ACTN2_MOUSE - dbPTM
ACTN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTN2_MOUSE
UniProt AC Q9JI91
Protein Name Alpha-actinin-2
Gene Name Actn2
Organism Mus musculus (Mouse).
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 (By similarity)..
Protein Sequence MNQIEPGVQYNYVYDEDEYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLNEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERTEKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADGERQSILAIQNEVEKVIQSYSIRISSSNPYSTVTMDELRNKWDKVKQLVPVRDQSLQEELARQHANERLRRQFAAQANAIGPWIQNKMEEIARSSIQITGALEDQMNQLKQYEHNIINYKNNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRDAKGITQEQMNEFRASFNHFDRRKNGLMDHEDFRACLISMGYDLGEAEFARIMTLVDPNGQGTVTFQSFIDFMTRETADTDTAEQVIASFRILASDKPYILAEELRRELPPDQAQYCIKRMPPYSGPGSVPGALDYTAFSSALYGESDL
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		40.8222790023
38UbiquitinationLLDPAWEKQQRKTFT
CCCHHHHHHHHHHHH		40.8222790023
42UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH		43.5922790023
42UbiquitinationAWEKQQRKTFTAWCN
HHHHHHHHHHHHHHH		43.5922790023
45PhosphorylationKQQRKTFTAWCNSHL
HHHHHHHHHHHHHHH		25.2028542873
50PhosphorylationTFTAWCNSHLRKAGT
HHHHHHHHHHHHHCH		22.2928542873
54UbiquitinationWCNSHLRKAGTQIEN
HHHHHHHHHCHHHHC		58.4922790023
54UbiquitinationWCNSHLRKAGTQIEN
HHHHHHHHHCHHHHC		58.4922790023
57PhosphorylationSHLRKAGTQIENIEE
HHHHHHCHHHHCHHH		31.1022210690
96UbiquitinationRGKMRFHKIANVNKA
CCCCCHHHHCCHHHH		40.58-
102UbiquitinationHKIANVNKALDYIAS
HHHCCHHHHHHHHHH		46.1522790023
102UbiquitinationHKIANVNKALDYIAS
HHHCCHHHHHHHHHH		46.1522790023
113UbiquitinationYIASKGVKLVSIGAE
HHHHCCCEEEEECCH		52.4122790023
113UbiquitinationYIASKGVKLVSIGAE
HHHHCCCEEEEECCH		52.4122790023
147PhosphorylationRFAIQDISVEETSAK
HHHHHCCCCCCCCHH		31.5926824392
151PhosphorylationQDISVEETSAKEGLL
HCCCCCCCCHHHCCH		22.0727742792
152PhosphorylationDISVEETSAKEGLLL
CCCCCCCCHHHCCHH		40.3927742792
178PhosphorylationVNIQNFHTSWKDGLG
CCCCCCCCCCCCCHH		31.9523737553
179PhosphorylationNIQNFHTSWKDGLGL
CCCCCCCCCCCCHHH		24.4523737553
187S-nitrosylationWKDGLGLCALIHRHR
CCCCHHHHHHHHHHC		2.4821278135
187S-nitrosocysteineWKDGLGLCALIHRHR
CCCCHHHHHHHHHHC		2.48-
200PhosphorylationHRPDLIDYSKLNKDD
HCCCCCCHHHCCCCC		10.743840511
201PhosphorylationRPDLIDYSKLNKDDP
CCCCCCHHHCCCCCC		27.2446158703
237PhosphorylationDAEDIVNTPKPDERA
CHHHHHCCCCCCHHH		23.0723737553
239UbiquitinationEDIVNTPKPDERAIM
HHHHCCCCCCHHHHH		64.1622790023
239UbiquitinationEDIVNTPKPDERAIM
HHHHCCCCCCHHHHH		64.1622790023
271UbiquitinationTAANRICKVLAVNQE
HHHHHHHHHHHHCHH		55.3722790023
271UbiquitinationTAANRICKVLAVNQE
HHHHHHHHHHHHCHH		55.3722790023
291PhosphorylationEEYERLASELLEWIR
HHHHHHHHHHHHHHH		33.1123737553
308PhosphorylationIPWLENRTPEKTMQA
CHHHHCCCHHHHHHH		47.5928542873
311UbiquitinationLENRTPEKTMQAMQK
HHCCCHHHHHHHHHH		50.9622790023
311UbiquitinationLENRTPEKTMQAMQK
HHCCCHHHHHHHHHH		50.9622790023
319UbiquitinationTMQAMQKKLEDFRDY
HHHHHHHHHHHHHHH		39.9722790023
319UbiquitinationTMQAMQKKLEDFRDY
HHHHHHHHHHHHHHH		39.9722790023
338UbiquitinationKPPKVQEKCQLEINF
CCCHHHHHEEEEEEC		15.3622790023
338UbiquitinationKPPKVQEKCQLEINF
CCCHHHHHEEEEEEC		15.3622790023
347PhosphorylationQLEINFNTLQTKLRI
EEEEECCCHHHHHHH		18.9928464351
350PhosphorylationINFNTLQTKLRISNR
EECCCHHHHHHHCCC		34.8528464351
363PhosphorylationNRPAFMPSEGKMVSD
CCCCCCCCCCCCHHH		47.3928464351
369PhosphorylationPSEGKMVSDIAGAWQ
CCCCCCHHHHHHHHH		21.5727742792
405UbiquitinationRLEHLAEKFRQKAST
