dbPTM

ACTBL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACTBL_HUMAN
UniProt AC	Q562R1
Protein Name	Beta-actin-like protein 2
Gene Name	ACTBL2
Organism	Homo sapiens (Human).
Sequence Length	376
Subcellular Localization	Cytoplasm, cytoskeleton.
Protein Description	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells..
Protein Sequence	MTDNELSALVVDNGSGMCKAGFGGDDAPRAVFPSMIGRPRHQGVMVGMGQKDCYVGDEAQSKRGVLTLKYPIEHGVVTNWDDMEKIWYHTFYNELRVAPDEHPILLTEAPLNPKINREKMTQIMFEAFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHIVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYNFTTTAEREIVRDVKEKLCYVALDFEQEMVRAAASSSPERSYELPDGQVITIGNERFRCPEAIFQPSFLGIESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGSTMYPGIADRMQKEIITLAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPPIVHRKCF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTDNELSAL ------CCHHCCEEE	47.75	46105115
7	Phosphorylation	-MTDNELSALVVDNG -CCHHCCEEEEEECC	17.24	46105121
15	Phosphorylation	ALVVDNGSGMCKAGF EEEEECCCCCCCCCC	29.61	46105127
45	Sulfoxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	28183972
45	Oxidation	RPRHQGVMVGMGQKD CCCCCCEEEECCCCC	2.49	-
48	Sulfoxidation	HQGVMVGMGQKDCYV CCCEEEECCCCCEEC	3.32	28183972
48	Oxidation	HQGVMVGMGQKDCYV CCCEEEECCCCCEEC	3.32	-
51	Ubiquitination	VMVGMGQKDCYVGDE EEEECCCCCEECCCH	44.00	21906983
51	Methylation	VMVGMGQKDCYVGDE EEEECCCCCEECCCH	44.00	-
51	Acetylation	VMVGMGQKDCYVGDE EEEECCCCCEECCCH	44.00	160847
54	Phosphorylation	GMGQKDCYVGDEAQS ECCCCCEECCCHHHC	20.01	29396449
61	Phosphorylation	YVGDEAQSKRGVLTL ECCCHHHCCCCEEEE	31.22	29083192
62	Ubiquitination	VGDEAQSKRGVLTLK CCCHHHCCCCEEEEE	40.88	23503661
62	Acetylation	VGDEAQSKRGVLTLK CCCHHHCCCCEEEEE	40.88	30584977
69	Methylation	KRGVLTLKYPIEHGV CCCEEEEECEECCCC	43.69	23644510
69	Trimethylation	KRGVLTLKYPIEHGV CCCEEEEECEECCCC	43.69	-
70	Phosphorylation	RGVLTLKYPIEHGVV CCEEEEECEECCCCC	16.74	7941957
107	Phosphorylation	DEHPILLTEAPLNPK CCCCEEEECCCCCCC	27.01	28857561
121	Phosphorylation	KINREKMTQIMFEAF CCCHHHHHHHHHHHC	26.47	28464451
134	Phosphorylation	AFNTPAMYVAIQAVL HCCCHHHHHHHHHHH	6.71	28464451
144	Phosphorylation	IQAVLSLYASGRTTG HHHHHHHHHCCCCEE	8.71	30803939
149	Phosphorylation	SLYASGRTTGIVMDS HHHHCCCCEEEEEEC	32.66	30140170
150	Phosphorylation	LYASGRTTGIVMDSG HHHCCCCEEEEEECC	24.45	30140170
156	Phosphorylation	TTGIVMDSGDGVTHI CEEEEEECCCCEEEE	22.23	30140170
161	Phosphorylation	MDSGDGVTHIVPIYE EECCCCEEEEEEEEC	16.06	20058876
170	Phosphorylation	IVPIYEGYALPHAIL EEEEECCCCHHHHHH	7.94	20058876
187	Phosphorylation	DLAGRDLTDYLMKIL HHCCCCHHHHHHHHH	27.21	28152594
189	Phosphorylation	AGRDLTDYLMKILTE CCCCHHHHHHHHHHH	11.94	26846344
191	Sulfoxidation	RDLTDYLMKILTERG CCHHHHHHHHHHHCC	1.75	31801345
192	Acetylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	22646691
192	Ubiquitination	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	21906983
192	Ubiquitination	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	21890473
192	Methylation	DLTDYLMKILTERGY CHHHHHHHHHHHCCC	31.78	-
199	Phosphorylation	KILTERGYNFTTTAE HHHHHCCCCCCCCHH	17.21	23403867
219	Phosphorylation	DVKEKLCYVALDFEQ HHHHHHHEEECCCCH	10.13	150045
234	Phosphorylation	EMVRAAASSSPERSY HHHHHHHCCCCCCCE	26.99	28634120
240	Phosphorylation	ASSSPERSYELPDGQ HCCCCCCCEECCCCC	22.69	29255136
241	Phosphorylation	SSSPERSYELPDGQV CCCCCCCEECCCCCE	27.92	29255136
250	Phosphorylation	LPDGQVITIGNERFR CCCCCEEEECCCEEC	24.79	26846344
266	Phosphorylation	PEAIFQPSFLGIESS CHHHHCCHHCCCCCC	23.48	26657352
272	Phosphorylation	PSFLGIESSGIHETT CHHCCCCCCCCCCCC	31.76	27174698
273	Phosphorylation	SFLGIESSGIHETTF HHCCCCCCCCCCCCH	29.04	26657352
278	Phosphorylation	ESSGIHETTFNSIMK CCCCCCCCCHHHHHC	23.64	27174698
279	Phosphorylation	SSGIHETTFNSIMKC CCCCCCCCHHHHHCC	20.17	27174698
282	Phosphorylation	IHETTFNSIMKCDVD CCCCCHHHHHCCCCC	21.62	27174698
285	Ubiquitination	TTFNSIMKCDVDIRK CCHHHHHCCCCCCCC	26.13	22817900
286	S-nitrosylation	TFNSIMKCDVDIRKD CHHHHHCCCCCCCCH	3.22	2212679
286	S-palmitoylation	TFNSIMKCDVDIRKD CHHHHHCCCCCCCCH	3.22	29575903
292	Ubiquitination	KCDVDIRKDLYANTV CCCCCCCCHHHCCCE	53.04	27667366
292	Sumoylation	KCDVDIRKDLYANTV CCCCCCCCHHHCCCE	53.04	-
295	Phosphorylation	VDIRKDLYANTVLSG CCCCCHHHCCCEECC	14.13	24114839
298	Phosphorylation	RKDLYANTVLSGGST CCHHHCCCEECCCCC	18.04	62150881
301	Phosphorylation	LYANTVLSGGSTMYP HHCCCEECCCCCCCC	36.45	22210691
304	Phosphorylation	NTVLSGGSTMYPGIA CCEECCCCCCCCCHH	17.33	24114839
305	Phosphorylation	TVLSGGSTMYPGIAD CEECCCCCCCCCHHH	24.81	50563301
307	Phosphorylation	LSGGSTMYPGIADRM ECCCCCCCCCHHHHH	9.82	1950603
313	Methylation	MYPGIADRMQKEIIT CCCCHHHHHHHHHHE	22.02	-
320	Phosphorylation	RMQKEIITLAPSTMK HHHHHHHEECCCCCE	23.64	46105145
324	Phosphorylation	EIITLAPSTMKIKII HHHEECCCCCEEEEE	35.21	46105151
327	Ubiquitination	TLAPSTMKIKIIAPP EECCCCCEEEEECCC	40.72	22817900
329	Neddylation	APSTMKIKIIAPPER CCCCCEEEEECCCCC	23.65	32015554
329	Sumoylation	APSTMKIKIIAPPER CCCCCEEEEECCCCC	23.65	-
329	Acetylation	APSTMKIKIIAPPER CCCCCEEEEECCCCC	23.65	7629233
329	Sumoylation	APSTMKIKIIAPPER CCCCCEEEEECCCCC	23.65	-
329	Ubiquitination	APSTMKIKIIAPPER CCCCCEEEEECCCCC	23.65	21906983
337	Ubiquitination	IIAPPERKYSVWIGG EECCCCCCEEEEECH	39.97	25015289
337	Sumoylation	IIAPPERKYSVWIGG EECCCCCCEEEEECH	39.97	-
349	Phosphorylation	IGGSILASLSTFQQM ECHHHHHHHHHHHHH	21.29	-
356	Sulfoxidation	SLSTFQQMWISKQEY HHHHHHHHHHHHHHH	2.09	28183972

