Tag | Content |
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CPLM ID | CPLM-001476 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein-methionine sulfoxide oxidase MICAL2 |
Protein Synonyms/Alias | Molecule interacting with CasL protein 2; MICAL-2 |
Gene Name | MICAL2 |
Gene Synonyms/Alias | KIAA0750; MICAL2PV1; MICAL2PV2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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458 | TTPENINKNFEQYTL | ubiquitination | [1] | 634 | RPVDSWRKNYGENAD | ubiquitination | [1] | 646 | NADLSLAKSSISNNY | ubiquitination | [1] |
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Reference | [1] 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 (By similarity). |
Sequence Annotation | DOMAIN 516 619 CH. DOMAIN 1000 1062 LIM zinc-binding. NP_BIND 97 125 FAD (By similarity). REGION 2 494 Monooxygenase domain (By similarity). BINDING 97 97 FAD (By similarity). BINDING 116 116 FAD (By similarity). BINDING 118 118 FAD (By similarity). BINDING 123 123 FAD (By similarity). BINDING 125 125 FAD (By similarity). BINDING 398 398 FAD (By similarity). |
Keyword | 3D-structure; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; FAD; Flavoprotein; LIM domain; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1124 AA |
Protein Sequence | MGENEDEKQA QAGQVFENFV QASTCKGTLQ AFNILTRHLD LDPLDHRNFY SKLKSKVTTW 60 KAKALWYKLD KRGSHKEYKR GKSCTNTKCL IVGGGPCGLR TAIELAYLGA KVVVVEKRDS 120 FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLILFKVA LMLGVEIHVN 180 VEFVKVLEPP EDQENQKIGW RAEFLPTDHS LSEFEFDVII GADGRRNTLE GFRRKEFRGK 240 LAIAITANFI NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDCTHYFV 300 MTAKKQSLLD KGVIINDYID TEMLLCAENV NQDNLLSYAR EAADFATNYQ LPSLDFAMNH 360 YGQPDVAMFD FTCMYASENA ALVRERQAHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD 420 TAWMVKSWNQ GTPPLELLAE RESLYRLLPQ TTPENINKNF EQYTLDPGTR YPNLNSHCVR 480 PHQVKHLYIT KELEHYPLER LGSVRRSVNL SRKESDIRPS KLLTWCQQQT EGYQHVNVTD 540 LTTSWRSGLA LCAIIHRFRP ELINFDSLNE DDAVENNQLA FDVAEREFGI PPVTTGKEMA 600 SAQEPDKLSM VMYLSKFYEL FRGTPLRPVD SWRKNYGENA DLSLAKSSIS NNYLNLTFPR 660 KRTPRVDGQT GENDMNKRRR KGFTNLDEPS NFSSRSLGSN QECGSSKEGG NQNKVKSMAN 720 QLLAKFEEST RNPSLMKQER RVSGIGKPVL CSSSGPPVHS CCPKPEEATP SPSPPLKRQF 780 PSVVVTGHVL RELKQVSAGS ECLSRPWRAR AKSDLQLGGT ENFATLPSTR PRAQALSGVL 840 WRLQQVEEKI LQKRAQNLAN REFHTKNIKE KAAHLASMFG HGDFPQNKLL SKGLSHTHPP 900 SPPSRLPSPD PAASSSPSTV DSASPARKEK KSPSGFHFHP SHLRTVHPQL TVGKVSSGIG 960 AAAEVLVNLY MNDHRPKAQA TSPDLESMRK SFPLNLGGSD TCYFCKKRVY VMERLSAEGH 1020 FFHRECFRCS ICATTLRLAA YTFDCDEGKF YCKPHFIHCK TNSKQRKRRA ELKQQREEEA 1080 TWQEQEAPRR DTPTESSCAV AAIGTLEGSP PVHFSLPVLH PLLG 1124 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. GO:0003779; F:actin binding; ISS:UniProtKB. GO:0071949; F:FAD binding; ISS: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; ISS:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0030042; P:actin filament depolymerization; ISS:UniProtKB. |
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SMART | |
PROSITE | |
PRINTS | |