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Q8VDP3

- MICA1_MOUSE

UniProt

Q8VDP3 - MICA1_MOUSE

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Protein

Protein-methionine sulfoxide oxidase MICAL1

Gene

Mical1

Organism
Mus musculus (Mouse)
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. 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 Publications

Catalytic activityi

[protein]-methionine + NADPH + O2 = [protein]-methionine-sulfoxide + NADP+ + H2O.1 Publication

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951FAD1 Publication
Binding sitei114 – 1141FAD1 Publication
Binding sitei116 – 1161FAD1 Publication
Binding sitei121 – 1211FAD1 Publication
Binding sitei123 – 1231FAD1 Publication
Binding sitei393 – 3931FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi95 – 12329FAD1 PublicationAdd
BLAST

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. FAD binding Source: UniProtKB
  3. monooxygenase activity Source: MGI
  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. Rab GTPase binding Source: UniProtKB
  6. SH3 domain binding Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. actin filament depolymerization Source: UniProtKB
  2. negative regulation of apoptotic process Source: UniProtKB
  3. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  4. negative regulation of protein phosphorylation Source: UniProtKB
  5. oxidation-reduction process Source: UniProtKB
  6. 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 MICAL1 (EC:1.14.13.-)
Alternative name(s):
Molecule interacting with CasL protein 1
Short name:
MICAL-1
Short name:
mMical1
NEDD9-interacting protein with calponin homology and LIM domains
Gene namesi
Name:Mical1
Synonyms:Mical, Nical
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:2385847. Mical1.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10481048Protein-methionine sulfoxide oxidase MICAL1PRO_0000075843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei616 – 6161PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VDP3.
PaxDbiQ8VDP3.
PRIDEiQ8VDP3.

PTM databases

PhosphoSiteiQ8VDP3.

Expressioni

Gene expression databases

BgeeiQ8VDP3.
ExpressionAtlasiQ8VDP3. baseline and differential.
GenevestigatoriQ8VDP3.

Interactioni

Subunit structurei

Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B (By similarity). Interacts with STK38 and STK38L. Interacts with RAB8A.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Stk38Q91VJ49EBI-4394891,EBI-2527046
Stk38lA4GW502EBI-4394891,EBI-4404035From a different organism.

Protein-protein interaction databases

IntActiQ8VDP3. 4 interactions.
STRINGi10090.ENSMUSP00000019967.

