MARK1_MOUSE - dbPTM
MARK1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARK1_MOUSE
UniProt AC Q8VHJ5
Protein Name Serine/threonine-protein kinase MARK1
Gene Name Mark1 {ECO:0000312|MGI:MGI:2664902}
Organism Mus musculus (Mouse).
Sequence Length 795
Subcellular Localization Cell membrane
Peripheral membrane protein. Cytoplasm, cytoskeleton. Cytoplasm . Cell projection, dendrite . Appears to localize to an intracellular network..
Protein Description Serine/threonine-protein kinase (By similarity). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (By similarity). Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3)..
Protein Sequence MSARTPLPTVNERDTENHTSVDGYTETHIPPAKSSSRQNLPRCRNSITSATDEQPHIGNYRLQKTIGKGNFAKVKLARHVLTGREVAVKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKCIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKLLVLNPIKRGSLEQIMKDRWMNVGHEEEELKPYSEPELDLSDAKRIDIMVTMGFARDEINDALVSQKYDEVMATYILLGRKPPEFEGGESLSSGSLCQRSRPSSDLNNSTLQSPAHLKVQRSISANQKQRRFSDHAGPSIPPAVSYTKRPQANSVESEQKEEWGKDTARRLGSTTVGSKSEVTASPLVGPDRKKSTASPSNNVYSGGSMARRNTYVCERSTDRYAALQNGRDSSLTEMSASSMSSAGSTVASAGPSARPRHQKSMSTSGHPIKVTLPTIKDGSEAYRPGAAQRVPAASPSAHSISASTPDRTRFPRGSSSRSTFHGEQLRERRSAAYNGPPASPSHETGAFAHARRGTSTGIISKITSKFVRRDPSEGEASGRADTARGSSGDPKERDKDEGKEAKPRSLRFTWSMKTTSSMDPNDMLREIRKVLDANTCDYEQKERFLLFCVHGDARQDSLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL
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
2Phosphorylation------MSARTPLPT
------CCCCCCCCC
26.8529514104
5Phosphorylation---MSARTPLPTVNE
---CCCCCCCCCCCC
28.97-
35PhosphorylationHIPPAKSSSRQNLPR
CCCCCCCCCCCCCHH
28.9129899451
36PhosphorylationIPPAKSSSRQNLPRC
CCCCCCCCCCCCHHH
45.0029514104
46PhosphorylationNLPRCRNSITSATDE
CCHHHHHCCCCCCCC
14.1126370283
48PhosphorylationPRCRNSITSATDEQP
HHHHHCCCCCCCCCC
16.4829899451
49PhosphorylationRCRNSITSATDEQPH
HHHHCCCCCCCCCCC
27.7429899451
51PhosphorylationRNSITSATDEQPHIG
HHCCCCCCCCCCCCC
39.5829899451
168PhosphorylationAKFRQIVSAVQYCHQ
HHHHHHHHHHHHHHH
25.09-
172PhosphorylationQIVSAVQYCHQKCIV
HHHHHHHHHHHHHCC
5.8226487105
208PhosphorylationFGFSNEFTVGNKLDT
CCCCCCEECCCCHHH
22.71-
215PhosphorylationTVGNKLDTFCGSPPY
ECCCCHHHCCCCCCC
31.1225521595
219PhosphorylationKLDTFCGSPPYAAPE
CHHHCCCCCCCCCHH
24.7122942356
222PhosphorylationTFCGSPPYAAPELFQ
HCCCCCCCCCHHHHC
20.8425159016
298UbiquitinationLLVLNPIKRGSLEQI
HHHHCCCCCCCHHHH
52.54-
380PhosphorylationPEFEGGESLSSGSLC
CCCCCCCCCCCCCCC
36.5022324799
382PhosphorylationFEGGESLSSGSLCQR
