ARP6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARP6_HUMAN
• UniProt AC: Q9GZN1
• Protein Name: Actin-related protein 6
• Gene Name: ACTR6
• Organism: Homo sapiens (Human).
• Sequence Length: 396
• Subcellular Localization: Cytoplasm, cytoskeleton. Nucleus . Colocalizes with HP1 family proteins at pericentric heterochromatin.
• Protein Sequence: MTTLVLDNGAYNAKIGYSHENVSVIPNCQFRSKTARLKTFTANQIDEIKDPSGLFYILPFQKGYLVNWDVQRQVWDYLFGKEMYQVDFLDTNIIITEPYFNFTSIQESMNEILFEEYQFQAVLRVNAGALSAHRYFRDNPSELCCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGKLLTNHLKEIISYRQLHVMDETHVINQVKEDVCYVSQDFYRDMDIAKLKGEENTVMIDYVLPDFSTIKKGFCKPREEMVLSGKYKSGEQILRLANERFAVPEILFNPSDIGIQEMGIPEAIVYSIQNLPEEMQPHFFKNIVLTGGNSLFPGFRDRVYSEVRCLTPTDYDVSVVLPENPITYAWEGGKLISENDDFEDMVVTREDYEENGHSVCEEKFDI

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTTLVLDNG ------CCEEEECCC	28.92	19413330
33	Ubiquitination	PNCQFRSKTARLKTF CCCEECCCCEECEEE	41.78	22817900
38	Ubiquitination	RSKTARLKTFTANQI CCCCEECEEEEHHHC	35.72	21890473
38	Ubiquitination	RSKTARLKTFTANQI CCCCEECEEEEHHHC	35.72	21890473
38	Ubiquitination	RSKTARLKTFTANQI CCCCEECEEEEHHHC	35.72	21906983
49	Ubiquitination	ANQIDEIKDPSGLFY HHHCCCCCCCCCCEE	62.63	22817900
70	Ubiquitination	GYLVNWDVQRQVWDY CEEECHHHHHHHHHH	3.69	21890473
84	Phosphorylation	YLFGKEMYQVDFLDT HHHCCEEEEEEEEEC	13.38	26074081
91	Phosphorylation	YQVDFLDTNIIITEP EEEEEEECCEEEEEC	30.39	26074081
96	Phosphorylation	LDTNIIITEPYFNFT EECCEEEEECCCCCC	22.09	26074081
99	Phosphorylation	NIIITEPYFNFTSIQ CEEEEECCCCCCCHH	12.62	26074081
116	Ubiquitination	MNEILFEEYQFQAVL HHHHHCHHHHHHHHH	36.98	27667366
152	Ubiquitination	CIIVDSGYSFTHIVP EEEECCCCCEEEEHH	12.45	27667366
154	Ubiquitination	IVDSGYSFTHIVPYC EECCCCCEEEEHHHH	4.31	27667366
178	Ubiquitination	IRINVGGKLLTNHLK EEEECCCHHHHHHHH	34.10	21906983
178	Ubiquitination	IRINVGGKLLTNHLK EEEECCCHHHHHHHH	34.10	21890473
185	Ubiquitination	KLLTNHLKEIISYRQ HHHHHHHHHHHHHHH	39.04	-
224	Ubiquitination	YRDMDIAKLKGEENT HHCCCHHHHCCCCCE	51.57	27667366
236	Phosphorylation	ENTVMIDYVLPDFST CCEEEEEEECCCHHH	7.92	46158869
245	Ubiquitination	LPDFSTIKKGFCKPR CCCHHHCCCCCCCCH	47.10	29967540
246	Ubiquitination	PDFSTIKKGFCKPRE CCHHHCCCCCCCCHH	54.06	-
260	Ubiquitination	EEMVLSGKYKSGEQI HHEEEEECCCCHHHH	46.24	27667366
260	Acetylation	EEMVLSGKYKSGEQI HHEEEEECCCCHHHH	46.24	19608861
262	Ubiquitination	MVLSGKYKSGEQILR EEEEECCCCHHHHHH	56.31	33845483
367	Phosphorylation	WEGGKLISENDDFED EECCEEECCCCCHHC	40.56	110758101
388	Phosphorylation	DYEENGHSVCEEKFD HHHHCCCCCCCCCCC	29.84	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ARP6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ARP6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ARP6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DMAP1_HUMAN	DMAP1	physical	26186194
SRCAP_HUMAN	SRCAP	physical	26186194
ZNHI1_HUMAN	ZNHIT1	physical	26186194
CHMP5_HUMAN	CHMP5	physical	26344197
PUS7_HUMAN	PUS7	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
1433E_HUMAN	YWHAE	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	28514442
RUVB2_HUMAN	RUVBL2	physical	28514442
ZNHI1_HUMAN	ZNHIT1	physical	28514442
SRCAP_HUMAN	SRCAP	physical	28514442
DMAP1_HUMAN	DMAP1	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-260, AND MASS SPECTROMETRY.
PubMed: 19608861