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Q7RTP6 (MICA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. 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 MICAL3

EC=1.14.13.-
Alternative name(s):
Molecule interacting with CasL protein 3
Short name=MICAL-3
Gene names
Name:MICAL3
Synonyms:KIAA0819, KIAA1364
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2002 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 By similarity. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process. Ref.12

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Interacts with RAB1B. Interacts with ERC1 and RAB8A. Ref.7 Ref.12

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton Ref.7.

Tissue specificity

Ubiquitous. Ref.7

Sequence similarities

Belongs to the Mical family.

Contains 1 CH (calponin-homology) domain.

Contains 1 LIM zinc-binding domain.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q7RTP6-1)

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: Q7RTP6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     934-948: SSSESEMEEEGEEEE → RSARRAAGRPPATRP
     949-2002: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q7RTP6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     746-746: R → RQLTQERGASQPSCCLPGQVRPAPTPRWK
     934-948: SSSESEMEEEGEEEE → RSARRAAGRPPATRP
     949-2002: Missing.
Isoform 4 (identifier: Q7RTP6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     934-966: SSSESEMEEEGEEEEEEPRLPPSDLGGVPWKEA → RDWVSPWLPRMVSNSWAQMIHPPQPPTVLGSQM
     967-2002: Missing.
Isoform 5 (identifier: Q7RTP6-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20022002Protein-methionine sulfoxide oxidase MICAL3
PRO_0000075846

Regions

Domain518 – 621104CH
Domain762 – 82463LIM zinc-binding
Nucleotide binding88 – 11730FAD Potential
Nucleotide binding97 – 12529FAD By similarity
Region2 – 494493Monooxygenase domain By similarity
Coiled coil1821 – 1992172 Potential
Compositional bias688 – 6914Poly-Glu
Compositional bias889 – 1138250Glu-rich
Compositional bias1141 – 1505365Pro-rich

Sites

Binding site971FAD By similarity
Binding site1161FAD By similarity
Binding site1181FAD By similarity
Binding site1231FAD By similarity
Binding site1251FAD By similarity
Binding site3981FAD By similarity

Amino acid modifications

Modified residue6491Phosphoserine Ref.9 Ref.11
Modified residue8871Phosphothreonine Ref.9
Modified residue13101Phosphoserine Ref.8 Ref.10
Modified residue13371Phosphoserine Ref.11
Modified residue13411Phosphothreonine Ref.11
Modified residue13711Phosphoserine Ref.9 Ref.13
Modified residue13841Phosphoserine Ref.9
Modified residue14541Phosphothreonine Ref.10

Natural variations

Alternative sequence7461R → RQLTQERGASQPSCCLPGQV RPAPTPRWK in isoform 3.
VSP_039485
Alternative sequence7471Q → QQREKECSRTCPKKVITLSP PPTPPPCRAHGGQQTYRDLD ADNRGKQSPHHERPEPEPPR RFFVDQWELSLSLRSSARPA SPSSDSLRQKYIKMYTGGVS SLAEQIANQLQRKEQPKALL DKKEL in isoform 5.
VSP_042600
Alternative sequence871 – 94979GVNGL…EEEEE → LTSLFGWVARHSLGLCDKAK GMSQHLQSNISSFGQQVAQN PLDSFFMCQLLAFGVPFLYG LSEVLVQIRGEFHWQAVAQ in isoform 5.
VSP_042601
Alternative sequence934 – 96633SSSES…PWKEA → RDWVSPWLPRMVSNSWAQMI HPPQPPTVLGSQM in isoform 4.
VSP_039486
Alternative sequence934 – 94815SSSES…GEEEE → RSARRAAGRPPATRP in isoform 2 and isoform 3.
VSP_039487
Alternative sequence949 – 20021054Missing in isoform 2 and isoform 3.
VSP_039488
Alternative sequence950 – 20021053Missing in isoform 5.
VSP_042602
Alternative sequence967 – 20021036Missing in isoform 4.
VSP_039489
Natural variant111P → A.
Corresponds to variant rs11913706 [ dbSNP | Ensembl ].
VAR_059451
Natural variant7451R → Q.
Corresponds to variant rs2289719 [ dbSNP | Ensembl ].
VAR_059452
Natural variant7501M → L.
Corresponds to variant rs5992128 [ dbSNP | Ensembl ].
VAR_018263

Experimental info

Mutagenesis93 – 986GAGPCG → WAWPCW: Abolishes Monooxygenase activity and impairs ability to control docking and fusion of exocytic carriers. Ref.12
Sequence conflict4141G → D in BX647382. Ref.2
Sequence conflict12451Q → R in BAA74842. Ref.5
Sequence conflict17171E → V in AAH06562. Ref.4
Isoform 4:
Sequence conflict9571Q → R in BX647382. Ref.2

Secondary structure

..................... 2002
Helix Strand Turn

Details...

