dbPTM

ACTN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACTN1_HUMAN
UniProt AC	P12814
Protein Name	Alpha-actinin-1
Gene Name	ACTN1
Organism	Homo sapiens (Human).
Sequence Length	892
Subcellular Localization	Cytoplasm, cytoskeleton . Cytoplasm, myofibril, sarcomere, Z line . Cell membrane . Cell junction . Cell projection, ruffle . Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and c
Protein Description	F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein..
Protein Sequence	MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMHAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQVEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHARQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITMDELRRELPPDQAEYCIARMAPYTGPDSVPGALDYMSFSTALYGESDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDHYDSQQ -------CCCCCCCC	6.90	21406692
1	Sulfoxidation	-------MDHYDSQQ -------CCCCCCCC	6.90	28465586
4	Phosphorylation	----MDHYDSQQTND ----CCCCCCCCCCC	17.02	23663014
6	Phosphorylation	--MDHYDSQQTNDYM --CCCCCCCCCCCCC	19.61	24043423
9	Phosphorylation	DHYDSQQTNDYMQPE CCCCCCCCCCCCCCH	23.55	23663014
12	Dephosphorylation	DSQQTNDYMQPEEDW CCCCCCCCCCCHHHC	10.34	16291744
12	Phosphorylation	DSQQTNDYMQPEEDW CCCCCCCCCCCHHHC	10.34	20940419
31	Ubiquitination	LLDPAWEKQQRKTFT CCCHHHHHHHHHHHH	40.82	-
35	Ubiquitination	AWEKQQRKTFTAWCN HHHHHHHHHHHHHHH	43.59	21890473
35	Ubiquitination	AWEKQQRKTFTAWCN HHHHHHHHHHHHHHH	43.59	21890473
35	Ubiquitination	AWEKQQRKTFTAWCN HHHHHHHHHHHHHHH	43.59	21890473
35	Ubiquitination	AWEKQQRKTFTAWCN HHHHHHHHHHHHHHH	43.59	21890473
35	Ubiquitination	AWEKQQRKTFTAWCN HHHHHHHHHHHHHHH	43.59	21890473
36	Phosphorylation	WEKQQRKTFTAWCNS HHHHHHHHHHHHHHH	28.54	26437602
38	Phosphorylation	KQQRKTFTAWCNSHL HHHHHHHHHHHHHHH	25.20	26437602
41	S-palmitoylation	RKTFTAWCNSHLRKA HHHHHHHHHHHHHHH	3.29	26865113
43	Phosphorylation	TFTAWCNSHLRKAGT HHHHHHHHHHHHHCH	22.29	26437602
47	Ubiquitination	WCNSHLRKAGTQIEN HHHHHHHHHCHHHHC	58.49	-
50	Phosphorylation	SHLRKAGTQIENIEE HHHHHHCHHHHCHHH	31.10	16097034
64	Ubiquitination	EDFRDGLKLMLLLEV HHCHHHHHHHHHHHH	37.06	-
73	Phosphorylation	MLLLEVISGERLAKP HHHHHHHCCCCCCCC	39.51	-
89	Ubiquitination	RGKMRVHKISNVNKA CCCCCEEECCCHHHH	45.00	-
91	Phosphorylation	KMRVHKISNVNKALD CCCEEECCCHHHHHH	39.26	23403867
95	Acetylation	HKISNVNKALDFIAS EECCCHHHHHHHHHH	46.15	19608861
102	Phosphorylation	KALDFIASKGVKLVS HHHHHHHHCCCEEEE	25.73	63745159
103	Ubiquitination	ALDFIASKGVKLVSI HHHHHHHCCCEEEEE	59.71	-
103	Ubiquitination	ALDFIASKGVKLVSI HHHHHHHCCCEEEEE	59.71	-
109	Phosphorylation	SKGVKLVSIGAEEIV HCCCEEEEECCHHEE	26.24	27251275
123	Phosphorylation	VDGNVKMTLGMIWTI ECCCCHHHHHHHHHH	17.91	-
