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O94851

- MICA2_HUMAN

UniProt

O94851 - MICA2_HUMAN

Protein

Protein-methionine sulfoxide oxidase MICAL2

Gene

MICAL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Nuclear monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin and regulates the SRF signaling. Acts by modifying nuclear actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization. Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA.2 Publications

    Catalytic activityi

    [protein]-methionine + NADPH + O2 = [protein]-methionine-sulfoxide + NADP+ + H2O.1 Publication

    Cofactori

    FAD.By similarity

    Enzyme regulationi

    Specifically inhibited by CCG-1423, a small molecule inhibitor of SRF:MKL1/MRTF-A-dependent transcription.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei97 – 971FADBy similarity
    Binding sitei116 – 1161FADBy similarity
    Binding sitei118 – 1181FADBy similarity
    Binding sitei123 – 1231FADBy similarity
    Binding sitei125 – 1251FADBy similarity
    Binding sitei398 – 3981FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi97 – 12529FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. FAD binding Source: UniProtKB
    3. NADPH:sulfur oxidoreductase activity Source: UniProtKB
    4. 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 Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin filament depolymerization Source: UniProtKB
    2. cytoskeleton organization Source: UniProtKB
    3. heart development Source: UniProtKB
    4. heart looping Source: UniProtKB
    5. oxidation-reduction process Source: UniProtKB
    6. positive regulation of transcription via serum response element binding Source: UniProtKB
    7. sulfur oxidation Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Actin-binding, FAD, Flavoprotein, Metal-binding, NADP, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-methionine sulfoxide oxidase MICAL2 (EC:1.14.13.-)
    Alternative name(s):
    Molecule interacting with CasL protein 2
    Short name:
    MICAL-2
    Gene namesi
    Name:MICAL2
    Synonyms:KIAA0750, MICAL2PV1, MICAL2PV2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:24693. MICAL2.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi95 – 951G → V: Blocks FAD binding and abolishes catalytic activity. 1 Publication
    Mutagenesisi677 – 6815KRRRK → AAAAA in MICAL-2NLSMut; abolishes nuclear localization.

    Organism-specific databases

    PharmGKBiPA142671453.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11241124Protein-methionine sulfoxide oxidase MICAL2PRO_0000075844Add
    BLAST

    Proteomic databases

    MaxQBiO94851.
    PaxDbiO94851.
    PRIDEiO94851.

    PTM databases

    PhosphoSiteiO94851.

    Expressioni

    Gene expression databases

    ArrayExpressiO94851.
    BgeeiO94851.
    CleanExiHS_MICAL2.
    GenevestigatoriO94851.

    Organism-specific databases

    HPAiHPA030437.

    Interactioni

    Subunit structurei

    Interacts with VIM and PLXNA4 By similarity. Interacts with RAB1B.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi115003. 1 interaction.
    IntActiO94851. 1 interaction.
    STRINGi9606.ENSP00000256194.

    Structurei

    Secondary structure

    1
    1124
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi520 – 53011
    Beta strandi540 – 5423
    Helixi543 – 5453
    Beta strandi546 – 5483
    Helixi549 – 55810
    Turni560 – 5623
    Turni565 – 5673
    Helixi570 – 5723
    Helixi573 – 58614
    Helixi596 – 6016
    Helixi607 – 62115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E9KNMR-A516-629[»]
    ProteinModelPortaliO94851.
    SMRiO94851. Positions 16-488, 511-629, 974-1056.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94851.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini516 – 619104CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini1000 – 106263LIM zinc-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 494493Monooxygenase domainBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi660 – 68122Nuclear localization signal1 PublicationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Mical family.Curated
    Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
    Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain

    Phylogenomic databases

    eggNOGiCOG5069.
    HOGENOMiHOG000047263.
    HOVERGENiHBG052474.
    InParanoidiO94851.
    OMAiCSVCATT.
    OrthoDBiEOG769ZHM.
    PhylomeDBiO94851.
    TreeFamiTF324129.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    2.10.110.10. 1 hit.
    InterProiIPR001715. CH-domain.
    IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    IPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00307. CH. 1 hit.
    PF01494. FAD_binding_3. 1 hit.
    PF00412. LIM. 1 hit.
    [Graphical view]
    PRINTSiPR00420. RNGMNOXGNASE.
    SMARTiSM00033. CH. 1 hit.
    SM00132. LIM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    PROSITEiPS50021. CH. 1 hit.
    PS00478. LIM_DOMAIN_1. 1 hit.
    PS50023. LIM_DOMAIN_2. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O94851-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGENEDEKQA QAGQVFENFV QASTCKGTLQ AFNILTRHLD LDPLDHRNFY     50
    SKLKSKVTTW KAKALWYKLD KRGSHKEYKR GKSCTNTKCL IVGGGPCGLR 100
    TAIELAYLGA KVVVVEKRDS FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC 150
    AGSIDHISIR QLQLILFKVA LMLGVEIHVN VEFVKVLEPP EDQENQKIGW 200
    RAEFLPTDHS LSEFEFDVII GADGRRNTLE GFRRKEFRGK LAIAITANFI 250
    NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDCTHYFV 300
    MTAKKQSLLD KGVIINDYID TEMLLCAENV NQDNLLSYAR EAADFATNYQ 350
    LPSLDFAMNH YGQPDVAMFD FTCMYASENA ALVRERQAHQ LLVALVGDSL 400
    LEPFWPMGTG CARGFLAAFD TAWMVKSWNQ GTPPLELLAE RESLYRLLPQ 450
    TTPENINKNF EQYTLDPGTR YPNLNSHCVR PHQVKHLYIT KELEHYPLER 500
    LGSVRRSVNL SRKESDIRPS KLLTWCQQQT EGYQHVNVTD LTTSWRSGLA 550
    LCAIIHRFRP ELINFDSLNE DDAVENNQLA FDVAEREFGI PPVTTGKEMA 600
    SAQEPDKLSM VMYLSKFYEL FRGTPLRPVD SWRKNYGENA DLSLAKSSIS 650
    NNYLNLTFPR KRTPRVDGQT GENDMNKRRR KGFTNLDEPS NFSSRSLGSN 700
    QECGSSKEGG NQNKVKSMAN QLLAKFEEST RNPSLMKQER RVSGIGKPVL 750
    CSSSGPPVHS CCPKPEEATP SPSPPLKRQF PSVVVTGHVL RELKQVSAGS 800
    ECLSRPWRAR AKSDLQLGGT ENFATLPSTR PRAQALSGVL WRLQQVEEKI 850
    LQKRAQNLAN REFHTKNIKE KAAHLASMFG HGDFPQNKLL SKGLSHTHPP 900
    SPPSRLPSPD PAASSSPSTV DSASPARKEK KSPSGFHFHP SHLRTVHPQL 950
    TVGKVSSGIG AAAEVLVNLY MNDHRPKAQA TSPDLESMRK SFPLNLGGSD 1000
    TCYFCKKRVY VMERLSAEGH FFHRECFRCS ICATTLRLAA YTFDCDEGKF 1050
    YCKPHFIHCK TNSKQRKRRA ELKQQREEEA TWQEQEAPRR DTPTESSCAV 1100
    AAIGTLEGSP PVHFSLPVLH PLLG 1124
    Length:1,124
    Mass (Da):126,689
    Last modified:May 1, 1999 - v1
    Checksum:i1C276C42D17B64DF
    GO
    Isoform 2 (identifier: O94851-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-171: Missing.
         740-986: Missing.
         1112-1124: VHFSLPVLHPLLG → GISTSFFRKV...VLRCFPVKLR

    Show »
    Length:784
    Mass (Da):89,890
    Checksum:i114E5873F13E5C61
    GO
    Isoform 3 (identifier: O94851-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         929-949: Missing.

