MARK4_HUMAN - dbPTM
MARK4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARK4_HUMAN
UniProt AC Q96L34
Protein Name MAP/microtubule affinity-regulating kinase 4
Gene Name MARK4
Organism Homo sapiens (Human).
Sequence Length 752
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm, cytoskeleton, cilium axoneme . Cytoplasm . Cell projection, dendrite . No
Protein Description Serine/threonine-protein kinase. [PubMed: 15009667]
Protein Sequence MSSRTVLAPGNDRNSDTHGTLGSGRSSDKGPSWSSRSLGARCRNSIASCPEEQPHVGNYRLLRTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPSSLQKLFREVRIMKGLNHPNIVKLFEVIETEKTLYLVMEYASAGEVFDYLVSHGRMKEKEARAKFRQIVSAVHYCHQKNIVHRDLKAENLLLDAEANIKIADFGFSNEFTLGSKLDTFCGSPPYAAPELFQGKKYDGPEVDIWSLGVILYTLVSGSLPFDGHNLKELRERVLRGKYRVPFYMSTDCESILRRFLVLNPAKRCTLEQIMKDKWINIGYEGEELKPYTEPEEDFGDTKRIEVMVGMGYTREEIKESLTSQKYNEVTATYLLLGRKTEEGGDRGAPGLALARVRAPSDTTNGTSSSKGTSHSKGQRSSSSTYHRQRRHSDFCGPSPAPLHPKRSPTSTGEAELKEERLPGRKASCSTAGSGSRGLPPSSPMVSSAHNPNKAEIPERRKDSTSTPNNLPPSMMTRRNTYVCTERPGAERPSLLPNGKENSSGTPRVPPASPSSHSLAPPSGERSRLARGSTIRSTFHGGQVRDRRAGGGGGGGVQNGPPASPTLAHEAAPLPAGRPRPTTNLFTKLTSKLTRRVADEPERIGGPEVTSCHLPWDQTETAPRLLRFPWSVKLTSSRPPEALMAALRQATAAARCRCRQPQPFLLACLHGGAGGPEPLSHFEVEVCQLPRPGLRGVLFRRVAGTALAFRTLVTRISNDLEL
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
2Acetylation------MSSRTVLAP
------CCCCEEECC
28.6419413330
2Phosphorylation------MSSRTVLAP
------CCCCEEECC
28.6419369195
2 (in isoform 2)Acetylation-28.64-
15PhosphorylationAPGNDRNSDTHGTLG
CCCCCCCCCCCCCCC
44.7922210691
17PhosphorylationGNDRNSDTHGTLGSG
CCCCCCCCCCCCCCC
23.2522210691
20PhosphorylationRNSDTHGTLGSGRSS
CCCCCCCCCCCCCCC
21.9723186163
23PhosphorylationDTHGTLGSGRSSDKG
CCCCCCCCCCCCCCC
33.8620071362
26PhosphorylationGTLGSGRSSDKGPSW
CCCCCCCCCCCCCCC
46.5517192257
26 (in isoform 2)Phosphorylation-46.55-
27PhosphorylationTLGSGRSSDKGPSWS
CCCCCCCCCCCCCCC
41.8222617229
29UbiquitinationGSGRSSDKGPSWSSR
CCCCCCCCCCCCCHH
74.7429967540
32PhosphorylationRSSDKGPSWSSRSLG
CCCCCCCCCCHHHHH
48.5427794612
34PhosphorylationSDKGPSWSSRSLGAR
CCCCCCCCHHHHHHH
21.8827794612
35UbiquitinationDKGPSWSSRSLGARC
CCCCCCCHHHHHHHH
21.4527667366
35PhosphorylationDKGPSWSSRSLGARC
CCCCCCCHHHHHHHH
21.4527794612
45PhosphorylationLGARCRNSIASCPEE
HHHHHHHCHHCCCCC
10.5329978859
48PhosphorylationRCRNSIASCPEEQPH
HHHHCHHCCCCCCCC
28.6529978859
60MethylationQPHVGNYRLLRTIGK
CCCCCCCHHHEEECC
31.1154557239
64PhosphorylationGNYRLLRTIGKGNFA
CCCHHHEEECCCCCH
33.7728152594
67UbiquitinationRLLRTIGKGNFAKVK
HHHEEECCCCCHHHH
46.99-
88UbiquitinationTGREVAIKIIDKTQL
CCCHHHEEECCCCCC
24.70-
92UbiquitinationVAIKIIDKTQLNPSS
HHEEECCCCCCCHHH
27.9729967540
93PhosphorylationAIKIIDKTQLNPSSL
HEEECCCCCCCHHHH
34.2430622161
98PhosphorylationDKTQLNPSSLQKLFR
CCCCCCHHHHHHHHH
42.4830622161
99PhosphorylationKTQLNPSSLQKLFRE
CCCCCHHHHHHHHHH
35.7630622161
102UbiquitinationLNPSSLQKLFREVRI
CCHHHHHHHHHHHHH
55.6927667366
111UbiquitinationFREVRIMKGLNHPNI
HHHHHHHCCCCCCCH
58.8529967540
116UbiquitinationIMKGLNHPNIVKLFE
HHCCCCCCCHHHHEE
31.0422817900
183UbiquitinationNIVHRDLKAENLLLD
CCCCCCCHHHHHEEE
58.9222817900
183 (in isoform 1)Ubiquitination-58.9221906983
183 (in isoform 2)Ubiquitination-58.9221906983
210PhosphorylationSNEFTLGSKLDTFCG
CCCEECCCCHHHCCC
32.9128464451
214 (in isoform 2)Phosphorylation-31.12-
214PhosphorylationTLGSKLDTFCGSPPY
ECCCCHHHCCCCCCC
31.1214976552
218 (in isoform 2)Phosphorylation-24.71-
218PhosphorylationKLDTFCGSPPYAAPE
CHHHCCCCCCCCCHH
24.7119664994
221PhosphorylationTFCGSPPYAAPELFQ
HCCCCCCCCCHHHHC
20.8423898821
230UbiquitinationAPELFQGKKYDGPEV
CHHHHCCCCCCCCCC
37.0627667366
231UbiquitinationPELFQGKKYDGPEVD
