MON2_HUMAN - dbPTM
MON2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MON2_HUMAN
UniProt AC Q7Z3U7
Protein Name Protein MON2 homolog
Gene Name MON2
Organism Homo sapiens (Human).
Sequence Length 1717
Subcellular Localization
Protein Description May be required for traffic between late Golgi and early endosomes..
Protein Sequence MSGTSSPEAVKKLLENMQSDLRALSLECKKKFPPVKEAAESGIIKVKTIAARNTEILAALKENSSEVVQPFLMGCGTKEPKITQLCLAAIQRLMSHEVVSETAAGNIINMLWQLMENSLEELKLLQTVLVLLTTNTVVHDEALSKAIVLCFRLHFTKDNITNNTAAATVRQVVTVVFERMVAEDERHRDIIEQPVLVQGNSNRRSVSTLKPCAKDAYMLFQDLCQLVNADAPYWLVGMTEMTRTFGLELLESVLNDFPQVFLQHQEFSFLLKERVCPLVIKLFSPNIKFRQGSSTSSSPAPVEKPYFPICMRLLRVVSVLIKQFYSLLVTECEIFLSLLVKFLDADKPQWLRAVAVESIHRFCVQPQLLRSFCQSYDMKQHSTKVFRDIVNALGSFIQSLFLVPPTGNPATSNQAGNNNLGGSVSAPANSGMVGIGGGVTLLPAFEYRGTWIPILTITVQGSAKATYLEMLDKVEPPTIPEGYAMSVAFHCLLDLVRGITSMIEGELGELETECQTTTEEGSSPTQSTEQQDLQSTSDQMDKEIVSRAVWEEMVNACWCGLLAALSLLLDASTDEAATENILKAELTMAALCGRLGLVTSRDAFITAICKGSLPPHYALTVLNTTTAATLSNKSYSVQGQSVMMISPSSESHQQVVAVGQPLAVQPQGTVMLTSKNIQCMRTLLNLAHCHGAVLGTSWQLVLATLQHLVWILGLKPSSGGALKPGRAVEGPSTVLTTAVMTDLPVISNILSRLFESSQYLDDVSLHHLINALCSLSLEAMDMAYGNNKEPSLFAVAKLLETGLVNMHRIEILWRPLTGHLLEVCQHPNSRMREWGAEALTSLIKAGLTFNHDPPLSQNQRLQLLLLNPLKEMSNINHPDIRLKQLECVLQILQSQGDSLGPGWPLVLGVMGAIRNDQGESLIRTAFQCLQLVVTDFLPTMPCTCLQIVVDVAGSFGLHNQELNISLTSIGLLWNISDYFFQRGETIEKELNKEEAAQQKQAEEKGVVLNRPFHPAPPFDCLWLCLYAKLGELCVDPRPAVRKSAGQTLFSTIGAHGTLLQHSTWHTVIWKVLFHLLDRVRESSTTADKEKIESGGGNILIHHSRDTAEKQWAETWVLTLAGVARIFNTRRYLLQPLGDFSRAWDVLLDHIQSAALSKNNEVSLAALKSFQEILQIVSPVRDSDKPETPPVVNVPVPVLIGPISGMSRPFVRTDSIGEKLGRYSSSEPPIVTDELEDLNLWWAAWNTWYRIGSESTKPPITFDKLTFIPSQPFLTALIQIFPALYQHIKTGFNMDDLQKLGVILHSAISVPISSDASPFILPSYTEAVLTSLQEAVLTALDVLQKAICVGPENMQIMYPAIFDQLLAFVEFSCKPPQYGQLETKHIANAKYNQIQLFAPAEWVALNYVPFAERSLEVVVDLYQKTACHKAVVNEKVLQNIIKTLRVPLSLKYSCPSESTWKLAVSSLLRVLSIGLPVARQHASSGKFDSMWPELANTFEDFLFTKSIPPDNLSIQEFQRNENIDVEVVQLISNEILPYANFIPKEFVGQIMTMLNKGSIHSQSSSFTEAEIDIRLREEFSKMCFETLLQFSFSNKVTTPQEGYISRMALSVLLKRSQDVLHRYIEDERLSGKCPLPRQQVTEIIFVLKAVSTLIDSLKKTQPENVDGNTWAQVIALYPTLVECITCSSSEVCSALKEALVPFKDFMQPPASRVQNGES
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------MSGTSSPEA
------CCCCCCHHH		63.1822814378
2Phosphorylation------MSGTSSPEA
------CCCCCCHHH		63.1820873877
2 (in isoform 4)Acetylation-63.18-
4Phosphorylation----MSGTSSPEAVK
----CCCCCCHHHHH		35.0129255136
4 (in isoform 4)Phosphorylation-35.0124719451
5Phosphorylation---MSGTSSPEAVKK
---CCCCCCHHHHHH		47.6325849741
5 (in isoform 4)Phosphorylation-47.6327251275
6Phosphorylation--MSGTSSPEAVKKL
--CCCCCCHHHHHHH		26.9725849741
6 (in isoform 4)Phosphorylation-26.97-
11MethylationTSSPEAVKKLLENMQ
CCCHHHHHHHHHHHH		44.76116253029
11 (in isoform 4)Methylation-44.76-
12MethylationSSPEAVKKLLENMQS
CCHHHHHHHHHHHHH		52.2754395339
12UbiquitinationSSPEAVKKLLENMQS
CCHHHHHHHHHHHHH		52.27-
12 (in isoform 4)Methylation-52.27-
19PhosphorylationKLLENMQSDLRALSL
HHHHHHHHHHHHHCH		28.0422210691
54PhosphorylationKTIAARNTEILAALK
