MARE1_HUMAN - dbPTM
MARE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARE1_HUMAN
UniProt AC Q15691
Protein Name Microtubule-associated protein RP/EB family member 1
Gene Name MAPRE1
Organism Homo sapiens (Human).
Sequence Length 268
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Golgi apparatus . Associated with the microtubule growing distal tips (PubMed:28814570). Recruitment to the Golgi apparatus requires the presence of PDE4DI
Protein Description Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. [PubMed: 12388762]
Protein Sequence MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQETAVAPSLVAPALNKPKKPLTSSSAAPQRPISTQRTAAAPKAGPGVVRKNPGVGNGDDEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY
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------MAVNVYSTS
------CCCEEEECC
11.1122223895
6Phosphorylation--MAVNVYSTSVTSD
--CCCEEEECCCCCC
10.8826552605
7Phosphorylation-MAVNVYSTSVTSDN
-CCCEEEECCCCCCC
15.2126552605
8PhosphorylationMAVNVYSTSVTSDNL
CCCEEEECCCCCCCC
14.9926552605
9PhosphorylationAVNVYSTSVTSDNLS
CCEEEECCCCCCCCC
19.9126552605
11PhosphorylationNVYSTSVTSDNLSRH
EEEECCCCCCCCCHH
30.0827732954
12PhosphorylationVYSTSVTSDNLSRHD
EEECCCCCCCCCHHH
23.5023186163
40PhosphorylationTKIEQLCSGAAYCQF
HHHHHHHCHHHHHHH
39.81-
60UbiquitinationPGSIALKKVKFQAKL
CCCEEEEECCHHHHC
52.0523000965
60AcetylationPGSIALKKVKFQAKL
CCCEEEEECCHHHHC
52.05129905
62UbiquitinationSIALKKVKFQAKLEH
CEEEEECCHHHHCCH
40.4123000965
66UbiquitinationKKVKFQAKLEHEYIQ
EECCHHHHCCHHHHH
43.5623000965
66MalonylationKKVKFQAKLEHEYIQ
EECCHHHHCCHHHHH
43.5626320211
66AcetylationKKVKFQAKLEHEYIQ
EECCHHHHCCHHHHH
43.5623236377
71PhosphorylationQAKLEHEYIQNFKIL
HHHCCHHHHHHHHHH
15.0928152594
76AcetylationHEYIQNFKILQAGFK
HHHHHHHHHHHHHHH
50.4823954790
76UbiquitinationHEYIQNFKILQAGFK
HHHHHHHHHHHHHHH
50.4823000965
76MethylationHEYIQNFKILQAGFK
HHHHHHHHHHHHHHH
50.48-
83AcetylationKILQAGFKRMGVDKI
HHHHHHHHHCCCCEE
40.3223749302
83UbiquitinationKILQAGFKRMGVDKI
HHHHHHHHHCCCCEE
40.3223000965
83MalonylationKILQAGFKRMGVDKI
HHHHHHHHHCCCCEE
40.3226320211
89UbiquitinationFKRMGVDKIIPVDKL
HHHCCCCEEEEHHHH
39.8823000965
89AcetylationFKRMGVDKIIPVDKL
HHHCCCCEEEEHHHH
39.8823749302
95UbiquitinationDKIIPVDKLVKGKFQ
CEEEEHHHHHCCCCC
56.2523000965
95AcetylationDKIIPVDKLVKGKFQ
CEEEEHHHHHCCCCC
56.2525953088
98UbiquitinationIPVDKLVKGKFQDNF
EEHHHHHCCCCCCCH
67.8123000965
100UbiquitinationVDKLVKGKFQDNFEF
HHHHHCCCCCCCHHH
33.8523000965
100AcetylationVDKLVKGKFQDNFEF
HHHHHCCCCCCCHHH
33.8525953088
112UbiquitinationFEFVQWFKKFFDANY
HHHHHHHHHHHCCCC
45.7922817900
113AcetylationEFVQWFKKFFDANYD
HHHHHHHHHHCCCCC
41.6125953088
113UbiquitinationEFVQWFKKFFDANYD
HHHHHHHHHHCCCCC
41.6121890473
