dbPTM

ARC1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARC1B_HUMAN
UniProt AC	O15143
Protein Name	Actin-related protein 2/3 complex subunit 1B
Gene Name	ARPC1B {ECO:0000312\|HGNC:HGNC:704}
Organism	Homo sapiens (Human).
Sequence Length	372
Subcellular Localization	Cytoplasm, cytoskeleton .
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	MAYHSFLVEPISCHAWNKDRTQIAICPNNHEVHIYEKSGAKWTKVHELKEHNGQVTGIDWAPESNRIVTCGTDRNAYVWTLKGRTWKPTLVILRINRAARCVRWAPNENKFAVGSGSRVISICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRIFSAYIKEVEERPAPTPWGSKMPFGELMFESSSSCGWVHGVCFSASGSRVAWVSHDSTVCLADADKKMAVATLASETLPLLALTFITDNSLVAAGHDCFPVLFTYDAAAGMLSFGGRLDVPKQSSQRGLTARERFQNLDKKASSEGGTAAGAGLDSLHKNSVSQISVLSGGKAKCSQFCTTGMDGGMSIWDVKSLESALKDLKIK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAYHSFLVE ------CCCEEEEEC	15.67	-
18	Acetylation	ISCHAWNKDRTQIAI CCEEEECCCCCEEEE	37.57	23749302
18	Ubiquitination	ISCHAWNKDRTQIAI CCEEEECCCCCEEEE	37.57	-
21	Phosphorylation	HAWNKDRTQIAICPN EEECCCCCEEEECCC	34.17	14749719
35	Phosphorylation	NNHEVHIYEKSGAKW CCCEEEEEECCCCCE	11.48	28152594
37	Acetylation	HEVHIYEKSGAKWTK CEEEEEECCCCCEEE	36.90	23749302
37	Ubiquitination	HEVHIYEKSGAKWTK CEEEEEECCCCCEEE	36.90	-
41	Acetylation	IYEKSGAKWTKVHEL EEECCCCCEEEEEEH	59.94	23749302
44	Acetylation	KSGAKWTKVHELKEH CCCCCEEEEEEHHHH	40.24	19608861
44	Ubiquitination	KSGAKWTKVHELKEH CCCCCEEEEEEHHHH	40.24	19608861
49	Ubiquitination	WTKVHELKEHNGQVT EEEEEEHHHHCCEEE	54.68	-
49	Malonylation	WTKVHELKEHNGQVT EEEEEEHHHHCCEEE	54.68	32601280
77	Phosphorylation	CGTDRNAYVWTLKGR EECCCCEEEEEECCC	10.48	-
80	Phosphorylation	DRNAYVWTLKGRTWK CCCEEEEEECCCCCC	14.46	22985185
82	Acetylation	NAYVWTLKGRTWKPT CEEEEEECCCCCCCE	38.68	23954790
82	Ubiquitination	NAYVWTLKGRTWKPT CEEEEEECCCCCCCE	38.68	21906983
85	Phosphorylation	VWTLKGRTWKPTLVI EEEECCCCCCCEEEE	46.65	20068231
87	Ubiquitination	TLKGRTWKPTLVILR EECCCCCCCEEEEEE	27.75	-
89	Phosphorylation	KGRTWKPTLVILRIN CCCCCCCEEEEEEEC	29.90	20068231
110	Ubiquitination	RWAPNENKFAVGSGS EECCCCCCEECCCCC	28.64	21890473
110	Acetylation	RWAPNENKFAVGSGS EECCCCCCEECCCCC	28.64	26051181
138	Ubiquitination	WWVCKHIKKPIRSTV EEEEEECCCCCEEEE	52.82	-
170	Phosphorylation	DFKCRIFSAYIKEVE CCEEEEEEEEEHHHH	20.14	20068231
172	Phosphorylation	KCRIFSAYIKEVEER EEEEEEEEEHHHHCC	16.01	28152594
174	Acetylation	RIFSAYIKEVEERPA EEEEEEEHHHHCCCC	42.93	23954790
174	Ubiquitination	RIFSAYIKEVEERPA EEEEEEEHHHHCCCC	42.93	-
