dbPTM

ARP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARP3_HUMAN
UniProt AC	P61158
Protein Name	Actin-related protein 3
Gene Name	ACTR3
Organism	Homo sapiens (Human).
Sequence Length	418
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection . In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) (PubMed:19109554).
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. Plays a role in ciliogenesis..
Protein Sequence	MAGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDFFIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTPENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVKEFNKYDTDGSKWIKQYTGINAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVVDEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKPKPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGRLPACV ------CCCCCCEEE	16.29	19413330
8	S-nitrosylation	MAGRLPACVVDCGTG CCCCCCEEEEECCCC	2.64	2212679
8	S-palmitoylation	MAGRLPACVVDCGTG CCCCCCEEEEECCCC	2.64	26865113
12	S-nitrosylation	LPACVVDCGTGYTKL CCEEEEECCCCCEEC	3.38	2212679
12	S-palmitoylation	LPACVVDCGTGYTKL CCEEEEECCCCCEEC	3.38	26865113
14	Phosphorylation	ACVVDCGTGYTKLGY EEEEECCCCCEECCC	33.09	28442448
16	Nitration	VVDCGTGYTKLGYAG EEECCCCCEECCCCC	10.67	-
16	Phosphorylation	VVDCGTGYTKLGYAG EEECCCCCEECCCCC	10.67	27155012
17	Phosphorylation	VDCGTGYTKLGYAGN EECCCCCEECCCCCC	22.57	28152594
18	Ubiquitination	DCGTGYTKLGYAGNT ECCCCCEECCCCCCC	31.28	-
25	Phosphorylation	KLGYAGNTEPQFIIP ECCCCCCCCCCEECC	48.39	28348404
38	Acetylation	IPSCIAIKESAKVGD CCCCEEEHHHHCCCH	36.27	25953088
38	Ubiquitination	IPSCIAIKESAKVGD CCCCEEEHHHHCCCH	36.27	-
42	Acetylation	IAIKESAKVGDQAQR EEEHHHHCCCHHHHH	56.90	25953088
42	Ubiquitination	IAIKESAKVGDQAQR EEEHHHHCCCHHHHH	56.90	21906983
53	Acetylation	QAQRRVMKGVDDLDF HHHHHHHCCCCCCCE	53.58	23954790
53	Ubiquitination	QAQRRVMKGVDDLDF HHHHHHHCCCCCCCE	53.58	21906983
53	Ubiquitination	QAQRRVMKGVDDLDF HHHHHHHCCCCCCCE	53.58	21890473
69	Acetylation	IGDEAIEKPTYATKW CCHHHCCCCCCCCCC	36.22	26051181
69	Ubiquitination	IGDEAIEKPTYATKW CCHHHCCCCCCCCCC	36.22	21906983
69	Ubiquitination	IGDEAIEKPTYATKW CCHHHCCCCCCCCCC	36.22	21890473
75	Ubiquitination	EKPTYATKWPIRHGI CCCCCCCCCCCCCCC	42.68	21906983
89	Sulfoxidation	IVEDWDLMERFMEQV CCCCHHHHHHHHHHH	3.01	30846556
99	Ubiquitination	FMEQVIFKYLRAEPE HHHHHHHHHHHCCCC	32.05	21906983
99	Ubiquitination	FMEQVIFKYLRAEPE HHHHHHHHHHHCCCC	32.05	21890473
100	Phosphorylation	MEQVIFKYLRAEPED HHHHHHHHHHCCCCC	7.23	22817900