119PhosphorylationKKFFDANYDGKDYDP
HHHHCCCCCCCCCCH
28.0026552605
122UbiquitinationFDANYDGKDYDPVAA
HCCCCCCCCCCHHHH
50.6632015554
122AcetylationFDANYDGKDYDPVAA
HCCCCCCCCCCHHHH
50.6626051181
124PhosphorylationANYDGKDYDPVAARQ
CCCCCCCCCHHHHHC
26.1528674151
135PhosphorylationAARQGQETAVAPSLV
HHHCCCCCCCCCHHH
20.6723312004
140PhosphorylationQETAVAPSLVAPALN
CCCCCCCHHHHHHHC
26.2426657352
148AcetylationLVAPALNKPKKPLTS
HHHHHHCCCCCCCCC
60.0923236377
148UbiquitinationLVAPALNKPKKPLTS
HHHHHHCCCCCCCCC
60.0923000965
150UbiquitinationAPALNKPKKPLTSSS
HHHHCCCCCCCCCCC
69.5023000965
151UbiquitinationPALNKPKKPLTSSSA
HHHCCCCCCCCCCCC
54.5123000965
151AcetylationPALNKPKKPLTSSSA
HHHCCCCCCCCCCCC
54.5126051181
151MethylationPALNKPKKPLTSSSA
HHHCCCCCCCCCCCC
54.51-
154PhosphorylationNKPKKPLTSSSAAPQ
CCCCCCCCCCCCCCC
34.7820201521
154O-linked_GlycosylationNKPKKPLTSSSAAPQ
CCCCCCCCCCCCCCC
34.7830059200
155PhosphorylationKPKKPLTSSSAAPQR
CCCCCCCCCCCCCCC
29.9423927012
155O-linked_GlycosylationKPKKPLTSSSAAPQR
CCCCCCCCCCCCCCC
29.9430059200
156O-linked_GlycosylationPKKPLTSSSAAPQRP
CCCCCCCCCCCCCCC
20.8230059200
156PhosphorylationPKKPLTSSSAAPQRP
CCCCCCCCCCCCCCC
20.8223927012
157PhosphorylationKKPLTSSSAAPQRPI
CCCCCCCCCCCCCCC
28.3723927012
157O-linked_GlycosylationKKPLTSSSAAPQRPI
CCCCCCCCCCCCCCC
28.3730059200
165PhosphorylationAAPQRPISTQRTAAA
CCCCCCCCCCCCCCC
22.5912857735
166PhosphorylationAPQRPISTQRTAAAP
CCCCCCCCCCCCCCC
23.8423927012
174UbiquitinationQRTAAAPKAGPGVVR
CCCCCCCCCCCCCEE
62.3423000965
182UbiquitinationAGPGVVRKNPGVGNG
CCCCCEECCCCCCCC
56.7529967540
197SulfoxidationDDEAAELMQQVNVLK
CHHHHHHHHHHCCEE
1.6521406390
204UbiquitinationMQQVNVLKLTVEDLE
HHHHCCEEEEHHHHH
37.5232015554
206PhosphorylationQVNVLKLTVEDLEKE
HHCCEEEEHHHHHHH
21.91-
212UbiquitinationLTVEDLEKERDFYFG
EEHHHHHHHCCEEEE
66.4021906983
212SumoylationLTVEDLEKERDFYFG
EEHHHHHHHCCEEEE
66.40-
212SumoylationLTVEDLEKERDFYFG
EEHHHHHHHCCEEEE
66.40-
217PhosphorylationLEKERDFYFGKLRNI
HHHHCCEEEEEEECE
18.73-
220UbiquitinationERDFYFGKLRNIELI
HCCEEEEEEECEEEE
34.0822817900
220AcetylationERDFYFGKLRNIELI
HCCEEEEEEECEEEE
34.0819608861
228GlutathionylationLRNIELICQENEGEN
EECEEEEEECCCCCC
6.9322555962
247PhosphorylationQRIVDILYATDEGFV
HHHHHHHHHCCCCCC
14.0626552605
249PhosphorylationIVDILYATDEGFVIP
HHHHHHHCCCCCCCC
22.4926552605
268PhosphorylationPQEEQEEY-------
CHHHHHCC-------
24.0926552605

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
40SPhosphorylationKinaseMAP3K5Q99683
GPS
154TPhosphorylationKinaseMAP3K5Q99683
GPS
155SPhosphorylationKinaseGSK3BP49841
PSP
156SPhosphorylationKinaseGSK3BP49841
PSP
206TPhosphorylationKinaseMAP3K5Q99683
GPS
247YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MARE1_HUMAN !!

