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Q8TDZ2

- MICA1_HUMAN

UniProt

Q8TDZ2 - MICA1_HUMAN

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Protein

Protein-methionine sulfoxide oxidase MICAL1

Gene

MICAL1

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

Functioni

Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (Probable). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4.2 PublicationsCurated

Catalytic activityi

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

Cofactori

FAD.1 Publication

Kineticsi

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

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi95 – 12329FADBy similarityAdd
BLAST

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. FAD binding Source: UniProtKB
  3. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: UniProtKB
  4. SH3 domain binding Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

SignaLinkiQ8TDZ2.

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:20619. MICAL1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. intermediate filament Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134900249.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8TDZ2.
PaxDbiQ8TDZ2.
PRIDEiQ8TDZ2.

PTM databases

PhosphoSiteiQ8TDZ2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8TDZ2.
CleanExiHS_MICAL1.
ExpressionAtlasiQ8TDZ2. baseline and differential.
GenevestigatoriQ8TDZ2.

Organism-specific databases

HPAiHPA030178.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi122290. 17 interactions.
IntActiQ8TDZ2. 7 interactions.
MINTiMINT-1343875.
STRINGi9606.ENSP00000351664.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8TDZ2.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

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

Domaini

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

Sequence similaritiesi

Belongs to the Mical family.Curated
Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, LIM domain

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000047263.
HOVERGENiHBG052474.
InParanoidiQ8TDZ2.
OMAiKQCLLRL.
OrthoDBiEOG769ZHM.
PhylomeDBiQ8TDZ2.
TreeFamiTF324129.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR002938. mOase_FAD-bd.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF01494. FAD_binding_3. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

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

Also known as: MICAL-1a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASPTSTNPA HAHFESFLQA QLCQDVLSSF QELCGALGLE PGGGLPQYHK
60 70 80 90 100
IKDQLNYWSA KSLWTKLDKR AGQPVYQQGR ACTSTKCLVV GAGPCGLRVA
110 120 130 140 150
VELALLGARV VLVEKRTKFS RHNVLHLWPF TIHDLRALGA KKFYGRFCTG
160 170 180 190 200
TLDHISIRQL QLLLLKVALL LGVEIHWGVT FTGLQPPPRK GSGWRAQLQP
210 220 230 240 250
NPPAQLANYE FDVLISAAGG KFVPEGFKVR EMRGKLAIGI TANFVNGRTV
260 270 280 290 300
EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK
310 320 330 340 350
QCLLRLGVLR QDWPDTNRLL GSANVVPEAL QRFTRAAADF ATHGKLGKLE
360 370 380 390 400
FAQDAHGQPD VSAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW
410 420 430 440 450
PLGTGVARGF LAAFDAAWMV KRWAEGAESL EVLAERESLY QLLSQTSPEN
460 470 480 490 500
MHRNVAQYGL DPATRYPNLN LRAVTPNQVR DLYDVLAKEP VQRNNDKTDT
510 520 530 540 550
GMPATGSAGT QEELLRWCQE QTAGYPGVHV SDLSSSWADG LALCALVYRL
560 570 580 590 600
QPGLLEPSEL QGLGALEATA WALKVAENEL GITPVVSAQA VVAGSDPLGL
610 620 630 640 650
IAYLSHFHSA FKSMAHSPGP VSQASPGTSS AVLFLSKLQR TLQRSRAKEN
660 670 680 690 700
AEDAGGKKLR LEMEAETPST EVPPDPEPGV PLTPPSQHQE AGAGDLCALC
710 720 730 740 750
GEHLYVLERL CVNGHFFHRS CFRCHTCEAT LWPGGYEQHP GDGHFYCLQH
760 770 780 790 800
LPQTDHKAEG SDRGPESPEL PTPSENSMPP GLSTPTASQE GAGPVPDPSQ
810 820 830 840 850
PTRRQIRLSS PERQRLSSLN LTPDPEMEPP PKPPRSCSAL ARHALESSFV
860 870 880 890 900
GWGLPVQSPQ ALVAMEKEEK ESPFSSEEEE EDVPLDSDVE QALQTFAKTS
910 920 930 940 950
GTMNNYPTWR RTLLRRAKEE EMKRFCKAQT IQRRLNEIEA ALRELEAEGV
960 970 980 990 1000
KLELALRRQS SSPEQQKKLW VGQLLQLVDK KNSLVAEEAE LMITVQELNL
1010 1020 1030 1040 1050
EEKQWQLDQE LRGYMNREEN LKTAADRQAE DQVLRKLVDL VNQRDALIRF
1060
QEERRLSELA LGTGAQG
Length:1,067
Mass (Da):117,875
Last modified:March 15, 2004 - v2
Checksum:i78C1BBF3E3CCD56B
GO
Isoform 2 (identifier: Q8TDZ2-2) [UniParc]FASTAAdd to Basket

Also known as: MICAL-1b

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

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

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

Note: No experimental confirmation available.