140	Phosphorylation	RFAIQDISVEETSAK HHHHHCCCCCCCCHH	31.59	19664994
144	Phosphorylation	QDISVEETSAKEGLL HCCCCCCCCHHHCEE	22.07	23927012
145	Phosphorylation	DISVEETSAKEGLLL CCCCCCCCHHHCEEH	40.39	23927012
154	Glutathionylation	KEGLLLWCQRKTAPY HHCEEHHHCCCCCCC	2.57	22555962
154	S-nitrosylation	KEGLLLWCQRKTAPY HHCEEHHHCCCCCCC	2.57	25040305
154	S-palmitoylation	KEGLLLWCQRKTAPY HHCEEHHHCCCCCCC	2.57	29575903
162	Malonylation	QRKTAPYKNVNIQNF CCCCCCCCCCCCCEE	54.05	26320211
162	Ubiquitination	QRKTAPYKNVNIQNF CCCCCCCCCCCCCEE	54.05	-
172	Phosphorylation	NIQNFHISWKDGLGF CCCEEEEEECCCCHH	21.36	26657352
193	Phosphorylation	HRPELIDYGKLRKDD CCHHHHCCCCCCCCC	14.79	21082442
195	Acetylation	PELIDYGKLRKDDPL HHHHCCCCCCCCCCC	38.60	-
195	Acetylation	PELIDYGKLRKDDPL HHHHCCCCCCCCCCC	38.60	19608861
195	Ubiquitination	PELIDYGKLRKDDPL HHHHCCCCCCCCCCC	38.60	-
198	Acetylation	IDYGKLRKDDPLTNL HCCCCCCCCCCCCCC	76.54	-
198	Acetylation	IDYGKLRKDDPLTNL HCCCCCCCCCCCCCC	76.54	23236377
198	Malonylation	IDYGKLRKDDPLTNL HCCCCCCCCCCCCCC	76.54	26320211
198	Ubiquitination	IDYGKLRKDDPLTNL HCCCCCCCCCCCCCC	76.54	-
203	Phosphorylation	LRKDDPLTNLNTAFD CCCCCCCCCCHHHHH	42.94	28851738
207	Phosphorylation	DPLTNLNTAFDVAEK CCCCCCHHHHHHHHH	31.69	28851738
214	Ubiquitination	TAFDVAEKYLDIPKM HHHHHHHHHCCCCCC	41.18	-
214	Ubiquitination	TAFDVAEKYLDIPKM HHHHHHHHHCCCCCC	41.18	-
214 (in isoform 2)	Ubiquitination	-	41.18	-
215	Phosphorylation	AFDVAEKYLDIPKML HHHHHHHHCCCCCCC	10.91	23403867
220	Ubiquitination	EKYLDIPKMLDAEDI HHHCCCCCCCCHHHH	53.05	-
221	Sulfoxidation	KYLDIPKMLDAEDIV HHCCCCCCCCHHHHC	3.25	30846556
230	Phosphorylation	DAEDIVGTARPDEKA CHHHHCCCCCCCHHH	14.48	26657352
240	Phosphorylation	PDEKAIMTYVSSFYH CCHHHHHHHHHHHHH	18.04	28152594
241	Phosphorylation	DEKAIMTYVSSFYHA CHHHHHHHHHHHHHH	4.87	28152594
243	Phosphorylation	KAIMTYVSSFYHAFS HHHHHHHHHHHHHHH	12.33	26657352
244	Phosphorylation	AIMTYVSSFYHAFSG HHHHHHHHHHHHHHC	21.56	28152594
246	Phosphorylation	MTYVSSFYHAFSGAQ HHHHHHHHHHHHCHH	8.32	22617229
250	Phosphorylation	SSFYHAFSGAQKAET HHHHHHHHCHHHHHH	33.72	22617229
257	Phosphorylation	SGAQKAETAANRICK HCHHHHHHHHHHHHH	35.61	25348954
261	Methylation	KAETAANRICKVLAV HHHHHHHHHHHHHHH	30.84	-
264	Malonylation	TAANRICKVLAVNQE HHHHHHHHHHHHCHH	37.60	26320211
276	Sulfoxidation	NQENEQLMEDYEKLA CHHHHHHHHHHHHHH	3.53	28465586
279	Phosphorylation	NEQLMEDYEKLASDL HHHHHHHHHHHHHHH	11.14	110740947
284	Phosphorylation	EDYEKLASDLLEWIR HHHHHHHHHHHHHHH	38.95	23403867
291	Methylation	SDLLEWIRRTIPWLE HHHHHHHHHHCHHHH	30.66	-
293	O-linked_Glycosylation	LLEWIRRTIPWLENR HHHHHHHHCHHHHHC	22.88	23301498
306	Sulfoxidation	NRVPENTMHAMQQKL HCCCHHHHHHHHHHH	2.60	30846556
