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Q8TDZ2

- MICA1_HUMAN

UniProt

Q8TDZ2 - MICA1_HUMAN

Protein

Protein-methionine sulfoxide oxidase MICAL1

Gene

MICAL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (15 Mar 2004)
      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 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/STK4.2 PublicationsCurated

    Catalytic activityi

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

    Cofactori

    FAD.1 Publication

    Kineticsi

    1. KM=4.7 µM for F-actin (at saturing NADPH concentration)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei95 – 951FADBy similarity
    Binding sitei114 – 1141FADBy similarity
    Binding sitei116 – 1161FADBy similarity
    Binding sitei121 – 1211FADBy similarity
    Binding sitei123 – 1231FADBy similarity
    Binding sitei393 – 3931FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi95 – 12329FADBy 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. protein binding Source: UniProtKB
    5. SH3 domain binding Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin filament depolymerization Source: UniProtKB
    2. cytoskeleton organization Source: UniProtKB
    3. negative regulation of apoptotic process Source: Ensembl
    4. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    5. negative regulation of protein phosphorylation Source: Ensembl
    6. oxidation-reduction process Source: UniProtKB
    7. signal transduction Source: UniProtKB
    8. sulfur oxidation Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SignaLinkiQ8TDZ2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-methionine sulfoxide oxidase MICAL1 (EC:1.14.13.-)
    Alternative name(s):
    Molecule interacting with CasL protein 1
    Short name:
    MICAL-1
    NEDD9-interacting protein with calponin homology and LIM domains
    Gene namesi
    Name:MICAL1
    Synonyms:MICAL, NICAL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20619. MICAL1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. intermediate filament Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134900249.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10671067Protein-methionine sulfoxide oxidase MICAL1PRO_0000075842Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei617 – 6171Phosphoserine1 Publication
    Modified residuei872 – 8721Phosphoserine2 Publications
    Modified residuei875 – 8751Phosphoserine2 Publications
    Modified residuei876 – 8761Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8TDZ2.
    PaxDbiQ8TDZ2.
    PRIDEiQ8TDZ2.

    PTM databases

    PhosphoSiteiQ8TDZ2.

    Expressioni

    Tissue specificityi

    Expressed in the thymus, lung, spleen, kidney, testis and hematopoietic cells.1 Publication

    Gene expression databases

    ArrayExpressiQ8TDZ2.
    BgeeiQ8TDZ2.
    CleanExiHS_MICAL1.
    GenevestigatoriQ8TDZ2.

    Organism-specific databases

    HPAiHPA030178.

    Interactioni

    Subunit structurei

    Interacts with STK38 and STK38L By similarity. Interacts with RAB8A By similarity. Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi122290. 15 interactions.
    IntActiQ8TDZ2. 7 interactions.
    MINTiMINT-1343875.
    STRINGi9606.ENSP00000351664.

    Structurei

    Secondary structure

    1
    1067
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi511 – 52414
    Turni533 – 5386
    Helixi541 – 55010
    Helixi552 – 5543
    Helixi560 – 5623
    Helixi565 – 57814
    Helixi588 – 5936
    Helixi597 – 61014
    Beta strandi698 – 7003
    Turni706 – 7083
    Turni719 – 7213
    Beta strandi725 – 7273
    Beta strandi735 – 7373
    Turni740 – 7423
    Turni748 – 7503

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WYLNMR-A510-612[»]
    2CO8NMR-A687-755[»]
    2DK9NMR-A506-614[»]
    ProteinModelPortaliQ8TDZ2.
    SMRiQ8TDZ2. Positions 8-484, 506-614, 687-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TDZ2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini508 – 609102CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini695 – 75763LIM zinc-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 489489Monooxygenase domainBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili646 – 66621Sequence AnalysisAdd
    BLAST
    Coiled coili919 – 96244Sequence AnalysisAdd
    BLAST
    Coiled coili999 – 102729Sequence AnalysisAdd
    BLAST

    Domaini

    The C-terminal coiled coil part contains the plexin-interacting region.

