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Q7RTP6

- MICA3_HUMAN

UniProt

Q7RTP6 - MICA3_HUMAN

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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

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
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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoskeleton Source: UniProtKB-KW
  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

BgeeiQ7RTP6.
CleanExiHS_MICAL3.
ExpressionAtlasiQ7RTP6. baseline and differential.
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.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000047263.
HOVERGENiHBG081827.
InParanoidiQ7RTP6.
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

        10         20         30         40         50
MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY
60 70 80 90 100
HKLKSKLNYW KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR
110 120 130 140 150
TAIDLSLLGA KVVVIEKRDA FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC
160 170 180 190 200
AGAIDHISIR QLQLILLKVA LILGIEIHVN VEFQGLIQPP EDQENERIGW
210 220 230 240 250
RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK LAIAITANFI
260 270 280 290 300
NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV
310 320 330 340 350
MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ
360 370 380 390 400
LPSLDFAINH YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL
410 420 430 440 450
LEPFWPMGTG IARGFLAAMD SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ
460 470 480 490 500
TTPENVSKNF SQYSIDPVTR YPNINVNFLR PSQVRHLYDT GETKDIHLEM
510 520 530 540 550
ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV TDLTMSWKSG
560 570 580 590 600
LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE
610 620 630 640 650
MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP
660 670 680 690 700
ISFLSKLGQT ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER
710 720 730 740 750
PTLVSTLTDR RMDVAVGNQN KVKYMATQLL AKFEENAPAQ SIGIRRQGSM
760 770 780 790 800
KKEFPQNLGG SDTCYFCQKR VYVMERLSAE GKFFHRSCFK CEYCATTLRL
810 820 830 840 850
SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE AKGPLQDGAT
860 870 880 890 900
TDANGRANAV ASSTERTPGS GVNGLEEPSI AKRLRGTPER IELENYRLSL
910 920 930 940 950
RQAEALQEVP EETQAEHNLS SVLDTGAEED VASSSSESEM EEEGEEEEEE
960 970 980 990 1000
PRLPPSDLGG VPWKEAVRIH ALLKGKSEEE LEASKSFGPG NEEEEEEEEE
1010 1020 1030 1040 1050
YEEEEEEDYD EEEEESSEAG NQRLQQVMHA ADPLEIQADV HWTHIREREE
1060 1070 1080 1090 1100
EERMAPASES SASGAPLDEN DLEEDVDSEP AEIEGEAAED GDPGDTGAEL
1110 1120 1130 1140 1150
DDDQHWSDSP SDADRELRLP CPAEGEAELE LRVSEDEEKL PASPKHQERG
1160 1170 1180 1190 1200
PSQATSPIRS PQESALLFIP VHSPSTEGPQ LPPVPAATQE KSPEERLFPE
1210 1220 1230 1240 1250
PLLPKEKPKA DAPSDLKAVH SPIRSQPVTL PEARTPVSPG SPQPQPPVAA
1260 1270 1280 1290 1300
STPPPSPLPI CSQPQPSTEA TVPSPTQSPI RFQPAPAKTS TPLAPLPVQS
1310 1320 1330 1340 1350
QSDTKDRLGS PLAVDEALRR SDLVEEFWMK SAEIRRSLGL TPVDRSKGPE
1360 1370 1380 1390 1400
PSFPTPAFRP VSLKSYSVEK SPQDEGLHLL KPLSIPKRLG LPKPEGEPLS
1410 1420 1430 1440 1450
LPTPRSPSDR ELRSAQEERR ELSSSSGLGL HGSSSNMKTL GSQSFNTSDS
1460 1470 1480 1490 1500
AMLTPPSSPP PPPPPGEEPA TLRRKLREAE PNASVVPPPL PATWMRPPRE
1510 1520 1530 1540 1550
PAQPPREEVR KSFVESVEEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW
1560 1570 1580 1590 1600
PRPEKPRHPP LAKENGRLPA LEGTLQPQKR GLPLVSAEAK ELAEERMRAR
1610 1620 1630 1640 1650
EKSVKSQALR DAMARQLSRM QQMELASGAP RPRKASSAPS QGKERRPDSP
1660 1670 1680 1690 1700
TRPTLRGSEE PTLKHEATSE EVLSPPSDSG GPDGSFTSSE GSSGKSKKRS
1710 1720 1730 1740 1750
SLFSPRRNKK EKKSKGEGRP PEKPSSNLLE EAAAKPKSLW KSVFSGYKKD
1760 1770 1780 1790 1800
KKKKADDKSC PSTPSSGATV DSGKHRVLPV VRAELQLRRQ LSFSEDSDLS
1810 1820 1830 1840 1850
SDDVLEKSSQ KSRREPRTYT EEELNAKLTR RVQKAARRQA KQEELKRLHR
1860 1870 1880 1890 1900
AQIIQRQLQQ VEERQRRLEE RGVAVEKALR GEAGMGKKDD PKLMQEWFKL
1910 1920 1930 1940 1950
VQEKNAMVRY ESELMIFARE LELEDRQSRL QQELRERMAV EDHLKTEEEL
1960 1970 1980 1990 2000
SEEKQILNEM LEVVEQRDSL VALLEEQRLR EREEDKDLEA AMLSKGFSLN

WS
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.
GeneTreei ENSGT00760000118856.
HOGENOMi HOG000047263.
HOVERGENi HBG081827.
InParanoidi Q7RTP6.
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

Bgeei Q7RTP6.
CleanExi HS_MICAL3.
ExpressionAtlasi Q7RTP6. baseline and differential.
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: October 29, 2014
This is version 118 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