183	Phosphorylation	VEERPAPTPWGSKMP HHCCCCCCCCCCCCC	33.51	-
187	Phosphorylation	PAPTPWGSKMPFGEL CCCCCCCCCCCCCCE	23.16	27251275
233	Acetylation	VCLADADKKMAVATL EEEECCCHHHHHHHH	46.28	25953088
289	Ubiquitination	GGRLDVPKQSSQRGL CCCCCCCCCCHHCCC	63.76	-
291	Phosphorylation	RLDVPKQSSQRGLTA CCCCCCCCHHCCCCH	34.27	22985185
292	Phosphorylation	LDVPKQSSQRGLTAR CCCCCCCHHCCCCHH	22.77	24719451
297	Phosphorylation	QSSQRGLTARERFQN CCHHCCCCHHHHHHC	26.88	22817900
307	2-Hydroxyisobutyrylation	ERFQNLDKKASSEGG HHHHCHHHHHHCCCC	54.10	-
307	Ubiquitination	ERFQNLDKKASSEGG HHHHCHHHHHHCCCC	54.10	-
307	Acetylation	ERFQNLDKKASSEGG HHHHCHHHHHHCCCC	54.10	27452117
308	Malonylation	RFQNLDKKASSEGGT HHHCHHHHHHCCCCC	53.84	32601280
308	Ubiquitination	RFQNLDKKASSEGGT HHHCHHHHHHCCCCC	53.84	-
310	Phosphorylation	QNLDKKASSEGGTAA HCHHHHHHCCCCCCC	37.49	29255136
311	Phosphorylation	NLDKKASSEGGTAAG CHHHHHHCCCCCCCC	45.16	23401153
315	Phosphorylation	KASSEGGTAAGAGLD HHHCCCCCCCCCCCH	24.96	21712546
323	Phosphorylation	AAGAGLDSLHKNSVS CCCCCCHHHHCCCCC	37.10	23403867
326	Ubiquitination	AGLDSLHKNSVSQIS CCCHHHHCCCCCEEE	57.10	-
326	Acetylation	AGLDSLHKNSVSQIS CCCHHHHCCCCCEEE	57.10	25953088
326	Methylation	AGLDSLHKNSVSQIS CCCHHHHCCCCCEEE	57.10	-
326	Malonylation	AGLDSLHKNSVSQIS CCCHHHHCCCCCEEE	57.10	26320211
328	Phosphorylation	LDSLHKNSVSQISVL CHHHHCCCCCEEEEE	28.13	20068231
330	Phosphorylation	SLHKNSVSQISVLSG HHHCCCCCEEEEEEC	22.93	20068231
333	Phosphorylation	KNSVSQISVLSGGKA CCCCCEEEEEECCEE	14.90	28857561
336	Phosphorylation	VSQISVLSGGKAKCS CCEEEEEECCEEEHH	43.26	25159151
339	Ubiquitination	ISVLSGGKAKCSQFC EEEEECCEEEHHHCC	48.47	-
341	Ubiquitination	VLSGGKAKCSQFCTT EEECCEEEHHHCCCC	37.59	-
355	Phosphorylation	TGMDGGMSIWDVKSL CCCCCCCCHHHHHHH	24.65	22817900
360	Ubiquitination	GMSIWDVKSLESALK CCCHHHHHHHHHHHH	47.02	-
361	Phosphorylation	MSIWDVKSLESALKD CCHHHHHHHHHHHHH	36.90	20873877
364	Phosphorylation	WDVKSLESALKDLKI HHHHHHHHHHHHCCC	44.16	23312004
367	2-Hydroxyisobutyrylation	KSLESALKDLKIK-- HHHHHHHHHCCCC--	61.81	-
367	Malonylation	KSLESALKDLKIK-- HHHHHHHHHCCCC--	61.81	26320211
367	Ubiquitination	KSLESALKDLKIK-- HHHHHHHHHCCCC--	61.81	-
367	Acetylation	KSLESALKDLKIK-- HHHHHHHHHCCCC--	61.81	25953088
370	Ubiquitination	ESALKDLKIK----- HHHHHHCCCC-----	59.59	-
372	Ubiquitination	ALKDLKIK------- HHHHCCCC-------	53.34	-

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
21	T	Phosphorylation	Kinase	AURKA	O14965	GPS