Structurei

Secondary structure

1
1048
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911Combined sources
Helixi23 – 3715Combined sources
Helixi44 – 5310Combined sources
Turni58 – 603Combined sources
Helixi61 – 7111Combined sources
Helixi74 – 796Combined sources
Turni80 – 845Combined sources
Beta strandi86 – 905Combined sources
Helixi94 – 10512Combined sources
Beta strandi109 – 1157Combined sources
Beta strandi124 – 1263Combined sources
Helixi129 – 1368Combined sources
Turni137 – 1393Combined sources
Helixi140 – 1434Combined sources
Turni145 – 1484Combined sources
Beta strandi154 – 1563Combined sources
Helixi157 – 17014Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi194 – 2007Combined sources
Helixi204 – 2074Combined sources
Beta strandi211 – 2166Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi238 – 2458Combined sources
Helixi250 – 2534Combined sources
Turni263 – 2664Combined sources
Helixi269 – 2779Combined sources
Beta strandi281 – 29818Combined sources
Helixi300 – 3056Combined sources
Beta strandi308 – 3114Combined sources
Helixi316 – 3194Combined sources
Turni322 – 3243Combined sources
Helixi327 – 34115Combined sources
Turni342 – 3465Combined sources
Beta strandi357 – 3593Combined sources
Beta strandi361 – 3655Combined sources
Beta strandi367 – 3737Combined sources
Beta strandi375 – 3817Combined sources
Beta strandi384 – 3907Combined sources
Helixi392 – 3943Combined sources
Helixi400 – 4023Combined sources
Helixi405 – 42420Combined sources
Helixi429 – 44012Combined sources
Helixi441 – 4455Combined sources
Turni448 – 4503Combined sources
Helixi455 – 4573Combined sources
Helixi462 – 4643Combined sources
Beta strandi466 – 4683Combined sources
Helixi476 – 4827Combined sources
Beta strandi483 – 4853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BRAX-ray2.00A/B1-484[»]
2BRYX-ray1.45A/B1-489[»]
2C4CX-ray2.90A/B1-489[»]
ProteinModelPortaliQ8VDP3.
SMRiQ8VDP3. Positions 7-489, 506-612, 673-741.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VDP3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini507 – 608102CHPROSITE-ProRule annotationAdd
BLAST
Domaini681 – 74363LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili847 – 86721Sequence AnalysisAdd
BLAST
Coiled coili906 – 94944Sequence AnalysisAdd
BLAST
Coiled coili974 – 103158Sequence 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.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000047263.
HOVERGENiHBG052474.
InParanoidiQ8VDP3.
OMAiKQCLLRL.
OrthoDBiEOG769ZHM.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8VDP3-1) [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
MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK
60 70 80 90 100
IKAQLNYWSA KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA
110 120 130 140 150
VELALLGARV VLVEKRIKFS RHNVLHLWPF TIHDLRALGA KKFYGRFCTG
160 170 180 190 200
TLDHISIRQL QLLLLKVALL LGVEIHWGVK FTGLQPPPRK GSGWRAQLQP
210 220 230 240 250
NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI TANFVNGRTV
260 270 280 290 300
EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK
310 320 330 340 350
QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE
360 370 380 390 400
FAQDARGRPD VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW
410 420 430 440 450
PLGTGVARGF LAAFDAAWMV KRWAEGAGPL EVLAERESLY QLLSQTSPEN
460 470 480 490 500
MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ DLYDMMDKEH AQRKSDEPDS
510 520 530 540 550
RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL ALCALVHHLQ
560 570 580 590 600
PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI
610 620 630 640 650
AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE
660 670 680 690 700
TPSTEEPPVS EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG
710 720 730 740 750
HFFHRSCFCC HTCEATLWPG GYGQHPGDGH FYCLQHLPQE DQKEADNNGS
760 770 780 790 800
LESQELPTPG DSNMQPDPSS PPVTRVSPVP SPSQPARRLI RLSSLERLRL
810 820 830 840 850
SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV QAPQVPEAIE
860 870 880 890 900
KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL
910 920 930 940 950
MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP
960 970 980 990 1000
EQQKKLWLDQ LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG
1010 1020 1030 1040
YMNREETMKT EADLQSENQV LRKLLEVVNQ RDALIQFQEE RRLREMPA
Length:1,048
Mass (Da):116,785
Last modified:March 1, 2002 - v1
Checksum:iC31A392A4AE222FC
GO
Isoform 2 (identifier: Q8VDP3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-159: Missing.

Show »
Length:975
Mass (Da):108,692
Checksum:iB2D2BF964B034CBC
GO
Isoform 3 (identifier: Q8VDP3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     192-192: S → D

Show »
Length:1,048
Mass (Da):116,813
Checksum:iAF50CC8B1FBBBAE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti871 – 8711P → H in BAE35027. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei87 – 15973Missing in isoform 2. 1 PublicationVSP_042591Add
BLAST
Alternative sequencei192 – 1921S → D in isoform 3. CuratedVSP_042592

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159369 mRNA. Translation: BAE35027.1.
AK170881 mRNA. Translation: BAE42090.1.
AK171234 mRNA. Translation: BAE42330.1.
AK171411 mRNA. Translation: BAE42437.1.
AK171429 mRNA. Translation: BAE42447.1.
AK171479 mRNA. Translation: BAE42481.1.
AC153360 Genomic DNA. No translation available.
BC021477 mRNA. Translation: AAH21477.1.
BC034682 mRNA. Translation: AAH34682.1.
CCDSiCCDS35888.1. [Q8VDP3-1]
CCDS48547.1. [Q8VDP3-2]
RefSeqiNP_001157905.1. NM_001164433.1. [Q8VDP3-2]
NP_612188.1. NM_138315.2. [Q8VDP3-1]
UniGeneiMm.290431.

