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Q7RTP6

- MICA3_HUMAN

UniProt

Q7RTP6 - MICA3_HUMAN

Protein

Protein-methionine sulfoxide oxidase MICAL3

Gene

MICAL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    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. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process.2 Publications

    Catalytic activityi

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

    Cofactori

    FAD.By similarity

    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 bindingi88 – 11730FADSequence AnalysisAdd
    BLAST
    Nucleotide bindingi97 – 12529FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. FAD binding Source: UniProtKB
    3. 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
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin filament depolymerization Source: UniProtKB
    2. cytoskeleton organization Source: UniProtKB
    3. exocytosis Source: UniProtKB-KW
    4. oxidation-reduction process Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Exocytosis

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-methionine sulfoxide oxidase MICAL3 (EC:1.14.13.-)
    Alternative name(s):
    Molecule interacting with CasL protein 3
    Short name:
    MICAL-3
    Gene namesi
    Name:MICAL3
    Synonyms:KIAA0819, KIAA1364
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:24694. MICAL3.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. Nucleus
    Note: Mainly localizes in the nucleus.1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoskeleton Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi93 – 986GAGPCG → WAWPCW: Abolishes Monooxygenase activity and impairs ability to control docking and fusion of exocytic carriers.
    Mutagenesisi680 – 6834KRRK → AAAA in MICAL-3NLSMut; abolishes nuclear localization.

    Organism-specific databases

    PharmGKBiPA142671454.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20022002Protein-methionine sulfoxide oxidase MICAL3PRO_0000075846Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei649 – 6491Phosphoserine2 Publications
    Modified residuei887 – 8871Phosphothreonine1 Publication
    Modified residuei1310 – 13101Phosphoserine2 Publications
    Modified residuei1337 – 13371Phosphoserine1 Publication
    Modified residuei1341 – 13411Phosphothreonine1 Publication
    Modified residuei1371 – 13711Phosphoserine2 Publications
    Modified residuei1384 – 13841Phosphoserine1 Publication
    Modified residuei1454 – 14541Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7RTP6.
    PaxDbiQ7RTP6.
    PeptideAtlasiO94909.
    PRIDEiQ7RTP6.

    PTM databases

    PhosphoSiteiQ7RTP6.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ7RTP6.
    BgeeiQ7RTP6.
    CleanExiHS_MICAL3.
    GenevestigatoriQ7RTP6.

    Organism-specific databases

    HPAiHPA000639.
    HPA003421.
    HPA034882.

    Interactioni

    Subunit structurei

    Interacts with RAB1B. Interacts with ERC1 and RAB8A.2 Publications

    Protein-protein interaction databases

    BioGridi121609. 8 interactions.
    IntActiQ7RTP6. 3 interactions.
    STRINGi9606.ENSP00000414846.

    Structurei

    Secondary structure

    1
    2002
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi519 – 5213
    Helixi523 – 5319
    Beta strandi535 – 5373
    Helixi545 – 5484
    Helixi551 – 56010
    Turni562 – 5643
    Turni567 – 5693
    Helixi575 – 58915
    Helixi598 – 6036
    Helixi609 – 62315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D88NMR-A518-625[»]
    ProteinModelPortaliQ7RTP6.
    SMRiQ7RTP6. Positions 10-489, 515-630, 762-818.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7RTP6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini518 – 621104CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini762 – 82463LIM zinc-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1821 – 1992172Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi663 – 68422Nuclear localization signal1 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi688 – 6914Poly-Glu
    Compositional biasi889 – 1138250Glu-richAdd
    BLAST
    Compositional biasi1141 – 1505365Pro-richAdd
    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