21	T	Phosphorylation	Kinase	PAK1	Q13153	PSP
21	T	Phosphorylation	Kinase	PAK1	O88643	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARC1B_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 ARC1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAK1_HUMAN	PAK1	physical	14749719
ARPC2_HUMAN	ARPC2	physical	20603326
AURKA_HUMAN	AURKA	physical	20603326
ARP3_HUMAN	ACTR3	physical	20603326
A4_HUMAN	APP	physical	21832049
ARP3_HUMAN	ACTR3	physical	22939629
ARP2_HUMAN	ACTR2	physical	22939629
ARPC4_HUMAN	ARPC4	physical	22939629
ARPC2_HUMAN	ARPC2	physical	22939629
ARPC5_HUMAN	ARPC5	physical	22939629
ARPC3_HUMAN	ARPC3	physical	22939629
ARP5L_HUMAN	ARPC5L	physical	22939629
SYAC_HUMAN	AARS	physical	22863883
ARP2_HUMAN	ACTR2	physical	22863883
ARP3_HUMAN	ACTR3	physical	22863883
ARPC2_HUMAN	ARPC2	physical	22863883
ARPC3_HUMAN	ARPC3	physical	22863883
GON7_HUMAN	C14orf142	physical	22863883
NC2B_HUMAN	DR1	physical	22863883
HSF1_HUMAN	HSF1	physical	22863883
IPO11_HUMAN	IPO11	physical	22863883
2A5D_HUMAN	PPP2R5D	physical	22863883
KAPCB_HUMAN	PRKACB	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
RFA2_HUMAN	RPA2	physical	22863883
TPD54_HUMAN	TPD52L2	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
UBE3A_HUMAN	UBE3A	physical	22863883
PFD3_HUMAN	VBP1	physical	22863883
ARPC2_HUMAN	ARPC2	physical	26186194
ARP5L_HUMAN	ARPC5L	physical	26186194
ARPC5_HUMAN	ARPC5	physical	26186194
ARP2_HUMAN	ACTR2	physical	26186194
ARPC3_HUMAN	ARPC3	physical	26186194
ARP3B_HUMAN	ACTR3B	physical	26186194
ARP3_HUMAN	ACTR3	physical	26186194
ARPC4_HUMAN	ARPC4	physical	26186194
POGK_HUMAN	POGK	physical	26186194
NT5C_HUMAN	NT5C	physical	26186194
ARP2_HUMAN	ACTR2	physical	26344197
ARP3_HUMAN	ACTR3	physical	26344197
ARPC2_HUMAN	ARPC2	physical	26344197
ARPC3_HUMAN	ARPC3	physical	26344197
ARPC5_HUMAN	ARPC5	physical	26344197
ARP5L_HUMAN	ARPC5L	physical	26344197
POGK_HUMAN	POGK	physical	28514442
ARP3B_HUMAN	ACTR3B	physical	28514442
NT5C_HUMAN	NT5C	physical	28514442
ARPC5_HUMAN	ARPC5	physical	28514442
ARP2_HUMAN	ACTR2	physical	28514442
ARPC2_HUMAN	ARPC2	physical	28514442
ARP3_HUMAN	ACTR3	physical	28514442
ARP5L_HUMAN	ARPC5L	physical	28514442
ARPC4_HUMAN	ARPC4	physical	28514442

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 ARC1B_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-44 AND LYS-82, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASSSPECTROMETRY.	17287340 [Abstract]