Sequences

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

Last modified July 13, 2010. Version 2.
Checksum: F85C97FD4D647B80

FASTA2,002224,295
        10         20         30         40         50         60 
MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY HKLKSKLNYW 

        70         80         90        100        110        120 
KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA 

       130        140        150        160        170        180 
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN 

       190        200        210        220        230        240 
VEFQGLIQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK 

       250        260        270        280        290        300 
LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV 

       310        320        330        340        350        360 
MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH 

       370        380        390        400        410        420 
YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD 

       430        440        450        460        470        480 
SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNINVNFLR 

       490        500        510        520        530        540 
PSQVRHLYDT GETKDIHLEM ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV 

       550        560        570        580        590        600 
TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE 

       610        620        630        640        650        660 
MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP ISFLSKLGQT 

       670        680        690        700        710        720 
ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER PTLVSTLTDR RMDVAVGNQN 

       730        740        750        760        770        780 
KVKYMATQLL AKFEENAPAQ SIGIRRQGSM KKEFPQNLGG SDTCYFCQKR VYVMERLSAE 

       790        800        810        820        830        840 
GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE 

       850        860        870        880        890        900 
AKGPLQDGAT TDANGRANAV ASSTERTPGS GVNGLEEPSI AKRLRGTPER IELENYRLSL 

       910        920        930        940        950        960 
RQAEALQEVP EETQAEHNLS SVLDTGAEED VASSSSESEM EEEGEEEEEE PRLPPSDLGG 

       970        980        990       1000       1010       1020 
VPWKEAVRIH ALLKGKSEEE LEASKSFGPG NEEEEEEEEE YEEEEEEDYD EEEEESSEAG 

      1030       1040       1050       1060       1070       1080 
NQRLQQVMHA ADPLEIQADV HWTHIREREE EERMAPASES SASGAPLDEN DLEEDVDSEP 

      1090       1100       1110       1120       1130       1140 
AEIEGEAAED GDPGDTGAEL DDDQHWSDSP SDADRELRLP CPAEGEAELE LRVSEDEEKL 

      1150       1160       1170       1180       1190       1200 
PASPKHQERG PSQATSPIRS PQESALLFIP VHSPSTEGPQ LPPVPAATQE KSPEERLFPE 

      1210       1220       1230       1240       1250       1260 
PLLPKEKPKA DAPSDLKAVH SPIRSQPVTL PEARTPVSPG SPQPQPPVAA STPPPSPLPI 

      1270       1280       1290       1300       1310       1320 
CSQPQPSTEA TVPSPTQSPI RFQPAPAKTS TPLAPLPVQS QSDTKDRLGS PLAVDEALRR 

      1330       1340       1350       1360       1370       1380 
SDLVEEFWMK SAEIRRSLGL TPVDRSKGPE PSFPTPAFRP VSLKSYSVEK SPQDEGLHLL 

      1390       1400       1410       1420       1430       1440 
KPLSIPKRLG LPKPEGEPLS LPTPRSPSDR ELRSAQEERR ELSSSSGLGL HGSSSNMKTL 

      1450       1460       1470       1480       1490       1500 
GSQSFNTSDS AMLTPPSSPP PPPPPGEEPA TLRRKLREAE PNASVVPPPL PATWMRPPRE 

      1510       1520       1530       1540       1550       1560 
PAQPPREEVR KSFVESVEEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW PRPEKPRHPP 

      1570       1580       1590       1600       1610       1620 
LAKENGRLPA LEGTLQPQKR GLPLVSAEAK ELAEERMRAR EKSVKSQALR DAMARQLSRM 

      1630       1640       1650       1660       1670       1680 
QQMELASGAP RPRKASSAPS QGKERRPDSP TRPTLRGSEE PTLKHEATSE EVLSPPSDSG 

      1690       1700       1710       1720       1730       1740 
GPDGSFTSSE GSSGKSKKRS SLFSPRRNKK EKKSKGEGRP PEKPSSNLLE EAAAKPKSLW 

      1750       1760       1770       1780       1790       1800 
KSVFSGYKKD KKKKADDKSC PSTPSSGATV DSGKHRVLPV VRAELQLRRQ LSFSEDSDLS 

      1810       1820       1830       1840       1850       1860 
SDDVLEKSSQ KSRREPRTYT EEELNAKLTR RVQKAARRQA KQEELKRLHR AQIIQRQLQQ 

      1870       1880       1890       1900       1910       1920 
VEERQRRLEE RGVAVEKALR GEAGMGKKDD PKLMQEWFKL VQEKNAMVRY ESELMIFARE 

      1930       1940       1950       1960       1970       1980 
LELEDRQSRL QQELRERMAV EDHLKTEEEL SEEKQILNEM LEVVEQRDSL VALLEEQRLR 

      1990       2000 
EREEDKDLEA AMLSKGFSLN WS 

« Hide

Isoform 2 [UniParc].