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 ACTBL_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
45	M	Oxidation	-
Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
48	M	Oxidation	-
Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization.
85	K	Methylation	-
Monomethylation at Lys-85 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes.

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 ACTBL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRK1_HUMAN	BRK1	physical	22863883
CAP1_HUMAN	CAP1	physical	22863883
CDN2A_HUMAN	CDKN2A	physical	22863883
ARF_HUMAN	CDKN2A	physical	22863883
MCM3_HUMAN	MCM3	physical	22863883
M3K4_HUMAN	MAP3K4	physical	28514442
PDCL3_HUMAN	PDCL3	physical	28514442
POTEF_HUMAN	POTEF	physical	28514442
BCL7B_HUMAN	BCL7B	physical	28514442
TCPH_HUMAN	CCT7	physical	28514442
LRC20_HUMAN	LRRC20	physical	28514442
GELS_HUMAN	GSN	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
DNLZ_HUMAN	DNLZ	physical	28514442
SRCAP_HUMAN	SRCAP	physical	28514442
TCPB_HUMAN	CCT2	physical	28514442
MYO6_HUMAN	MYO6	physical	28514442
DCTN3_HUMAN	DCTN3	physical	28514442
TCPW_HUMAN	CCT6B	physical	28514442
SMRD1_HUMAN	SMARCD1	physical	28514442
TCPG_HUMAN	CCT3	physical	28514442
ARP10_HUMAN	ACTR10	physical	28514442
TCPD_HUMAN	CCT4	physical	28514442
SMCA2_HUMAN	SMARCA2	physical	28514442
TCPZ_HUMAN	CCT6A	physical	28514442
TCPQ_HUMAN	CCT8	physical	28514442
YETS4_HUMAN	YEATS4	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 ACTBL_HUMAN

Related Literatures of Post-Translational Modification

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