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 MARE1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERF1_HUMANTERF1physical
11943150
CSN5_HUMANCOPS5physical
17350042
CSN8_HUMANCOPS8physical
17350042
CASK_HUMANCSN3physical
17350042
TBB5_HUMANTUBBphysical
23128140
A4_HUMANAPPphysical
21832049
SPTN1_HUMANSPTAN1physical
22939629
AURKB_HUMANAURKBphysical
18477699
TBB5_PIGTUBB2Aphysical
23864329
LIS1_HUMANPAFAH1B1physical
22863883
NAV1_HUMANNAV1physical
25065758
NAV2_HUMANNAV2physical
25065758
NAV3_HUMANNAV3physical
25065758
TRIO_HUMANTRIOphysical
25065758
MARE1_HUMANMAPRE1physical
25416956
MARE3_HUMANMAPRE3physical
25416956
SPDE2_HUMANSPDYE2physical
25416956
CYLD_HUMANCYLDphysical
24552808
NEMO_HUMANIKBKGphysical
24552808
TRAF2_HUMANTRAF2physical
24552808
MDR1_HUMANABCB1physical
24552808
STK11_HUMANSTK11physical
24552808
BCL3_HUMANBCL3physical
24552808
KAT2B_HUMANKAT2Bphysical
23001180
KAT5_HUMANKAT5physical
23001180
MARE1_HUMANMAPRE1physical
23001180
MARE3_HUMANMAPRE3physical
23001180
MTUS2_HUMANMTUS2physical
23001180
KIF2C_HUMANKIF2Cphysical
23001180
MACF1_HUMANMACF1physical
23001180
CLAP1_HUMANCLASP1physical
23001180
CLAP2_HUMANCLASP2physical
23001180
APC_HUMANAPCphysical
23001180
DYST_HUMANDSTphysical
26186194
MACF1_HUMANMACF1physical
26186194
IASPP_HUMANPPP1R13Lphysical
26186194
AKAP9_HUMANAKAP9physical
26186194
CLAP2_HUMANCLASP2physical
26186194
MARE2_HUMANMAPRE2physical
26186194
MARE3_HUMANMAPRE3physical
26186194
KI18B_HUMANKIF18Bphysical
26186194
MYOME_HUMANPDE4DIPphysical
26186194
IPL1_YEASTIPL1physical
22696216
ACTN4_HUMANACTN4physical
26496610
ACTN1_HUMANACTN1physical
26496610
ADDA_HUMANADD1physical
26496610
ADDG_HUMANADD3physical
26496610
APC_HUMANAPCphysical
26496610
BLMH_HUMANBLMHphysical
26496610
DYST_HUMANDSTphysical
26496610
CALL3_HUMANCALML3physical
26496610
CAZA1_HUMANCAPZA1physical
26496610
CD59_HUMANCD59physical
26496610
CLCA_HUMANCLTAphysical
26496610
CLCB_HUMANCLTBphysical
26496610
CLH1_HUMANCLTCphysical
26496610
CBPM_HUMANCPMphysical
26496610
CTNA1_HUMANCTNNA1physical
26496610
CTNB1_HUMANCTNNB1physical
26496610
DAB2_HUMANDAB2physical
26496610
DREB_HUMANDBN1physical
26496610
DCTN1_HUMANDCTN1physical
26496610
DYHC1_HUMANDYNC1H1physical
26496610
DC1I2_HUMANDYNC1I2physical
26496610
EPS15_HUMANEPS15physical
26496610
FLNA_HUMANFLNAphysical
26496610
FYN_HUMANFYNphysical
26496610
GNAI2_HUMANGNAI2physical
26496610
HS90B_HUMANHSP90AB1physical
26496610
ABLM1_HUMANABLIM1physical
26496610
MYO1E_HUMANMYO1Ephysical
26496610
PCM1_HUMANPCM1physical
26496610
PCNT_HUMANPCNTphysical
26496610
PLEC_HUMANPLECphysical
26496610
KAPCB_HUMANPRKACBphysical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
SYQ_HUMANQARSphysical
26496610
CLIP1_HUMANCLIP1physical
