
TCPG_HUMAN	CCT3	physical	26496610
LUZP1_HUMAN	LUZP1	physical	26496610
RAI3_HUMAN	GPRC5A	physical	26496610
ARPC5_HUMAN	ARPC5	physical	26496610
ARPC4_HUMAN	ARPC4	physical	26496610
ARPC3_HUMAN	ARPC3	physical	26496610
ARC1B_HUMAN	ARPC1B	physical	26496610
ARP3_HUMAN	ACTR3	physical	26496610
ARPC2_HUMAN	ARPC2	physical	26496610
BASP1_HUMAN	BASP1	physical	26496610
ARC1A_HUMAN	ARPC1A	physical	26496610
TCPH_HUMAN	CCT7	physical	26496610
TCPD_HUMAN	CCT4	physical	26496610
TCPB_HUMAN	CCT2	physical	26496610
TCPQ_HUMAN	CCT8	physical	26496610
TCPE_HUMAN	CCT5	physical	26496610
COBL_HUMAN	COBL	physical	26496610
COR1C_HUMAN	CORO1C	physical	26496610
LIMA1_HUMAN	LIMA1	physical	26496610
RBM27_HUMAN	RBM27	physical	26496610
MTA70_HUMAN	METTL3	physical	26496610
INF2_HUMAN	INF2	physical	26496610
PDCL3_HUMAN	PDCL3	physical	26496610
CYBR1_HUMAN	CYBRD1	physical	26496610
ARP5L_HUMAN	ARPC5L	physical	26496610
CHUR_HUMAN	CHURC1	physical	26496610
CYTSB_HUMAN	SPECC1	physical	26496610
MISP_HUMAN	MISP	physical	26496610

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 ARP2_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-299 AND LYS-322, AND MASSSPECTROMETRY.	19608861 [Abstract]