MON1A_HUMAN - dbPTM
MON1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MON1A_HUMAN
UniProt AC Q86VX9
Protein Name Vacuolar fusion protein MON1 homolog A
Gene Name MON1A
Organism Homo sapiens (Human).
Sequence Length 652
Subcellular Localization
Protein Description Plays an important role in membrane trafficking through the secretory apparatus. Not involved in endocytic trafficking to lysosomes (By similarity). Acts in concert with CCZ1, as a guanine exchange factor (GEF) for RAB7, promotes the exchange of GDP to GTP, converting it from an inactive GDP-bound form into an active GTP-bound form. [PubMed: 23084991]
Protein Sequence MHPGGGPSRAERLELGLGRERPAKAIFLHRRPGEGGGRERCLRCGHVCVRRGPGPREAVPSGRPRPDTLTPPWVRQRAVTGTFCASWTPLRNRRAQRMATDMQRKRSSECLDGTLTPSDGQSMERAESPTPGMAQGMEPGAGQEGAMFVHARSYEDLTESEDGAASGDSHKEGTRGPPPLPTDMRQISQDFSELSTQLTGVARDLQEEMLPGSSEDWLEPPGAVGRPATEPPREGTTEGDEEDATEAWRLHQKHVFVLSEAGKPVYSRYGSEEALSSTMGVMVALVSFLEADKNAIRSIHADGYKVVFVRRSPLVLVAVARTRQSAQELAQELLYIYYQILSLLTGAQLSHIFQQKQNYDLRRLLSGSERITDNLLQLMARDPSFLMGAARCLPLAAAVRDTVSASLQQARARSLVFSILLARNQLVALVRRKDQFLHPIDLHLLFNLISSSSSFREGEAWTPVCLPKFNAAGFFHAHISYLEPDTDLCLLLVSTDREDFFAVSDCRRRFQERLRKRGAHLALREALRTPYYSVAQVGIPDLRHFLYKSKSSGLFTSPEIEAPYTSEEEQERLLGLYQYLHSRAHNASRPLKTIYYTGPNENLLAWVTGAFELYMCYSPLGTKASAVSAIHKLMRWIRKEEDRLFILTPLTY
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
10PhosphorylationPGGGPSRAERLELGL
CCCCCCHHHHHHHCC
33.2623401153
11PhosphorylationGGGPSRAERLELGLG
CCCCCHHHHHHHCCC
36.0423927012
17PhosphorylationAERLELGLGRERPAK
HHHHHHCCCCCCCCE
27.4229496963
19PhosphorylationRLELGLGRERPAKAI
HHHHCCCCCCCCEEE
22.1523312004
21PhosphorylationELGLGRERPAKAIFL
HHCCCCCCCCEEEEE
49.4923312004
31PhosphorylationKAIFLHRRPGEGGGR
EEEEEECCCCCCCCC
32.8423401153
33PhosphorylationIFLHRRPGEGGGRER
EEEECCCCCCCCCHH
41.5829255136
56PhosphorylationVRRGPGPREAVPSGR
EECCCCCHHCCCCCC
33.3922167270
57PhosphorylationRRGPGPREAVPSGRP
ECCCCCHHCCCCCCC
14.1222167270
61PhosphorylationGPREAVPSGRPRPDT
CCHHCCCCCCCCCCC
50.1923927012
63PhosphorylationREAVPSGRPRPDTLT
HHCCCCCCCCCCCCC
35.4323403867
68PhosphorylationSGRPRPDTLTPPWVR
CCCCCCCCCCCCCHH
21.4124719451
68 (in isoform 4)Phosphorylation-21.4124719451
68PhosphorylationSGRPRPDTLTPPWVR
CCCCCCCCCCCCCHH
21.4124719451
69PhosphorylationGRPRPDTLTPPWVRQ
CCCCCCCCCCCCHHH
42.4723403867
70PhosphorylationRPRPDTLTPPWVRQR
CCCCCCCCCCCHHHC
35.4024719451
70PhosphorylationRPRPDTLTPPWVRQR
CCCCCCCCCCCHHHC
35.4024719451
70 (in isoform 4)Phosphorylation-35.4024719451
72PhosphorylationRPDTLTPPWVRQRAV
CCCCCCCCCHHHCCC
39.7323403867
77PhosphorylationTPPWVRQRAVTGTFC
CCCCHHHCCCCCCCC
33.2823186163
91PhosphorylationCASWTPLRNRRAQRM
CCCCHHHHCHHHHHH
18.5023898821
95PhosphorylationTPLRNRRAQRMATDM
HHHHCHHHHHHHHHH
46.0128464451
98PhosphorylationRNRRAQRMATDMQRK
HCHHHHHHHHHHHHH
15.2828450419
99PhosphorylationNRRAQRMATDMQRKR
CHHHHHHHHHHHHHH
39.98-
100PhosphorylationRRAQRMATDMQRKRS
HHHHHHHHHHHHHHH
33.3822210691
100 (in isoform 4)Phosphorylation-33.3822210691
102PhosphorylationAQRMATDMQRKRSSE
HHHHHHHHHHHHHHH
21.57-
107PhosphorylationTDMQRKRSSECLDGT
HHHHHHHHHHCCCCC
42.8624719451
108PhosphorylationDMQRKRSSECLDGTL
HHHHHHHHHCCCCCC
6.0229743597
108 (in isoform 4)Phosphorylation-6.0229743597
108PhosphorylationDMQRKRSSECLDGTL
HHHHHHHHHCCCCCC
6.02-
128PhosphorylationQSMERAESPTPGMAQ
CCCCCCCCCCCCCCC
29.3523186163
153PhosphorylationAMFVHARSYEDLTES
CEEEEEECHHHCCCC
3.3233259812
154PhosphorylationMFVHARSYEDLTESE
EEEEEECHHHCCCCC
26.5218452278
158PhosphorylationARSYEDLTESEDGAA
EECHHHCCCCCCCCC
4.5823186163
160PhosphorylationSYEDLTESEDGAASG
CHHHCCCCCCCCCCC
5.8227251275
166UbiquitinationESEDGAASGDSHKEG
CCCCCCCCCCCCCCC
38.06-
188PhosphorylationPTDMRQISQDFSELS
CCCHHHHHHHHHHHH
1.9524719451
215PhosphorylationEMLPGSSEDWLEPPG
HCCCCCCCCCCCCCC
16.4222210691
263UbiquitinationFVLSEAGKPVYSRYG
EEEECCCCCCCCCCC
41.05-
275PhosphorylationRYGSEEALSSTMGVM
CCCCHHHHHHHHHHH
25.6729759185
287PhosphorylationGVMVALVSFLEADKN
HHHHHHHHHHHHCHH
34.9929759185
291 (in isoform 2)Ubiquitination-20.4521906983
317PhosphorylationRRSPLVLVAVARTRQ
ECCCCHHEEHHCCHH
28.0926434776
321PhosphorylationLVLVAVARTRQSAQE
CHHEEHHCCHHHHHH
12.5926434776
353PhosphorylationGAQLSHIFQQKQNYD
HHHHHHHHHHHCCCC
27.60-
365PhosphorylationNYDLRRLLSGSERIT
CCCHHHHHCCCHHHH
16.9424850871
386UbiquitinationMARDPSFLMGAARCL
HHCCHHHHHHHHHHH
32.6622817900
388UbiquitinationRDPSFLMGAARCLPL
CCHHHHHHHHHHHHH
43.4022817900
450PhosphorylationHLLFNLISSSSSFRE
HHHHHHHHCCCCCCC
16.57-
451UbiquitinationLLFNLISSSSSFREG
HHHHHHHCCCCCCCC
54.2622817900
453UbiquitinationFNLISSSSSFREGEA
HHHHHCCCCCCCCCC
44.4822817900
453 (in isoform 1)Ubiquitination-44.4821906983
454PhosphorylationNLISSSSSFREGEAW
HHHHCCCCCCCCCCC
36.4123403867
455PhosphorylationLISSSSSFREGEAWT
HHHCCCCCCCCCCCC
43.1623403867
459PhosphorylationSSSFREGEAWTPVCL
CCCCCCCCCCCCEEC
48.7123403867
460PhosphorylationSSFREGEAWTPVCLP
CCCCCCCCCCCEECC
17.1323403867
468PhosphorylationWTPVCLPKFNAAGFF
CCCEECCCCCCCCEE
28.7123403867
482PhosphorylationFHAHISYLEPDTDLC
EEEEEECCCCCCCEE
7.8823403867
528PhosphorylationLALREALRTPYYSVA
HHHHHHHCCCCCCHH
30.66-
531PhosphorylationREALRTPYYSVAQVG
HHHHCCCCCCHHHCC
22.6328857561
548UbiquitinationDLRHFLYKSKSSGLF
HHHHHHHHCCCCCCC
4.4722817900
550UbiquitinationRHFLYKSKSSGLFTS
HHHHHHCCCCCCCCC
2.9422817900

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

Oops, there are no upstream regulatory protein records of MON1A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MON1A_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 MON1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RABX5_HUMANRABGEF1physical
20434987
VP33A_HUMANVPS33Aphysical
20434987

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 MON1A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-31, AND MASSSPECTROMETRY.

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