MARK1_HUMAN - dbPTM
MARK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARK1_HUMAN
UniProt AC Q9P0L2
Protein Name Serine/threonine-protein kinase MARK1
Gene Name MARK1 {ECO:0000312|HGNC:HGNC:6896}
Organism Homo sapiens (Human).
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. [PubMed: 23666762 Involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU]
Protein Sequence MSARTPLPTVNERDTENHTSVDGYTEPHIQPTKSSSRQNIPRCRNSITSATDEQPHIGNYRLQKTIGKGNFAKVKLARHVLTGREVAVKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKYIVHRDLKAENLLLDGDMNIKIADFGFSNEFTVGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKLLVLNPIKRGSLEQIMKDRWMNVGHEEEELKPYTEPDPDFNDTKRIDIMVTMGFARDEINDALINQKYDEVMATYILLGRKPPEFEGGESLSSGNLCQRSRPSSDLNNSTLQSPAHLKVQRSISANQKQRRFSDHAGPSIPPAVSYTKRPQANSVESEQKEEWDKDVARKLGSTTVGSKSEMTASPLVGPERKKSSTIPSNNVYSGGSMARRNTYVCERTTDRYVALQNGKDSSLTEMSVSSISSAGSSVASAVPSARPRHQKSMSTSGHPIKVTLPTIKDGSEAYRPGTTQRVPAASPSAHSISTATPDRTRFPRGSSSRSTFHGEQLRERRSVAYNGPPASPSHETGAFAHARRGTSTGIISKITSKFVRRDPSEGEASGRTDTSRSTSGEPKERDKEEGKDSKPRSLRFTWSMKTTSSMDPNDMMREIRKVLDANNCDYEQKERFLLFCVHGDARQDSLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL
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
5Phosphorylation---MSARTPLPTVNE
---CCCCCCCCCCCC
28.9717192257
15PhosphorylationPTVNERDTENHTSVD
CCCCCCCCCCCCCCC
44.9320873877
19PhosphorylationERDTENHTSVDGYTE
CCCCCCCCCCCCCCC
41.8620873877
20PhosphorylationRDTENHTSVDGYTEP
CCCCCCCCCCCCCCC
15.6230576142
24PhosphorylationNHTSVDGYTEPHIQP
CCCCCCCCCCCCCCC
11.9429978859
25PhosphorylationHTSVDGYTEPHIQPT
CCCCCCCCCCCCCCC
48.8729978859
34PhosphorylationPHIQPTKSSSRQNIP
CCCCCCCCCCCCCCC
35.7030576142
36PhosphorylationIQPTKSSSRQNIPRC
CCCCCCCCCCCCCCH
45.00-
46PhosphorylationNIPRCRNSITSATDE
CCCCHHHCCCCCCCC
14.1121082442
48PhosphorylationPRCRNSITSATDEQP
CCHHHCCCCCCCCCC
16.4820873877
49PhosphorylationRCRNSITSATDEQPH
CHHHCCCCCCCCCCC
27.7429978859
51PhosphorylationRNSITSATDEQPHIG
HHCCCCCCCCCCCCC
39.5829978859
65PhosphorylationGNYRLQKTIGKGNFA
CCEEECEEECCCCHH
23.2328152594
68UbiquitinationRLQKTIGKGNFAKVK
EECEEECCCCHHHHH
46.99-
89UbiquitinationTGREVAVKIIDKTQL
CCCHHHEEECCCCCC
24.98-
93UbiquitinationVAVKIIDKTQLNPTS
HHEEECCCCCCCHHH
27.97-
94PhosphorylationAVKIIDKTQLNPTSL
HEEECCCCCCCHHHH
34.2420068231
99PhosphorylationDKTQLNPTSLQKLFR
CCCCCCHHHHHHHHH
40.78-
100PhosphorylationKTQLNPTSLQKLFRE
CCCCCHHHHHHHHHH
30.02-
131PhosphorylationEVIETEKTLYLVMEY
EEECCCCEEEEEEHH
17.8825921289
140PhosphorylationYLVMEYASGGEVFDY
EEEEHHHCCHHHHHH
46.5625921289
184UbiquitinationYIVHRDLKAENLLLD
CCCCCCCCHHHEEEC
58.9221906983
204PhosphorylationKIADFGFSNEFTVGN
EECCCCCCCCEECCC
35.5130206219
208PhosphorylationFGFSNEFTVGNKLDT
CCCCCCEECCCCHHH
22.7117573348
215PhosphorylationTVGNKLDTFCGSPPY
ECCCCHHHCCCCCCC
31.1214976552
219PhosphorylationKLDTFCGSPPYAAPE
CHHHCCCCCCCCCHH
24.7119664994
222PhosphorylationTFCGSPPYAAPELFQ
HCCCCCCCCCHHHHC
20.8423898821
231UbiquitinationAPELFQGKKYDGPEV
CHHHHCCCCCCCCCC
37.06-
