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O94851

- MICA2_HUMAN

UniProt

O94851 - MICA2_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication

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

BgeeiO94851.
CleanExiHS_MICAL2.
ExpressionAtlasiO94851. baseline and differential.
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, 1000-1056.
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.
GeneTreeiENSGT00760000118856.
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

        10         20         30         40         50
MGENEDEKQA QAGQVFENFV QASTCKGTLQ AFNILTRHLD LDPLDHRNFY
60 70 80 90 100
SKLKSKVTTW KAKALWYKLD KRGSHKEYKR GKSCTNTKCL IVGGGPCGLR
110 120 130 140 150
TAIELAYLGA KVVVVEKRDS FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC
160 170 180 190 200
AGSIDHISIR QLQLILFKVA LMLGVEIHVN VEFVKVLEPP EDQENQKIGW
210 220 230 240 250
RAEFLPTDHS LSEFEFDVII GADGRRNTLE GFRRKEFRGK LAIAITANFI
260 270 280 290 300
NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDCTHYFV
310 320 330 340 350
MTAKKQSLLD KGVIINDYID TEMLLCAENV NQDNLLSYAR EAADFATNYQ
360 370 380 390 400
LPSLDFAMNH YGQPDVAMFD FTCMYASENA ALVRERQAHQ LLVALVGDSL
410 420 430 440 450
LEPFWPMGTG CARGFLAAFD TAWMVKSWNQ GTPPLELLAE RESLYRLLPQ
460 470 480 490 500
TTPENINKNF EQYTLDPGTR YPNLNSHCVR PHQVKHLYIT KELEHYPLER
510 520 530 540 550
LGSVRRSVNL SRKESDIRPS KLLTWCQQQT EGYQHVNVTD LTTSWRSGLA
560 570 580 590 600
LCAIIHRFRP ELINFDSLNE DDAVENNQLA FDVAEREFGI PPVTTGKEMA
610 620 630 640 650
SAQEPDKLSM VMYLSKFYEL FRGTPLRPVD SWRKNYGENA DLSLAKSSIS
660 670 680 690 700
NNYLNLTFPR KRTPRVDGQT GENDMNKRRR KGFTNLDEPS NFSSRSLGSN
710 720 730 740 750
QECGSSKEGG NQNKVKSMAN QLLAKFEEST RNPSLMKQER RVSGIGKPVL
760 770 780 790 800
CSSSGPPVHS CCPKPEEATP SPSPPLKRQF PSVVVTGHVL RELKQVSAGS
810 820 830 840 850
ECLSRPWRAR AKSDLQLGGT ENFATLPSTR PRAQALSGVL WRLQQVEEKI
860 870 880 890 900
LQKRAQNLAN REFHTKNIKE KAAHLASMFG HGDFPQNKLL SKGLSHTHPP
910 920 930 940 950
SPPSRLPSPD PAASSSPSTV DSASPARKEK KSPSGFHFHP SHLRTVHPQL
960 970 980 990 1000
TVGKVSSGIG AAAEVLVNLY MNDHRPKAQA TSPDLESMRK SFPLNLGGSD
1010 1020 1030 1040 1050
TCYFCKKRVY VMERLSAEGH FFHRECFRCS ICATTLRLAA YTFDCDEGKF
1060 1070 1080 1090 1100
YCKPHFIHCK TNSKQRKRRA ELKQQREEEA TWQEQEAPRR DTPTESSCAV
1110 1120
AAIGTLEGSP PVHFSLPVLH PLLG
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. [O94851-1]
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, 1000-1056.
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 . [O94851-1 ]
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.
GeneTreei ENSGT00760000118856.
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

Bgeei O94851.
CleanExi HS_MICAL2.
ExpressionAtlasi O94851. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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