HHHHCCCCCCCCCCC
56.23-
297UbiquitinationFLVLNPAKRCTLEQI
HHHCCHHHCCCHHHH
49.6227667366
306UbiquitinationCTLEQIMKDKWINIG
CCHHHHHHCCCEECC
58.7629967540
320UbiquitinationGYEGEELKPYTEPEE
CCCCCCCCCCCCCHH
38.9829967540
351PhosphorylationTREEIKESLTSQKYN
CHHHHHHHHHHCHHH
31.7623403867
353PhosphorylationEEIKESLTSQKYNEV
HHHHHHHHHCHHHHH
38.0929496907
356UbiquitinationKESLTSQKYNEVTAT
HHHHHHCHHHHHHHH
50.22-
364PhosphorylationYNEVTATYLLLGRKT
HHHHHHHHHHHCCCC
7.9029496907
391PhosphorylationLARVRAPSDTTNGTS
EEEEECCCCCCCCCC
46.7521712546
393PhosphorylationRVRAPSDTTNGTSSS
EEECCCCCCCCCCCC
26.8830576142
394PhosphorylationVRAPSDTTNGTSSSK
EECCCCCCCCCCCCC
36.3230576142
398PhosphorylationSDTTNGTSSSKGTSH
CCCCCCCCCCCCCCC
33.7328985074
400PhosphorylationTTNGTSSSKGTSHSK
CCCCCCCCCCCCCCC
34.5728985074
403PhosphorylationGTSSSKGTSHSKGQR
CCCCCCCCCCCCCCC
27.3130576142
404PhosphorylationTSSSKGTSHSKGQRS
CCCCCCCCCCCCCCC
34.1421712546
423PhosphorylationYHRQRRHSDFCGPSP
HCHHHCCCCCCCCCC
30.4827273156
429PhosphorylationHSDFCGPSPAPLHPK
CCCCCCCCCCCCCCC
20.9823927012
438PhosphorylationAPLHPKRSPTSTGEA
CCCCCCCCCCCCCCH
38.3629255136
440PhosphorylationLHPKRSPTSTGEAEL
CCCCCCCCCCCCHHH
39.9229255136
441PhosphorylationHPKRSPTSTGEAELK
CCCCCCCCCCCHHHH
37.4929255136
442PhosphorylationPKRSPTSTGEAELKE
CCCCCCCCCCHHHHH
41.3329255136
458PhosphorylationRLPGRKASCSTAGSG
CCCCCCCCCCCCCCC
16.1924719451
460PhosphorylationPGRKASCSTAGSGSR
CCCCCCCCCCCCCCC
20.8523403867
461PhosphorylationGRKASCSTAGSGSRG
CCCCCCCCCCCCCCC
39.0923403867
464PhosphorylationASCSTAGSGSRGLPP
CCCCCCCCCCCCCCC
31.0023403867
466PhosphorylationCSTAGSGSRGLPPSS
CCCCCCCCCCCCCCC
25.5223403867
472PhosphorylationGSRGLPPSSPMVSSA
CCCCCCCCCCCCCCC
45.1728348404
473PhosphorylationSRGLPPSSPMVSSAH
CCCCCCCCCCCCCCC
23.8428348404
478PhosphorylationPSSPMVSSAHNPNKA
CCCCCCCCCCCCCCC
23.3325022875
494PhosphorylationIPERRKDSTSTPNNL
CCHHHCCCCCCCCCC
27.5622210691
495PhosphorylationPERRKDSTSTPNNLP
CHHHCCCCCCCCCCC
46.9122210691
496PhosphorylationERRKDSTSTPNNLPP
HHHCCCCCCCCCCCH
45.9130576142
496 (in isoform 2)Phosphorylation-45.91-
497PhosphorylationRRKDSTSTPNNLPPS
HHCCCCCCCCCCCHH
30.0830576142
504 (in isoform 2)Phosphorylation-21.17-
504PhosphorylationTPNNLPPSMMTRRNT
CCCCCCHHHHCCCCE
21.1729759185
507 (in isoform 2)Phosphorylation-20.17-
507PhosphorylationNLPPSMMTRRNTYVC
CCCHHHHCCCCEEEE
20.1719651622
511PhosphorylationSMMTRRNTYVCTERP
HHHCCCCEEEEECCC
18.6030576142
512PhosphorylationMMTRRNTYVCTERPG
HHCCCCEEEEECCCC
9.3323312004
543PhosphorylationTPRVPPASPSSHSLA
CCCCCCCCCCCCCCC
30.9614976552
545PhosphorylationRVPPASPSSHSLAPP
CCCCCCCCCCCCCCC
37.8823403867
546PhosphorylationVPPASPSSHSLAPPS
CCCCCCCCCCCCCCC
22.0823403867
548PhosphorylationPASPSSHSLAPPSGE
CCCCCCCCCCCCCCC
28.3323186163
553PhosphorylationSHSLAPPSGERSRLA
CCCCCCCCCCCHHHC
52.8323186163
561MethylationGERSRLARGSTIRST
CCCHHHCCCCCCCCE
44.16115482595
563PhosphorylationRSRLARGSTIRSTFH
CHHHCCCCCCCCEEC
18.3324719451
564PhosphorylationSRLARGSTIRSTFHG
HHHCCCCCCCCEECC
24.19-
567PhosphorylationARGSTIRSTFHGGQV
CCCCCCCCEECCCEE
31.4123312004
568PhosphorylationRGSTIRSTFHGGQVR
CCCCCCCEECCCEEE
15.1423312004
594PhosphorylationVQNGPPASPTLAHEA
CCCCCCCCCCCCCCC
24.9626657352
596PhosphorylationNGPPASPTLAHEAAP
CCCCCCCCCCCCCCC
33.8028152594
612PhosphorylationPAGRPRPTTNLFTKL
CCCCCCCCCCHHHHH
29.6028152594
613PhosphorylationAGRPRPTTNLFTKLT
CCCCCCCCCHHHHHH
32.3828152594
617PhosphorylationRPTTNLFTKLTSKLT
CCCCCHHHHHHHHHH
28.4528152594
622UbiquitinationLFTKLTSKLTRRVAD
HHHHHHHHHHHHHCC
48.95-
628 (in isoform 2)Phosphorylation-17.4026437602
650 (in isoform 2)Phosphorylation-37.02-