309	Sulfoxidation	PENTMHAMQQKLEDF CHHHHHHHHHHHHHH	2.35	30846556
319	Phosphorylation	KLEDFRDYRRLHKPP HHHHHHHHHHHCCCC	8.06	28152594
324	Ubiquitination	RDYRRLHKPPKVQEK HHHHHHCCCCCHHHC	68.55	-
327	Ubiquitination	RRLHKPPKVQEKCQL HHHCCCCCHHHCEEE	66.14	-
331	Ubiquitination	KPPKVQEKCQLEINF CCCCHHHCEEEEEEC	15.36	21890473
331	Ubiquitination	KPPKVQEKCQLEINF CCCCHHHCEEEEEEC	15.36	21890473
332	S-nitrosocysteine	PPKVQEKCQLEINFN CCCHHHCEEEEEECC	5.70	-
332	Glutathionylation	PPKVQEKCQLEINFN CCCHHHCEEEEEECC	5.70	22555962
332	S-nitrosylation	PPKVQEKCQLEINFN CCCHHHCEEEEEECC	5.70	20140087
332	S-palmitoylation	PPKVQEKCQLEINFN CCCHHHCEEEEEECC	5.70	29575903
340	Phosphorylation	QLEINFNTLQTKLRL EEEEECCHHHHHHHH	18.99	26657352
343	Phosphorylation	INFNTLQTKLRLSNR EECCHHHHHHHHHCC	34.85	21712546
348	Phosphorylation	LQTKLRLSNRPAFMP HHHHHHHHCCCCCCC	25.10	54885953
354	Sulfoxidation	LSNRPAFMPSEGRMV HHCCCCCCCCCCCCC	3.76	28465586
356	Phosphorylation	NRPAFMPSEGRMVSD CCCCCCCCCCCCCCH	40.68	27251275
360	Sulfoxidation	FMPSEGRMVSDINNA CCCCCCCCCCHHHHH	5.07	28465586
362	Phosphorylation	PSEGRMVSDINNAWG CCCCCCCCHHHHHHH	24.35	57405029
378	Phosphorylation	LEQVEKGYEEWLLNE HHHHHHHHHHHHHHH	23.03	110740955
398	Ubiquitination	RLDHLAEKFRQKASI HHHHHHHHHHHHHHH	39.99	21890473
398	Ubiquitination	RLDHLAEKFRQKASI HHHHHHHHHHHHHHH	39.99	21890473
398	Acetylation	RLDHLAEKFRQKASI HHHHHHHHHHHHHHH	39.99	-
398	Ubiquitination	RLDHLAEKFRQKASI HHHHHHHHHHHHHHH	39.99	21890473
398	Acetylation	RLDHLAEKFRQKASI HHHHHHHHHHHHHHH	39.99	130093
398	Ubiquitination	RLDHLAEKFRQKASI HHHHHHHHHHHHHHH	39.99	21890473
398	Ubiquitination	RLDHLAEKFRQKASI HHHHHHHHHHHHHHH	39.99	21890473
402	Ubiquitination	LAEKFRQKASIHEAW HHHHHHHHHHHHHHC	39.58	21890473
402	Ubiquitination	LAEKFRQKASIHEAW HHHHHHHHHHHHHHC	39.58	21890473
404	Phosphorylation	EKFRQKASIHEAWTD HHHHHHHHHHHHCCC	31.36	26657352
410	Phosphorylation	ASIHEAWTDGKEAML HHHHHHCCCHHHHHH	41.75	23927012
413	Ubiquitination	HEAWTDGKEAMLRQK HHHCCCHHHHHHHHC	45.14	-
420	Malonylation	KEAMLRQKDYETATL HHHHHHHCCHHHCHH	56.71	26320211
422	Phosphorylation	AMLRQKDYETATLSE HHHHHCCHHHCHHHH	23.40	28152594
424	Phosphorylation	LRQKDYETATLSEIK HHHCCHHHCHHHHHH	20.79	26657352
426	Phosphorylation	QKDYETATLSEIKAL HCCHHHCHHHHHHHH	37.93	28152594
428	Phosphorylation	DYETATLSEIKALLK CHHHCHHHHHHHHHH	32.68	54885897
431	Ubiquitination	TATLSEIKALLKKHE HCHHHHHHHHHHHHH	29.00	-
436	Acetylation	EIKALLKKHEAFESD HHHHHHHHHHHHHHH	46.80	-
436	Ubiquitination	EIKALLKKHEAFESD HHHHHHHHHHHHHHH	46.80	-
442	Phosphorylation	KKHEAFESDLAAHQD HHHHHHHHHHHHCHH	31.32	26657352
466	Phosphorylation	QELNELDYYDSPSVN HHHHHCCCCCCCCHH	23.07	110740971