    Coiled coil, LIM domain

    Phylogenomic databases

    eggNOGiCOG5069.
    HOGENOMiHOG000047263.
    HOVERGENiHBG081827.
    InParanoidiO94909.
    OMAiMHAADPL.
    OrthoDBiEOG769ZHM.
    PhylomeDBiQ7RTP6.
    TreeFamiTF324129.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    2.10.110.10. 1 hit.
    InterProiIPR001715. CH-domain.
    IPR022735. DUF3585.
    IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    IPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00307. CH. 1 hit.
    PF12130. DUF3585. 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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q7RTP6-1) [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

    MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY     50
    HKLKSKLNYW KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR 100
    TAIDLSLLGA KVVVIEKRDA FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC 150
    AGAIDHISIR QLQLILLKVA LILGIEIHVN VEFQGLIQPP EDQENERIGW 200
    RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK LAIAITANFI 250
    NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV 300
    MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ 350
    LPSLDFAINH YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL 400
    LEPFWPMGTG IARGFLAAMD SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ 450
    TTPENVSKNF SQYSIDPVTR YPNINVNFLR PSQVRHLYDT GETKDIHLEM 500
    ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV TDLTMSWKSG 550
    LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE 600
    MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP 650
    ISFLSKLGQT ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER 700
    PTLVSTLTDR RMDVAVGNQN KVKYMATQLL AKFEENAPAQ SIGIRRQGSM 750
    KKEFPQNLGG SDTCYFCQKR VYVMERLSAE GKFFHRSCFK CEYCATTLRL 800
    SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE AKGPLQDGAT 850
    TDANGRANAV ASSTERTPGS GVNGLEEPSI AKRLRGTPER IELENYRLSL 900
    RQAEALQEVP EETQAEHNLS SVLDTGAEED VASSSSESEM EEEGEEEEEE 950
    PRLPPSDLGG VPWKEAVRIH ALLKGKSEEE LEASKSFGPG NEEEEEEEEE 1000
    YEEEEEEDYD EEEEESSEAG NQRLQQVMHA ADPLEIQADV HWTHIREREE 1050
    EERMAPASES SASGAPLDEN DLEEDVDSEP AEIEGEAAED GDPGDTGAEL 1100
    DDDQHWSDSP SDADRELRLP CPAEGEAELE LRVSEDEEKL PASPKHQERG 1150
    PSQATSPIRS PQESALLFIP VHSPSTEGPQ LPPVPAATQE KSPEERLFPE 1200
    PLLPKEKPKA DAPSDLKAVH SPIRSQPVTL PEARTPVSPG SPQPQPPVAA 1250
    STPPPSPLPI CSQPQPSTEA TVPSPTQSPI RFQPAPAKTS TPLAPLPVQS 1300
    QSDTKDRLGS PLAVDEALRR SDLVEEFWMK SAEIRRSLGL TPVDRSKGPE 1350
    PSFPTPAFRP VSLKSYSVEK SPQDEGLHLL KPLSIPKRLG LPKPEGEPLS 1400
    LPTPRSPSDR ELRSAQEERR ELSSSSGLGL HGSSSNMKTL GSQSFNTSDS 1450
    AMLTPPSSPP PPPPPGEEPA TLRRKLREAE PNASVVPPPL PATWMRPPRE 1500
    PAQPPREEVR KSFVESVEEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW 1550
    PRPEKPRHPP LAKENGRLPA LEGTLQPQKR GLPLVSAEAK ELAEERMRAR 1600
    EKSVKSQALR DAMARQLSRM QQMELASGAP RPRKASSAPS QGKERRPDSP 1650
    TRPTLRGSEE PTLKHEATSE EVLSPPSDSG GPDGSFTSSE GSSGKSKKRS 1700
    SLFSPRRNKK EKKSKGEGRP PEKPSSNLLE EAAAKPKSLW KSVFSGYKKD 1750
    KKKKADDKSC PSTPSSGATV DSGKHRVLPV VRAELQLRRQ LSFSEDSDLS 1800
    SDDVLEKSSQ KSRREPRTYT EEELNAKLTR RVQKAARRQA KQEELKRLHR 1850
    AQIIQRQLQQ VEERQRRLEE RGVAVEKALR GEAGMGKKDD PKLMQEWFKL 1900
    VQEKNAMVRY ESELMIFARE LELEDRQSRL QQELRERMAV EDHLKTEEEL 1950
    SEEKQILNEM LEVVEQRDSL VALLEEQRLR EREEDKDLEA AMLSKGFSLN 2000
    WS 2002
    Length:2,002
    Mass (Da):224,295
    Last modified:July 13, 2010 - v2
    Checksum:iF85C97FD4D647B80
    GO
    Isoform 2 (identifier: Q7RTP6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         934-948: SSSESEMEEEGEEEE → RSARRAAGRPPATRP
         949-2002: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:948
    Mass (Da):106,837
    Checksum:iD50FC4EC6F46D30C
    GO
    Isoform 3 (identifier: Q7RTP6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         746-746: R → RQLTQERGASQPSCCLPGQVRPAPTPRWK
         934-948: SSSESEMEEEGEEEE → RSARRAAGRPPATRP
         949-2002: Missing.

