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Q7RTP6

- MICA3_HUMAN

UniProt

Q7RTP6 - MICA3_HUMAN

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Protein

Protein-methionine sulfoxide oxidase MICAL3

Gene
MICAL3, KIAA0819, KIAA1364
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 971FAD By similarity
Binding sitei116 – 1161FAD By similarity
Binding sitei118 – 1181FAD By similarity
Binding sitei123 – 1231FAD By similarity
Binding sitei125 – 1251FAD By similarity
Binding sitei398 – 3981FAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 11730FAD Reviewed predictionAdd
BLAST
Nucleotide bindingi97 – 12529FAD By 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
Complete GO annotation...

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).2 Publications

GO - Cellular componenti

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

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. 1 Publication
Mutagenesisi680 – 6834KRRK → AAAA in MICAL-3NLSMut; abolishes nuclear localization. 1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiQ7RTP6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini518 – 621104CHAdd
BLAST
Domaini762 – 82463LIM zinc-bindingAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1821 – 1992172 Reviewed predictionAdd
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.

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

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. VSP_039485
Alternative sequencei747 – 7471Q → QQREKECSRTCPKKVITLSP PPTPPPCRAHGGQQTYRDLD ADNRGKQSPHHERPEPEPPR RFFVDQWELSLSLRSSARPA SPSSDSLRQKYIKMYTGGVS SLAEQIANQLQRKEQPKALL DKKEL in isoform 5. VSP_042600
Alternative sequencei871 – 94979GVNGL…EEEEE → LTSLFGWVARHSLGLCDKAK GMSQHLQSNISSFGQQVAQN PLDSFFMCQLLAFGVPFLYG LSEVLVQIRGEFHWQAVAQ in isoform 5. VSP_042601Add
BLAST
Alternative sequencei934 – 96633SSSES…PWKEA → RDWVSPWLPRMVSNSWAQMI HPPQPPTVLGSQM in isoform 4. VSP_039486Add
BLAST
Alternative sequencei934 – 94815SSSES…GEEEE → RSARRAAGRPPATRP in isoform 2 and isoform 3. VSP_039487Add
BLAST
Alternative sequencei949 – 20021054Missing in isoform 2 and isoform 3. VSP_039488Add
BLAST
Alternative sequencei950 – 20021053Missing in isoform 5. VSP_042602Add
BLAST
Alternative sequencei967 – 20021036Missing in isoform 4. VSP_039489Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti414 – 4141G → D in BX647382. 1 Publication
Sequence conflicti1245 – 12451Q → R in BAA74842. 1 Publication
Sequence conflicti1717 – 17171E → V in AAH06562. 1 Publication
Isoform 4 (identifier: Q7RTP6-4)
Sequence conflicti957 – 9571Q → R in BX647382. 1 Publication

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

EnsembliENST00000207726; ENSP00000207726; ENSG00000243156. [Q7RTP6-3]
ENST00000383094; ENSP00000372574; ENSG00000243156. [Q7RTP6-2]
ENST00000400561; ENSP00000383406; ENSG00000243156. [Q7RTP6-4]
ENST00000414725; ENSP00000391827; ENSG00000243156. [Q7RTP6-3]
ENST00000429452; ENSP00000414846; ENSG00000243156. [Q7RTP6-5]
ENST00000441493; ENSP00000416015; ENSG00000243156. [Q7RTP6-1]
ENST00000444520; ENSP00000410315; ENSG00000243156. [Q7RTP6-4]
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 ENST00000207726 ; ENSP00000207726 ; ENSG00000243156 . [Q7RTP6-3 ]
ENST00000383094 ; ENSP00000372574 ; ENSG00000243156 . [Q7RTP6-2 ]
ENST00000400561 ; ENSP00000383406 ; ENSG00000243156 . [Q7RTP6-4 ]
ENST00000414725 ; ENSP00000391827 ; ENSG00000243156 . [Q7RTP6-3 ]
ENST00000429452 ; ENSP00000414846 ; ENSG00000243156 . [Q7RTP6-5 ]
ENST00000441493 ; ENSP00000416015 ; ENSG00000243156 . [Q7RTP6-1 ]
ENST00000444520 ; ENSP00000410315 ; ENSG00000243156 . [Q7RTP6-4 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 116 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

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