109	Phosphorylation	RAEPEDHYFLLTEPP HCCCCCCEEECCCCC	14.29	17360941
113	Phosphorylation	EDHYFLLTEPPLNTP CCCEEECCCCCCCCC	48.90	29255136
119	Phosphorylation	LTEPPLNTPENREYT CCCCCCCCCCCCCEE	39.40	29255136
133	Phosphorylation	TAEIMFESFNVPGLY EEEEEEHHCCCCHHH	15.74	-
140	Phosphorylation	SFNVPGLYIAVQAVL HCCCCHHHHHHHHHH	7.86	-
152	Phosphorylation	AVLALAASWTSRQVG HHHHHHHHHHCCCCC	25.86	-
184	Phosphorylation	VIPVAEGYVIGSCIK EEEECCCEEEHHHHH	4.76	20090780
188	Phosphorylation	AEGYVIGSCIKHIPI CCCEEEHHHHHCCCC	11.09	-
189	S-palmitoylation	EGYVIGSCIKHIPIA CCEEEHHHHHCCCCC	3.97	29575903
191	Acetylation	YVIGSCIKHIPIAGR EEEHHHHHCCCCCCC	39.55	26051181
191	Ubiquitination	YVIGSCIKHIPIAGR EEEHHHHHCCCCCCC	39.55	-
201	Phosphorylation	PIAGRDITYFIQQLL CCCCCHHHHHHHHHH	19.37	28450419
202	Phosphorylation	IAGRDITYFIQQLLR CCCCHHHHHHHHHHH	10.06	22115753
225	Acetylation	EQSLETAKAVKERYS HHHHHHHHHHHHHHH	62.22	25953088
225	Ubiquitination	EQSLETAKAVKERYS HHHHHHHHHHHHHHH	62.22	21906983
228	Ubiquitination	LETAKAVKERYSYVC HHHHHHHHHHHHCCC	41.14	-
231	Phosphorylation	AKAVKERYSYVCPDL HHHHHHHHHCCCHHH	12.87	21082442
232	Phosphorylation	KAVKERYSYVCPDLV HHHHHHHHCCCHHHH	19.81	28152594
233	Phosphorylation	AVKERYSYVCPDLVK HHHHHHHCCCHHHHH	9.35	28152594
240	2-Hydroxyisobutyrylation	YVCPDLVKEFNKYDT CCCHHHHHHHHHCCC	64.98	-
240	Acetylation	YVCPDLVKEFNKYDT CCCHHHHHHHHHCCC	64.98	19608861
240	Malonylation	YVCPDLVKEFNKYDT CCCHHHHHHHHHCCC	64.98	26320211
240	Ubiquitination	YVCPDLVKEFNKYDT CCCHHHHHHHHHCCC	64.98	21890473
240	Ubiquitination	YVCPDLVKEFNKYDT CCCHHHHHHHHHCCC	64.98	21890473
244	2-Hydroxyisobutyrylation	DLVKEFNKYDTDGSK HHHHHHHHCCCCCHH	50.23	-
244	Acetylation	DLVKEFNKYDTDGSK HHHHHHHHCCCCCHH	50.23	19608861
244	Malonylation	DLVKEFNKYDTDGSK HHHHHHHHCCCCCHH	50.23	26320211
244	Ubiquitination	DLVKEFNKYDTDGSK HHHHHHHHCCCCCHH	50.23	19608861
251	Acetylation	KYDTDGSKWIKQYTG HCCCCCHHHHHHHHC	59.47	19608861
251	Malonylation	KYDTDGSKWIKQYTG HCCCCCHHHHHHHHC	59.47	26320211
251	Ubiquitination	KYDTDGSKWIKQYTG HCCCCCHHHHHHHHC	59.47	21890473
251	Ubiquitination	KYDTDGSKWIKQYTG HCCCCCHHHHHHHHC	59.47	21890473
254	2-Hydroxyisobutyrylation	TDGSKWIKQYTGINA CCCHHHHHHHHCCCC	35.82	-
254	Acetylation	TDGSKWIKQYTGINA CCCHHHHHHHHCCCC	35.82	19608861
254	Malonylation	TDGSKWIKQYTGINA CCCHHHHHHHHCCCC	35.82	26320211
254	Ubiquitination	TDGSKWIKQYTGINA CCCHHHHHHHHCCCC	35.82	21890473
254	Ubiquitination	TDGSKWIKQYTGINA CCCHHHHHHHHCCCC	35.82	21890473