    Show »
    Length:976
    Mass (Da):109,911
    Checksum:iD94482577189AD04
    GO
    Isoform 4 (identifier: Q7RTP6-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         934-966: SSSESEMEEEGEEEEEEPRLPPSDLGGVPWKEA → RDWVSPWLPRMVSNSWAQMIHPPQPPTVLGSQM
         967-2002: Missing.

    Show »
    Length:966
    Mass (Da):109,047
    Checksum:iDC1B9C83CB4D3E35
    GO
    Isoform 5 (identifier: Q7RTP6-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         747-747: Q → QQREKECSRT...PKALLDKKEL
         871-949: GVNGLEEPSI...MEEEGEEEEE → LTSLFGWVAR...GEFHWQAVAQ
         950-2002: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,073
    Mass (Da):121,173
    Checksum:iC550AC7BE7536179
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti414 – 4141G → D in BX647382. (PubMed:17974005)Curated
    Sequence conflicti1245 – 12451Q → R in BAA74842. (PubMed:10718198)Curated
    Sequence conflicti1717 – 17171E → V in AAH06562. (PubMed:15489334)Curated
    Isoform 4 (identifier: Q7RTP6-4)
    Sequence conflicti957 – 9571Q → R in BX647382. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111P → A.
    Corresponds to variant rs11913706 [ dbSNP | Ensembl ].
    VAR_059451
    Natural varianti745 – 7451R → Q.
    Corresponds to variant rs2289719 [ dbSNP | Ensembl ].
    VAR_059452
    Natural varianti750 – 7501M → L.
    Corresponds to variant rs5992128 [ dbSNP | Ensembl ].
    VAR_018263