    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.
    HOVERGENiHBG052474.
    InParanoidiQ8TDZ2.
    OMAiKQCLLRL.
    OrthoDBiEOG769ZHM.
    PhylomeDBiQ8TDZ2.
    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.
    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]
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TDZ2-1) [UniParc]FASTAAdd to Basket

    Also known as: MICAL-1a

    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

    MASPTSTNPA HAHFESFLQA QLCQDVLSSF QELCGALGLE PGGGLPQYHK     50
    IKDQLNYWSA KSLWTKLDKR AGQPVYQQGR ACTSTKCLVV GAGPCGLRVA 100
    VELALLGARV VLVEKRTKFS RHNVLHLWPF TIHDLRALGA KKFYGRFCTG 150
    TLDHISIRQL QLLLLKVALL LGVEIHWGVT FTGLQPPPRK GSGWRAQLQP 200
    NPPAQLANYE FDVLISAAGG KFVPEGFKVR EMRGKLAIGI TANFVNGRTV 250
    EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK 300
    QCLLRLGVLR QDWPDTNRLL GSANVVPEAL QRFTRAAADF ATHGKLGKLE 350
    FAQDAHGQPD VSAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW 400
    PLGTGVARGF LAAFDAAWMV KRWAEGAESL EVLAERESLY QLLSQTSPEN 450
    MHRNVAQYGL DPATRYPNLN LRAVTPNQVR DLYDVLAKEP VQRNNDKTDT 500
    GMPATGSAGT QEELLRWCQE QTAGYPGVHV SDLSSSWADG LALCALVYRL 550
    QPGLLEPSEL QGLGALEATA WALKVAENEL GITPVVSAQA VVAGSDPLGL 600
    IAYLSHFHSA FKSMAHSPGP VSQASPGTSS AVLFLSKLQR TLQRSRAKEN 650
    AEDAGGKKLR LEMEAETPST EVPPDPEPGV PLTPPSQHQE AGAGDLCALC 700
    GEHLYVLERL CVNGHFFHRS CFRCHTCEAT LWPGGYEQHP GDGHFYCLQH 750
    LPQTDHKAEG SDRGPESPEL PTPSENSMPP GLSTPTASQE GAGPVPDPSQ 800
    PTRRQIRLSS PERQRLSSLN LTPDPEMEPP PKPPRSCSAL ARHALESSFV 850
    GWGLPVQSPQ ALVAMEKEEK ESPFSSEEEE EDVPLDSDVE QALQTFAKTS 900
    GTMNNYPTWR RTLLRRAKEE EMKRFCKAQT IQRRLNEIEA ALRELEAEGV 950
    KLELALRRQS SSPEQQKKLW VGQLLQLVDK KNSLVAEEAE LMITVQELNL 1000
    EEKQWQLDQE LRGYMNREEN LKTAADRQAE DQVLRKLVDL VNQRDALIRF 1050
    QEERRLSELA LGTGAQG 1067
    Length:1,067
    Mass (Da):117,875
    Last modified:March 15, 2004 - v2
    Checksum:i78C1BBF3E3CCD56B
    GO
    Isoform 2 (identifier: Q8TDZ2-2) [UniParc]FASTAAdd to Basket

    Also known as: MICAL-1b

    The sequence of this isoform differs from the canonical sequence as follows:
         312-397: Missing.

    Show »
    Length:981
    Mass (Da):108,552
    Checksum:i8EC7E9C12989C1E9
    GO
    Isoform 3 (identifier: Q8TDZ2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-735: Missing.
         736-768: YEQHPGDGHFYCLQHLPQTDHKAEGSDRGPESP → MPRLTFAPKGWPHPPTSLHPGQVTDQTTWWLFQ

    Note: No experimental confirmation available.

    Show »
    Length:332
    Mass (Da):37,715
    Checksum:i7FF1E955AE2204DB
    GO
    Isoform 4 (identifier: Q8TDZ2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSCLSHSSLPSCCPPQEASM

    Note: No experimental confirmation available.

    Show »
    Length:1,086
    Mass (Da):119,821
    Checksum:i947094500071E091
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti767 – 7671S → C in BAB15124. (PubMed:14702039)Curated
    Sequence conflicti816 – 8161L → S in BAH12301. (PubMed:14702039)Curated
    Sequence conflicti877 – 8771E → V in BAH12301. (PubMed:14702039)Curated
    Sequence conflicti887 – 8871S → L in CAB59266. (PubMed:17974005)Curated
    Sequence conflicti981 – 9811K → N in BAB13949. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121A → S.
    Corresponds to variant rs4946977 [ dbSNP | Ensembl ].
    VAR_067063
    Natural varianti12 – 121A → T.
    Corresponds to variant rs4946977 [ dbSNP | Ensembl ].
    VAR_050153
    Natural varianti153 – 1531D → A.
    Corresponds to variant rs34726911 [ dbSNP | Ensembl ].
    VAR_050154
    Natural varianti195 – 1951R → H.
    Corresponds to variant rs34699467 [ dbSNP | Ensembl ].
    VAR_067064
    Natural varianti309 – 3091L → M in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036191
    Natural varianti453 – 4531R → C.1 Publication
    Corresponds to variant rs17854785 [ dbSNP | Ensembl ].
    VAR_067065
    Natural varianti624 – 6241A → T.1 Publication
    Corresponds to variant rs17850590 [ dbSNP | Ensembl ].
    VAR_067066
    Natural varianti758 – 7581A → E.
    Corresponds to variant rs9320288 [ dbSNP | Ensembl ].
    VAR_017903
    Natural varianti758 – 7581A → K Requires 2 nucleotide substitutions. 3 Publications
    Corresponds to variant rs35260632 [ dbSNP | Ensembl ].
    VAR_067067
    Natural varianti758 – 7581A → S.
    Corresponds to variant rs59056467 [ dbSNP | Ensembl ].
    VAR_067068
    Natural varianti758 – 7581A → T.
    Corresponds to variant rs59056467 [ dbSNP | Ensembl ].
    VAR_061355

