Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Microtubule-associated protein 4  

UniProtKB / Swiss-Prot ID :  MAP4_MOUSE

Gene Name (Synonyms) : 
Map4, Mtap4  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm, cytoskeleton. 

Protein Function :  Non-neuronal microtubule-associated protein. Promotes microtubule assembly. 

Protein Sequence MADLSLVDALTEPPPEIEGEIKRDFMAALEAEPYDDIVGETVEKTEFIPLLDGDEKTGNSESKKKPCLDT...
Predicted Secondary Structure CCCHHHHHHHCCCCHHHHHHHHHHHHHHHHCCHHHHHHHHHHCCCEEEEEEECCCCCCCCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
99PhosphoserineNTAGSPTDF
CCCCCCCCC
23.35Phosphositeplus
Link-
176PhosphotyrosineSEDSYGMLP
CCCCCCCCC
20.90Phosphositeplus
Link-
176PhosphotyrosineSEDSYGMLP
CCCCCCCCC
20.90SysPTM
Link-
231PhosphoserineAEVESVKEQ
CCCCCCCCC
43.60Phosphositeplus
Link-
254PhosphoserineDVVHSPSTD
CCCCCCCCC
14.67PhosphoELM
Link-
254PhosphoserineDVVHSPSTD
CCCCCCCCC
14.67Phosphositeplus
Link-
254Phosphoserine.DVVHSPSTD
CCCCCCCCC
14.67UniProtKB
Link-
260PhosphothreonineSTDTTPGPD
CCCCCCCCC
29.11PhosphoELM
Link-
260PhosphothreonineSTDTTPGPD
CCCCCCCCC
29.11Phosphositeplus
Link-
260Phosphothreonine.STDTTPGPD
CCCCCCCCC
29.11UniProtKB
Link-
343PhosphothreoninePGNDTTSPK
CCCCCCCCC
32.92Phosphositeplus
Link-
344PhosphothreonineGNDTTSPKE
CCCCCCCCC
45.99Phosphositeplus
Link-
344PhosphothreonineGNDTTSPKE
CCCCCCCCC
45.99SysPTM
Link-
345PhosphoserineNDTTSPKET
CCCCCCCCC
35.75Phosphositeplus
Link-
345PhosphoserineNDTTSPKET
CCCCCCCCC
35.75SysPTM
Link-
349PhosphothreonineSPKETETTL
CCCCCCEEC
44.77Phosphositeplus
Link-
381PhosphoserineKGMVSLSEI
CCCCCCCCC
19.79Phosphositeplus
Link-
381PhosphoserineKGMVSLSEI
CCCCCCCCC
19.79SysPTM
Link-
447PhosphothreonineVTDMTPSLE
CCCCCCCCC
16.73Phosphositeplus
Link-
452PhosphothreoninePSLETEMTL
CCCCCCCCC
36.03Phosphositeplus
Link-
474Methionine sulfoneMAKDMSPLP
CCCCCCCCC
4.36SysPTM
Link-
475PhosphoserineAKDMSPLPE
CCCCCCCCC
33.16PhosphoELM
Link-
475PhosphoserineAKDMSPLPE
CCCCCCCCC
33.16Phosphositeplus
Link-
475PhosphoserineAKDMSPLPE
CCCCCCCCC
33.16SysPTM
Link-
475Phosphoserine.AKDMSPLPE
CCCCCCCCC
33.16UniProtKB
Link-
503PhosphothreonineFNNVTPLSE
CCCCCCCCC
22.19PhosphoELM
Link-
503PhosphothreonineFNNVTPLSE
CCCCCCCCC
22.19Phosphositeplus
Link-
503PhosphothreonineFNNVTPLSE
CCCCCCCCC
22.19SysPTM
Link-
503Phosphothreonine.FNNVTPLSE
CCCCCCCCC
22.19UniProtKB
Link-
506PhosphoserineVTPLSEEEV
CCCCCCCCC
44.13PhosphoELM
Link-
506PhosphoserineVTPLSEEEV
CCCCCCCCC
44.13Phosphositeplus
Link-
506PhosphoserineVTPLSEEEV
CCCCCCCCC
44.13SysPTM
Link-
506Phosphoserine.VTPLSEEEV
CCCCCCCCC
44.13UniProtKB
Link-
511PhosphothreonineEEEVTSVKD
CCCCCCCCC
30.96PhosphoELM
Link-
511PhosphothreonineEEEVTSVKD
