MACOI_HUMAN - dbPTM
MACOI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MACOI_HUMAN
UniProt AC Q8N5G2
Protein Name Macoilin {ECO:0000303|PubMed:21589894}
Gene Name MACO1 {ECO:0000312|HGNC:HGNC:25572}
Organism Homo sapiens (Human).
Sequence Length 664
Subcellular Localization Nucleus membrane
Multi-pass membrane protein . Cell projection, axon . Rough endoplasmic reticulum membrane
Multi-pass membrane protein . Detected in the nucleus membrane of non-neuronal cells and in axonal outgrowths of neuronal cells.
Protein Description Plays a role in the regulation of neuronal activity..
Protein Sequence MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPANKKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSKNYKNASGVVNSSPRSHSATNGSIPSSSSKNEKKQKCTSKSPSTHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISSLSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRNRIRELEAEGKKLTMDMKVKEDQIRELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAATSPLSPVSPHYSSKFVETSPSGLDPNASVYQPLKK
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
25 (in isoform 2)Phosphorylation-18.8426437602
64UbiquitinationPFWLFIRSVYDSFRY
HHHHHHHHHHHHHCH		21.8822817900
65UbiquitinationFWLFIRSVYDSFRYQ
HHHHHHHHHHHHCHH		4.4021890473
80 (in isoform 2)Ubiquitination-3.7921890473
84UbiquitinationSVFFVCVAFTSNIIC
HHHHHHHHHCCCHHH		9.2522817900
87UbiquitinationFVCVAFTSNIICLLF
HHHHHHCCCHHHHHH		21.4122817900
88UbiquitinationVCVAFTSNIICLLFI
HHHHHCCCHHHHHHH		25.2921963094
105UbiquitinationQWLFFAASTYVWVQY
HHHHHHHHHHHHHHH		19.4921963094
119UbiquitinationYVWHTERGVCLPTVS
HHHHCCCCCCCCHHH		14.3021890473
134UbiquitinationLWILFVYIEAAIRFK
HHHHHHHHHHHHHCC		2.1421963094
143UbiquitinationAAIRFKDLKNFHVDL
HHHHCCCCCCCCCCC		5.1423000965
146UbiquitinationRFKDLKNFHVDLCRP
HCCCCCCCCCCCHHH		5.9323000965
164UbiquitinationHCIGYPVVTLGFGFK
HHHCCCEEEECCCHH		2.9432142685
177UbiquitinationFKSYVSYKMRLRKQK
HHHHHHHHHHHHHHH		15.27-
178UbiquitinationKSYVSYKMRLRKQKE
HHHHHHHHHHHHHHH		3.5627667366
188AcetylationRKQKEVQKENEFYMQ
HHHHHHHHHHHHHHH		68.6220167786
188UbiquitinationRKQKEVQKENEFYMQ
HHHHHHHHHHHHHHH		68.6221890473
210UbiquitinationPEQQMLQKQEKEAEE
HHHHHHHHHHHHHHH		57.3629967540
211UbiquitinationEQQMLQKQEKEAEEA
HHHHHHHHHHHHHHH		54.7722817900
211 (in isoform 3)Ubiquitination-54.7721890473
214UbiquitinationMLQKQEKEAEEAAKG
HHHHHHHHHHHHHCC		61.6427667366
221 (in isoform 2)Ubiquitination-37.4021890473
227PhosphorylationKGLPDMDSSILIHHN
CCCCCCCCCEEEECC		16.7925627689
228PhosphorylationGLPDMDSSILIHHNG
CCCCCCCCEEEECCC		19.7028555341
231UbiquitinationDMDSSILIHHNGGIP
CCCCCEEEECCCCCC		2.7127667366
241UbiquitinationNGGIPANKKLSTTLP
CCCCCCCCCCCCCCC		58.1422817900
242UbiquitinationGGIPANKKLSTTLPE
CCCCCCCCCCCCCCC		47.6922817900
242UbiquitinationGGIPANKKLSTTLPE
CCCCCCCCCCCCCCC		47.6921890473
242 (in isoform 1)Ubiquitination-47.6921890473
244PhosphorylationIPANKKLSTTLPEIE
CCCCCCCCCCCCCHH		28.3830266825
245PhosphorylationPANKKLSTTLPEIEY
CCCCCCCCCCCCHHH		42.6730266825
246PhosphorylationANKKLSTTLPEIEYR
CCCCCCCCCCCHHHH		36.6230266825
252PhosphorylationTTLPEIEYREKGKEK
CCCCCHHHHHCCCCC		29.7228102081
261UbiquitinationEKGKEKDKDAKKHNL
HCCCCCCCCHHHCCC		71.3221890473
264UbiquitinationKEKDKDAKKHNLGIN
CCCCCCHHHCCCCCC		65.7722817900
265UbiquitinationEKDKDAKKHNLGINN
CCCCCHHHCCCCCCC		39.1721963094
281UbiquitinationNILQPVDSKIQEIEY
CCCCCCCHHHHHHHH		31.7127667366
282UbiquitinationILQPVDSKIQEIEYM
CCCCCCHHHHHHHHH		43.9021963094
288PhosphorylationSKIQEIEYMENHINS
HHHHHHHHHHHHCCC		18.5227642862
296UbiquitinationMENHINSKRLNNDLV
HHHHCCCCCCCCCCC		57.3123000965
296UbiquitinationMENHINSKRLNNDLV
HHHHCCCCCCCCCCC		57.3121890473
296 (in isoform 1)Ubiquitination-57.3121890473
305PhosphorylationLNNDLVGSTENLLKE
CCCCCCCCHHHHHHH		25.6823401153
306PhosphorylationNNDLVGSTENLLKED
CCCCCCCHHHHHHHC		23.9819664994
310UbiquitinationVGSTENLLKEDSCTA
CCCHHHHHHHCCCCC		9.5929967540
311UbiquitinationGSTENLLKEDSCTAS
CCHHHHHHHCCCCCC		63.7421963094
314PhosphorylationENLLKEDSCTASSKN
HHHHHHCCCCCCCCC		17.9223312004
316PhosphorylationLLKEDSCTASSKNYK
HHHHCCCCCCCCCCC		33.2623312004
318PhosphorylationKEDSCTASSKNYKNA
HHCCCCCCCCCCCCC		24.5623312004
319PhosphorylationEDSCTASSKNYKNAS
HCCCCCCCCCCCCCC		23.5823312004
320UbiquitinationDSCTASSKNYKNASG
CCCCCCCCCCCCCCC		62.9023000965
323UbiquitinationTASSKNYKNASGVVN
CCCCCCCCCCCCCCC		56.2723000965
324N-linked_GlycosylationASSKNYKNASGVVNS
CCCCCCCCCCCCCCC		29.04UniProtKB CARBOHYD
326PhosphorylationSKNYKNASGVVNSSP
CCCCCCCCCCCCCCC		41.3230266825
331PhosphorylationNASGVVNSSPRSHSA
CCCCCCCCCCCCCCC		30.0629255136
332PhosphorylationASGVVNSSPRSHSAT
CCCCCCCCCCCCCCC		21.0929255136
335PhosphorylationVVNSSPRSHSATNGS
CCCCCCCCCCCCCCC		25.7725159151
337PhosphorylationNSSPRSHSATNGSIP
CCCCCCCCCCCCCCC		37.7325159151
339PhosphorylationSPRSHSATNGSIPSS
CCCCCCCCCCCCCCC		43.0326074081
340N-linked_GlycosylationPRSHSATNGSIPSSS
CCCCCCCCCCCCCCC		41.76UniProtKB CARBOHYD
342PhosphorylationSHSATNGSIPSSSSK
CCCCCCCCCCCCCCC		33.1426074081
345PhosphorylationATNGSIPSSSSKNEK
CCCCCCCCCCCCCHH		40.9826074081
346PhosphorylationTNGSIPSSSSKNEKK
CCCCCCCCCCCCHHH		33.0226074081
347PhosphorylationNGSIPSSSSKNEKKQ
CCCCCCCCCCCHHHC		50.0626074081
348PhosphorylationGSIPSSSSKNEKKQK
CCCCCCCCCCHHHCC		41.2625159151
352UbiquitinationSSSSKNEKKQKCTSK
CCCCCCHHHCCCCCC		70.6521890473
352 (in isoform 3)Ubiquitination-70.6521890473
355UbiquitinationSKNEKKQKCTSKSPS
CCCHHHCCCCCCCCC		48.6527667366
357PhosphorylationNEKKQKCTSKSPSTH
CHHHCCCCCCCCCHH		46.3428348404
358PhosphorylationEKKQKCTSKSPSTHK
HHHCCCCCCCCCHHH		40.3828348404
360PhosphorylationKQKCTSKSPSTHKDL
HCCCCCCCCCHHHHH		24.6922210691
362PhosphorylationKCTSKSPSTHKDLME
CCCCCCCCHHHHHHH		50.6822210691
365UbiquitinationSKSPSTHKDLMENCI
CCCCCHHHHHHHHCC		53.2821963094
365UbiquitinationSKSPSTHKDLMENCI
CCCCCHHHHHHHHCC		53.2821890473
365 (in isoform 1)Ubiquitination-53.2821890473
391UbiquitinationVRLEQDIKKLKADLQ
HHHHHHHHHHHHHHH		61.4132142685
394UbiquitinationEQDIKKLKADLQASR
HHHHHHHHHHHHHHH		49.0529967540
402UbiquitinationADLQASRQVEQELRS
HHHHHHHHHHHHHHH		40.3721890473
438UbiquitinationENELLQNKLHNAVQM
HHHHHHHHHHHHHHH		37.8622817900
438UbiquitinationENELLQNKLHNAVQM
HHHHHHHHHHHHHHH		37.8621890473
438 (in isoform 1)Ubiquitination-37.8621890473
452N-linked_GlycosylationMKQKDKQNISQLEKK
HHHHHHHCHHHHHHH		41.44UniProtKB CARBOHYD
458UbiquitinationQNISQLEKKLKAEQE
HCHHHHHHHHHHHHH		72.5027667366
472AcetylationEARSFVEKQLMEEKK
HHHHHHHHHHHHHHH		43.3519820271
521PhosphorylationEAEGKKLTMDMKVKE
HHCCCCCCCCEECCH		21.72-
537UbiquitinationQIRELELKVQELRKY
HHHHHHHHHHHHHHH		32.2829967540
551PhosphorylationYKENEKDTEVLMSAL
HHHCHHHHHHHHHHH		38.7823403867
556PhosphorylationKDTEVLMSALSAMQD
HHHHHHHHHHHHHHH		23.1523403867
559PhosphorylationEVLMSALSAMQDKTQ
HHHHHHHHHHHHHHH		22.7823403867
579UbiquitinationLSAETRIKLDLFSAL
CCHHHHHHHHHHHHH		32.4322817900
579UbiquitinationLSAETRIKLDLFSAL
CCHHHHHHHHHHHHH		32.4321890473
579 (in isoform 1)Ubiquitination-32.4321890473
584PhosphorylationRIKLDLFSALGDAKR
HHHHHHHHHHHHHHH		29.86-
5902-HydroxyisobutyrylationFSALGDAKRQLEIAQ
HHHHHHHHHHHHHHH		45.47-
626PhosphorylationAVMPSITYSAATSPL
HHCCCCCCEECCCCC		8.4727251275
627PhosphorylationVMPSITYSAATSPLS
HCCCCCCEECCCCCC		11.6327251275
630PhosphorylationSITYSAATSPLSPVS
CCCCEECCCCCCCCC		30.5128450419
631PhosphorylationITYSAATSPLSPVSP
CCCEECCCCCCCCCC		21.0828450419
634PhosphorylationSAATSPLSPVSPHYS
EECCCCCCCCCCCCC		27.0028450419
637PhosphorylationTSPLSPVSPHYSSKF
CCCCCCCCCCCCCCC		14.8928450419
640PhosphorylationLSPVSPHYSSKFVET
CCCCCCCCCCCCCCC		20.3028450419
641PhosphorylationSPVSPHYSSKFVETS
CCCCCCCCCCCCCCC		24.8228450419
642PhosphorylationPVSPHYSSKFVETSP
CCCCCCCCCCCCCCC		23.9728450419
647PhosphorylationYSSKFVETSPSGLDP
CCCCCCCCCCCCCCC		40.4130266825
648PhosphorylationSSKFVETSPSGLDPN
CCCCCCCCCCCCCCC		11.9930266825
650PhosphorylationKFVETSPSGLDPNAS
CCCCCCCCCCCCCCC		52.3230266825
655N-linked_GlycosylationSPSGLDPNASVYQPL
CCCCCCCCCCCCCCC		44.51UniProtKB CARBOHYD
657PhosphorylationSGLDPNASVYQPLKK
CCCCCCCCCCCCCCC		28.1830266825
659PhosphorylationLDPNASVYQPLKK--
CCCCCCCCCCCCC--		11.2630266825
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 MACOI_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MACOI_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 MACOI_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MACOI_HUMAN !!
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 MACOI_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-634, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, 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-332; SER-631; SER-634AND SER-637, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASSSPECTROMETRY.

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