EEEHHCCHHHHHHHH		20.8928555341
83PhosphorylationGTKEPKITQLCLAAI
CCCCCHHHHHHHHHH		22.9326699800
201PhosphorylationPVLVQGNSNRRSVST
CEEECCCCCCCCCCC		38.2426074081
205PhosphorylationQGNSNRRSVSTLKPC
CCCCCCCCCCCCCCC		19.7223401153
205 (in isoform 4)Phosphorylation-19.7224719451
207PhosphorylationNSNRRSVSTLKPCAK
CCCCCCCCCCCCCHH		29.3023927012
208PhosphorylationSNRRSVSTLKPCAKD
CCCCCCCCCCCCHHH		36.3223663014
281UbiquitinationRVCPLVIKLFSPNIK
CCHHHHHHHCCCCCE		35.6821890473
281UbiquitinationRVCPLVIKLFSPNIK
CCHHHHHHHCCCCCE		35.6821890473
281 (in isoform 1)Ubiquitination-35.6821890473
281 (in isoform 2)Ubiquitination-35.6821890473
281 (in isoform 4)Ubiquitination-35.68-
288UbiquitinationKLFSPNIKFRQGSST
HHCCCCCEECCCCCC		40.9321890473
288UbiquitinationKLFSPNIKFRQGSST
HHCCCCCEECCCCCC		40.932189047
288 (in isoform 1)Ubiquitination-40.9321890473
288 (in isoform 2)Ubiquitination-40.9321890473
288 (in isoform 4)Ubiquitination-40.93-
293PhosphorylationNIKFRQGSSTSSSPA
CCEECCCCCCCCCCC		23.3129978859
294PhosphorylationIKFRQGSSTSSSPAP
CEECCCCCCCCCCCC		38.8529978859
295PhosphorylationKFRQGSSTSSSPAPV
EECCCCCCCCCCCCC		34.0325159151
296PhosphorylationFRQGSSTSSSPAPVE
ECCCCCCCCCCCCCC		30.6625159151
297PhosphorylationRQGSSTSSSPAPVEK
CCCCCCCCCCCCCCC		40.1929978859
298PhosphorylationQGSSTSSSPAPVEKP
CCCCCCCCCCCCCCC		25.5025849741
298 (in isoform 4)Phosphorylation-25.50-
306PhosphorylationPAPVEKPYFPICMRL
CCCCCCCCHHHHHHH		32.8123312004
456PhosphorylationGTWIPILTITVQGSA
CEEEEEEEEEECCCC		18.4726074081
458PhosphorylationWIPILTITVQGSAKA
EEEEEEEEECCCCCH		11.0926074081
512PhosphorylationGELGELETECQTTTE
CCCCCCEEEEEECCC		55.4728348404
516PhosphorylationELETECQTTTEEGSS
CCEEEEEECCCCCCC		47.5528348404
517PhosphorylationLETECQTTTEEGSSP
CEEEEEECCCCCCCC		13.3128348404
518PhosphorylationETECQTTTEEGSSPT
EEEEEECCCCCCCCC		35.1128348404
522PhosphorylationQTTTEEGSSPTQSTE
EECCCCCCCCCCCHH		36.1028348404
523PhosphorylationTTTEEGSSPTQSTEQ
ECCCCCCCCCCCHHH		42.7128348404
525PhosphorylationTEEGSSPTQSTEQQD
CCCCCCCCCCHHHHH		36.7828348404
527PhosphorylationEGSSPTQSTEQQDLQ
CCCCCCCCHHHHHHH		36.0728348404
528PhosphorylationGSSPTQSTEQQDLQS
CCCCCCCHHHHHHHC		28.1728348404
535PhosphorylationTEQQDLQSTSDQMDK
HHHHHHHCCCHHHHH		36.8624275569
535 (in isoform 4)Phosphorylation-36.86-
536PhosphorylationEQQDLQSTSDQMDKE
HHHHHHCCCHHHHHH		24.3024275569
537PhosphorylationQQDLQSTSDQMDKEI
HHHHHCCCHHHHHHH		30.96-
537 (in isoform 4)Phosphorylation-30.96-
587PhosphorylationNILKAELTMAALCGR
HHHHHHHHHHHHHHH		9.0323403867
599PhosphorylationCGRLGLVTSRDAFIT
HHHHCCCCCHHHHHH		24.0823403867
600PhosphorylationGRLGLVTSRDAFITA
HHHCCCCCHHHHHHH		22.2323403867
646PhosphorylationGQSVMMISPSSESHQ
CEEEEEECCCCCCCC		10.7925627689
648PhosphorylationSVMMISPSSESHQQV
EEEEECCCCCCCCEE		39.6925627689
649PhosphorylationVMMISPSSESHQQVV
EEEECCCCCCCCEEE		46.6425627689
651PhosphorylationMISPSSESHQQVVAV
EECCCCCCCCEEEEE		28.6625627689
669PhosphorylationLAVQPQGTVMLTSKN
EEECCCCEEEECCCC		9.48-
669 (in isoform 4)Phosphorylation-9.48-
736PhosphorylationEGPSTVLTTAVMTDL
CCCCCCEECHHHCCH		14.3622210691
737PhosphorylationGPSTVLTTAVMTDLP
CCCCCEECHHHCCHH		17.0622210691
747PhosphorylationMTDLPVISNILSRLF
HCCHHHHHHHHHHHH		20.3222210691
756PhosphorylationILSRLFESSQYLDDV
HHHHHHHCCCCCCCC		18.5323401153
757PhosphorylationLSRLFESSQYLDDVS
HHHHHHCCCCCCCCC		18.6923401153
764PhosphorylationSQYLDDVSLHHLINA
CCCCCCCCHHHHHHH		29.0423401153
774PhosphorylationHLINALCSLSLEAMD
HHHHHHHHCCHHHHH		23.1123401153
784PhosphorylationLEAMDMAYGNNKEPS
HHHHHHHHCCCCCCH		17.47-
784 (in isoform 4)Phosphorylation-17.47-
841PhosphorylationWGAEALTSLIKAGLT
HHHHHHHHHHHHCCC		28.6524719451
870UbiquitinationLLLLNPLKEMSNINH
HHHHHHHHHHCCCCC		7.74-
870UbiquitinationLLLLNPLKEMSNINH
HHHHHHHHHHCCCCC		7.74-
870 (in isoform 4)Ubiquitination-7.74-
1093PhosphorylationADKEKIESGGGNILI
CCHHHHHCCCCCEEE		55.1628555341
1162PhosphorylationLSKNNEVSLAALKSF
HCCCCHHHHHHHHHH		6.5424719451
1177PhosphorylationQEILQIVSPVRDSDK
HHHHHHHCCCCCCCC		3.2225849741
1177 (in isoform 4)Phosphorylation-3.2224719451
1182PhosphorylationIVSPVRDSDKPETPP
HHCCCCCCCCCCCCC		62.5129255136
1182 (in isoform 4)Phosphorylation-62.51-
1187PhosphorylationRDSDKPETPPVVNVP
CCCCCCCCCCCCCCC		78.6229255136
1187 (in isoform 4)Phosphorylation-78.6224719451
1212PhosphorylationMSRPFVRTDSIGEKL
CCCCCEECCCHHHHH		32.9423927012
1212 (in isoform 4)Phosphorylation-32.94-
1214PhosphorylationRPFVRTDSIGEKLGR
CCCEECCCHHHHHCC		27.9123401153
1214 (in isoform 4)Phosphorylation-27.9124719451
1218UbiquitinationRTDSIGEKLGRYSSS
ECCCHHHHHCCCCCC		43.36-
1218UbiquitinationRTDSIGEKLGRYSSS
ECCCHHHHHCCCCCC		43.36-
1218 (in isoform 4)Ubiquitination-43.36-
1423AcetylationVVVDLYQKTACHKAV
HHHHHHHHHCCCHHH		43.8725953088
1423MalonylationVVVDLYQKTACHKAV
HHHHHHHHHCCCHHH		43.8732601280
1464PhosphorylationSTWKLAVSSLLRVLS
HHHHHHHHHHHHHHH		6.0620068231
1465PhosphorylationTWKLAVSSLLRVLSI
HHHHHHHHHHHHHHC		15.0620068231
1465 (in isoform 4)Phosphorylation-15.06-
1579PhosphorylationIRLREEFSKMCFETL
HHHHHHHHHHHHHHH		7.9329083192
1585PhosphorylationFSKMCFETLLQFSFS
HHHHHHHHHHHHHHC		33.3529083192
1602PhosphorylationVTTPQEGYISRMALS
CCCCCCCHHHHHHHH		21.59-
1602 (in isoform 4)Phosphorylation-21.59-
1622PhosphorylationSQDVLHRYIEDERLS
CHHHHHHHHHCCCCC		29.9328060719
1622 (in isoform 4)Phosphorylation-29.93-
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 MON2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MON2_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 MON2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GAG_HV1H2gagphysical
21450827
ANFY1_HUMANANKFY1physical
22863883
PAAF1_HUMANPAAF1physical
22863883
STOM_HUMANSTOMphysical
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 MON2_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-205, AND MASSSPECTROMETRY.
"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 SER-205, AND MASSSPECTROMETRY.

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