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
214TPhosphorylationKinaseSTK11Q15831
PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
29KPhosphorylation

14976552
29Kubiquitylation

14976552
214TPhosphorylation

14976552

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 MARK4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYH9_HUMANMYH9physical
14594945
MYH10_HUMANMYH10physical
14594945
HSP74_HUMANHSPA4physical
14594945
TBG1_HUMANTUBG1physical
14594945
ACTS_HUMANACTA1physical
14594945
TBB5_HUMANTUBBphysical
14594945
TBA1A_HUMANTUBA1Aphysical
14594945
MTAP2_HUMANMAP2physical
14594945
TAU_HUMANMAPTphysical
14594945
MAP4_HUMANMAP4physical
14594945
USP9X_HUMANUSP9Xphysical
18254724
ARHG2_HUMANARHGEF2physical
14676191
MTCL1_HUMANMTCL1physical
14676191
KCD20_HUMANKCTD20physical
14676191
2AAA_HUMANPPP2R1Aphysical
14676191
PNMA1_HUMANPNMA1physical
14676191
USP9X_HUMANUSP9Xphysical
14676191
SOGA1_HUMANSOGA1physical
14676191
RNF41_HUMANRNF41physical
14676191
MY18A_HUMANMYO18Aphysical
14676191
1433F_HUMANYWHAHphysical
14676191
MBB1A_HUMANMYBBP1Aphysical
14676191
PP2AB_HUMANPPP2CBphysical
14676191
SMCA4_HUMANSMARCA4physical
14676191
TBG1_HUMANTUBG1physical
14676191
CDC42_HUMANCDC42physical
14676191
PNMA2_HUMANPNMA2physical
14676191
KPCI_HUMANPRKCIphysical
14676191
DOCK7_HUMANDOCK7physical
14676191
UBP7_HUMANUSP7physical
14676191
CYFP1_HUMANCYFIP1physical
14676191
CYFP2_HUMANCYFIP2physical
14676191
RPTOR_HUMANRPTORphysical
23184942
TAU_HUMANMAPTphysical
23666762
ODFP2_HUMANODF2physical
23400999
K1C40_HUMANKRT40physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
RPIA_HUMANRPIAphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MARK4_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-2; THR-17; SER-23;SER-26; SER-423; SER-438 AND SER-545, AND MASS 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-26 AND THR-214, 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: ENZYME REGULATION, PHOSPHORYLATION AT THR-214, AND MUTAGENESIS OFTHR-214.

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