    Show »
    Length:1,103
    Mass (Da):124,253
    Checksum:iEAB33EE2B2DB4BA1
    GO
    Isoform 4 (identifier: O94851-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         739-928: Missing.
         950-985: Missing.
         1112-1124: VHFSLPVLHPLLG → GISTSFFRKV...VLRCFPVKLR

    Show »
    Length:976
    Mass (Da):111,652
    Checksum:iD8B4E819D43FDA7E
    GO
    Isoform 5 (identifier: O94851-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         739-928: Missing.

    Show »
    Length:934
    Mass (Da):106,211
    Checksum:i5CB357AB0F7D4B9E
    GO
    Isoform 6 (identifier: O94851-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         739-985: Missing.
         1112-1124: VHFSLPVLHPLLG → GISTSFFRKV...VLRCFPVKLR

    Show »
    Length:955
    Mass (Da):109,216
    Checksum:i583E6EF7AC29A939
    GO

    Sequence cautioni

    The sequence BAA34470.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191F → S in BAG57951. (PubMed:14702039)Curated
    Sequence conflicti208 – 2081D → G in CAD97967. (PubMed:17974005)Curated
    Sequence conflicti296 – 2961T → A in CAD97967. (PubMed:17974005)Curated
    Sequence conflicti529 – 5291Q → H in BAG57951. (PubMed:14702039)Curated
    Sequence conflicti563 – 5631I → V in BAG57951. (PubMed:14702039)Curated
    Sequence conflicti631 – 6311S → Y in CAD97967. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti145 – 1451F → L.
    Corresponds to variant rs2706656 [ dbSNP | Ensembl ].
    VAR_050155
    Natural varianti220 – 2201I → V.
    Corresponds to variant rs2306727 [ dbSNP | Ensembl ].
    VAR_021992
    Natural varianti687 – 6871D → E.
    Corresponds to variant rs3794084 [ dbSNP | Ensembl ].
    VAR_050156
    Natural varianti1089 – 10891R → Q.
    Corresponds to variant rs2270515 [ dbSNP | Ensembl ].
    VAR_020257
    Natural varianti1106 – 11061L → P.1 Publication
    Corresponds to variant rs1027335 [ dbSNP | Ensembl ].
    VAR_024523
    Natural varianti1110 – 11101P → S.
    Corresponds to variant rs35518829 [ dbSNP | Ensembl ].
    VAR_050157

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 171171Missing in isoform 2. 1 PublicationVSP_009859Add
    BLAST
    Alternative sequencei739 – 985247Missing in isoform 6. 1 PublicationVSP_042593Add
    BLAST
    Alternative sequencei739 – 928190Missing in isoform 4 and isoform 5. 2 PublicationsVSP_042594Add
    BLAST
    Alternative sequencei740 – 986247Missing in isoform 2. 1 PublicationVSP_009860Add
    BLAST
    Alternative sequencei929 – 94921Missing in isoform 3. 1 PublicationVSP_042595Add
    BLAST
    Alternative sequencei950 – 98536Missing in isoform 4. 1 PublicationVSP_042596Add
    BLAST
    Alternative sequencei1112 – 112413VHFSL…HPLLG → GISTSFFRKVLGWPLRLPRD LCNWMQGLLQAAGLHIRDNA YNYCYMYELLSLGLPLLWAF SEVLAAMYRESEGSLESICN WVLRCFPVKLR in isoform 2, isoform 4 and isoform 6. 2 PublicationsVSP_009861Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB110785 mRNA. Translation: BAD83656.1.
    AB110786 mRNA. Translation: BAD83657.1.
    AB018293 mRNA. Translation: BAA34470.2. Different initiation.
    AK294845 mRNA. Translation: BAG57951.1.
    AK302893 mRNA. Translation: BAH13835.1.
    BX538021 mRNA. Translation: CAD97967.1.
    BX641163 mRNA. Translation: CAE46072.1.
    AC025106 Genomic DNA. No translation available.
    AC079329 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68528.1.
    CH471064 Genomic DNA. Translation: EAW68529.1.
    CH471064 Genomic DNA. Translation: EAW68531.1.
    BC044577 mRNA. Translation: AAH44577.1.
    BK000462 mRNA. Translation: DAA01341.1.
    CCDSiCCDS60726.1. [O94851-3]
    CCDS60727.1. [O94851-5]
    CCDS60728.1. [O94851-4]
    CCDS7809.1. [O94851-1]
    RefSeqiNP_001269592.1. NM_001282663.1. [O94851-1]
    NP_001269593.1. NM_001282664.1. [O94851-3]
    NP_001269594.1. NM_001282665.1. [O94851-5]
    NP_001269595.1. NM_001282666.1. [O94851-4]
    NP_001269596.1. NM_001282667.1. [O94851-6]
    NP_055447.1. NM_014632.3. [O94851-1]
    XP_005253306.1. XM_005253249.1. [O94851-3]
    UniGeneiHs.501928.

    Genome annotation databases

    EnsembliENST00000256194; ENSP00000256194; ENSG00000133816. [O94851-1]
    ENST00000342902; ENSP00000344894; ENSG00000133816. [O94851-3]
    ENST00000379612; ENSP00000368932; ENSG00000133816. [O94851-4]
    ENST00000527546; ENSP00000433965; ENSG00000133816. [O94851-5]
    ENST00000537344; ENSP00000441689; ENSG00000133816. [O94851-5]
    GeneIDi9645.
    KEGGihsa:9645.
    UCSCiuc001mjz.3. human. [O94851-1]
    uc001mkb.3. human. [O94851-4]
    uc001mkc.3. human. [O94851-6]
    uc001mkd.3. human. [O94851-2]
    uc010rch.1. human. [O94851-5]
    uc010rci.2. human. [O94851-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB110785 mRNA. Translation: BAD83656.1 .
    AB110786 mRNA. Translation: BAD83657.1 .
    AB018293 mRNA. Translation: BAA34470.2 . Different initiation.
    AK294845 mRNA. Translation: BAG57951.1 .
    AK302893 mRNA. Translation: BAH13835.1 .
    BX538021 mRNA. Translation: CAD97967.1 .
    BX641163 mRNA. Translation: CAE46072.1 .
    AC025106 Genomic DNA. No translation available.
    AC079329 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68528.1 .
    CH471064 Genomic DNA. Translation: EAW68529.1 .
    CH471064 Genomic DNA. Translation: EAW68531.1 .
    BC044577 mRNA. Translation: AAH44577.1 .
    BK000462 mRNA. Translation: DAA01341.1 .
    CCDSi CCDS60726.1. [O94851-3 ]
    CCDS60727.1. [O94851-5 ]
    CCDS60728.1. [O94851-4 ]
    CCDS7809.1. [O94851-1 ]
    RefSeqi NP_001269592.1. NM_001282663.1. [O94851-1 ]
    NP_001269593.1. NM_001282664.1. [O94851-3 ]
    NP_001269594.1. NM_001282665.1. [O94851-5 ]
    NP_001269595.1. NM_001282666.1. [O94851-4 ]
    NP_001269596.1. NM_001282667.1. [O94851-6 ]
    NP_055447.1. NM_014632.3. [O94851-1 ]
    XP_005253306.1. XM_005253249.1. [O94851-3 ]
    UniGenei Hs.501928.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E9K NMR - A 516-629 [» ]
    ProteinModelPortali O94851.
    SMRi O94851. Positions 16-488, 511-629, 974-1056.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115003. 1 interaction.
    IntActi O94851. 1 interaction.
    STRINGi 9606.ENSP00000256194.

    PTM databases

    PhosphoSitei O94851.