279PhosphorylationGKYRIPFYMSTDCEN
CCCCCCEEECCCHHH
5.7029496907
281PhosphorylationYRIPFYMSTDCENLL
CCCCEEECCCHHHHH
15.0921082442
282PhosphorylationRIPFYMSTDCENLLK
CCCEEECCCHHHHHH
28.3021082442
301PhosphorylationLNPIKRGSLEQIMKD
HCCCCCCCHHHHHHH
32.5325332170
307UbiquitinationGSLEQIMKDRWMNVG
CCHHHHHHHCCCCCC
45.85-
333PhosphorylationPDPDFNDTKRIDIMV
CCCCCCCCCCEEEEE
24.2719369195
380PhosphorylationPEFEGGESLSSGNLC
CCCCCCCCCCCCCCC
36.5027251275
382PhosphorylationFEGGESLSSGNLCQR
CCCCCCCCCCCCCCC
45.5420873877
383PhosphorylationEGGESLSSGNLCQRS
CCCCCCCCCCCCCCC
36.6727251275
390PhosphorylationSGNLCQRSRPSSDLN
CCCCCCCCCCCCCCC
23.7523403867
393PhosphorylationLCQRSRPSSDLNNST
CCCCCCCCCCCCCCC
35.0623898821
394PhosphorylationCQRSRPSSDLNNSTL
CCCCCCCCCCCCCCC
49.1221082442
399PhosphorylationPSSDLNNSTLQSPAH
CCCCCCCCCCCCHHH
29.4425159151
400PhosphorylationSSDLNNSTLQSPAHL
CCCCCCCCCCCHHHH
30.8223403867
403PhosphorylationLNNSTLQSPAHLKVQ
CCCCCCCCHHHHHHH
27.4525159151
412PhosphorylationAHLKVQRSISANQKQ
HHHHHHHHCCCHHHC
12.1029514088
414PhosphorylationLKVQRSISANQKQRR
HHHHHHCCCHHHCCC
23.5529900121
423PhosphorylationNQKQRRFSDHAGPSI
HHHCCCCCCCCCCCC
27.0325159151
429PhosphorylationFSDHAGPSIPPAVSY
CCCCCCCCCCCCCCC
46.9727732954
444PhosphorylationTKRPQANSVESEQKE
CCCCCCCCCCHHHHH
30.2225159151
463PhosphorylationDVARKLGSTTVGSKS
HHHHHHCCCCCCCCC
31.2028857561
464PhosphorylationVARKLGSTTVGSKSE
HHHHHCCCCCCCCCC
24.5728857561
465PhosphorylationARKLGSTTVGSKSEM
HHHHCCCCCCCCCCC
25.2728857561
468PhosphorylationLGSTTVGSKSEMTAS
HCCCCCCCCCCCCCC
28.7725159151
470PhosphorylationSTTVGSKSEMTASPL
CCCCCCCCCCCCCCC
34.0128857561
473PhosphorylationVGSKSEMTASPLVGP
CCCCCCCCCCCCCCC
21.6728857561
475PhosphorylationSKSEMTASPLVGPER
CCCCCCCCCCCCCCC
15.0325159151
485PhosphorylationVGPERKKSSTIPSNN
CCCCCCCCCCCCCCC
35.4321945579
486PhosphorylationGPERKKSSTIPSNNV
CCCCCCCCCCCCCCC
38.9621945579
487PhosphorylationPERKKSSTIPSNNVY
CCCCCCCCCCCCCCC
43.9521945579
490PhosphorylationKKSSTIPSNNVYSGG
CCCCCCCCCCCCCCC
36.8721945579
494PhosphorylationTIPSNNVYSGGSMAR
CCCCCCCCCCCCCHH
12.0621945579
495PhosphorylationIPSNNVYSGGSMARR
CCCCCCCCCCCCHHC
32.1821945579
498PhosphorylationNNVYSGGSMARRNTY
CCCCCCCCCHHCCEE
16.8821945579
504PhosphorylationGSMARRNTYVCERTT
CCCHHCCEEEEECCC
18.6028857561
505PhosphorylationSMARRNTYVCERTTD
CCHHCCEEEEECCCC
13.4723312004
514PhosphorylationCERTTDRYVALQNGK
EECCCCCEEEEECCC
7.9027642862
514 (in isoform 2)Phosphorylation-7.9025159151
523PhosphorylationALQNGKDSSLTEMSV
EEECCCCCCCCEEEH
30.6322496350
524PhosphorylationLQNGKDSSLTEMSVS
EECCCCCCCCEEEHH
49.8227732954
526PhosphorylationNGKDSSLTEMSVSSI
CCCCCCCCEEEHHHH
31.4327732954
529PhosphorylationDSSLTEMSVSSISSA
CCCCCEEEHHHHHHC
16.7727732954
531PhosphorylationSLTEMSVSSISSAGS
CCCEEEHHHHHHCCH
18.0427732954
532PhosphorylationLTEMSVSSISSAGSS
CCEEEHHHHHHCCHH
25.0827732954
534PhosphorylationEMSVSSISSAGSSVA
EEEHHHHHHCCHHHH
18.9827732954
535PhosphorylationMSVSSISSAGSSVAS
EEHHHHHHCCHHHHH
34.6727732954
538PhosphorylationSSISSAGSSVASAVP