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 735735Missing in isoform 3. 1 PublicationVSP_009637Add
    BLAST
    Alternative sequencei1 – 11M → MSCLSHSSLPSCCPPQEASM in isoform 4. 1 PublicationVSP_042590
    Alternative sequencei312 – 39786Missing in isoform 2. 1 PublicationVSP_009639Add
    BLAST
    Alternative sequencei736 – 76833YEQHP…GPESP → MPRLTFAPKGWPHPPTSLHP GQVTDQTTWWLFQ in isoform 3. 1 PublicationVSP_009638Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB048948 mRNA. Translation: BAB86289.1.
    AK024500 mRNA. Translation: BAB15790.1.
    AK021999 mRNA. Translation: BAB13949.1.
    AK025392 mRNA. Translation: BAB15124.1.
    AK296284 mRNA. Translation: BAH12301.1.
    AL109947 Genomic DNA. Translation: CAI23343.1.
    CH471051 Genomic DNA. Translation: EAW48344.1.
    CH471051 Genomic DNA. Translation: EAW48345.1.
    BC009972 mRNA. Translation: AAH09972.2.
    BC042144 mRNA. Translation: AAH42144.1.
    BC052983 mRNA. Translation: AAH52983.1.
    AL122098 mRNA. Translation: CAB59266.1.
    CCDSiCCDS5076.1. [Q8TDZ2-1]
    CCDS55047.1. [Q8TDZ2-2]
    CCDS69170.1. [Q8TDZ2-4]
    PIRiT34532.
    RefSeqiNP_001152763.1. NM_001159291.1. [Q8TDZ2-2]
    NP_001273542.1. NM_001286613.1. [Q8TDZ2-4]
    NP_073602.3. NM_022765.3. [Q8TDZ2-1]
    UniGeneiHs.33476.

    Genome annotation databases

    EnsembliENST00000358577; ENSP00000351385; ENSG00000135596. [Q8TDZ2-2]
    ENST00000358807; ENSP00000351664; ENSG00000135596. [Q8TDZ2-1]
    GeneIDi64780.
    KEGGihsa:64780.
    UCSCiuc003ptj.3. human. [Q8TDZ2-1]
    uc010kdr.3. human. [Q8TDZ2-2]
    uc011eaq.2. human. [Q8TDZ2-4]

    Polymorphism databases

    DMDMi45593495.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB048948 mRNA. Translation: BAB86289.1 .
    AK024500 mRNA. Translation: BAB15790.1 .
    AK021999 mRNA. Translation: BAB13949.1 .
    AK025392 mRNA. Translation: BAB15124.1 .
    AK296284 mRNA. Translation: BAH12301.1 .
    AL109947 Genomic DNA. Translation: CAI23343.1 .
    CH471051 Genomic DNA. Translation: EAW48344.1 .
    CH471051 Genomic DNA. Translation: EAW48345.1 .
    BC009972 mRNA. Translation: AAH09972.2 .
    BC042144 mRNA. Translation: AAH42144.1 .
    BC052983 mRNA. Translation: AAH52983.1 .
    AL122098 mRNA. Translation: CAB59266.1 .
    CCDSi CCDS5076.1. [Q8TDZ2-1 ]
    CCDS55047.1. [Q8TDZ2-2 ]
    CCDS69170.1. [Q8TDZ2-4 ]
    PIRi T34532.
    RefSeqi NP_001152763.1. NM_001159291.1. [Q8TDZ2-2 ]
    NP_001273542.1. NM_001286613.1. [Q8TDZ2-4 ]
    NP_073602.3. NM_022765.3. [Q8TDZ2-1 ]
    UniGenei Hs.33476.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WYL NMR - A 510-612 [» ]
    2CO8 NMR - A 687-755 [» ]
    2DK9 NMR - A 506-614 [» ]
    ProteinModelPortali Q8TDZ2.
    SMRi Q8TDZ2. Positions 8-484, 506-614, 687-755.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122290. 15 interactions.
    IntActi Q8TDZ2. 7 interactions.
    MINTi MINT-1343875.
    STRINGi 9606.ENSP00000351664.

