ACTN2_HUMAN - dbPTM
ACTN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTN2_HUMAN
UniProt AC P35609
Protein Name Alpha-actinin-2
Gene Name ACTN2
Organism Homo sapiens (Human).
Sequence Length 894
Subcellular Localization Cytoplasm, myofibril, sarcomere, Z line . Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle.
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 MNQIEPGVQYNYVYDEDEYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLNEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERMEKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADGERQSIMAIQNEVEKVIQSYNIRISSSNPYSTVTMDELRTKWDKVKQLVPIRDQSLQEELARQHANERLRRQFAAQANAIGPWIQNKMEEIARSSIQITGALEDQMNQLKQYEHNIINYKNNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRDAKGITQEQMNEFRASFNHFDRRKNGLMDHEDFRACLISMGYDLGEAEFARIMTLVDPNGQGTVTFQSFIDFMTRETADTDTAEQVIASFRILASDKPYILAEELRRELPPDQAQYCIKRMPAYSGPGSVPGALDYAAFSSALYGESDL
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 Orthologous
Protein Cluster
38UbiquitinationLLDPAWEKQQRKTFT
CCCHHHHHHHHHHHH
40.82-
38UbiquitinationLLDPAWEKQQRKTFT
CCCHHHHHHHHHHHH
40.82-
42UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.5921890473
42UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.5921890473
42UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH
43.5921890473
43PhosphorylationWEKQQRKTFTAWCNS
HHHHHHHHHHHHHHH
28.5426437602
45PhosphorylationKQQRKTFTAWCNSHL
HHHHHHHHHHHHHHH
25.2026437602
50PhosphorylationTFTAWCNSHLRKAGT
HHHHHHHHHHHHHCH
22.2926437602
54UbiquitinationWCNSHLRKAGTQIEN
HHHHHHHHHCHHHHC
58.49-
57PhosphorylationSHLRKAGTQIENIEE
HHHHHHCHHHHCHHH
31.1016097034
80PhosphorylationMLLLEVISGERLPKP
HHHHHHHCCCCCCCC
39.51-
83MethylationLEVISGERLPKPDRG
HHHHCCCCCCCCCCC
60.87-
86MethylationISGERLPKPDRGKMR
HCCCCCCCCCCCCCC
65.23-
106PhosphorylationNVNKALDYIASKGVK
CHHHHHHHHHHCCCE
10.1520068231
109PhosphorylationKALDYIASKGVKLVS
HHHHHHHHCCCEEEE
22.0026437602
116PhosphorylationSKGVKLVSIGAEEIV
HCCCEEEEECCHHEE
26.2427251275
130PhosphorylationVDGNVKMTLGMIWTI
ECCCCHHHHHHHHHH
17.91-
147PhosphorylationRFAIQDISVEETSAK
HHHHHCCCCCCCCHH
31.5919664994
151PhosphorylationQDISVEETSAKEGLL
HCCCCCCCCHHHCCH
22.0723927012
152PhosphorylationDISVEETSAKEGLLL
CCCCCCCCHHHCCHH
40.3923927012
161S-palmitoylationKEGLLLWCQRKTAPY
HHCCHHHHHCCCCCC
2.5729575903
178PhosphorylationVNIQNFHTSWKDGLG
CCCCCCCCCCCCCHH
31.9526437602
179PhosphorylationNIQNFHTSWKDGLGL
CCCCCCCCCCCCHHH
24.4526437602
181AcetylationQNFHTSWKDGLGLCA
CCCCCCCCCCHHHHH
41.5130586715
200PhosphorylationHRPDLIDYSKLNKDD
HCCCCCCHHHCCCCC
10.743832141
201PhosphorylationRPDLIDYSKLNKDDP
CCCCCCHHHCCCCCC
27.2426437602
237PhosphorylationDAEDIVNTPKPDERA
CHHHHHCCCCCCHHH
23.0719764811
250PhosphorylationRAIMTYVSCFYHAFA
HHHHHHHHHHHHHHC
6.52-
253PhosphorylationMTYVSCFYHAFAGAE
HHHHHHHHHHHCCHH