CCCCCCCCC
30.96Phosphositeplus
Link-
511Phosphothreonine.EEEVTSVKD
CCCCCCCCC
30.96UniProtKB
Link-
512PhosphoserineEEVTSVKDM
CCCCCCCCC
32.14Phosphositeplus
Link-
516Methionine sulfoneSVKDMSPSA
CCCCCCCCC
5.41SysPTM
Link-
517PhosphoserineVKDMSPSAE
CCCCCCCCC
26.32PhosphoELM
Link-
517PhosphoserineVKDMSPSAE
CCCCCCCCC
26.32Phosphositeplus
Link-
517PhosphoserineVKDMSPSAE
CCCCCCCCC
26.32SysPTM
Link-
517Phosphoserine.VKDMSPSAE
CCCCCCCCC
26.32UniProtKB
Link-
519PhosphoserineDMSPSAETE
CCCCCCCCC
31.28PhosphoELM
Link-
519PhosphoserineDMSPSAETE
CCCCCCCCC
31.28Phosphositeplus
Link-
519Phosphoserine.DMSPSAETE
CCCCCCCCC
31.28UniProtKB
Link-
583PhosphoserineSQLASMQHK
CCCCCCCCC
27.80Phosphositeplus
Link-
583PhosphoserineSQLASMQHK
CCCCCCCCC
27.80SysPTM
Link-
595S-nitrosocysteineTVPPCTASP
CCCCCCCCC
3.98dbSNO
Link-
596PhosphothreonineVPPCTASPE
CCCCCCCCC
35.62Phosphositeplus
Link-
598PhosphoserinePCTASPEPV
CCCCCCCCC
16.19PhosphoELM
Link-
598PhosphoserinePCTASPEPV
CCCCCCCCC
16.19Phosphositeplus
Link-
598PhosphoserinePCTASPEPV
CCCCCCCCC
16.19SysPTM
Link-
598Phosphoserine.PCTASPEPV
CCCCCCCCC
16.19UniProtKB
Link-
617PhosphoserineIDAPSPLEN
CCCCCCCCC
43.78PhosphoELM
Link-
617PhosphoserineIDAPSPLEN
CCCCCCCCC
43.78Phosphositeplus
Link-
617Phosphoserine.IDAPSPLEN
CCCCCCCCC
43.78UniProtKB
Link-
630PhosphoserineETPGSQPSE
CCCCCCCCC
39.87PhosphoELM
Link-
630Phosphoserine.ETPGSQPSE
CCCCCCCCC
39.87UniProtKB
Link-
636S-nitrosocysteinePSEPCSGVS
CCCCCCCCC
4.92dbSNO
Link-
657PhosphothreonineGNDITTPPN
CCCCCCCCC
35.79Phosphositeplus
Link-
658PhosphothreonineNDITTPPNK
CCCCCCCCC
36.76Phosphositeplus
Link-
667PhosphoserineEPPPSPEKK
CCCCCCCCC
52.01PhosphoELM
Link-
667PhosphoserineEPPPSPEKK
CCCCCCCCC
52.01Phosphositeplus
Link-
667PhosphoserineEPPPSPEKK
CCCCCCCCC
52.01SysPTM
Link-
667Phosphoserine.EPPPSPEKK
CCCCCCCCC
52.01UniProtKB
Link-
713PhosphoserineKKPMSLASG
CCCCCCCCC
29.34Phosphositeplus
Link-
716PhosphoserineMSLASGSVP
CCCCCCCCC
36.57Phosphositeplus
Link-
759PhosphothreonineAEKRTSPSK
CCCCCCCCC
56.93Phosphositeplus
Link-
760PhosphoserineEKRTSPSKP
CCCCCCCCC
31.07PhosphoELM
Link-
760PhosphoserineEKRTSPSKP
CCCCCCCCC
31.07Phosphositeplus
Link-
760PhosphoserineEKRTSPSKP
CCCCCCCCC
31.07SysPTM
Link-
762PhosphoserineRTSPSKPSS
CCCCCCCCC
57.89Phosphositeplus
Link-
765PhosphoserinePSKPSSAPA
CCCCCCCCC
42.75Phosphositeplus
Link-
777PhosphothreonineGPKTTPTVS
CCCCCCCCC
24.08Phosphositeplus
Link-
777PhosphothreonineGPKTTPTVS
CCCCCCCCC
24.08SysPTM
Link-
784PhosphothreonineVSKATSPST
CCCCCCCCC
44.93PhosphoELM
Link-
784PhosphothreonineVSKATSPST
CCCCCCCCC
44.93Phosphositeplus
Link-
784PhosphothreonineVSKATSPST
CCCCCCCCC
44.93SysPTM
Link-
784Phosphothreonine.VSKATSPST
CCCCCCCCC