26496610
SPTN1_HUMANSPTAN1physical
26496610
SPTB2_HUMANSPTBN1physical
26496610
SSFA2_HUMANSSFA2physical
26496610
SVIL_HUMANSVILphysical
26496610
TMOD1_HUMANTMOD1physical
26496610
TPM4_HUMANTPM4physical
26496610
CLIP2_HUMANCLIP2physical
26496610
YES_HUMANYES1physical
26496610
LUZP1_HUMANLUZP1physical
26496610
AXIN1_HUMANAXIN1physical
26496610
SRBS2_HUMANSORBS2physical
26496610
OFD1_HUMANOFD1physical
26496610
TAOK2_HUMANTAOK2physical
26496610
MYOME_HUMANPDE4DIPphysical
26496610
CE350_HUMANCEP350physical
26496610
CE170_HUMANCEP170physical
26496610
SC16A_HUMANSEC16Aphysical
26496610
WDR1_HUMANWDR1physical
26496610
ACTZ_HUMANACTR1Aphysical
26496610
AKAP9_HUMANAKAP9physical
26496610
PIBF1_HUMANPIBF1physical
26496610
DCTN2_HUMANDCTN2physical
26496610
SPAG5_HUMANSPAG5physical
26496610
GA2L1_HUMANGAS2L1physical
26496610
IASPP_HUMANPPP1R13Lphysical
26496610
KIF2C_HUMANKIF2Cphysical
26496610
RAB35_HUMANRAB35physical
26496610
FR1OP_HUMANFGFR1OPphysical
26496610
SYNPO_HUMANSYNPOphysical
26496610
CE162_HUMANCEP162physical
26496610
CP131_HUMANCEP131physical
26496610
RB6I2_HUMANERC1physical
26496610
CLAP2_HUMANCLASP2physical
26496610
COBL_HUMANCOBLphysical
26496610
CLAP1_HUMANCLASP1physical
26496610
LIMA1_HUMANLIMA1physical
26496610
SYBU_HUMANSYBUphysical
26496610
CEP72_HUMANCEP72physical
26496610
CK5P2_HUMANCDK5RAP2physical
26496610
MIB1_HUMANMIB1physical
26496610
AFAP1_HUMANAFAP1physical
26496610
HYI_HUMANHYIphysical
26496610
DLRB1_HUMANDYNLRB1physical
26496610
CCD77_HUMANCCDC77physical
26496610
SKAP_HUMANKNSTRNphysical
26496610
NEXN_HUMANNEXNphysical
26496610
CYTSB_HUMANSPECC1physical
26496610
TBC31_HUMANTBC1D31physical
26496610
ADIP_HUMANSSX2IPphysical
26496610
MISP_HUMANMISPphysical
26496610
CD109_HUMANCD109physical
26496610
KI18B_HUMANKIF18Bphysical
26496610
WDR90_HUMANWDR90physical
26496610
TPRN_HUMANTPRNphysical
26496610
KAPCA_HUMANPRKACAphysical
26496610
KLH21_HUMANKLHL21physical
27641145
DYST_HUMANDSTphysical
28514442
MARE3_HUMANMAPRE3physical
28514442
CLAP2_HUMANCLASP2physical
28514442
MARE2_HUMANMAPRE2physical
28514442
MYOME_HUMANPDE4DIPphysical
28514442
KI18B_HUMANKIF18Bphysical
28514442
IASPP_HUMANPPP1R13Lphysical
28514442
MACF1_HUMANMACF1physical
28514442
AKAP9_HUMANAKAP9physical
28514442
KAP3_HUMANPRKAR2Bphysical
28514442
CLAP2_HUMANCLASP2physical
27173435
MARE3_HUMANMAPRE3physical
27173435
MARE2_HUMANMAPRE2physical
27173435
DCTN1_HUMANDCTN1physical
27173435
DCTN2_HUMANDCTN2physical
27173435
IFT52_HUMANIFT52physical
27173435

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 MARE1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND THR-166, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND MASSSPECTROMETRY.

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