Genome annotation databases

EnsembliENSMUST00000019967; ENSMUSP00000019967; ENSMUSG00000019823. [Q8VDP3-1]
ENSMUST00000099934; ENSMUSP00000097519; ENSMUSG00000019823. [Q8VDP3-2]
ENSMUST00000119962; ENSMUSP00000113783; ENSMUSG00000019823. [Q8VDP3-3]
GeneIDi171580.
KEGGimmu:171580.
UCSCiuc007exn.2. mouse. [Q8VDP3-1]
uc007exp.2. mouse. [Q8VDP3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159369 mRNA. Translation: BAE35027.1 .
AK170881 mRNA. Translation: BAE42090.1 .
AK171234 mRNA. Translation: BAE42330.1 .
AK171411 mRNA. Translation: BAE42437.1 .
AK171429 mRNA. Translation: BAE42447.1 .
AK171479 mRNA. Translation: BAE42481.1 .
AC153360 Genomic DNA. No translation available.
BC021477 mRNA. Translation: AAH21477.1 .
BC034682 mRNA. Translation: AAH34682.1 .
CCDSi CCDS35888.1. [Q8VDP3-1 ]
CCDS48547.1. [Q8VDP3-2 ]
RefSeqi NP_001157905.1. NM_001164433.1. [Q8VDP3-2 ]
NP_612188.1. NM_138315.2. [Q8VDP3-1 ]
UniGenei Mm.290431.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BRA X-ray 2.00 A/B 1-484 [» ]
2BRY X-ray 1.45 A/B 1-489 [» ]
2C4C X-ray 2.90 A/B 1-489 [» ]
ProteinModelPortali Q8VDP3.
SMRi Q8VDP3. Positions 7-489, 506-612, 673-741.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8VDP3. 4 interactions.
STRINGi 10090.ENSMUSP00000019967.

PTM databases

PhosphoSitei Q8VDP3.

Proteomic databases

MaxQBi Q8VDP3.
PaxDbi Q8VDP3.
PRIDEi Q8VDP3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000019967 ; ENSMUSP00000019967 ; ENSMUSG00000019823 . [Q8VDP3-1 ]
ENSMUST00000099934 ; ENSMUSP00000097519 ; ENSMUSG00000019823 . [Q8VDP3-2 ]
ENSMUST00000119962 ; ENSMUSP00000113783 ; ENSMUSG00000019823 . [Q8VDP3-3 ]
GeneIDi 171580.
KEGGi mmu:171580.
UCSCi uc007exn.2. mouse. [Q8VDP3-1 ]
uc007exp.2. mouse. [Q8VDP3-2 ]

Organism-specific databases

CTDi 64780.
MGIi MGI:2385847. Mical1.

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000118856.
HOGENOMi HOG000047263.
HOVERGENi HBG052474.
InParanoidi Q8VDP3.
OMAi KQCLLRL.
OrthoDBi EOG769ZHM.
TreeFami TF324129.

Miscellaneous databases

ChiTaRSi Mical1. mouse.
EvolutionaryTracei Q8VDP3.
NextBioi 371076.
PROi Q8VDP3.
SOURCEi Search...

Gene expression databases

Bgeei Q8VDP3.
ExpressionAtlasi Q8VDP3. baseline and differential.
Genevestigatori Q8VDP3.

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

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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: Mammary tumor.
  4. "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions."
    Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.
    Mol. Biol. Cell 19:971-983(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB8A.
  5. Cited for: FUNCTION, INTERACTION WITH STK38 AND STK38L.
  6. "MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
    Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
    Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  7. "High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule."
    Siebold C., Berrow N., Walter T.S., Harlos K., Owens R.J., Stuart D.I., Terman J.R., Kolodkin A.L., Pasterkamp R.J., Jones E.Y.
    Proc. Natl. Acad. Sci. U.S.A. 102:16836-16841(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-489 IN COMPLEX WITH FAD.

Entry informationi

Entry nameiMICA1_MOUSE
AccessioniPrimary (citable) accession number: Q8VDP3
Secondary accession number(s): D3Z4C6
, E9PXR1, Q3TB77, Q3TBH9, Q3TX89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2002
Last modified: November 26, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3