Checksum: D50FC4EC6F46D30C
Show »

FASTA948106,837
Isoform 3 [UniParc].

Checksum: D94482577189AD04
Show »

FASTA976109,911
Isoform 4 [UniParc].

Checksum: DC1B9C83CB4D3E35
Show »

FASTA966109,047
Isoform 5 [UniParc].

Checksum: C550AC7BE7536179
Show »

FASTA1,073121,173

References

« Hide 'large scale' references
[1]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[2]"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] (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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Rab6, Rab8, and MICAL3 cooperate in controlling docking and fusion of exocytotic carriers."
Grigoriev I., Yu K.L., Martinez-Sanchez E., Serra-Marques A., Smal I., Meijering E., Demmers J., Peranen J., Pasterkamp R.J., van der Sluijs P., Hoogenraad C.C., Akhmanova A.
Curr. Biol. 21:967-974(2011) [PubMed] [Europe PMC] [Abstract]
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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001116203.1. NM_001122731.2.
NP_001129476.1. NM_001136004.3.
NP_056056.2. NM_015241.2.
XP_005261319.1. XM_005261262.1.
UniGeneHs.528024.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D88NMR-A518-625[»]
ProteinModelPortalQ7RTP6.
SMRQ7RTP6. Positions 10-489, 515-630, 762-818.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121609. 8 interactions.
IntActQ7RTP6. 3 interactions.
STRING9606.ENSP00000414846.

PTM databases

PhosphoSiteQ7RTP6.

Polymorphism databases

DMDM300669653.

Proteomic databases

PaxDbQ7RTP6.
PeptideAtlasO94909.
PRIDEQ7RTP6.

Protocols and materials databases

DNASU57553.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000207726; ENSP00000207726; ENSG00000243156. [Q7RTP6-3]
ENST00000383094; ENSP00000372574; ENSG00000243156. [Q7RTP6-2]
ENST00000400561; ENSP00000383406; ENSG00000243156. [Q7RTP6-4]
ENST00000414725; ENSP00000391827; ENSG00000243156. [Q7RTP6-3]
ENST00000429452; ENSP00000414846; ENSG00000243156. [Q7RTP6-5]
ENST00000441493; ENSP00000416015; ENSG00000243156. [Q7RTP6-1]
ENST00000444520; ENSP00000410315; ENSG00000243156. [Q7RTP6-4]
ENST00000585038; ENSP00000462033; ENSG00000243156. [Q7RTP6-5]
GeneID57553.
KEGGhsa:57553.
UCSCuc002zng.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

CTD57553.
GeneCardsGC22M018271.
H-InvDBHIX0213260.
HGNCHGNC:24694. MICAL3.
HPAHPA000639.
HPA003421.
HPA034882.
MIM608882. gene.
neXtProtNX_Q7RTP6.
PharmGKBPA142671454.
HUGESearch...
Search...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000047263.
HOVERGENHBG081827.
InParanoidO94909.
OMASTGIRRQ.
OrthoDBEOG769ZHM.
PhylomeDBQ7RTP6.
TreeFamTF324129.

Gene expression databases

ArrayExpressQ7RTP6.
BgeeQ7RTP6.
CleanExHS_MICAL3.
GenevestigatorQ7RTP6.

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.
IPR003042. Rng_hydrolase-like.
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]
PRINTSPR00420. RNGMNOXGNASE.
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

ChiTaRSMICAL3. human.
EvolutionaryTraceQ7RTP6.
GeneWikiMICAL3.
GenomeRNAi57553.
NextBio64022.
PROQ7RTP6.
SOURCESearch...

Entry information

Entry nameMICA3_HUMAN
AccessionPrimary (citable) accession number: Q7RTP6
Secondary accession number(s): B2RXJ5 expand/collapse secondary AC list , E9PEF0, O94909, Q5U4P4, Q6ICK4, Q96DF2, Q9P2I3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: July 13, 2010
Last modified: April 16, 2014
This is version 113 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 22

Human chromosome 22: entries, gene names and cross-references to MIM