MLXIP_HUMAN - dbPTM
MLXIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MLXIP_HUMAN
UniProt AC Q9HAP2
Protein Name MLX-interacting protein
Gene Name MLXIP {ECO:0000312|HGNC:HGNC:17055}
Organism Homo sapiens (Human).
Sequence Length 919
Subcellular Localization Cytoplasm . Nucleus . Mitochondrion outer membrane . Predominantly cytoplasmic but shuttles between cytoplasm and nucleus when associated with MLX. Also associates with the outer mitochondrial membrane and may shuttle between the outer mitochondrial
Protein Description Binds DNA as a heterodimer with MLX and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation..
Protein Sequence MAADVFMCSPRRPRSRGRQVLLKPQVSEDDDDSDTDEPSPPPASGAATPARAHASAAPPPPRAGPGREEPPRRQQIIHSGHFMVSSPHREHPPKKGYDFDTVNKQTCQTYSFGKTSSCHLSIDASLTKLFECMTLAYSGKLVSPKWKNFKGLKLQWRDKIRLNNAIWRAWYMQYLEKRKNPVCHFVTPLDGSVDVDEHRRPEAITTEGKYWKSRIEIVIREYHKWRTYFKKRLQQHKDEDLSSLVQDDDMLYWHKHGDGWKTPVPMEEDPLLDTDMLMSEFSDTLFSTLSSHQPVAWPNPREIAHLGNADMIQPGLIPLQPNLDFMDTFEPFQDLFSSSRSIFGSMLPASASAPVPDPNNPPAQESILPTTALPTVSLPDSLIAPPTAPSLAHMDEQGCEHTSRTEDPFIQPTDFGPSEPPLSVPQPFLPVFTMPLLSPSPAPPPISPVLPLVPPPATALNPPAPPTFHQPQKFAGVNKAPSVITHTASATLTHDAPATTFSQSQGLVITTHHPAPSAAPCGLALSPVTRPPQPRLTFVHPKPVSLTGGRPKQPHKIVPAPKPEPVSLVLKNARIAPAAFSGQPQAVIMTSGPLKREGMLASTVSQSNVVIAPAAIARAPGVPEFHSSILVTDLGHGTSSPPAPVSRLFPSTAQDPLGKGEQVPLHGGSPQVTVTGPSRDCPNSGQASPCASEQSPSPQSPQNNCSGKSDPKNVAALKNRQMKHISAEQKRRFNIKMCFDMLNSLISNNSKLTSHAITLQKTVEYITKLQQERGQMQEEARRLREEIEELNATIISCQQLLPATGVPVTRRQFDHMKDMFDEYVKTRTLQNWKFWIFSIIIKPLFESFKGMVSTSSLEELHRTALSWLDQHCSLPILRPMVLSTLRQLSTSTSILTDPAQLPEQASKAVTRIGKRLGES
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------MAADVFMCS
------CCCCEEECC		16.6322814378
9PhosphorylationAADVFMCSPRRPRSR
CCCEEECCCCCCCCC		15.0623401153
27PhosphorylationVLLKPQVSEDDDDSD
EEECCCCCCCCCCCC		30.0230278072
33PhosphorylationVSEDDDDSDTDEPSP
CCCCCCCCCCCCCCC		49.7830278072
35PhosphorylationEDDDDSDTDEPSPPP
CCCCCCCCCCCCCCC		46.3323927012
39PhosphorylationDSDTDEPSPPPASGA
CCCCCCCCCCCCCCC		48.2530278072
44PhosphorylationEPSPPPASGAATPAR
CCCCCCCCCCCCCCC		34.4423927012
48PhosphorylationPPASGAATPARAHAS
CCCCCCCCCCCHHHH		19.5623927012
79PhosphorylationRRQQIIHSGHFMVSS
HHHHEEECCCEECCC		24.4523312004
85PhosphorylationHSGHFMVSSPHREHP
ECCCEECCCCCCCCC		26.7728122231
86PhosphorylationSGHFMVSSPHREHPP
CCCEECCCCCCCCCC		17.2028985074
117PhosphorylationYSFGKTSSCHLSIDA
ECCCCCCCCEEEECH		15.7025627689
140"N6,N6-dimethyllysine"MTLAYSGKLVSPKWK
HHHHHCCCCCCCCCC		39.51-
140MethylationMTLAYSGKLVSPKWK
HHHHHCCCCCCCCCC		39.51-
143PhosphorylationAYSGKLVSPKWKNFK
HHCCCCCCCCCCCCC		31.0624719451
209UbiquitinationEAITTEGKYWKSRIE
CCEECCCCHHHHHHH		41.5329967540
252PhosphorylationVQDDDMLYWHKHGDG
CCCCCCCEEEECCCC		9.99-
262PhosphorylationKHGDGWKTPVPMEED
ECCCCCCCCCCCCCC		24.0226074081
482O-linked_GlycosylationAGVNKAPSVITHTAS
CCCCCCCCEEEEECC		30.8930059200
485O-linked_GlycosylationNKAPSVITHTASATL
CCCCCEEEEECCEEE		15.8330059200
487O-linked_GlycosylationAPSVITHTASATLTH
CCCEEEEECCEEECC		17.4130059200
489O-linked_GlycosylationSVITHTASATLTHDA
CEEEEECCEEECCCC		23.9630059200
595SumoylationIMTSGPLKREGMLAS
EEECCCCCCCCCEEE		52.08-
595SumoylationIMTSGPLKREGMLAS
EEECCCCCCCCCEEE		52.08-
603O-linked_GlycosylationREGMLASTVSQSNVV
CCCCEEEEECCCCEE		20.6930059200
605O-linked_GlycosylationGMLASTVSQSNVVIA
CCEEEEECCCCEEEE		28.1630059200
607O-linked_GlycosylationLASTVSQSNVVIAPA
EEEEECCCCEEEEEH		24.8830059200
627PhosphorylationPGVPEFHSSILVTDL
CCCCCCCCCEEEEEC		25.1323312004
628PhosphorylationGVPEFHSSILVTDLG
CCCCCCCCEEEEECC		16.0423312004
632PhosphorylationFHSSILVTDLGHGTS
CCCCEEEEECCCCCC		23.2828348404
638PhosphorylationVTDLGHGTSSPPAPV
EEECCCCCCCCCCCH		21.9825159151
639PhosphorylationTDLGHGTSSPPAPVS
EECCCCCCCCCCCHH		45.5025159151
640PhosphorylationDLGHGTSSPPAPVSR
ECCCCCCCCCCCHHH		34.4425159151
646PhosphorylationSSPPAPVSRLFPSTA
CCCCCCHHHCCCCCC		23.3925627689
669PhosphorylationQVPLHGGSPQVTVTG
CCCCCCCCCCEEEEC		19.4229496963
673PhosphorylationHGGSPQVTVTGPSRD
CCCCCCEEEECCCCC		13.7023186163
675O-linked_GlycosylationGSPQVTVTGPSRDCP
CCCCEEEECCCCCCC		33.7330059200
675PhosphorylationGSPQVTVTGPSRDCP
CCCCEEEECCCCCCC		33.7323186163
678PhosphorylationQVTVTGPSRDCPNSG
CEEEECCCCCCCCCC		41.9423186163
684PhosphorylationPSRDCPNSGQASPCA
CCCCCCCCCCCCCCC		19.8827732954
688PhosphorylationCPNSGQASPCASEQS
CCCCCCCCCCCCCCC		16.7827732954
692PhosphorylationGQASPCASEQSPSPQ
CCCCCCCCCCCCCCC		42.7727732954
695PhosphorylationSPCASEQSPSPQSPQ
CCCCCCCCCCCCCCC		24.2428450419
697PhosphorylationCASEQSPSPQSPQNN
CCCCCCCCCCCCCCC		40.6028450419
700PhosphorylationEQSPSPQSPQNNCSG
CCCCCCCCCCCCCCC		31.6628450419
706PhosphorylationQSPQNNCSGKSDPKN
CCCCCCCCCCCCHHH		51.9128450419
7182-HydroxyisobutyrylationPKNVAALKNRQMKHI
HHHHHHHHHHHHHCC		45.41-
883PhosphorylationILRPMVLSTLRQLST
HHHHHHHHHHHHHHC		17.6222210691
884PhosphorylationLRPMVLSTLRQLSTS
HHHHHHHHHHHHHCC		23.0722210691
893PhosphorylationRQLSTSTSILTDPAQ
HHHHCCCCCCCCHHH		18.5029900121
906PhosphorylationAQLPEQASKAVTRIG
HHCHHHHHHHHHHHH		22.3529900121
919PhosphorylationIGKRLGES-------
HHHHHCCC-------		43.6624702127
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 MLXIP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MLXIP_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 MLXIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLX_HUMANMLXphysical
11073985
MLX_HUMANMLXphysical
12446771
1433B_HUMANYWHABphysical
12446771
MLX_HUMANMLXphysical
20027290
MTOR_HUMANMTORphysical
25332233
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 MLXIP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-700, AND MASSSPECTROMETRY.
"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-27 AND SER-33, AND MASSSPECTROMETRY.

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