MICA1_HUMAN - dbPTM
MICA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MICA1_HUMAN
UniProt AC Q8TDZ2
Protein Name [F-actin]-monooxygenase MICAL1 {ECO:0000305}
Gene Name MICAL1
Organism Homo sapiens (Human).
Sequence Length 1067
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Midbody . Accumulates transiently at the abscission site before abscission occurs.
Protein Description Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (By similarity). In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). [PubMed: 21864500]
Protein Sequence MASPTSTNPAHAHFESFLQAQLCQDVLSSFQELCGALGLEPGGGLPQYHKIKDQLNYWSAKSLWTKLDKRAGQPVYQQGRACTSTKCLVVGAGPCGLRVAVELALLGARVVLVEKRTKFSRHNVLHLWPFTIHDLRALGAKKFYGRFCTGTLDHISIRQLQLLLLKVALLLGVEIHWGVTFTGLQPPPRKGSGWRAQLQPNPPAQLANYEFDVLISAAGGKFVPEGFKVREMRGKLAIGITANFVNGRTVEETQVPEISGVARIYNQSFFQSLLKATGIDLENIVYYKDDTHYFVMTAKKQCLLRLGVLRQDWPDTNRLLGSANVVPEALQRFTRAAADFATHGKLGKLEFAQDAHGQPDVSAFDFTSMMRAESSARVQEKHGARLLLGLVGDCLVEPFWPLGTGVARGFLAAFDAAWMVKRWAEGAESLEVLAERESLYQLLSQTSPENMHRNVAQYGLDPATRYPNLNLRAVTPNQVRDLYDVLAKEPVQRNNDKTDTGMPATGSAGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQAVVAGSDPLGLIAYLSHFHSAFKSMAHSPGPVSQASPGTSSAVLFLSKLQRTLQRSRAKENAEDAGGKKLRLEMEAETPSTEVPPDPEPGVPLTPPSQHQEAGAGDLCALCGEHLYVLERLCVNGHFFHRSCFRCHTCEATLWPGGYEQHPGDGHFYCLQHLPQTDHKAEGSDRGPESPELPTPSENSMPPGLSTPTASQEGAGPVPDPSQPTRRQIRLSSPERQRLSSLNLTPDPEMEPPPKPPRSCSALARHALESSFVGWGLPVQSPQALVAMEKEEKESPFSSEEEEEDVPLDSDVEQALQTFAKTSGTMNNYPTWRRTLLRRAKEEEMKRFCKAQTIQRRLNEIEAALRELEAEGVKLELALRRQSSSPEQQKKLWVGQLLQLVDKKNSLVAEEAELMITVQELNLEEKQWQLDQELRGYMNREENLKTAADRQAEDQVLRKLVDLVNQRDALIRFQEERRLSELALGTGAQG
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
3Phosphorylation-----MASPTSTNPA
-----CCCCCCCCHH		40.3426074081
5Phosphorylation---MASPTSTNPAHA
---CCCCCCCCHHHH		45.7626074081
52UbiquitinationLPQYHKIKDQLNYWS
CCCHHHHHHHHHHCC		44.2029967540
61UbiquitinationQLNYWSAKSLWTKLD
HHHHCCHHHHHHHHH		40.3329967540
66UbiquitinationSAKSLWTKLDKRAGQ
CHHHHHHHHHHCCCC		43.01-
71UbiquitinationWTKLDKRAGQPVYQQ
HHHHHHCCCCCCHHC		27.0629967540
71 (in isoform 4)Ubiquitination-27.06-
80UbiquitinationQPVYQQGRACTSTKC
CCCHHCCCCCCCCCE		23.3529967540
85 (in isoform 4)Ubiquitination-13.97-
115MalonylationARVVLVEKRTKFSRH
CEEEEEECCCCCCCC		58.8726320211
156PhosphorylationTGTLDHISIRQLQLL
CCCCCCCCHHHHHHH		14.3224719451
228UbiquitinationKFVPEGFKVREMRGK
CCCCCCCEEEEECCC		51.7629967540
241PhosphorylationGKLAIGITANFVNGR
CCEEEEEEEECCCCC		15.4421406692
247UbiquitinationITANFVNGRTVEETQ
EEEECCCCCEEEECC		22.7229967540
247 (in isoform 4)Ubiquitination-22.72-
259PhosphorylationETQVPEISGVARIYN
ECCCCCCCCHHHHCC		26.0822210691
265PhosphorylationISGVARIYNQSFFQS
CCCHHHHCCHHHHHH		11.12-
272PhosphorylationYNQSFFQSLLKATGI
CCHHHHHHHHHHHCC		30.4324719451
301 (in isoform 3)Ubiquitination-23.5321906983
316PhosphorylationLRQDWPDTNRLLGSA
CCCCCCCHHHHCCCC		20.4025599653
348UbiquitinationATHGKLGKLEFAQDA
HHHCCCCCCHHCCCC		56.1129967540
367UbiquitinationDVSAFDFTSMMRAES
CCCCHHHHHHHHHHH		19.9829967540
402UbiquitinationLVEPFWPLGTGVARG
EECCCCCCCCHHHHH		7.5632015554
402 (in isoform 2)Ubiquitination-7.5621890473
411UbiquitinationTGVARGFLAAFDAAW
CHHHHHHHHHHHHHH		3.6124816145
444PhosphorylationESLYQLLSQTSPENM
HHHHHHHHCCCCCHH		39.7518077418
446PhosphorylationLYQLLSQTSPENMHR
HHHHHHCCCCCHHHH		42.7618077418
447PhosphorylationYQLLSQTSPENMHRN
HHHHHCCCCCHHHHH		23.6818077418
466PhosphorylationGLDPATRYPNLNLRA
CCCHHHCCCCCCEEE		7.6623403867
475PhosphorylationNLNLRAVTPNQVRDL
CCCEEECCHHHHHHH		18.6122199227
483PhosphorylationPNQVRDLYDVLAKEP
HHHHHHHHHHHHCCC		14.3228796482
488UbiquitinationDLYDVLAKEPVQRNN
HHHHHHHCCCCCCCC		59.3929967540
497UbiquitinationPVQRNNDKTDTGMPA
CCCCCCCCCCCCCCC		50.8824816145
498PhosphorylationVQRNNDKTDTGMPAT
CCCCCCCCCCCCCCC		41.47-
498O-linked_GlycosylationVQRNNDKTDTGMPAT
CCCCCCCCCCCCCCC		41.4729351928
500PhosphorylationRNNDKTDTGMPATGS
CCCCCCCCCCCCCCC		40.38-
502 (in isoform 4)Phosphorylation-1.9027642862
502SulfoxidationNDKTDTGMPATGSAG
CCCCCCCCCCCCCCC		1.9021406390
507UbiquitinationTGMPATGSAGTQEEL
CCCCCCCCCCCHHHH		21.1232015554
507 (in isoform 4)Ubiquitination-21.12-
507UbiquitinationTGMPATGSAGTQEEL
CCCCCCCCCCCHHHH		21.1221890473
507 (in isoform 1)Ubiquitination-21.1221890473
516UbiquitinationGTQEELLRWCQEQTA
CCHHHHHHHHHHHCC		44.7624816145
516 (in isoform 4)Ubiquitination-44.76-
531PhosphorylationGYPGVHVSDLSSSWA
CCCCCCHHHCCCCHH		20.2532645325
539PhosphorylationDLSSSWADGLALCAL
HCCCCHHHHHHHHHH		46.5133259812
551UbiquitinationCALVYRLQPGLLEPS
HHHHHHHCCCCCCHH		22.4821890473
551 (in isoform 2)Ubiquitination-22.4821890473
572UbiquitinationALEATAWALKVAENE
HHHHHHHHHHHHHHH		8.6124816145
613PhosphorylationHFHSAFKSMAHSPGP
HHHHHHHHHCCCCCC		18.1023401153
617PhosphorylationAFKSMAHSPGPVSQA
HHHHHCCCCCCCHHC		23.2429255136
622PhosphorylationAHSPGPVSQASPGTS
CCCCCCCHHCCCCHH		24.1429255136
625PhosphorylationPGPVSQASPGTSSAV
CCCCHHCCCCHHHHH		19.0725159151
628PhosphorylationVSQASPGTSSAVLFL
CHHCCCCHHHHHHHH		23.9226329039
629PhosphorylationSQASPGTSSAVLFLS
HHCCCCHHHHHHHHH		23.4026329039
630PhosphorylationQASPGTSSAVLFLSK
HCCCCHHHHHHHHHH		23.4126329039
636PhosphorylationSSAVLFLSKLQRTLQ
HHHHHHHHHHHHHHH		24.8026329039
637UbiquitinationSAVLFLSKLQRTLQR
HHHHHHHHHHHHHHH		51.2721890473
641PhosphorylationFLSKLQRTLQRSRAK
HHHHHHHHHHHHHHH		17.8127251275
644PhosphorylationKLQRTLQRSRAKENA
HHHHHHHHHHHHHHH		31.0933259812
656UbiquitinationENAEDAGGKKLRLEM
HHHHHCCCCEEEEEE		26.1621890473
656UbiquitinationENAEDAGGKKLRLEM
HHHHHCCCCEEEEEE		26.1621890473
656 (in isoform 1)Ubiquitination-26.1621890473
658UbiquitinationAEDAGGKKLRLEMEA
HHHCCCCEEEEEEEE		41.9624816145
669PhosphorylationEMEAETPSTEVPPDP
EEEEECCCCCCCCCC		44.6228348404
670PhosphorylationMEAETPSTEVPPDPE
EEEECCCCCCCCCCC		42.0528348404
677UbiquitinationTEVPPDPEPGVPLTP
CCCCCCCCCCCCCCC		63.1724816145
683PhosphorylationPEPGVPLTPPSQHQE
CCCCCCCCCHHHHCC		27.3828348404
761PhosphorylationTDHKAEGSDRGPESP
CCCCCCCCCCCCCCC		18.6826074081
767PhosphorylationGSDRGPESPELPTPS
CCCCCCCCCCCCCCC		27.1426074081
772PhosphorylationPESPELPTPSENSMP
CCCCCCCCCCCCCCC		52.6626074081
774PhosphorylationSPELPTPSENSMPPG
CCCCCCCCCCCCCCC		52.4626074081
777PhosphorylationLPTPSENSMPPGLST
CCCCCCCCCCCCCCC		28.7228348404
809PhosphorylationTRRQIRLSSPERQRL
CCHHCCCCCHHHHHH		33.7223403867
810PhosphorylationRRQIRLSSPERQRLS
CHHCCCCCHHHHHHH		35.0628355574
817PhosphorylationSPERQRLSSLNLTPD
CHHHHHHHHCCCCCC		34.6629255136
818PhosphorylationPERQRLSSLNLTPDP
HHHHHHHHCCCCCCC		26.3529255136
822PhosphorylationRLSSLNLTPDPEMEP
HHHHCCCCCCCCCCC		25.2729255136
836PhosphorylationPPPKPPRSCSALARH
CCCCCCCCHHHHHHH		20.4228674419
838PhosphorylationPKPPRSCSALARHAL
CCCCCCHHHHHHHHH		27.8028857561
847PhosphorylationLARHALESSFVGWGL
HHHHHHHHCCCCCCC		29.9021712546
848PhosphorylationARHALESSFVGWGLP
HHHHHHHCCCCCCCC		17.9921712546
858PhosphorylationGWGLPVQSPQALVAM
CCCCCCCCHHHHHHC		21.1528464451
872PhosphorylationMEKEEKESPFSSEEE
CCHHHCCCCCCCCCH		42.1726503892
875PhosphorylationEEKESPFSSEEEEED
HHCCCCCCCCCHHCC		39.9826503892
876PhosphorylationEKESPFSSEEEEEDV
HCCCCCCCCCHHCCC		49.7826503892
887PhosphorylationEEDVPLDSDVEQALQ
HCCCCCCCHHHHHHH		51.7626657352
900PhosphorylationLQTFAKTSGTMNNYP
HHHHHHHHCCCCCCH		31.4021945579
902PhosphorylationTFAKTSGTMNNYPTW
HHHHHHCCCCCCHHH		19.2521945579
906PhosphorylationTSGTMNNYPTWRRTL
HHCCCCCCHHHHHHH		9.3121945579
908PhosphorylationGTMNNYPTWRRTLLR
CCCCCCHHHHHHHHH		22.6521945579
912PhosphorylationNYPTWRRTLLRRAKE
CCHHHHHHHHHHHHH		22.90-
925 (in isoform 4)Phosphorylation-4.1227642862
927UbiquitinationEEMKRFCKAQTIQRR
HHHHHHHHHHHHHHH		40.60-
936UbiquitinationQTIQRRLNEIEAALR
HHHHHHHHHHHHHHH		46.5224816145
946 (in isoform 4)Ubiquitination-39.66-
950UbiquitinationRELEAEGVKLELALR
HHHHHCCHHHHHHHH		4.8729967540
950 (in isoform 2)Ubiquitination-4.8721890473
960PhosphorylationELALRRQSSSPEQQK
HHHHHHCCCCHHHHH		30.8527273156
961PhosphorylationLALRRQSSSPEQQKK
HHHHHCCCCHHHHHH		41.3925884760
962PhosphorylationALRRQSSSPEQQKKL
HHHHCCCCHHHHHHH		37.3926699800
1022UbiquitinationMNREENLKTAADRQA
CCHHHHHHHHHHHHH		47.9324816145
1036UbiquitinationAEDQVLRKLVDLVNQ
HHHHHHHHHHHHHHH		49.022190698
1041UbiquitinationLRKLVDLVNQRDALI
HHHHHHHHHHHHHHH		5.0524816145
1055UbiquitinationIRFQEERRLSELALG
HHHHHHHHHHHHHHC		45.9329967540
1055 (in isoform 1)Ubiquitination-45.9321890473
1057PhosphorylationFQEERRLSELALGTG
HHHHHHHHHHHHCCC		28.8429255136
1063PhosphorylationLSELALGTGAQG---
HHHHHHCCCCCC---		30.1421406692
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 MICA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MICA1_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 MICA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB1A_HUMANRAB1Aphysical
12788069
CASL_HUMANNEDD9physical
11827972
EHD1_HUMANEHD1physical
20106972
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 MICA1_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-617; SER-875; SER-876AND SER-1057, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872; SER-875 ANDSER-876, AND MASS SPECTROMETRY.

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