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei746 – 7461R → RQLTQERGASQPSCCLPGQV RPAPTPRWK in isoform 3. 1 PublicationVSP_039485
    Alternative sequencei747 – 7471Q → QQREKECSRTCPKKVITLSP PPTPPPCRAHGGQQTYRDLD ADNRGKQSPHHERPEPEPPR RFFVDQWELSLSLRSSARPA SPSSDSLRQKYIKMYTGGVS SLAEQIANQLQRKEQPKALL DKKEL in isoform 5. 1 PublicationVSP_042600
    Alternative sequencei871 – 94979GVNGL…EEEEE → LTSLFGWVARHSLGLCDKAK GMSQHLQSNISSFGQQVAQN PLDSFFMCQLLAFGVPFLYG LSEVLVQIRGEFHWQAVAQ in isoform 5. 1 PublicationVSP_042601Add
    BLAST
    Alternative sequencei934 – 96633SSSES…PWKEA → RDWVSPWLPRMVSNSWAQMI HPPQPPTVLGSQM in isoform 4. 2 PublicationsVSP_039486Add
    BLAST
    Alternative sequencei934 – 94815SSSES…GEEEE → RSARRAAGRPPATRP in isoform 2 and isoform 3. 2 PublicationsVSP_039487Add
    BLAST
    Alternative sequencei949 – 20021054Missing in isoform 2 and isoform 3. 2 PublicationsVSP_039488Add
    BLAST
    Alternative sequencei950 – 20021053Missing in isoform 5. 1 PublicationVSP_042602Add
    BLAST
    Alternative sequencei967 – 20021036Missing in isoform 4. 2 PublicationsVSP_039489Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR456364 mRNA. Translation: CAG30250.1.
    BX647382 mRNA. No translation available.
    AC016026 Genomic DNA. No translation available.
    AC016027 Genomic DNA. No translation available.
    BC006562 mRNA. Translation: AAH06562.2.
    BC085009 mRNA. Translation: AAH85009.1.
    BC157876 mRNA. Translation: AAI57877.1.
    BC171887 mRNA. Translation: AAI71887.1.
    AB020626 mRNA. Translation: BAA74842.1.
    AB037785 mRNA. Translation: BAA92602.1.
    BK000464 mRNA. Translation: DAA01343.1.
    BK000465 mRNA. Translation: DAA01344.1.
    CCDSiCCDS46659.1. [Q7RTP6-1]
    CCDS46660.1. [Q7RTP6-4]
    CCDS46661.1. [Q7RTP6-5]
    RefSeqiNP_001116203.1. NM_001122731.2. [Q7RTP6-4]
    NP_001129476.1. NM_001136004.3. [Q7RTP6-5]
    NP_056056.2. NM_015241.2. [Q7RTP6-1]
    XP_005261319.1. XM_005261262.1. [Q7RTP6-1]
    UniGeneiHs.528024.

    Genome annotation databases

    EnsembliENST00000383094; ENSP00000372574; ENSG00000243156. [Q7RTP6-2]
    ENST00000400561; ENSP00000383406; ENSG00000243156. [Q7RTP6-4]
    ENST00000414725; ENSP00000391827; ENSG00000243156. [Q7RTP6-3]
    ENST00000441493; ENSP00000416015; ENSG00000243156. [Q7RTP6-1]
    ENST00000585038; ENSP00000462033; ENSG00000243156. [Q7RTP6-5]
    GeneIDi57553.
    KEGGihsa:57553.
    UCSCiuc002zng.4. human. [Q7RTP6-1]
    uc002znh.2. human. [Q7RTP6-4]
    uc002znj.1. human. [Q7RTP6-3]
    uc002znk.1. human. [Q7RTP6-2]
    uc010grf.3. human. [Q7RTP6-5]

    Polymorphism databases

    DMDMi300669653.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR456364 mRNA. Translation: CAG30250.1 .
    BX647382 mRNA. No translation available.
    AC016026 Genomic DNA. No translation available.
    AC016027 Genomic DNA. No translation available.
    BC006562 mRNA. Translation: AAH06562.2 .
    BC085009 mRNA. Translation: AAH85009.1 .
    BC157876 mRNA. Translation: AAI57877.1 .
    BC171887 mRNA. Translation: AAI71887.1 .
    AB020626 mRNA. Translation: BAA74842.1 .
    AB037785 mRNA. Translation: BAA92602.1 .
    BK000464 mRNA. Translation: DAA01343.1 .
    BK000465 mRNA. Translation: DAA01344.1 .
    CCDSi CCDS46659.1. [Q7RTP6-1 ]
    CCDS46660.1. [Q7RTP6-4 ]
    CCDS46661.1. [Q7RTP6-5 ]
    RefSeqi NP_001116203.1. NM_001122731.2. [Q7RTP6-4 ]
    NP_001129476.1. NM_001136004.3. [Q7RTP6-5 ]
    NP_056056.2. NM_015241.2. [Q7RTP6-1 ]
    XP_005261319.1. XM_005261262.1. [Q7RTP6-1 ]
    UniGenei Hs.528024.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D88 NMR - A 518-625 [» ]
    ProteinModelPortali Q7RTP6.
    SMRi Q7RTP6. Positions 10-489, 515-630, 762-818.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121609. 8 interactions.
    IntActi Q7RTP6. 3 interactions.
    STRINGi 9606.ENSP00000414846.