256	Phosphorylation	GSKWIKQYTGINAIS CHHHHHHHHCCCCCC	11.26	28152594
257	Phosphorylation	SKWIKQYTGINAISK HHHHHHHHCCCCCCC	29.14	28152594
264	Sumoylation	TGINAISKKEFSIDV HCCCCCCCCEEEEEC	50.65	-
264	2-Hydroxyisobutyrylation	TGINAISKKEFSIDV HCCCCCCCCEEEEEC	50.65	-
264	Acetylation	TGINAISKKEFSIDV HCCCCCCCCEEEEEC	50.65	25953088
264	Succinylation	TGINAISKKEFSIDV HCCCCCCCCEEEEEC	50.65	23954790
264	Sumoylation	TGINAISKKEFSIDV HCCCCCCCCEEEEEC	50.65	-
264	Ubiquitination	TGINAISKKEFSIDV HCCCCCCCCEEEEEC	50.65	-
265	Ubiquitination	GINAISKKEFSIDVG CCCCCCCCEEEEECC	58.14	21906983
265	Ubiquitination	GINAISKKEFSIDVG CCCCCCCCEEEEECC	58.14	21890473
268	Phosphorylation	AISKKEFSIDVGYER CCCCCEEEEECCCHH	20.97	24719451
273	Phosphorylation	EFSIDVGYERFLGPE EEEEECCCHHHCCCE	12.09	28152594
317	Acetylation	DVRRPLYKNIVLSGG CCCCCCCCCEEECCC	48.13	25953088
317	Ubiquitination	DVRRPLYKNIVLSGG CCCCCCCCCEEECCC	48.13	-
322	Phosphorylation	LYKNIVLSGGSTMFR CCCCEEECCCCHHHH	30.16	30108239
325	Phosphorylation	NIVLSGGSTMFRDFG CEEECCCCHHHHHHH	21.89	30108239
326	Phosphorylation	IVLSGGSTMFRDFGR EEECCCCHHHHHHHH	24.49	30108239
327	Sulfoxidation	VLSGGSTMFRDFGRR EECCCCHHHHHHHHH	2.51	30846556
348	2-Hydroxyisobutyrylation	RTVDARLKLSEELSG HHHHHHHHCCHHHCC	44.40	-
348	Acetylation	RTVDARLKLSEELSG HHHHHHHHCCHHHCC	44.40	25953088
348	Malonylation	RTVDARLKLSEELSG HHHHHHHHCCHHHCC	44.40	26320211
348	Ubiquitination	RTVDARLKLSEELSG HHHHHHHHCCHHHCC	44.40	21906983
350	Phosphorylation	VDARLKLSEELSGGR HHHHHHCCHHHCCCC	27.69	23911959
354	Phosphorylation	LKLSEELSGGRLKPK HHCCHHHCCCCCCCC	42.34	27251275
359	Ubiquitination	ELSGGRLKPKPIDVQ HHCCCCCCCCCCCHH	50.03	21906983
359	Ubiquitination	ELSGGRLKPKPIDVQ HHCCCCCCCCCCCHH	50.03	21890473
361	Ubiquitination	SGGRLKPKPIDVQVI CCCCCCCCCCCHHHH	53.68	21906983
361	Ubiquitination	SGGRLKPKPIDVQVI CCCCCCCCCCCHHHH	53.68	21890473
375	Phosphorylation	ITHHMQRYAVWFGGS HCCCHHHHHHHHCCC	6.66	20068231
383	Sulfoxidation	AVWFGGSMLASTPEF HHHHCCCHHCCCHHH	4.02	30846556
387	Phosphorylation	GGSMLASTPEFYQVC CCCHHCCCHHHHHHH	22.64	20068231
391	Phosphorylation	LASTPEFYQVCHTKK HCCCHHHHHHHCCCC	9.81	20068231
396	Phosphorylation	EFYQVCHTKKDYEEI HHHHHHCCCCCHHHH	34.36	20068231
398	2-Hydroxyisobutyrylation	YQVCHTKKDYEEIGP HHHHCCCCCHHHHCH	67.70	-
398	Acetylation	YQVCHTKKDYEEIGP HHHHCCCCCHHHHCH	67.70	26051181
398	Malonylation	YQVCHTKKDYEEIGP HHHHCCCCCHHHHCH	67.70	26320211
398	Succinylation	YQVCHTKKDYEEIGP HHHHCCCCCHHHHCH	67.70	23954790