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

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

Note: No experimental confirmation available.

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

Experimental Info

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

Natural variant

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

Alternative sequence

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

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi45593495.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi 122290. 17 interactions.
IntActi Q8TDZ2. 7 interactions.
MINTi MINT-1343875.
STRINGi 9606.ENSP00000351664.

PTM databases

PhosphoSitei Q8TDZ2.

Polymorphism databases

DMDMi 45593495.

Proteomic databases

MaxQBi Q8TDZ2.
PaxDbi Q8TDZ2.
PRIDEi Q8TDZ2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000118856.
HOGENOMi HOG000047263.
HOVERGENi HBG052474.
InParanoidi Q8TDZ2.
OMAi KQCLLRL.
OrthoDBi EOG769ZHM.
PhylomeDBi Q8TDZ2.
TreeFami TF324129.

Enzyme and pathway databases

SignaLinki Q8TDZ2.

Miscellaneous databases

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

Gene expression databases

Bgeei Q8TDZ2.
CleanExi HS_MICAL1.
ExpressionAtlasi Q8TDZ2. baseline and differential.
Genevestigatori Q8TDZ2.

Family and domain databases

Gene3Di 1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProi IPR001715. CH-domain.
IPR022735. DUF3585.
IPR002938. mOase_FAD-bd.
IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF01494. FAD_binding_3. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view ]
SMARTi SM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi PS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MICAL, a novel CasL interacting molecule, associates with vimentin."
    Suzuki T., Nakamoto T., Ogawa S., Seo S., Matsumura T., Tachibana K., Morimoto C., Hirai H.
    J. Biol. Chem. 277:14933-14941(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NEDD9 AND VIM, VARIANT LYS-758.
  2. "Characterization of long cDNA clones from human adult spleen."
    Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.
    DNA Res. 7:357-366(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Spleen.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), VARIANTS LYS-758 AND LYS-758.
    Tissue: Colon mucosa, Embryo, Spleen and Thalamus.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS CYS-453; THR-624 AND LYS-758.
    Tissue: Blood, Lymph and Uterus.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-1067 (ISOFORMS 1/2).
    Tissue: Testis.
  8. "MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion."
    Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.
    Cell 109:887-900(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLXNA3.
  9. Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH VIM.
  10. "The MICAL proteins and rab1: a possible link to the cytoskeleton?"
    Fischer J., Weide T., Barnekow A.
    Biochem. Biophys. Res. Commun. 328:415-423(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB1B, SUBCELLULAR LOCATION.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein."
    Schmidt E.F., Shim S.O., Strittmatter S.M.
    J. Neurosci. 28:2287-2297(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617; SER-875 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1."
    Zucchini D., Caprini G., Pasterkamp R.J., Tedeschi G., Vanoni M.A.
    Arch. Biochem. Biophys. 515:1-13(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872; SER-875 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Redox modification of nuclear actin by MICAL-2 regulates SRF signaling."
    Lundquist M.R., Storaska A.J., Liu T.C., Larsen S.D., Evans T., Neubig R.R., Jaffrey S.R.
    Cell 156:563-576(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. "Solution structure of the CH domain of human NEDD9-interacting protein with calponin homology and LIM domains."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 506-613.
  19. "Solution structure of calponin homology domain of Human MICAL-1."
    Sun H., Dai H., Zhang J., Jin X., Xiong S., Xu J., Wu J., Shi Y.
    J. Biomol. NMR 36:295-300(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 506-614.
  20. "Investigation of the four cooperative unfolding units existing in the MICAL-1 CH domain."
    Jin X., Zhang J., Dai H., Sun H., Wang D., Wu J., Shi Y.
    Biophys. Chem. 129:269-278(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 506-614.
  21. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-309.

Entry informationi

Entry nameiMICA1_HUMAN
AccessioniPrimary (citable) accession number: Q8TDZ2
Secondary accession number(s): B7Z3R5
, E1P5F0, Q7Z633, Q8IVS9, Q96G47, Q9H6X6, Q9H7I0, Q9HAA1, Q9UFF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: March 15, 2004
Last modified: October 29, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3