    Proteomic databases

    MaxQBi O94851.
    PaxDbi O94851.
    PRIDEi O94851.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256194 ; ENSP00000256194 ; ENSG00000133816 . [O94851-1 ]
    ENST00000342902 ; ENSP00000344894 ; ENSG00000133816 . [O94851-3 ]
    ENST00000379612 ; ENSP00000368932 ; ENSG00000133816 . [O94851-4 ]
    ENST00000527546 ; ENSP00000433965 ; ENSG00000133816 . [O94851-5 ]
    ENST00000537344 ; ENSP00000441689 ; ENSG00000133816 . [O94851-5 ]
    GeneIDi 9645.
    KEGGi hsa:9645.
    UCSCi uc001mjz.3. human. [O94851-1 ]
    uc001mkb.3. human. [O94851-4 ]
    uc001mkc.3. human. [O94851-6 ]
    uc001mkd.3. human. [O94851-2 ]
    uc010rch.1. human. [O94851-5 ]
    uc010rci.2. human. [O94851-3 ]

    Organism-specific databases

    CTDi 9645.
    GeneCardsi GC11P012115.
    HGNCi HGNC:24693. MICAL2.
    HPAi HPA030437.
    MIMi 608881. gene.
    neXtProti NX_O94851.
    PharmGKBi PA142671453.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000047263.
    HOVERGENi HBG052474.
    InParanoidi O94851.
    OMAi CSVCATT.
    OrthoDBi EOG769ZHM.
    PhylomeDBi O94851.
    TreeFami TF324129.

    Miscellaneous databases

    ChiTaRSi MICAL2. human.
    EvolutionaryTracei O94851.
    GeneWikii MICAL2.
    GenomeRNAii 9645.
    NextBioi 36203.
    PROi O94851.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94851.
    Bgeei O94851.
    CleanExi HS_MICAL2.
    Genevestigatori O94851.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    2.10.110.10. 1 hit.
    InterProi IPR001715. CH-domain.
    IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00307. CH. 1 hit.
    PF01494. FAD_binding_3. 1 hit.
    PF00412. LIM. 1 hit.
    [Graphical view ]
    PRINTSi PR00420. RNGMNOXGNASE.
    SMARTi SM00033. CH. 1 hit.
    SM00132. LIM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    PROSITEi PS50021. CH. 1 hit.
    PS00478. LIM_DOMAIN_1. 1 hit.
    PS50023. LIM_DOMAIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of novel molecules, MICAL2-PV (MICAL2 prostate cancer variants), increases with high Gleason score and prostate cancer progression."
      Ashida S., Furihata M., Katagiri T., Tamura K., Anazawa Y., Yoshioka H., Miki T., Fujioka T., Shuin T., Nakamura Y., Nakagawa H.
      Clin. Cancer Res. 12:2767-2773(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 6).
      Tissue: Prostate.
    2. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5), VARIANT PRO-1106.
      Tissue: Brain and Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Colon endothelium and Endometrium.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    8. "MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion."
      Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.
      Cell 109:887-900(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE STRUCTURE.
    9. "The MICAL proteins and rab1: a possible link to the cytoskeleton?"
      Fischer J., Weide T., Barnekow A.
      Biochem. Biophys. Res. Commun. 328:415-423(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB1B.
    10. "Actin stimulates reduction of the MICAL-2 monooxygenase domain."
      McDonald C.A., Liu Y.Y., Palfey B.A.
      Biochemistry 52:6076-6084(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Redox modification of nuclear actin by MICAL-2 regulates SRF signaling."
      Lundquist M.R., Storaska A.J., Liu T.C., Larsen S.D., Evans T., Neubig R.R., Jaffrey S.R.
      Cell 156:563-576(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF GLY-95 AND 677-LYS--LYS-681, ENZYME REGULATION.
    12. "Solution structure of the CH domain from human MICAL-2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 511-629.

    Entry informationi

    Entry nameiMICA2_HUMAN
    AccessioniPrimary (citable) accession number: O94851
    Secondary accession number(s): B4DGZ0
    , B7Z849, D3DQW5, G3XAC8, Q5KTR3, Q5KTR4, Q7Z3A8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3