9.14-
268MethylationQAETAANRICKVLAV
HHHHHHHHHHHHHHH
30.84-
291PhosphorylationEEYERLASELLEWIR
HHHHHHHHHHHHHHH
33.1173403065
300PhosphorylationLLEWIRRTIPWLENR
HHHHHHHHCHHHHCC
22.8826437602
308PhosphorylationIPWLENRTPEKTMQA
CHHHHCCCHHHHHHH
47.5926437602
312PhosphorylationENRTPEKTMQAMQKK
HCCCHHHHHHHHHHH
16.9226437602
326PhosphorylationKLEDFRDYRRKHKPP
HHHHHHHHHHHCCCC
14.2028152594
338UbiquitinationKPPKVQEKCQLEINF
CCCHHHHHEEEEEEC
15.3621890473
338UbiquitinationKPPKVQEKCQLEINF
CCCHHHHHEEEEEEC
15.36-
339S-palmitoylationPPKVQEKCQLEINFN
CCHHHHHEEEEEECC
5.7029575903
347PhosphorylationQLEINFNTLQTKLRI
EEEEECCCHHHHHHH
18.9926657352
350PhosphorylationINFNTLQTKLRISNR
EECCCHHHHHHHCCC
34.8521712546
355PhosphorylationLQTKLRISNRPAFMP
HHHHHHHCCCCCCCC
21.9826657352
361SulfoxidationISNRPAFMPSEGKMV
HCCCCCCCCCCCCCH
3.7621406390
363PhosphorylationNRPAFMPSEGKMVSD
CCCCCCCCCCCCHHH
47.3926437602
385PhosphorylationLEQAEKGYEEWLLNE
HHHHHHHHHHHHHHH
23.03110744103
405UbiquitinationRLEHLAEKFRQKAST
HHHHHHHHHHHHHHH
39.99-
409UbiquitinationLAEKFRQKASTHETW
HHHHHHHHHHHHHHH
39.80-
411PhosphorylationEKFRQKASTHETWAY
HHHHHHHHHHHHHHH
37.0126437602
412PhosphorylationKFRQKASTHETWAYG
HHHHHHHHHHHHHHC
28.7026437602
415PhosphorylationQKASTHETWAYGKEQ
HHHHHHHHHHHCHHH
14.0626437602
418PhosphorylationSTHETWAYGKEQILL
HHHHHHHHCHHHEEE
21.9426437602
420UbiquitinationHETWAYGKEQILLQK
HHHHHHCHHHEEECC
33.50-
427UbiquitinationKEQILLQKDYESASL
HHHEEECCCHHHCCH
63.35-
431PhosphorylationLLQKDYESASLTEVR
EECCCHHHCCHHHHH
19.5419764811
431O-linked_GlycosylationLLQKDYESASLTEVR
EECCCHHHCCHHHHH
19.5430379171
433PhosphorylationQKDYESASLTEVRAL
CCCHHHCCHHHHHHH
45.1419764811
435PhosphorylationDYESASLTEVRALLR
CHHHCCHHHHHHHHH
29.9119764811
435O-linked_GlycosylationDYESASLTEVRALLR
CHHHCCHHHHHHHHH
29.9130379171
443UbiquitinationEVRALLRKHEAFESD
HHHHHHHHHHHHHHH
45.85-
443AcetylationEVRALLRKHEAFESD
HHHHHHHHHHHHHHH
45.85-
449PhosphorylationRKHEAFESDLAAHQD
HHHHHHHHHHHHCHH
31.3226657352
495PhosphorylationDQWDRLGTLTQKRRE
HHHHHHHHHHHHHHH
31.0920068231
497PhosphorylationWDRLGTLTQKRREAL
HHHHHHHHHHHHHHH
31.7026437602
499AcetylationRLGTLTQKRREALER
HHHHHHHHHHHHHHH
48.4630586709
523AcetylationQLHLEFAKRAAPFNN
HHHHHHHHHCCCCCH
48.1430586721
574PhosphorylationEADGERQSIMAIQNE
CCCCCHHHHHHHHHH
22.1326437602
588PhosphorylationEVEKVIQSYNIRISS
HHHHHHHHCCCEECC
14.7126437602
589PhosphorylationVEKVIQSYNIRISSS
HHHHHHHCCCEECCC
9.7624426439
594PhosphorylationQSYNIRISSSNPYST
HHCCCEECCCCCCCC
20.1919764811
595PhosphorylationSYNIRISSSNPYSTV
HCCCEECCCCCCCCC
31.5920873877
596PhosphorylationYNIRISSSNPYSTVT
CCCEECCCCCCCCCC
34.7320873877
599PhosphorylationRISSSNPYSTVTMDE
EECCCCCCCCCCHHH
22.6420873877
600PhosphorylationISSSNPYSTVTMDEL
ECCCCCCCCCCHHHH
20.0522673903
601PhosphorylationSSSNPYSTVTMDELR
CCCCCCCCCCHHHHH