HHHHHCCHHHHHHCC
22.7429449344
554PhosphorylationARPRHQKSMSTSGHP
CCCCCCCCCCCCCCC
16.0524719451
556PhosphorylationPRHQKSMSTSGHPIK
CCCCCCCCCCCCCCE
26.8928857561
557PhosphorylationRHQKSMSTSGHPIKV
CCCCCCCCCCCCCEE
30.0427732954
558PhosphorylationHQKSMSTSGHPIKVT
CCCCCCCCCCCCEEE
28.0027732954
573PhosphorylationLPTIKDGSEAYRPGT
ECCCCCCCCCCCCCC
29.2324719451
580PhosphorylationSEAYRPGTTQRVPAA
CCCCCCCCCCCCCCC
23.57-
581PhosphorylationEAYRPGTTQRVPAAS
CCCCCCCCCCCCCCC
21.94-
588PhosphorylationTQRVPAASPSAHSIS
CCCCCCCCCCCCCCC
22.8426055452
590PhosphorylationRVPAASPSAHSISTA
CCCCCCCCCCCCCCC
35.8021712546
593PhosphorylationAASPSAHSISTATPD
CCCCCCCCCCCCCCC
20.2523403867
595PhosphorylationSPSAHSISTATPDRT
CCCCCCCCCCCCCCC
18.2723403867
596PhosphorylationPSAHSISTATPDRTR
CCCCCCCCCCCCCCC
32.6421712546
598PhosphorylationAHSISTATPDRTRFP
CCCCCCCCCCCCCCC
26.3023403867
602PhosphorylationSTATPDRTRFPRGSS
CCCCCCCCCCCCCCC
44.0029449344
612PhosphorylationPRGSSSRSTFHGEQL
CCCCCCCCCCCHHHH
37.0619276368
613PhosphorylationRGSSSRSTFHGEQLR
CCCCCCCCCCHHHHH
20.6721712546
624PhosphorylationEQLRERRSVAYNGPP
HHHHHHHCHHHCCCC
19.8130177828
627PhosphorylationRERRSVAYNGPPASP
HHHHCHHHCCCCCCC
20.6323186163
627 (in isoform 3)Phosphorylation-20.6325159151
633PhosphorylationAYNGPPASPSHETGA
HHCCCCCCCCHHCCC
32.4825159151
635PhosphorylationNGPPASPSHETGAFA
CCCCCCCCHHCCCCC
31.3129978859
638PhosphorylationPASPSHETGAFAHAR
CCCCCHHCCCCCHHH
28.5228857561
646MethylationGAFAHARRGTSTGII
CCCCHHHCCCCCCHH
54.2382797037
648PhosphorylationFAHARRGTSTGIISK
CCHHHCCCCCCHHHH
22.7025159151
649PhosphorylationAHARRGTSTGIISKI
CHHHCCCCCCHHHHH
27.7125159151
650PhosphorylationHARRGTSTGIISKIT
HHHCCCCCCHHHHHH
32.0322496350
654PhosphorylationGTSTGIISKITSKFV
CCCCCHHHHHHHHHC
18.9823312004
666PhosphorylationKFVRRDPSEGEASGR
HHCCCCCCCCCCCCC
63.62-
679PhosphorylationGRTDTSRSTSGEPKE
CCCCCCCCCCCCCCC
27.05-
681PhosphorylationTDTSRSTSGEPKERD
CCCCCCCCCCCCCCC
42.26-
699PhosphorylationGKDSKPRSLRFTWSM
CCCCCCCEEEEEEEC
32.2120860994
703PhosphorylationKPRSLRFTWSMKTTS
CCCEEEEEEECEECC
15.3629759185
705PhosphorylationRSLRFTWSMKTTSSM
CEEEEEEECEECCCC
13.82-
708PhosphorylationRFTWSMKTTSSMDPN
EEEEECEECCCCCHH
24.2221130716
709PhosphorylationFTWSMKTTSSMDPND
EEEECEECCCCCHHH
17.1821130716
710PhosphorylationTWSMKTTSSMDPNDM
EEECEECCCCCHHHH
28.9721130716
711PhosphorylationWSMKTTSSMDPNDMM
EECEECCCCCHHHHH
25.7221130716
723UbiquitinationDMMREIRKVLDANNC
HHHHHHHHHHHHCCC
53.46-
746 (in isoform 3)Ubiquitination-24.5721890473
766PhosphorylationVCKLPRLSLNGVRFK
HHCCCCEEECCEEEE
22.5227067055
768 (in isoform 2)Ubiquitination-43.4621890473
776PhosphorylationGVRFKRISGTSIAFK
CEEEEECCCCHHHHH
39.8029514088
778PhosphorylationRFKRISGTSIAFKNI
EEEECCCCHHHHHHH
15.3529514088
779PhosphorylationFKRISGTSIAFKNIA
EEECCCCHHHHHHHH
18.5529514088
783UbiquitinationSGTSIAFKNIASKIA
CCCHHHHHHHHHHHH
38.12-
783 (in isoform 1)Ubiquitination-38.1221890473
787PhosphorylationIAFKNIASKIANELK
HHHHHHHHHHHHHHC
22.31-

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
215TPhosphorylationKinaseSTK11Q15831
PhosphoELM
215TPhosphorylationKinaseTAOK1Q7L7X3
Uniprot
219SPhosphorylationKinaseGSK3BP49841
GPS
613TPhosphorylationKinasePRKCZQ05513
Uniprot

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

14976552
215TPhosphorylation

14976552
219SPhosphorylation

17573348
613TPhosphorylation

17573348

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTAP2_RATMap2physical
8631898
MAP4_MOUSEMap4physical
8631898
TAU_HUMANMAPTphysical
8631898
TAU_HUMANMAPTphysical
10090741
TAU_HUMANMAPTphysical
23666762
C102B_HUMANCCDC102Bphysical
24722188

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MARK1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463; SER-468; SER-470;SER-475; SER-588 AND SER-633, AND MASS SPECTROMETRY.
"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-588 AND THR-596, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; SER-46; THR-215;SER-219; SER-403; SER-423; SER-475; SER-588 AND SER-633, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-598, ANDMASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND MASSSPECTROMETRY.
"LKB1 is a master kinase that activates 13 kinases of the AMPKsubfamily, including MARK/PAR-1.";
Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,Alessi D.R.;
EMBO J. 23:833-843(2004).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION,PHOSPHORYLATION AT THR-215, AND MUTAGENESIS OF THR-215.

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