467	Phosphorylation	ELNELDYYDSPSVNA HHHHCCCCCCCCHHH	15.04	46158695
471	Phosphorylation	LDYYDSPSVNARCQK CCCCCCCCHHHHHHH	31.77	26657352
478	Acetylation	SVNARCQKICDQWDN CHHHHHHHHHHHHHH	49.26	25953088
478	Ubiquitination	SVNARCQKICDQWDN CHHHHHHHHHHHHHH	49.26	-
480	S-nitrosocysteine	NARCQKICDQWDNLG HHHHHHHHHHHHHHH	4.02	-
480	Glutathionylation	NARCQKICDQWDNLG HHHHHHHHHHHHHHH	4.02	22555962
480	S-nitrosylation	NARCQKICDQWDNLG HHHHHHHHHHHHHHH	4.02	20140087
492	Acetylation	NLGALTQKRREALER HHHHHHHHHHHHHHH	48.46	25953088
492	Malonylation	NLGALTQKRREALER HHHHHHHHHHHHHHH	48.46	26320211
492	Ubiquitination	NLGALTQKRREALER HHHHHHHHHHHHHHH	48.46	-
502	Ubiquitination	EALERTEKLLETIDQ HHHHHHHHHHHHHHH	58.73	-
511	Phosphorylation	LETIDQLYLEYAKRA HHHHHHHHHHHHHHH	7.58	27642862
514	Phosphorylation	IDQLYLEYAKRAAPF HHHHHHHHHHHHCCC	18.15	25884760
516	Ubiquitination	QLYLEYAKRAAPFNN HHHHHHHHHHCCCCH	41.49	-
516 (in isoform 2)	Ubiquitination	-	41.49	-
563	Acetylation	ATLPDADKERLAILG HHCCCCCHHHHEEEE	46.59	25953088
576	Phosphorylation	LGIHNEVSKIVQTYH EEECHHHHHHHHHCC	15.53	23312004
582	Phosphorylation	VSKIVQTYHVNMAGT HHHHHHHCCCCCCCC	6.15	75139
633	Ubiquitination	QHNERLRKQFGAQAN HHHHHHHHHHCCCCC	55.35	21890473
633	Ubiquitination	QHNERLRKQFGAQAN HHHHHHHHHHCCCCC	55.35	21890473
633	Ubiquitination	QHNERLRKQFGAQAN HHHHHHHHHHCCCCC	55.35	21890473
633	Malonylation	QHNERLRKQFGAQAN HHHHHHHHHHCCCCC	55.35	26320211
633	Ubiquitination	QHNERLRKQFGAQAN HHHHHHHHHHCCCCC	55.35	-
633	Ubiquitination	QHNERLRKQFGAQAN HHHHHHHHHHCCCCC	55.35	21890473
649	Ubiquitination	IGPWIQTKMEEIGRI CCHHHHHHHHHHHCC	28.12	-
660	Sulfoxidation	IGRISIEMHGTLEDQ HHCCEEEECCCHHHH	3.17	30846556
669	Phosphorylation	GTLEDQLSHLRQYEK CCHHHHHHHHHHHHH	18.16	46158671
674	Phosphorylation	QLSHLRQYEKSIVNY HHHHHHHHHHHHHCC	20.91	23312004
676	Acetylation	SHLRQYEKSIVNYKP HHHHHHHHHHHCCCC	40.32	-
676	Acetylation	SHLRQYEKSIVNYKP HHHHHHHHHHHCCCC	40.32	19608861
676	Malonylation	SHLRQYEKSIVNYKP HHHHHHHHHHHCCCC	40.32	26320211
676	Ubiquitination	SHLRQYEKSIVNYKP HHHHHHHHHHHCCCC	40.32	-
677	Phosphorylation	HLRQYEKSIVNYKPK HHHHHHHHHHCCCCC	21.59	26657352
681	Phosphorylation	YEKSIVNYKPKIDQL HHHHHHCCCCCHHHC	20.13	28152594
682	Acetylation	EKSIVNYKPKIDQLE HHHHHCCCCCHHHCC	34.33	25953088
684	Ubiquitination	SIVNYKPKIDQLEGD HHHCCCCCHHHCCCC	55.55	-
706	Phosphorylation	LIFDNKHTNYTMEHI HCCCCCCCCCCHHHH	31.37	28152594
708	Phosphorylation	FDNKHTNYTMEHIRV CCCCCCCCCHHHHHH	14.49	28152594
709	Phosphorylation	DNKHTNYTMEHIRVG CCCCCCCCHHHHHHC	20.39	26437602
722	Phosphorylation	VGWEQLLTTIARTIN HCHHHHHHHHHHHHH	25.42	21712546
727	Phosphorylation	LLTTIARTINEVENQ HHHHHHHHHHHHHHH	21.09	20860994