17.7222673903
603PhosphorylationSNPYSTVTMDELRTK
CCCCCCCCHHHHHHH
20.9925332170
609PhosphorylationVTMDELRTKWDKVKQ
CCHHHHHHHHHHHHH
49.4626437602
624PhosphorylationLVPIRDQSLQEELAR
HCCCCCHHHHHHHHH
35.9926437602
681PhosphorylationQMNQLKQYEHNIINY
HHHHHHHHHHHHHHH
19.9826437602
688PhosphorylationYEHNIINYKNNIDKL
HHHHHHHHHCCHHHC
12.5126437602
713PhosphorylationLVFDNKHTNYTMEHI
HCCCCCCCCCCHHHH
31.3728152594
715PhosphorylationFDNKHTNYTMEHIRV
CCCCCCCCCHHHHHH
14.4928152594
716PhosphorylationDNKHTNYTMEHIRVG
CCCCCCCCHHHHHHH
20.3926437602
734PhosphorylationLLTTIARTINEVETQ
HHHHHHHHHHHHHHH
21.0926437602
744PhosphorylationEVETQILTRDAKGIT
HHHHHHHCCCCCCCC
28.2926437602
748UbiquitinationQILTRDAKGITQEQM
HHHCCCCCCCCHHHH
55.95-
751PhosphorylationTRDAKGITQEQMNEF
CCCCCCCCHHHHHHH
34.4226437602
761PhosphorylationQMNEFRASFNHFDRR
HHHHHHHHHCHHHHH
23.4826437602
840PhosphorylationASFRILASDKPYILA
HHHHHHHCCCCEEEH
42.6019764811
844PhosphorylationILASDKPYILAEELR
HHHCCCCEEEHHHHH
17.8238017421
861PhosphorylationLPPDQAQYCIKRMPA
CCCCHHHHHHHHCCC
10.1246158725
892PhosphorylationSSALYGESDL-----
HHHHHCCCCC-----
39.5922673903

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
-KUbiquitinationE3 ubiquitin ligaseFBXL22Q6P050
PMID:22972877

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACTN2_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 ACTN2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG1_HUMANDLG1physical
12860415
TBA1A_MOUSETuba1aphysical
16169070
KCNA5_HUMANKCNA5physical
10812072
NMDE2_HUMANGRIN2Bphysical
9009191
ADA12_HUMANADAM12physical
10788519
MYOZ1_HUMANMYOZ1physical
10984498
TENN_HUMANTNNphysical
9817758
MYPN_HUMANMYPNphysical
11309420
PDLI1_HUMANPDLIM1physical
10861853
ACTN3_HUMANACTN3physical
9675099
KCNA5_HUMANKCNA5physical
11389904
ACTN4_HUMANACTN4physical
22939629
RL35_HUMANRPL35physical
21988832
ZN446_HUMANZNF446physical
21988832
ACTN2_HUMANACTN2physical
25416956
MOS_HUMANMOSphysical
25416956
SNAI1_HUMANSNAI1physical
25416956
SP100_HUMANSP100physical
25416956
PDLI3_HUMANPDLIM3physical
25416956
MYOZ2_HUMANMYOZ2physical
25416956
MILK2_HUMANMICALL2physical
25416956
BRM1L_HUMANBRMS1Lphysical
25416956
SAXO1_HUMANFAM154Aphysical
25416956
RTP5_HUMANRTP5physical
25416956
TNNI1_HUMANTNNI1physical
26344197
TPM1_HUMANTPM1physical
26344197
TPM2_HUMANTPM2physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612158Cardiomyopathy, familial hypertrophic 23, with or without left ventricular non-compaction (CMH23)
612158Cardiomyopathy, dilated 1AA, with or without left ventricular non-compaction (CMD1AA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACTN2_HUMAN

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Related Literatures of Post-Translational Modification

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