398	Ubiquitination	YQVCHTKKDYEEIGP HHHHCCCCCHHHHCH	67.70	-
400	Phosphorylation	VCHTKKDYEEIGPSI HHCCCCCHHHHCHHH	25.09	28152594
406	Phosphorylation	DYEEIGPSICRHNPV CHHHHCHHHHCCCCC	29.16	20068231
408	Glutathionylation	EEIGPSICRHNPVFG HHHCHHHHCCCCCCC	4.20	22555962
417	Sulfoxidation	HNPVFGVMS------ CCCCCCCCC------	3.94	28183972
418	Phosphorylation	NPVFGVMS------- CCCCCCCC-------	34.36	25159151

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 ARP3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARP3_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 ARP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARP2_HUMAN	ACTR2	physical	11741539
ARC1B_HUMAN	ARPC1B	physical	11741539
ARPC2_HUMAN	ARPC2	physical	11741539
ARPC3_HUMAN	ARPC3	physical	11741539
ARPC4_HUMAN	ARPC4	physical	11741539
SRC8_HUMAN	CTTN	physical	12176742
ARPC2_HUMAN	ARPC2	physical	22939629
ARPC4_HUMAN	ARPC4	physical	22939629
ARPC3_HUMAN	ARPC3	physical	22939629
ARPC5_HUMAN	ARPC5	physical	22939629
ARP5L_HUMAN	ARPC5L	physical	22939629
ARPC4_HUMAN	ARPC4	physical	22863883
ARPC5_HUMAN	ARPC5	physical	22863883
CALU_HUMAN	CALU	physical	22863883
FUBP1_HUMAN	FUBP1	physical	22863883
KBP_HUMAN	KIAA1279	physical	22863883
TRMB_HUMAN	METTL1	physical	22863883
NIF3L_HUMAN	NIF3L1	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
KAPCB_HUMAN	PRKACB	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
RPR1B_HUMAN	RPRD1B	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	22863883
PRPK_HUMAN	TP53RK	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
UGGG1_HUMAN	UGGT1	physical	22863883
ZPR1_HUMAN	ZPR1	physical	22863883
RHG17_HUMAN	ARHGAP17	physical	26344197
COG3_HUMAN	COG3	physical	26344197
COR1B_HUMAN	CORO1B	physical	26344197
STXB1_HUMAN	STXBP1	physical	26344197
ARP2_HUMAN	ACTR2	physical	28514442
CYTN_HUMAN	CST1	physical	28514442
CYTS_HUMAN	CST4	physical	28514442
ARPC2_HUMAN	ARPC2	physical	28514442
ARP5L_HUMAN	ARPC5L	physical	28514442
ARPC4_HUMAN	ARPC4	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
TCPH_HUMAN	CCT7	physical	28514442
TCPG_HUMAN	CCT3	physical	28514442
TCPZ_HUMAN	CCT6A	physical	28514442
TCPD_HUMAN	CCT4	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ARP3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-240; LYS-244; LYS-251 ANDLYS-254, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-16; TYR-202 AND TYR-231,AND MASS SPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-231, AND MASSSPECTROMETRY.	15592455 [Abstract]