737	Phosphorylation	EVENQILTRDAKGIS HHHHHHHCCCCCCCC	28.29	7303829
741	Ubiquitination	QILTRDAKGISQEQM HHHCCCCCCCCHHHH	62.15	-
741	Malonylation	QILTRDAKGISQEQM HHHCCCCCCCCHHHH	62.15	26320211
744	Phosphorylation	TRDAKGISQEQMNEF CCCCCCCCHHHHHHH	36.01	63728045
748	Sulfoxidation	KGISQEQMNEFRASF CCCCHHHHHHHHHHH	5.23	28465586
754	Phosphorylation	QMNEFRASFNHFDRD HHHHHHHHHCCCCCC	23.48	26437602
763	Phosphorylation	NHFDRDHSGTLGPEE CCCCCCCCCCCCHHH	37.45	29255136
763 (in isoform 2)	Phosphorylation	-	37.45	24043423
763 (in isoform 4)	Phosphorylation	-	37.45	24043423
765	Phosphorylation	FDRDHSGTLGPEEFK CCCCCCCCCCHHHHH	31.40	29255136
768 (in isoform 2)	Phosphorylation	-	40.85	24043423
768 (in isoform 4)	Phosphorylation	-	40.85	24043423
777 (in isoform 2)	Phosphorylation	-	11.64	24043423
777 (in isoform 4)	Phosphorylation	-	11.64	24043423
780 (in isoform 2)	Phosphorylation	-	15.07	24043423
780 (in isoform 4)	Phosphorylation	-	15.07	24043423
790 (in isoform 3)	Phosphorylation	-	24.83	24043423
795 (in isoform 3)	Phosphorylation	-	1.97	24043423
796	Sulfoxidation	EAEFARIMSIVDPNR HHHHHHHHHHCCCCC	1.54	30846556
797	Phosphorylation	AEFARIMSIVDPNRL HHHHHHHHHCCCCCC	19.65	63744995
804 (in isoform 3)	Phosphorylation	-	8.52	24043423
807 (in isoform 3)	Phosphorylation	-	4.15	24043423
820	Phosphorylation	IDFMSRETADTDTAD HHHHCCCCCCCCCHH	28.82	22499768
823	Phosphorylation	MSRETADTDTADQVM HCCCCCCCCCHHHHH	32.55	110740987
825	Phosphorylation	RETADTDTADQVMAS CCCCCCCCHHHHHHH	33.94	110740995
830	Sulfoxidation	TDTADQVMASFKILA CCCHHHHHHHHHHHH	1.83	28465586
832	Phosphorylation	TADQVMASFKILAGD CHHHHHHHHHHHHCC	14.69	24719451
842	Phosphorylation	ILAGDKNYITMDELR HHHCCCCEECHHHHH	11.96	20068231
844	Phosphorylation	AGDKNYITMDELRRE HCCCCEECHHHHHHH	14.28	110741003
845	Sulfoxidation	GDKNYITMDELRREL CCCCEECHHHHHHHC	2.46	30846556
859	Phosphorylation	LPPDQAEYCIARMAP CCCCHHHHHHHHCCC	7.68	28152594
864	Phosphorylation	AEYCIARMAPYTGPD HHHHHHHCCCCCCCC	3.05	27642862
873 (in isoform 4)	Phosphorylation	-	7.08	22210691
876 (in isoform 4)	Phosphorylation	-	7.38	22210691
881	Phosphorylation	PGALDYMSFSTALYG CCHHHHHCHHHHHHC	15.15	27251275
882 (in isoform 4)	Phosphorylation	-	4.25	22210691
883	Phosphorylation	ALDYMSFSTALYGES HHHHHCHHHHHHCCC	12.88	27251275
884	Phosphorylation	LDYMSFSTALYGESD HHHHCHHHHHHCCCC	20.76	28152594
887	Phosphorylation	MSFSTALYGESDL-- HCHHHHHHCCCCC--	19.18	28152594
890	Phosphorylation	STALYGESDL----- HHHHHCCCCC-----	39.59	28152594

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
12	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ACTN1_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 ACTN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC4_HUMAN	XRCC4	physical	16189514