CCCCCCCCCCCCCCC
41.7622324799
383PhosphorylationEGGESLSSGSLCQRS
CCCCCCCCCCCCCCC
37.3825521595
385PhosphorylationGESLSSGSLCQRSRP
CCCCCCCCCCCCCCC
28.1125521595
390PhosphorylationSGSLCQRSRPSSDLN
CCCCCCCCCCCCCCC
23.7525521595
393PhosphorylationLCQRSRPSSDLNNST
CCCCCCCCCCCCCCC
35.0625521595
394PhosphorylationCQRSRPSSDLNNSTL
CCCCCCCCCCCCCCC
49.1225521595
399PhosphorylationPSSDLNNSTLQSPAH
CCCCCCCCCCCCHHH
29.4425521595
400PhosphorylationSSDLNNSTLQSPAHL
CCCCCCCCCCCHHHH
30.8229899451
403PhosphorylationLNNSTLQSPAHLKVQ
CCCCCCCCHHHHHHH
27.4525521595
412PhosphorylationAHLKVQRSISANQKQ
HHHHHHHHCCCHHHC
12.1022324799
414PhosphorylationLKVQRSISANQKQRR
HHHHHHCCCHHHCCC
23.5525521595
423PhosphorylationNQKQRRFSDHAGPSI
HHHCCCCCCCCCCCC
27.0322817900
429PhosphorylationFSDHAGPSIPPAVSY
CCCCCCCCCCCCCCC
46.9729472430
444PhosphorylationTKRPQANSVESEQKE
CCCCCCCCCCHHHHH
30.2225521595
447PhosphorylationPQANSVESEQKEEWG
CCCCCCCHHHHHHHC
43.0822324799
457PhosphorylationKEEWGKDTARRLGST
HHHHCHHHHHHHCCC
26.0822324799
463PhosphorylationDTARRLGSTTVGSKS
HHHHHHCCCCCCCCC
26.0422324799
464PhosphorylationTARRLGSTTVGSKSE
HHHHHCCCCCCCCCE
24.5729899451
465PhosphorylationARRLGSTTVGSKSEV
HHHHCCCCCCCCCEE
25.2722324799
468PhosphorylationLGSTTVGSKSEVTAS
HCCCCCCCCCEEEEC
28.7729899451
470PhosphorylationSTTVGSKSEVTASPL
CCCCCCCCEEEECCC
38.7123527152
473PhosphorylationVGSKSEVTASPLVGP
CCCCCEEEECCCCCC
19.8429514104
475PhosphorylationSKSEVTASPLVGPDR
CCCEEEECCCCCCCC
14.9223527152
485PhosphorylationVGPDRKKSTASPSNN
CCCCCCCCCCCCCCC
32.0423527152
486PhosphorylationGPDRKKSTASPSNNV
CCCCCCCCCCCCCCC
39.7825521595
488PhosphorylationDRKKSTASPSNNVYS
CCCCCCCCCCCCCCC
29.0223527152
490PhosphorylationKKSTASPSNNVYSGG
CCCCCCCCCCCCCCC
38.2429899451
494PhosphorylationASPSNNVYSGGSMAR
CCCCCCCCCCCCCHH
12.0629514104
495PhosphorylationSPSNNVYSGGSMARR
CCCCCCCCCCCCHHC
32.1829899451
498PhosphorylationNNVYSGGSMARRNTY
CCCCCCCCCHHCCCE
16.8829899451
504PhosphorylationGSMARRNTYVCERST
CCCHHCCCEEECCCH
18.6025521595
505PhosphorylationSMARRNTYVCERSTD
CCHHCCCEEECCCHH
13.4729514104
523PhosphorylationALQNGRDSSLTEMSA
HHHCCCCCCCHHHCH
26.3629899451
524PhosphorylationLQNGRDSSLTEMSAS
HHCCCCCCCHHHCHH
43.5329899451
546PhosphorylationTVASAGPSARPRHQK
CHHCCCCCCCCCCCC
35.67-
554PhosphorylationARPRHQKSMSTSGHP
CCCCCCCCCCCCCCC
16.0529899451
556PhosphorylationPRHQKSMSTSGHPIK
CCCCCCCCCCCCCCE
26.8922817900
557PhosphorylationRHQKSMSTSGHPIKV
CCCCCCCCCCCCCEE
30.0426804993
558PhosphorylationHQKSMSTSGHPIKVT
CCCCCCCCCCCCEEE
28.0029472430
565PhosphorylationSGHPIKVTLPTIKDG
CCCCCEEEECCCCCC
23.2426804993
568PhosphorylationPIKVTLPTIKDGSEA
CCEEEECCCCCCCCC
43.7126804993
588PhosphorylationAQRVPAASPSAHSIS
HHCCCCCCCCCCCCC
22.8429514104
590PhosphorylationRVPAASPSAHSISAS
CCCCCCCCCCCCCCC
35.8029899451
593PhosphorylationAASPSAHSISASTPD
CCCCCCCCCCCCCCC
20.2522817900
595PhosphorylationSPSAHSISASTPDRT
CCCCCCCCCCCCCCC
21.1229899451
597PhosphorylationSAHSISASTPDRTRF
CCCCCCCCCCCCCCC
33.4129899451
598PhosphorylationAHSISASTPDRTRFP
CCCCCCCCCCCCCCC
29.0029899451
609PhosphorylationTRFPRGSSSRSTFHG
CCCCCCCCCCCCCCH
32.3729514104
612PhosphorylationPRGSSSRSTFHGEQL
CCCCCCCCCCCHHHH
37.0622817900
613PhosphorylationRGSSSRSTFHGEQLR
CCCCCCCCCCHHHHH
20.6722817900
624PhosphorylationEQLRERRSAAYNGPP
HHHHHHHHHHHCCCC
24.3829514104
627PhosphorylationRERRSAAYNGPPASP
HHHHHHHHCCCCCCC
21.9929514104
633PhosphorylationAYNGPPASPSHETGA
HHCCCCCCCCHHCCC
32.4830372032
635PhosphorylationNGPPASPSHETGAFA
CCCCCCCCHHCCCCC
31.3129899451
638PhosphorylationPASPSHETGAFAHAR
CCCCCHHCCCCCHHH
28.5229899451
648PhosphorylationFAHARRGTSTGIISK
CCHHHCCCCCCHHHH
22.7029899451
649PhosphorylationAHARRGTSTGIISKI
CHHHCCCCCCHHHHH
27.7122324799
649O-linked_GlycosylationAHARRGTSTGIISKI
CHHHCCCCCCHHHHH
27.7122645316
650PhosphorylationHARRGTSTGIISKIT
HHHCCCCCCHHHHHH
32.0322324799
666PhosphorylationKFVRRDPSEGEASGR
HHCCCCCCCCCCCCC
63.6225521595
671PhosphorylationDPSEGEASGRADTAR
CCCCCCCCCCCCCCC
25.2225521595
680PhosphorylationRADTARGSSGDPKER
CCCCCCCCCCCHHHC
26.1229899451
699PhosphorylationGKEAKPRSLRFTWSM
CCCCCCCCEEEEEEC
32.21-
705PhosphorylationRSLRFTWSMKTTSSM
CCEEEEEECCCCCCC
13.8222006019
766PhosphorylationVCKLPRLSLNGVRFK
HHCCCCEEECCEEEE
22.5221183079
783UbiquitinationSGTSIAFKNIASKIA
CCCHHHHHHHHHHHH
38.12-

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
215TPhosphorylationKinaseLKB1Q9WTK7
Uniprot
215TPhosphorylationKinaseTAOK1Q5F2E8
Uniprot
219SPhosphorylationKinaseGSK3-BETAQ9WV60
Uniprot
613TPhosphorylationKinasePRKCZQ02956
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
215TPhosphorylation

-
215TPhosphorylation

-
219SPhosphorylation

-
613TPhosphorylation

-

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 MARK1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MARK1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MARK1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-403 ANDSER-666, AND MASS SPECTROMETRY.

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