dbPTM

ARC1B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARC1B_MOUSE
UniProt AC	Q9WV32
Protein Name	Actin-related protein 2/3 complex subunit 1B
Gene Name	Arpc1b
Organism	Mus musculus (Mouse).
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	MAYHSFLVEPISCHAWNKDRTQIAICPNNHEVHIYEKSGAKWNKVHELKEHNGQVTGIDWAPESNRIVTCGTDRNAYVWTLKGRTWKPTLVILRINRAARCVRWAPNENKFAVGSGSRVISICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRIFSAYIKEVEERPAPTPWGSKMPFGELMFESSSSCGWVHGVCFSASGSRVAWVSHDSTVCLVDADKKMAVATLASETLPLLAVTFITENSLVAAGHDCFPVLFTYDNAAVTLSFGGRLDVPKQSSQRGMTARERFQNLDKKASSEGGAATGAGLDSLHKNSVSQISVLSGGKAKCSQFCTTGMDGGMSIWDVKSLESALKDLKIK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAYHSFLVE ------CCCEEEEEC	15.67	-
3	Phosphorylation	-----MAYHSFLVEP -----CCCEEEEECC	9.19	29514104
21	Phosphorylation	HAWNKDRTQIAICPN EEECCCCCEEEECCC	34.17	21659604
26	S-palmitoylation	DRTQIAICPNNHEVH CCCEEEECCCCCEEE	1.87	28526873
26	Glutathionylation	DRTQIAICPNNHEVH CCCEEEECCCCCEEE	1.87	24333276
35	Phosphorylation	NNHEVHIYEKSGAKW CCCEEEEEECCCCCC	11.48	25367039
41	Malonylation	IYEKSGAKWNKVHEL EEECCCCCCCCCEEH	55.62	26320211
70	Glutathionylation	ESNRIVTCGTDRNAY CCCCEEEEECCCCEE	3.70	24333276
80	Phosphorylation	DRNAYVWTLKGRTWK CCCEEEEEECCCCCC	14.46	19060867
82	Malonylation	NAYVWTLKGRTWKPT CEEEEEECCCCCCCE	38.68	26320211
82	Acetylation	NAYVWTLKGRTWKPT CEEEEEECCCCCCCE	38.68	22645737
87	Acetylation	TLKGRTWKPTLVILR EECCCCCCCEEEEEE	27.75	-
165	Acetylation	AAGSCDFKCRIFSAY EECCCCCEEEEEEEE	14.89	30985473
170	Phosphorylation	DFKCRIFSAYIKEVE CCEEEEEEEEEHHHH	20.14	-
174	Acetylation	RIFSAYIKEVEERPA EEEEEEEHHHHCCCC	42.93	66695507
174	Malonylation	RIFSAYIKEVEERPA EEEEEEEHHHHCCCC	42.93	26320211
174	Ubiquitination	RIFSAYIKEVEERPA EEEEEEEHHHHCCCC	42.93	-
280	Phosphorylation	DNAAVTLSFGGRLDV CCEEEEEEECCEECC	16.69	29899451
289	Malonylation	GGRLDVPKQSSQRGM CCEECCCCCCHHCCC	63.76	26320211
291	Phosphorylation	RLDVPKQSSQRGMTA EECCCCCCHHCCCCH	34.27	25338131
308	Malonylation	RFQNLDKKASSEGGA HHHHHHHHHHCCCCC	53.84	26320211
310	Phosphorylation	QNLDKKASSEGGAAT HHHHHHHHCCCCCCC	37.49	26824392
311	Phosphorylation	NLDKKASSEGGAATG HHHHHHHCCCCCCCC	45.16	27742792
317	Phosphorylation	SSEGGAATGAGLDSL HCCCCCCCCCCCHHH	27.34	25619855
330	Phosphorylation	SLHKNSVSQISVLSG HHHCCCCCEEEEEEC	22.93	29472430
333	Phosphorylation	KNSVSQISVLSGGKA CCCCCEEEEEECCEE	14.90	29472430
336	Phosphorylation	VSQISVLSGGKAKCS CCEEEEEECCEEEHH	43.26	29472430
346	Glutathionylation	KAKCSQFCTTGMDGG EEEHHHCCCCCCCCC	2.30	24333276
361	Phosphorylation	MSIWDVKSLESALKD CCHHHHHHHHHHHHH	36.90	25338131
367	Acetylation	KSLESALKDLKIK-- HHHHHHHHHCCCC--	61.81	-
367	Malonylation	KSLESALKDLKIK-- HHHHHHHHHCCCC--	61.81	26320211
367	Ubiquitination	KSLESALKDLKIK-- HHHHHHHHHCCCC--	61.81	-

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 ARC1B_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARC1B_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ARC1B_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of ARC1B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASSSPECTROMETRY.	19367708 [Abstract]