MAGAB_HUMAN	MAGEA11	physical	16189514
MYOZ1_HUMAN	MYOZ1	physical	16189514
ADIP_HUMAN	SSX2IP	physical	12446711
PKN1_HUMAN	PKN1	physical	11802708
MYOTI_HUMAN	MYOT	physical	12499399
TITIN_HUMAN	TTN	physical	11305911
ACTN1_HUMAN	ACTN1	physical	11470434
PYGB_HUMAN	PYGB	physical	12211109
ZYX_HUMAN	ZYX	physical	11423549
PDLI1_HUMAN	PDLIM1	physical	11110697
CD5R2_HUMAN	CDK5R2	physical	12223541
CTNA1_HUMAN	CTNNA1	physical	7790378
TBA1A_HUMAN	TUBA1A	physical	18341635
DAG1_HUMAN	DAG1	physical	18341635
SRBS2_HUMAN	SORBS2	physical	16125169
EZRI_HUMAN	EZR	physical	22939629
ACTN4_HUMAN	ACTN4	physical	22939629
ACTN2_HUMAN	ACTN2	physical	22939629
CALD1_HUMAN	CALD1	physical	22939629
FAF2_HUMAN	FAF2	physical	22939629
CSRP1_HUMAN	CSRP1	physical	10926853
IGSF8_HUMAN	IGSF8	physical	23463506
CD81_HUMAN	CD81	physical	23463506
ICAM1_HUMAN	ICAM1	physical	23463506
RS27_HUMAN	RPS27	physical	21988832
NUMBL_HUMAN	NUMBL	physical	21988832
GIT2_HUMAN	GIT2	physical	21988832
TF2H1_HUMAN	GTF2H1	physical	21988832
IMA1_HUMAN	KPNA2	physical	21988832
PIAS4_HUMAN	PIAS4	physical	21988832
PSA1_HUMAN	PSMA1	physical	21988832
ODPX_HUMAN	PDHX	physical	21988832
SF3A3_HUMAN	SF3A3	physical	22863883
SRP19_HUMAN	SRP19	physical	22863883
STAM2_HUMAN	STAM2	physical	22863883
ACTN1_HUMAN	ACTN1	physical	25416956
ACTN3_HUMAN	ACTN3	physical	25416956
OAS1_HUMAN	OAS1	physical	25416956
EPMIP_HUMAN	EPM2AIP1	physical	25416956
MYOZ2_HUMAN	MYOZ2	physical	25416956
MILK2_HUMAN	MICALL2	physical	25416956
KCTD6_HUMAN	KCTD6	physical	25416956
SPERT_HUMAN	SPERT	physical	25416956
KCRB_HUMAN	CKB	physical	26344197
CY1_HUMAN	CYC1	physical	26344197
ECSIT_HUMAN	ECSIT	physical	26344197
KDM5C_HUMAN	KDM5C	physical	26344197
TPM3_HUMAN	TPM3	physical	26344197
CTNA1_HUMAN	CTNNA1	physical	25241761
KCC2A_HUMAN	CAMK2A	physical	25241761

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615193	Bleeding disorder, platelet-type 15 (BDPLT15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ACTN1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-95; LYS-195 AND LYS-676, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-50, AND MASSSPECTROMETRY.	16097034 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-193, AND MASSSPECTROMETRY.	18083107 [Abstract]
"The cytoskeletal/non-muscle isoform of alpha-actinin isphosphorylated on its actin-binding domain by the focal adhesionkinase."; Izaguirre G., Aguirre L., Hu Y.P., Lee H.Y., Schlaepfer D.D.,Aneskievich B.J., Haimovich B.; J. Biol. Chem. 276:28676-28685(2001). Cited for: PHOSPHORYLATION AT TYR-12.	11369769 [Abstract]