dbPTM

ACTY_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACTY_HUMAN
UniProt AC	P42025
Protein Name	Beta-centractin
Gene Name	ACTR1B
Organism	Homo sapiens (Human).
Sequence Length	376
Subcellular Localization	Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Description	Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome..
Protein Sequence	MESYDIIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHMRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFHTSAEFEVVRTIKERACYLSINPQKDEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MESYDIIA -------CCCCCEEC	7.52	22223895
3	Phosphorylation	-----MESYDIIANQ -----CCCCCEECCC	27.14	23401153
4	Nitrated tyrosine	----MESYDIIANQP ----CCCCCEECCCC	9.61	-
4	Phosphorylation	----MESYDIIANQP ----CCCCCEECCCC	9.61	23401153
4	Nitration	----MESYDIIANQP ----CCCCCEECCCC	9.61	-
17	Ubiquitination	QPVVIDNGSGVIKAG CCEEEECCCCEEECC	23.25	22817900
18	Phosphorylation	PVVIDNGSGVIKAGF CEEEECCCCEEECCC	35.82	23401153
22	Ubiquitination	DNGSGVIKAGFAGDQ ECCCCEEECCCCCCC	39.80	22817900
32	Acetylation	FAGDQIPKYCFPNYV CCCCCCCCCCCCCCC	57.17	25953088
32	Ubiquitination	FAGDQIPKYCFPNYV CCCCCCCCCCCCCCC	57.17	-
33	Phosphorylation	AGDQIPKYCFPNYVG CCCCCCCCCCCCCCC	8.25	29496907
38	Phosphorylation	PKYCFPNYVGRPKHM CCCCCCCCCCCCHHH	12.43	29496907
52	Ubiquitination	MRVMAGALEGDLFIG HHHHHHHEECCEEEC	8.06	22817900
61	Acetylation	GDLFIGPKAEEHRGL CCEEECCCCHHCCCC	64.32	26051181
61	Ubiquitination	GDLFIGPKAEEHRGL CCEEECCCCHHCCCC	64.32	22817900
75	Sulfoxidation	LLTIRYPMEHGVVRD CEEEECCCCCCCCCC	4.38	30846556
96	Ubiquitination	IWQYVYSKDQLQTFS HHHHHCCHHHHHCCC	31.63	22817900
119	Ubiquitination	EAPLNPSKNREKAAE ECCCCCCCCHHHHHH	62.37	29967540
171	Phosphorylation	VTHAVPIYEGFAMPH CEEEEEEECCCCCCC	12.15	82341
230	Ubiquitination	YLSINPQKDEALETE EEEECCCCCCHHHEE	59.81	29967540
234	Ubiquitination	NPQKDEALETEKVQY CCCCCCHHHEEEEEE	8.66	23000965
238	Ubiquitination	DEALETEKVQYTLPD CCHHHEEEEEEECCC	41.90	29967540
247	Phosphorylation	QYTLPDGSTLDVGPA EEECCCCCCEECCCC	32.93	46158797
248	Phosphorylation	YTLPDGSTLDVGPAR EECCCCCCEECCCCC	32.29	46158803
264	Ubiquitination	RAPELLFQPDLVGDE CCCHHHCCCCCCCCC	30.48	23000965
293	Phosphorylation	SDMDLRRTLFANIVL CCHHHHHHHHHHEEE	21.57	63738509
304	Phosphorylation	NIVLSGGSTLFKGFG HEEECCCCHHHCCHH	26.01	29138933
305	Phosphorylation	IVLSGGSTLFKGFGD EEECCCCHHHCCHHH	39.22	21712546
308	Ubiquitination	SGGSTLFKGFGDRLL CCCCHHHCCHHHHHH	57.34	23000965
313	Methylation	LFKGFGDRLLSEVKK HHCCHHHHHHHHHHH	37.60	-
319	Ubiquitination	DRLLSEVKKLAPKDI HHHHHHHHHHCCCCC	37.71	-
319	Malonylation	DRLLSEVKKLAPKDI HHHHHHHHHHCCCCC	37.71	26320211
319	Acetylation	DRLLSEVKKLAPKDI HHHHHHHHHHCCCCC	37.71	25953088
320	Ubiquitination	RLLSEVKKLAPKDIK HHHHHHHHHCCCCCE	55.87	-
338	Phosphorylation	SAPQERLYSTWIGGS CCCHHHHHCCCHHHH	15.41	-

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 ACTY_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
DCTN2_HUMAN	DCTN2	physical	22939629
ACTZ_HUMAN	ACTR1A	physical	22939629
DCTN3_HUMAN	DCTN3	physical	22939629
ARP10_HUMAN	ACTR10	physical	22863883
ACTZ_HUMAN	ACTR1A	physical	22863883
LMNB1_HUMAN	LMNB1	physical	22863883
RABE1_HUMAN	RABEP1	physical	22863883
SEH1_HUMAN	SEH1L	physical	22863883
DCTN3_HUMAN	DCTN3	physical	26186194
TCPD_HUMAN	CCT4	physical	26186194
DCTN4_HUMAN	DCTN4	physical	26186194
ACTZ_HUMAN	ACTR1A	physical	26186194
ARP10_HUMAN	ACTR10	physical	26186194
DCTN5_HUMAN	DCTN5	physical	26186194
TCPG_HUMAN	CCT3	physical	26186194
DCTN6_HUMAN	DCTN6	physical	26186194
SCPDL_HUMAN	SCCPDH	physical	26186194
TCPH_HUMAN	CCT7	physical	26186194
GELS_HUMAN	GSN	physical	26186194
TCPW_HUMAN	CCT6B	physical	26186194
TCPZ_HUMAN	CCT6A	physical	26186194
TCPB_HUMAN	CCT2	physical	26186194
PDCL3_HUMAN	PDCL3	physical	26186194
ADSV_HUMAN	SCIN	physical	26186194
DCTN1_HUMAN	DCTN1	physical	26186194
ARP10_HUMAN	ACTR10	physical	26344197
TCPB_HUMAN	CCT2	physical	26344197
CYFP1_HUMAN	CYFIP1	physical	26344197
DCTN1_HUMAN	DCTN1	physical	26344197
DCTN2_HUMAN	DCTN2	physical	26344197
DCTN5_HUMAN	DCTN5	physical	26344197
KDM2A_HUMAN	KDM2A	physical	26344197
PACN3_HUMAN	PACSIN3	physical	26344197
SCYL1_HUMAN	SCYL1	physical	26344197
ADSV_HUMAN	SCIN	physical	28514442
ARP10_HUMAN	ACTR10	physical	28514442
ACTZ_HUMAN	ACTR1A	physical	28514442
DCTN4_HUMAN	DCTN4	physical	28514442
DCTN5_HUMAN	DCTN5	physical	28514442
GELS_HUMAN	GSN	physical	28514442
DCTN3_HUMAN	DCTN3	physical	28514442
PDCL3_HUMAN	PDCL3	physical	28514442
SCPDL_HUMAN	SCCPDH	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
TCPH_HUMAN	CCT7	physical	28514442
TCPG_HUMAN	CCT3	physical	28514442
CAPZB_HUMAN	CAPZB	physical	28514442
DCTN2_HUMAN	DCTN2	physical	27173435

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 ACTY_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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]