    PTM databases

    PhosphoSitei Q8TDZ2.

    Polymorphism databases

    DMDMi 45593495.

    Proteomic databases

    MaxQBi Q8TDZ2.
    PaxDbi Q8TDZ2.
    PRIDEi Q8TDZ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358577 ; ENSP00000351385 ; ENSG00000135596 . [Q8TDZ2-2 ]
    ENST00000358807 ; ENSP00000351664 ; ENSG00000135596 . [Q8TDZ2-1 ]
    GeneIDi 64780.
    KEGGi hsa:64780.
    UCSCi uc003ptj.3. human. [Q8TDZ2-1 ]
    uc010kdr.3. human. [Q8TDZ2-2 ]
    uc011eaq.2. human. [Q8TDZ2-4 ]

    Organism-specific databases

    CTDi 64780.
    GeneCardsi GC06M109766.
    HGNCi HGNC:20619. MICAL1.
    HPAi HPA030178.
    MIMi 607129. gene.
    neXtProti NX_Q8TDZ2.
    PharmGKBi PA134900249.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000047263.
    HOVERGENi HBG052474.
    InParanoidi Q8TDZ2.
    OMAi KQCLLRL.
    OrthoDBi EOG769ZHM.
    PhylomeDBi Q8TDZ2.
    TreeFami TF324129.

    Enzyme and pathway databases

    SignaLinki Q8TDZ2.

    Miscellaneous databases

    ChiTaRSi MICAL1. human.
    EvolutionaryTracei Q8TDZ2.
    GeneWikii MICAL1.
    GenomeRNAii 64780.
    NextBioi 66810.
    PROi Q8TDZ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TDZ2.
    Bgeei Q8TDZ2.
    CleanExi HS_MICAL1.
    Genevestigatori Q8TDZ2.

    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.
    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 ]
    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. "MICAL, a novel CasL interacting molecule, associates with vimentin."
      Suzuki T., Nakamoto T., Ogawa S., Seo S., Matsumura T., Tachibana K., Morimoto C., Hirai H.
      J. Biol. Chem. 277:14933-14941(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NEDD9 AND VIM, VARIANT LYS-758.
    2. "Characterization of long cDNA clones from human adult spleen."
      Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.
      DNA Res. 7:357-366(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Spleen.
    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 1 AND 4), VARIANTS LYS-758 AND LYS-758.
      Tissue: Colon mucosa, Embryo, Spleen and Thalamus.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2), VARIANTS CYS-453; THR-624 AND LYS-758.
      Tissue: Blood, Lymph and Uterus.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-1067 (ISOFORMS 1/2).
      Tissue: Testis.
    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: INTERACTION WITH PLXNA3.
    9. Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH VIM.
    10. "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.
    11. "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-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein."
      Schmidt E.F., Shim S.O., Strittmatter S.M.
      J. Neurosci. 28:2287-2297(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "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-617; SER-875 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1."
      Zucchini D., Caprini G., Pasterkamp R.J., Tedeschi G., Vanoni M.A.
      Arch. Biochem. Biophys. 515:1-13(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-872; SER-875 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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.
    18. "Solution structure of the CH domain of human NEDD9-interacting protein with calponin homology and LIM domains."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 506-613.
    19. "Solution structure of calponin homology domain of Human MICAL-1."
      Sun H., Dai H., Zhang J., Jin X., Xiong S., Xu J., Wu J., Shi Y.
      J. Biomol. NMR 36:295-300(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 506-614.
    20. "Investigation of the four cooperative unfolding units existing in the MICAL-1 CH domain."
      Jin X., Zhang J., Dai H., Sun H., Wang D., Wu J., Shi Y.
      Biophys. Chem. 129:269-278(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 506-614.
    21. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-309.

    Entry informationi

    Entry nameiMICA1_HUMAN
    AccessioniPrimary (citable) accession number: Q8TDZ2
    Secondary accession number(s): B7Z3R5
    , E1P5F0, Q7Z633, Q8IVS9, Q96G47, Q9H6X6, Q9H7I0, Q9HAA1, Q9UFF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: March 15, 2004
    Last modified: October 1, 2014
    This is version 131 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 6
      Human chromosome 6: 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