Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8TDZ2 (MICA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MICAL1
Synonyms:MICAL, NICAL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1067 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.14

Catalytic activity

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

Cofactor

FAD. Ref.14

Subunit structure

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. Ref.1 Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton Ref.1 Ref.9 Ref.10.

Tissue specificity

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

Domain

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

Sequence similarities

Belongs to the Mical family.

Contains 1 CH (calponin-homology) domain.

Contains 1 LIM zinc-binding domain.

Biophysicochemical properties

Kinetic parameters:

KM=4.7 µM for F-actin (at saturing NADPH concentration) Ref.14

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
LIM domain
   LigandActin-binding
FAD
Flavoprotein
Metal-binding
NADP
Zinc
   Molecular functionMonooxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament depolymerization

Inferred from direct assay Ref.14. Source: UniProtKB

cytoskeleton organization

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Inferred from direct assay Ref.14. Source: UniProtKB

signal transduction

Non-traceable author statement Ref.1. Source: UniProtKB

sulfur oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

intermediate filament

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionFAD binding

Inferred from direct assay Ref.14. Source: UniProtKB

SH3 domain binding

Inferred from physical interaction Ref.1. Source: UniProtKB

actin binding

Inferred from direct assay Ref.14. Source: UniProtKB

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

Inferred from direct assay Ref.14. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TDZ2-1)

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.
Isoform 2 (identifier: Q8TDZ2-2)

Also known as: MICAL-1b;

The sequence of this isoform differs from the canonical sequence as follows:
     312-397: Missing.
Isoform 3 (identifier: Q8TDZ2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-735: Missing.
     736-768: YEQHPGDGHFYCLQHLPQTDHKAEGSDRGPESP → MPRLTFAPKGWPHPPTSLHPGQVTDQTTWWLFQ
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8TDZ2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSCLSHSSLPSCCPPQEASM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10671067Protein-methionine sulfoxide oxidase MICAL1
PRO_0000075842

Regions

Domain508 – 609102CH
Domain695 – 75763LIM zinc-binding
Nucleotide binding95 – 12329FAD By similarity
Region1 – 489489Monooxygenase domain By similarity
Coiled coil646 – 66621 Potential
Coiled coil919 – 96244 Potential
Coiled coil999 – 102729 Potential

Sites

Binding site951FAD By similarity
Binding site1141FAD By similarity
Binding site1161FAD By similarity
Binding site1211FAD By similarity
Binding site1231FAD By similarity
Binding site3931FAD By similarity

Amino acid modifications

Modified residue6171Phosphoserine Ref.13
Modified residue8721Phosphoserine Ref.11 Ref.16
Modified residue8751Phosphoserine Ref.13 Ref.16
Modified residue8761Phosphoserine Ref.13 Ref.16

Natural variations

Alternative sequence1 – 735735Missing in isoform 3.
VSP_009637
Alternative sequence11M → MSCLSHSSLPSCCPPQEASM in isoform 4.
VSP_042590
Alternative sequence312 – 39786Missing in isoform 2.
VSP_009639
Alternative sequence736 – 76833YEQHP…GPESP → MPRLTFAPKGWPHPPTSLHP GQVTDQTTWWLFQ in isoform 3.
VSP_009638
Natural variant121A → S.
Corresponds to variant rs4946977 [ dbSNP | Ensembl ].
VAR_067063
Natural variant121A → T.
Corresponds to variant rs4946977 [ dbSNP | Ensembl ].
VAR_050153
Natural variant1531D → A.
Corresponds to variant rs34726911 [ dbSNP | Ensembl ].
VAR_050154
Natural variant1951R → H.
Corresponds to variant rs34699467 [ dbSNP | Ensembl ].
VAR_067064
Natural variant3091L → M in a breast cancer sample; somatic mutation. Ref.20
VAR_036191
Natural variant4531R → C. Ref.6
Corresponds to variant rs17854785 [ dbSNP | Ensembl ].
VAR_067065
Natural variant6241A → T. Ref.6
Corresponds to variant rs17850590 [ dbSNP | Ensembl ].
VAR_067066
Natural variant7581A → E.
Corresponds to variant rs9320288 [ dbSNP | Ensembl ].
VAR_017903
Natural variant7581A → K Requires 2 nucleotide substitutions. Ref.1 Ref.3 Ref.6
Corresponds to variant rs35260632 [ dbSNP | Ensembl ].
VAR_067067
Natural variant7581A → S.
Corresponds to variant rs59056467 [ dbSNP | Ensembl ].
VAR_067068
Natural variant7581A → T.
Corresponds to variant rs59056467 [ dbSNP | Ensembl ].
VAR_061355

Experimental info

Sequence conflict7671S → C in BAB15124. Ref.3
Sequence conflict8161L → S in BAH12301. Ref.3
Sequence conflict8771E → V in BAH12301. Ref.3
Sequence conflict8871S → L in CAB59266. Ref.7
Sequence conflict9811K → N in BAB13949. Ref.3

Secondary structure

............................... 1067
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MICAL-1a) [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: 78C1BBF3E3CCD56B

FASTA1,067117,875
        10         20         30         40         50         60 
MASPTSTNPA HAHFESFLQA QLCQDVLSSF QELCGALGLE PGGGLPQYHK IKDQLNYWSA 

        70         80         90        100        110        120 
KSLWTKLDKR AGQPVYQQGR ACTSTKCLVV GAGPCGLRVA VELALLGARV VLVEKRTKFS 

       130        140        150        160        170        180 
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVT 

       190        200        210        220        230        240 
FTGLQPPPRK GSGWRAQLQP NPPAQLANYE FDVLISAAGG KFVPEGFKVR EMRGKLAIGI 

       250        260        270        280        290        300 
TANFVNGRTV EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK 

       310        320        330        340        350        360 
QCLLRLGVLR QDWPDTNRLL GSANVVPEAL QRFTRAAADF ATHGKLGKLE FAQDAHGQPD 

       370        380        390        400        410        420 
VSAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV 

       430        440        450        460        470        480 
KRWAEGAESL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVR 

       490        500        510        520        530        540 
DLYDVLAKEP VQRNNDKTDT GMPATGSAGT QEELLRWCQE QTAGYPGVHV SDLSSSWADG 

       550        560        570        580        590        600 
LALCALVYRL QPGLLEPSEL QGLGALEATA WALKVAENEL GITPVVSAQA VVAGSDPLGL 

       610        620        630        640        650        660 
IAYLSHFHSA FKSMAHSPGP VSQASPGTSS AVLFLSKLQR TLQRSRAKEN AEDAGGKKLR 

       670        680        690        700        710        720 
LEMEAETPST EVPPDPEPGV PLTPPSQHQE AGAGDLCALC GEHLYVLERL CVNGHFFHRS 

       730        740        750        760        770        780 
CFRCHTCEAT LWPGGYEQHP GDGHFYCLQH LPQTDHKAEG SDRGPESPEL PTPSENSMPP 

       790        800        810        820        830        840 
GLSTPTASQE GAGPVPDPSQ PTRRQIRLSS PERQRLSSLN LTPDPEMEPP PKPPRSCSAL 

       850        860        870        880        890        900 
ARHALESSFV GWGLPVQSPQ ALVAMEKEEK ESPFSSEEEE EDVPLDSDVE QALQTFAKTS 

       910        920        930        940        950        960 
GTMNNYPTWR RTLLRRAKEE EMKRFCKAQT IQRRLNEIEA ALRELEAEGV KLELALRRQS 

       970        980        990       1000       1010       1020 
SSPEQQKKLW VGQLLQLVDK KNSLVAEEAE LMITVQELNL EEKQWQLDQE LRGYMNREEN 

      1030       1040       1050       1060 
LKTAADRQAE DQVLRKLVDL VNQRDALIRF QEERRLSELA LGTGAQG 

« Hide

Isoform 2 (MICAL-1b) [UniParc].

Checksum: 8EC7E9C12989C1E9
Show »

FASTA981108,552
Isoform 3 [UniParc].

Checksum: 7FF1E955AE2204DB
Show »

FASTA33237,715
Isoform 4 [UniParc].

Checksum: 947094500071E091
Show »

FASTA1,086119,821

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"MICAL-1 isoforms, novel rab1 interacting proteins."
Weide T., Teuber J., Bayer M., Barnekow A.
Biochem. Biophys. Res. Commun. 306:79-86(2003) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"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.
[18]"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.
[19]"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.
[20]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-309.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT34532.
RefSeqNP_001152763.1. NM_001159291.1.
NP_001273542.1. NM_001286613.1.
NP_073602.3. NM_022765.3.
UniGeneHs.33476.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYLNMR-A510-612[»]
2CO8NMR-A687-755[»]
2DK9NMR-A506-614[»]
ProteinModelPortalQ8TDZ2.
SMRQ8TDZ2. Positions 8-484, 506-614, 687-755.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122290. 15 interactions.
IntActQ8TDZ2. 7 interactions.
MINTMINT-1343875.
STRING9606.ENSP00000351664.

PTM databases

PhosphoSiteQ8TDZ2.

Polymorphism databases

DMDM45593495.

Proteomic databases

PaxDbQ8TDZ2.
PRIDEQ8TDZ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358577; ENSP00000351385; ENSG00000135596. [Q8TDZ2-2]
ENST00000358807; ENSP00000351664; ENSG00000135596. [Q8TDZ2-1]
ENST00000368952; ENSP00000357948; ENSG00000135596. [Q8TDZ2-4]
GeneID64780.
KEGGhsa:64780.
UCSCuc003ptj.3. human. [Q8TDZ2-1]
uc010kdr.3. human. [Q8TDZ2-2]
uc011eaq.2. human. [Q8TDZ2-4]

Organism-specific databases

CTD64780.
GeneCardsGC06M109766.
HGNCHGNC:20619. MICAL1.
HPAHPA030178.
MIM607129. gene.
neXtProtNX_Q8TDZ2.
PharmGKBPA134900249.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000047263.
HOVERGENHBG052474.
InParanoidQ8TDZ2.
OMAKQCLLRL.
OrthoDBEOG769ZHM.
PhylomeDBQ8TDZ2.
TreeFamTF324129.

Enzyme and pathway databases

SignaLinkQ8TDZ2.

Gene expression databases

ArrayExpressQ8TDZ2.
BgeeQ8TDZ2.
CleanExHS_MICAL1.
GenevestigatorQ8TDZ2.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProIPR001715. CH-domain.
IPR022735. DUF3585.
IPR002938. mOase_FAD-bd.
IPR001781. Znf_LIM.
[Graphical view]
PfamPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF01494. FAD_binding_3. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view]
SMARTSM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMICAL1. human.
EvolutionaryTraceQ8TDZ2.
GeneWikiMICAL1.
GenomeRNAi64780.
NextBio66810.
PROQ8TDZ2.
SOURCESearch...

Entry information

Entry nameMICA1_HUMAN
AccessionPrimary (citable) accession number: Q8TDZ2
Secondary accession number(s): B7Z3R5 expand/collapse secondary AC list , E1P5F0, Q7Z633, Q8IVS9, Q96G47, Q9H6X6, Q9H7I0, Q9HAA1, Q9UFF7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: March 15, 2004
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM