MARK2_MOUSE - dbPTM
MARK2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARK2_MOUSE
UniProt AC Q05512
Protein Name Serine/threonine-protein kinase MARK2
Gene Name Mark2
Organism Mus musculus (Mouse).
Sequence Length 776
Subcellular Localization Cell membrane
Peripheral membrane protein. Lateral cell membrane. Cytoplasm, cytoskeleton. Cell projection, dendrite . Cytoplasm . Phosphorylation at Thr-593 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from
Protein Description Serine/threonine-protein kinase. Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells..
Protein Sequence MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMLRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKIDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRSSDQAVPAIPTSNSYSKKTQSNNAENKRPEEETGRKASSTAKVPASPLPGLDRKKTTPAPSTNSVLSTSTNRSRNSPLLDRASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSSGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLNEPESKDRVETLRPHVVGSGGTDKDKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL
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
6Phosphorylation--MSSARTPLPTLNE
--CCCCCCCCCCCCC		28.9729514104
29PhosphorylationGHLDSKPSSKSNMLR
CCCCCCCCHHHHCCC		54.8829899451
40PhosphorylationNMLRGRNSATSADEQ
HCCCCCCCCCCCCCC		31.4025521595
42PhosphorylationLRGRNSATSADEQPH
CCCCCCCCCCCCCCC		25.0323684622
43PhosphorylationRGRNSATSADEQPHI
CCCCCCCCCCCCCCC		33.1823684622
58PhosphorylationGNYRLLKTIGKGNFA
CCCCHHHHHCCCCCH		34.6318056256
91PhosphorylationIDKTQLNSSSLQKLF
CCHHHCCHHHHHHHH		29.87-
92PhosphorylationDKTQLNSSSLQKLFR
CHHHCCHHHHHHHHH		33.71-
93PhosphorylationKTQLNSSSLQKLFRE
HHHCCHHHHHHHHHH		34.34-
161PhosphorylationAKFRQIVSAVQYCHQ
HHHHHHHHHHHHHHH		25.09-
165PhosphorylationQIVSAVQYCHQKFIV
HHHHHHHHHHHHHCC		5.8226487105
197PhosphorylationKIADFGFSNEFTFGN
EECCCCCCCCEECCC		35.5126239621
201PhosphorylationFGFSNEFTFGNKLDT
CCCCCCEECCCCHHH		25.1826239621
208PhosphorylationTFGNKLDTFCGSPPY
ECCCCHHHCCCCCCC		31.1225521595
212PhosphorylationKLDTFCGSPPYAAPE
CHHHCCCCCCCCCHH		24.7122942356
215PhosphorylationTFCGSPPYAAPELFQ
HCCCCCCCCCHHHHC		20.8425159016
274PhosphorylationYRIPFYMSTDCENLL
CCCCEEECCCHHHHH		15.09-
275PhosphorylationRIPFYMSTDCENLLK
CCCEEECCCHHHHHH		28.30-
294PhosphorylationLNPSKRGTLEQIMKD
CCHHHCCCHHHHHHH		31.02-
365PhosphorylationYLLLGYKSSELEGDT
HHHHCCCCHHCCCCE		22.1426160508
366PhosphorylationLLLGYKSSELEGDTI
HHHCCCCHHCCCCEE		41.8926160508
372PhosphorylationSSELEGDTITLKPRP
CHHCCCCEEEEEECC		27.0726160508
374PhosphorylationELEGDTITLKPRPSA
HCCCCEEEEEECCCC		30.7126160508
380PhosphorylationITLKPRPSADLTNSS
EEEEECCCCCCCCCC		35.3826239621
384PhosphorylationPRPSADLTNSSAPSP
ECCCCCCCCCCCCCC		33.3325293948
386PhosphorylationPSADLTNSSAPSPSH
CCCCCCCCCCCCCCC		23.7326239621
387PhosphorylationSADLTNSSAPSPSHK
CCCCCCCCCCCCCCC		46.3926239621
390PhosphorylationLTNSSAPSPSHKVQR
CCCCCCCCCCCCCHH		38.4626824392
392PhosphorylationNSSAPSPSHKVQRSV
CCCCCCCCCCCHHCC		40.0325263469
398PhosphorylationPSHKVQRSVSANPKQ
CCCCCHHCCCCCHHH		11.8823375375
400PhosphorylationHKVQRSVSANPKQRR
CCCHHCCCCCHHHCC		24.4724453211
408PhosphorylationANPKQRRSSDQAVPA
CCHHHCCCCCCCCCC		40.2225521595
409PhosphorylationNPKQRRSSDQAVPAI
CHHHCCCCCCCCCCC		31.7525521595
418PhosphorylationQAVPAIPTSNSYSKK
CCCCCCCCCCCCCCC		34.1326239621
419PhosphorylationAVPAIPTSNSYSKKT
CCCCCCCCCCCCCCC		20.5825521595
421PhosphorylationPAIPTSNSYSKKTQS
CCCCCCCCCCCCCCC		30.4726239621
422PhosphorylationAIPTSNSYSKKTQSN
CCCCCCCCCCCCCCC		28.8526239621
423PhosphorylationIPTSNSYSKKTQSNN
CCCCCCCCCCCCCCC		27.7426239621
426PhosphorylationSNSYSKKTQSNNAEN
CCCCCCCCCCCCCCC		40.7522802335
428PhosphorylationSYSKKTQSNNAENKR
CCCCCCCCCCCCCCC		36.9622802335
445PhosphorylationEETGRKASSTAKVPA
HHHCCCCCCCCCCCC		31.1225266776
446PhosphorylationETGRKASSTAKVPAS
HHCCCCCCCCCCCCC		36.9326239621
447PhosphorylationTGRKASSTAKVPASP
HCCCCCCCCCCCCCC		28.1826239621
453PhosphorylationSTAKVPASPLPGLDR
CCCCCCCCCCCCCCC		22.3927087446
463PhosphorylationPGLDRKKTTPAPSTN
CCCCCCCCCCCCCCC		40.8425266776
464PhosphorylationGLDRKKTTPAPSTNS
CCCCCCCCCCCCCCC		26.7429472430
468PhosphorylationKKTTPAPSTNSVLST
CCCCCCCCCCCCCCC		42.1826643407
469PhosphorylationKTTPAPSTNSVLSTS
CCCCCCCCCCCCCCC		30.3825293948
471PhosphorylationTPAPSTNSVLSTSTN
CCCCCCCCCCCCCCC		25.2326643407
474PhosphorylationPSTNSVLSTSTNRSR
CCCCCCCCCCCCCCC		20.3926643407
475PhosphorylationSTNSVLSTSTNRSRN
CCCCCCCCCCCCCCC		35.1026643407
476PhosphorylationTNSVLSTSTNRSRNS
CCCCCCCCCCCCCCC		21.9525266776
477PhosphorylationNSVLSTSTNRSRNSP
CCCCCCCCCCCCCCC		34.4425293948
480PhosphorylationLSTSTNRSRNSPLLD
CCCCCCCCCCCCCCC		37.5727087446
483PhosphorylationSTNRSRNSPLLDRAS
CCCCCCCCCCCCHHH		18.8027087446
490PhosphorylationSPLLDRASLGQASIQ
CCCCCHHHHCCHHHH		33.6526745281
490 (in isoform 3)Phosphorylation-33.6529514104
490 (in isoform 4)Phosphorylation-33.6529514104
495PhosphorylationRASLGQASIQNGKDS
HHHHCCHHHHCCCCC		19.4726745281
495 (in isoform 3)Phosphorylation-19.4729514104
495 (in isoform 4)Phosphorylation-19.4729514104
502 (in isoform 3)Phosphorylation-29.2618846507
502 (in isoform 4)Phosphorylation-29.2618846507
503 (in isoform 3)Phosphorylation-7.3429899451
503 (in isoform 4)Phosphorylation-7.3429899451
508PhosphorylationDSLTMPGSRASTASA
CCCCCCCCHHHHHHH		20.8526643407
511PhosphorylationTMPGSRASTASASAA
CCCCCHHHHHHHHHH		24.3226239621
512PhosphorylationMPGSRASTASASAAV
CCCCHHHHHHHHHHH		24.5228066266
512 (in isoform 3)Phosphorylation-24.5225266776
512 (in isoform 4)Phosphorylation-24.5225266776
514PhosphorylationGSRASTASASAAVSA
CCHHHHHHHHHHHHH		23.8926643407
514 (in isoform 3)Phosphorylation-23.8925266776
514 (in isoform 4)Phosphorylation-23.8925266776
516PhosphorylationRASTASASAAVSAAR
HHHHHHHHHHHHHHC		17.7926643407
519 (in isoform 3)Phosphorylation-3.9123984901
519 (in isoform 4)Phosphorylation-3.9123984901
520PhosphorylationASASAAVSAARPRQH
HHHHHHHHHHCHHHH		16.1026643407
520 (in isoform 3)Phosphorylation-16.1023984901
520 (in isoform 4)Phosphorylation-16.1023984901
521 (in isoform 3)Phosphorylation-10.8223984901
521 (in isoform 4)Phosphorylation-10.8223984901
522 (in isoform 3)Phosphorylation-17.9523984901
522 (in isoform 4)Phosphorylation-17.9523984901
528 (in isoform 3)Phosphorylation-31.0525367039
528 (in isoform 4)Phosphorylation-31.0525367039
530PhosphorylationRPRQHQKSMSASVHP
CHHHHHHHCCCCCCC		16.0523984901
532PhosphorylationRQHQKSMSASVHPNK
HHHHHHCCCCCCCCC		25.2023684622
534PhosphorylationHQKSMSASVHPNKAS
HHHHCCCCCCCCCCC		17.4123984901
566PhosphorylationPQRVPVASPSAHNIS
CCCCCCCCCCCCCCC		21.4428725479
568PhosphorylationRVPVASPSAHNISSS
CCCCCCCCCCCCCCC		39.4027087446
573PhosphorylationSPSAHNISSSSGAPD
CCCCCCCCCCCCCCC		29.5025619855
574PhosphorylationPSAHNISSSSGAPDR
CCCCCCCCCCCCCCC		25.4025619855
575PhosphorylationSAHNISSSSGAPDRT
CCCCCCCCCCCCCCC		26.4625619855
576PhosphorylationAHNISSSSGAPDRTN
CCCCCCCCCCCCCCC		40.7025619855
576 (in isoform 4)Phosphorylation-40.7029514104
579 (in isoform 4)Phosphorylation-34.8329514104
582PhosphorylationSSGAPDRTNFPRGVS
CCCCCCCCCCCCCCC		48.9026643407
589PhosphorylationTNFPRGVSSRSTFHA
CCCCCCCCCCCCEEC		23.9027841257
590PhosphorylationNFPRGVSSRSTFHAG
CCCCCCCCCCCEECC		28.0421454597
591 (in isoform 4)Phosphorylation-32.0126745281
592PhosphorylationPRGVSSRSTFHAGQL
CCCCCCCCCEECCCC		37.0622322096
593PhosphorylationRGVSSRSTFHAGQLR
CCCCCCCCEECCCCC		20.5222322096
610PhosphorylationRDQQNLPYGVTPASP
CCCCCCCCCCCCCCC		27.6525619855
613PhosphorylationQNLPYGVTPASPSGH
CCCCCCCCCCCCCCC		14.5825619855
616PhosphorylationPYGVTPASPSGHSQG
CCCCCCCCCCCCCCC		22.3227087446
618PhosphorylationGVTPASPSGHSQGRR
CCCCCCCCCCCCCCC		46.7922942356
621PhosphorylationPASPSGHSQGRRGAS
CCCCCCCCCCCCCCC		37.5422942356
628PhosphorylationSQGRRGASGSIFSKF
CCCCCCCCCCHHHHH		35.5826824392
630PhosphorylationGRRGASGSIFSKFTS
CCCCCCCCHHHHHHH		20.2627600695
633PhosphorylationGASGSIFSKFTSKFV
CCCCCHHHHHHHHHH		25.7821743459
636PhosphorylationGSIFSKFTSKFVRRN
CCHHHHHHHHHHHHH		34.4422817900
637PhosphorylationSIFSKFTSKFVRRNL
CHHHHHHHHHHHHHC		27.5122817900
655PhosphorylationESKDRVETLRPHVVG
CHHHHHHHHCCHHCC		25.8029899451
663PhosphorylationLRPHVVGSGGTDKDK
HCCHHCCCCCCCCCH		23.5721183079
666PhosphorylationHVVGSGGTDKDKEEF
HHCCCCCCCCCHHHH		43.3221082442
680PhosphorylationFREAKPRSLRFTWSM
HHHCCCCCEEEEEEC		32.21-
684O-linked_GlycosylationKPRSLRFTWSMKTTS
CCCCEEEEEECCCCC		15.3655412611
684PhosphorylationKPRSLRFTWSMKTTS
CCCCEEEEEECCCCC		15.36-
686PhosphorylationRSLRFTWSMKTTSSM
CCEEEEEECCCCCCC		13.8222006019
704UbiquitinationEMMREIRKVLDANSC
HHHHHHHHHHCCCCC		53.46-
710PhosphorylationRKVLDANSCQSELHE
HHHHCCCCCCHHHHH		18.4326824392
747PhosphorylationVCKLPRLSLNGVRFK
ECCCCCEEECCEEEE		22.5221183079
759PhosphorylationRFKRISGTSMAFKNI
EEEECCCCHHHHHHH		14.4529176673
760PhosphorylationFKRISGTSMAFKNIA
EEECCCCHHHHHHHH		16.1929176673
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
91SPhosphorylationKinaseCAMK1Q91YS8
Uniprot
92SPhosphorylationKinaseCAMK1Q91YS8
Uniprot
93SPhosphorylationKinaseCAMK1Q91YS8
Uniprot
208TPhosphorylationKinaseSTK11Q9WTK7
GPS
208TPhosphorylationKinaseTAOK1Q5F2E8
Uniprot
212SPhosphorylationKinaseGSK3-BETAQ9WV60
Uniprot
294TPhosphorylationKinaseCAMK1Q91YS8
Uniprot
593TPhosphorylationKinasePRKCZQ02956
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
208TPhosphorylation

-
208TPhosphorylation

-
212SPhosphorylation

-
593TPhosphorylation

-
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 MARK2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433B_MOUSEYwhabphysical
16959763
1433G_MOUSEYwhagphysical
16959763
1433F_MOUSEYwhahphysical
16959763
EEA1_HUMANEEA1physical
26496610
ARK72_HUMANAKR7A2physical
26496610
CYH1_HUMANCYTH1physical
26496610
RNF41_HUMANRNF41physical
26496610
SRSF8_HUMANSRSF8physical
26496610
CLAP2_HUMANCLASP2physical
26496610
MTCL1_HUMANMTCL1physical
26496610
PPHLN_HUMANPPHLN1physical
26496610
ERI3_HUMANERI3physical
26496610
SOGA1_HUMANSOGA1physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MARK2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND MASSSPECTROMETRY.
"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 SER-40; SER-483 AND SER-592,AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208 AND SER-568, ANDMASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208 AND SER-453, ANDMASS SPECTROMETRY.
"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-483, AND MASSSPECTROMETRY.

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