    PTM databases

    PhosphoSitei Q7RTP6.

    Polymorphism databases

    DMDMi 300669653.

    Proteomic databases

    MaxQBi Q7RTP6.
    PaxDbi Q7RTP6.
    PeptideAtlasi O94909.
    PRIDEi Q7RTP6.

    Protocols and materials databases

    DNASUi 57553.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000383094 ; ENSP00000372574 ; ENSG00000243156 . [Q7RTP6-2 ]
    ENST00000400561 ; ENSP00000383406 ; ENSG00000243156 . [Q7RTP6-4 ]
    ENST00000414725 ; ENSP00000391827 ; ENSG00000243156 . [Q7RTP6-3 ]
    ENST00000441493 ; ENSP00000416015 ; ENSG00000243156 . [Q7RTP6-1 ]
    ENST00000585038 ; ENSP00000462033 ; ENSG00000243156 . [Q7RTP6-5 ]
    GeneIDi 57553.
    KEGGi hsa:57553.
    UCSCi uc002zng.4. human. [Q7RTP6-1 ]
    uc002znh.2. human. [Q7RTP6-4 ]
    uc002znj.1. human. [Q7RTP6-3 ]
    uc002znk.1. human. [Q7RTP6-2 ]
    uc010grf.3. human. [Q7RTP6-5 ]

    Organism-specific databases

    CTDi 57553.
    GeneCardsi GC22M018271.
    H-InvDB HIX0213260.
    HGNCi HGNC:24694. MICAL3.
    HPAi HPA000639.
    HPA003421.
    HPA034882.
    MIMi 608882. gene.
    neXtProti NX_Q7RTP6.
    PharmGKBi PA142671454.
    HUGEi Search...
    Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000047263.
    HOVERGENi HBG081827.
    InParanoidi O94909.
    OMAi MHAADPL.
    OrthoDBi EOG769ZHM.
    PhylomeDBi Q7RTP6.
    TreeFami TF324129.

    Miscellaneous databases

    ChiTaRSi MICAL3. human.
    EvolutionaryTracei Q7RTP6.
    GeneWikii MICAL3.
    GenomeRNAii 57553.
    NextBioi 64022.
    PROi Q7RTP6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7RTP6.
    Bgeei Q7RTP6.
    CleanExi HS_MICAL3.
    Genevestigatori Q7RTP6.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    2.10.110.10. 1 hit.
    InterProi IPR001715. CH-domain.
    IPR022735. DUF3585.
    IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00307. CH. 1 hit.
    PF12130. DUF3585. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Testis.
    3. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1626-2002 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-966 (ISOFORM 4).
      Tissue: Lymph and Pancreas.
    5. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-2002 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1014-2002 (ISOFORM 1).
      Tissue: Brain.
    6. "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: IDENTIFICATION (ISOFORM 3 AND PARTIAL ISOFORM 1).
    7. "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, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; THR-887; SER-1371 AND SER-1384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310 AND THR-1454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-1337 AND THR-1341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: FUNCTION, INTERACTION WITH ERC1 AND RAB8A, MUTAGENESIS OF 93-GLY--GLY-98.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 680-LYS--LYS-683, FUNCTION.
    15. "Solution structure of the CH domain from human MICAL-3 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 515-630.

    Entry informationi

    Entry nameiMICA3_HUMAN
    AccessioniPrimary (citable) accession number: Q7RTP6
    Secondary accession number(s): B2RXJ5
    , E9PEF0, O94909, Q5U4P4, Q6ICK4, Q96DF2, Q9P2I3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 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 22
      Human chromosome 22: 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