HHHHHHHHHHHHHHH		39.9922790023
405UbiquitinationRLEHLAEKFRQKAST
HHHHHHHHHHHHHHH		39.9922790023
409UbiquitinationLAEKFRQKASTHETW
HHHHHHHHHHHHHHH		39.8022790023
409UbiquitinationLAEKFRQKASTHETW
HHHHHHHHHHHHHHH		39.8022790023
411PhosphorylationEKFRQKASTHETWAY
HHHHHHHHHHHHHHH		37.0123375375
412PhosphorylationKFRQKASTHETWAYG
HHHHHHHHHHHHHHC		28.7023375375
415PhosphorylationQKASTHETWAYGKEQ
HHHHHHHHHHHCHHH		14.0628464351
420UbiquitinationHETWAYGKEQILLQK
HHHHHHCHHHEEECC		33.5022790023
420UbiquitinationHETWAYGKEQILLQK
HHHHHHCHHHEEECC		33.5022790023
427UbiquitinationKEQILLQKDYESASL
HHHEEECCCHHHCCH		63.3522790023
427UbiquitinationKEQILLQKDYESASL
HHHEEECCCHHHCCH		63.3522790023
431PhosphorylationLLQKDYESASLTEVR
EECCCHHHCCHHHHH		19.5427742792
433PhosphorylationQKDYESASLTEVRAL
CCCHHHCCHHHHHHH		45.1423737553
435PhosphorylationDYESASLTEVRALLR
CHHHCCHHHHHHHHH		29.9127742792
449PhosphorylationRKHEAFESDLAAHQD
HHHHHHHHHHHHCHH		31.3227742792
487S-nitrosocysteineNDRCQKICDQWDRLG
HHHHHHHHHHHHHHH		4.02-
487S-nitrosylationNDRCQKICDQWDRLG
HHHHHHHHHHHHHHH		4.0221278135
495PhosphorylationDQWDRLGTLTQKRRE
HHHHHHHHHHHHHHH		31.0928542873
556PhosphorylationEEIQSLITAHEQFKA
HHHHHHHHHHHHHHH		27.5351458169
574PhosphorylationEADGERQSILAIQNE
CCCCCHHHHEHHHHH		26.2873665947
584UbiquitinationAIQNEVEKVIQSYSI
HHHHHHHHHHHHHEE		50.22-
588PhosphorylationEVEKVIQSYSIRISS
HHHHHHHHHEEEECC		15.1030165576
589PhosphorylationVEKVIQSYSIRISSS
HHHHHHHHEEEECCC		7.5530165576
590PhosphorylationEKVIQSYSIRISSSN
HHHHHHHEEEECCCC		15.619558999
594PhosphorylationQSYSIRISSSNPYST
HHHEEEECCCCCCCC		20.1923737553
595PhosphorylationSYSIRISSSNPYSTV
HHEEEECCCCCCCCC		31.5923737553
596PhosphorylationYSIRISSSNPYSTVT
HEEEECCCCCCCCCC		34.7323737553
599PhosphorylationRISSSNPYSTVTMDE
EECCCCCCCCCCHHH		22.6423737553
600PhosphorylationISSSNPYSTVTMDEL
ECCCCCCCCCCHHHH		20.0527742792
601PhosphorylationSSSNPYSTVTMDELR
CCCCCCCCCCHHHHH		17.7222210690
603PhosphorylationSNPYSTVTMDELRNK
CCCCCCCCHHHHHHH		20.9922210690
624PhosphorylationLVPVRDQSLQEELAR
HCCCCCHHHHHHHHH		35.9928464351
664PhosphorylationMEEIARSSIQITGAL
HHHHHHHHHHHHHHH		16.9828464351
681PhosphorylationQMNQLKQYEHNIINY
HHHHHHHHHHHHHHH		19.9828464351
715PhosphorylationFDNKHTNYTMEHIRV
CCCCCCCCCHHHHHH		14.4928464351
748UbiquitinationQILTRDAKGITQEQM
HHHCCCCCCCCHHHH		55.9522790023
748UbiquitinationQILTRDAKGITQEQM
HHHCCCCCCCCHHHH		55.9522790023
761PhosphorylationQMNEFRASFNHFDRR
HHHHHHHHHCHHHHH		23.4824899341
822PhosphorylationIDFMTRETADTDTAE
HHHHHCCCCCCCCHH		26.9223737553
825PhosphorylationMTRETADTDTAEQVI
HHCCCCCCCCHHHHH		32.559559029
827PhosphorylationRETADTDTAEQVIAS
CCCCCCCCHHHHHHH		33.9023737553
840PhosphorylationASFRILASDKPYILA
HHHHHHHCCCCEEEH		42.6023737553
842UbiquitinationFRILASDKPYILAEE
HHHHHCCCCEEEHHH		36.9122790023
842UbiquitinationFRILASDKPYILAEE
HHHHHCCCCEEEHHH		36.9122790023
864UbiquitinationDQAQYCIKRMPPYSG
CHHHHHHHHCCCCCC		38.8022790023
864UbiquitinationDQAQYCIKRMPPYSG
CHHHHHHHHCCCCCC		38.8022790023
889PhosphorylationTAFSSALYGESDL--
HHHHHHHHCCCCC--		20.6822210690
892PhosphorylationSSALYGESDL-----
HHHHHCCCCC-----		39.5951458161
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 ACTN2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACTN2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LDB3_MOUSELdb3physical
10391924
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACTN2_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory