CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018047
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein-methionine sulfoxide oxidase MICAL1 
Protein Synonyms/Alias
 Molecule interacting with CasL protein 1; MICAL-1; NEDD9-interacting protein with calponin homology and LIM domains 
Gene Name
 MICAL1 
Gene Synonyms/Alias
 MICAL; NICAL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
488DLYDVLAKEPVQRNNubiquitination[1, 2]
497PVQRNNDKTDTGMPAubiquitination[3]
637SAVLFLSKLQRTLQRubiquitination[1]
927EEMKRFCKAQTIQRRubiquitination[3]
1036AEDQVLRKLVDLVNQubiquitination[4]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (Probable). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4. 
Sequence Annotation
 DOMAIN 508 609 CH.
 DOMAIN 695 757 LIM zinc-binding.
 NP_BIND 95 123 FAD (By similarity).
 REGION 1 489 Monooxygenase domain (By similarity).
 BINDING 95 95 FAD (By similarity).
 BINDING 114 114 FAD (By similarity).
 BINDING 116 116 FAD (By similarity).
 BINDING 121 121 FAD (By similarity).
 BINDING 123 123 FAD (By similarity).
 BINDING 393 393 FAD (By similarity).
 MOD_RES 617 617 Phosphoserine.
 MOD_RES 872 872 Phosphoserine.
 MOD_RES 875 875 Phosphoserine.
 MOD_RES 876 876 Phosphoserine.  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; FAD; Flavoprotein; LIM domain; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1067 AA 
Protein Sequence
MASPTSTNPA HAHFESFLQA QLCQDVLSSF QELCGALGLE PGGGLPQYHK IKDQLNYWSA 60
KSLWTKLDKR AGQPVYQQGR ACTSTKCLVV GAGPCGLRVA VELALLGARV VLVEKRTKFS 120
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVT 180
FTGLQPPPRK GSGWRAQLQP NPPAQLANYE FDVLISAAGG KFVPEGFKVR EMRGKLAIGI 240
TANFVNGRTV EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK 300
QCLLRLGVLR QDWPDTNRLL GSANVVPEAL QRFTRAAADF ATHGKLGKLE FAQDAHGQPD 360
VSAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV 420
KRWAEGAESL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVR 480
DLYDVLAKEP VQRNNDKTDT GMPATGSAGT QEELLRWCQE QTAGYPGVHV SDLSSSWADG 540
LALCALVYRL QPGLLEPSEL QGLGALEATA WALKVAENEL GITPVVSAQA VVAGSDPLGL 600
IAYLSHFHSA FKSMAHSPGP VSQASPGTSS AVLFLSKLQR TLQRSRAKEN AEDAGGKKLR 660
LEMEAETPST EVPPDPEPGV PLTPPSQHQE AGAGDLCALC GEHLYVLERL CVNGHFFHRS 720
CFRCHTCEAT LWPGGYEQHP GDGHFYCLQH LPQTDHKAEG SDRGPESPEL PTPSENSMPP 780
GLSTPTASQE GAGPVPDPSQ PTRRQIRLSS PERQRLSSLN LTPDPEMEPP PKPPRSCSAL 840
ARHALESSFV GWGLPVQSPQ ALVAMEKEEK ESPFSSEEEE EDVPLDSDVE QALQTFAKTS 900
GTMNNYPTWR RTLLRRAKEE EMKRFCKAQT IQRRLNEIEA ALRELEAEGV KLELALRRQS 960
SSPEQQKKLW VGQLLQLVDK KNSLVAEEAE LMITVQELNL EEKQWQLDQE LRGYMNREEN 1020
LKTAADRQAE DQVLRKLVDL VNQRDALIRF QEERRLSELA LGTGAQG 1067 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005882; C:intermediate filament; NAS:UniProtKB.
 GO:0003779; F:actin binding; IDA:UniProtKB.
 GO:0071949; F:FAD binding; IDA:UniProtKB.
 GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
 GO:0001933; P:negative regulation of protein phosphorylation; IEA:Compara.
 GO:0007165; P:signal transduction; NAS:UniProtKB. 
Interpro
 IPR001715; CH-domain.
 IPR022735; DUF3585.
 IPR002938; mOase_FAD-bd.
 IPR001781; Znf_LIM. 
Pfam
 PF00307; CH
 PF12130; DUF3585
 PF01494; FAD_binding_3
 PF00412; LIM 
SMART
 SM00033; CH
 SM00132; LIM 
PROSITE
 PS50021; CH
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2 
PRINTS