44.93UniProtKB
Link-
785PhosphoserineSKATSPSTL
CCCCCCCCC
23.01PhosphoELM
Link-
785PhosphoserineSKATSPSTL
CCCCCCCCC
23.01Phosphositeplus
Link-
785PhosphoserineSKATSPSTL
CCCCCCCCC
23.01SysPTM
Link-
785Phosphoserine.SKATSPSTL
CCCCCCCCC
23.01UniProtKB
Link-
787PhosphoserineATSPSTLVS
CCCCCCCCC
33.85Phosphositeplus
Link-
787PhosphoserineATSPSTLVS
CCCCCCCCC
33.85SysPTM
Link-
788PhosphothreonineTSPSTLVST
CCCCCCCCC
34.27Phosphositeplus
Link-
796PhosphoserineTGPSSRSPA
CCCCCCCCC
39.65Phosphositeplus
Link-
798PhosphoserinePSSRSPATT
CCCCCCCCC
22.34Phosphositeplus
Link-
798PhosphoserinePSSRSPATT
CCCCCCCCC
22.34SysPTM
Link-
828PhosphoserineAKSASADLS
CCCCCCCCC
29.43Phosphositeplus
Link-
828PhosphoserineAKSASADLS
CCCCCCCCC
29.43SysPTM
Link-
840PhosphoserineTTSASSVKR
CCCCCCCCC
35.12Phosphositeplus
Link-
840PhosphoserineTTSASSVKR
CCCCCCCCC
35.12SysPTM
Link-
846PhosphothreonineVKRNTTPTG
CCCCCCCCC
37.88Phosphositeplus
Link-
847PhosphothreonineKRNTTPTGA
CCCCCCCCC
23.54PhosphoELM
Link-
847PhosphothreonineKRNTTPTGA
CCCCCCCCC
23.54Phosphositeplus
Link-
847PhosphothreonineKRNTTPTGA
CCCCCCCCC
23.54SysPTM
Link-
847Phosphothreonine.KRNTTPTGA
CCCCCCCCC
23.54UniProtKB
Link-
871PhosphoserineAPSRSSGAL
CCCCCCCCC
37.14Phosphositeplus
Link-
894PhosphoserineAPRVSRLAT
CCCCCCCCC
23.90Phosphositeplus
Link-
898PhosphothreonineSRLATTVSA
CCCCCCCCC
32.11Phosphositeplus
Link-
901PhosphoserineATTVSAPDL
CCCCCCCCC
31.80Phosphositeplus
Link-
914PhosphoserineSKVGSTENI
CCCCCCCCC
35.22Phosphositeplus
Link-
914PhosphoserineSKVGSTENI
CCCCCCCCC
35.22SysPTM
Link-
915PhosphothreonineKVGSTENIK
CCCCCCCCC
27.42Phosphositeplus
Link-
973PhosphoserineSKKVSYSHI
CCCCCCCCC
29.78Phosphositeplus
Link-
1046PhosphoserineAKVGSLDNV
HCCCCCCCC
35.22Phosphositeplus
Link-
1046PhosphoserineAKVGSLDNV
HCCCCCCCC
35.22SysPTM
Link-
1046Phosphoserine.AKVGSLDNV
HCCCCCCCC
35.22UniProtKB
Link-
1124PhosphoserineIQETSI
CHHCCC
26.08Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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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-475 AND SER-1046, ANDMASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-667, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; THR-260; THR-511;SER-517; SER-519 AND SER-617, AND MASS SPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND MASSSPECTROMETRY.
"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 SER-517; SER-598; THR-784AND THR-847, 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 SER-254; THR-503; SER-506;SER-517 AND SER-785, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630, 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-1046, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures