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Q3TYD6 (LMTK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase LMTK2

EC=2.7.11.1
Alternative name(s):
Brain-enriched kinase
Lemur tyrosine kinase 2
Gene names
Name:Lmtk2
Synonyms:Brek, Kiaa1079
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates PPP1C, phosphorylase b and CFTR By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with PPP1C and inhibitor-2 By similarity.

Subcellular location

Membrane By similarity; Multi-pass membrane protein.

Tissue specificity

Mainly expressed in brain, especially in the olfactory bulb, olfactory tubercle, hippocampus, striatum, cerebellum and cerebral cortex. Weakly expressed in skeletal muscle and not expressed in liver. Ref.5

Developmental stage

Expression observed during all tested stages from embryonic day 18 (E18) to postnatal week 6, but it was especially high during the early postnatal stage (postnatal weeks 0-2). Ref.5

Post-translational modification

Autophosphorylated. Phosphorylated By similarity. Ref.5

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from sequence alignment Ref.5. Source: MGI

early endosome to late endosome transport

Inferred from electronic annotation. Source: Ensembl

endocytic recycling

Inferred from electronic annotation. Source: Ensembl

negative regulation of catalytic activity

Inferred from electronic annotation. Source: GOC

neurotrophin TRK receptor signaling pathway

Inferred from sequence alignment Ref.5. Source: MGI

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: GOC

protein autophosphorylation

Inferred from sequence alignment Ref.5. Source: MGI

receptor recycling

Inferred from electronic annotation. Source: Ensembl

transferrin transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence alignment Ref.5. Source: MGI

early endosome

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

recycling endosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein phosphatase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

protein serine/threonine kinase activity

Inferred from sequence alignment Ref.5. Source: MGI

protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14711471Serine/threonine-protein kinase LMTK2
PRO_0000259459

Regions

Topological domain1 – 1010Cytoplasmic Potential
Transmembrane11 – 3121Helical; Potential
Topological domain32 – 4110Lumenal Potential
Transmembrane42 – 6221Helical; Potential
Topological domain63 – 14711409Cytoplasmic Potential
Domain136 – 406271Protein kinase
Nucleotide binding142 – 1509ATP By similarity

Sites

Active site2641Proton acceptor By similarity
Binding site1671ATP By similarity

Amino acid modifications

Modified residue7811Phosphoserine Ref.6
Modified residue7831Phosphothreonine Ref.6

Experimental info

Sequence conflict4211F → L in BAE34627. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3TYD6 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 13C0C905F585D23F

FASTA1,471160,508
        10         20         30         40         50         60 
MPGPPASPPP PMLLLLLLLT VGCARAAPLP QTGAGEVPVV EVPSLFVILS VCSLLILIVL 

        70         80         90        100        110        120 
IANCVSCCKD PEIDFKEFED NFDDEIDFTP PAEDTPSIQS PAEVFTLSVP NISLPAPSQF 

       130        140        150        160        170        180 
QASVEGLKSQ VARHSLNYIQ EIGSGWFGKV LLGETYTGTS VARVIVKELK VSASPKEQDT 

       190        200        210        220        230        240 
FLKSGEPYYI LQHPNVLQCV GQCVEAIPYL LVFEFCDLGD LKAYLHNEQE HVRGDSQTML 

       250        260        270        280        290        300 
LQRMACEIAA GLAAMHKLHF LHSDLALRNC YLTSDLNVKV GDYGIGFSRY KEDYIETDDK 

       310        320        330        340        350        360 
KVFPLRWTAP ELVTSFQDRL LTADQTKYSN IWSLGVTLWE LFNNAAQPYA NLSDLDVLNQ 

       370        380        390        400        410        420 
VIRERDMKLP KPQLEQPYSD RWYEVLQFCW LPPDKRPAAE DVHRLLTYLR MQSQRDSEVD 

       430        440        450        460        470        480 
FEQQWTALKP DTNSRDASSS AAFPILDHFA RDRLGREMEE VLTVTETSQG LSFEYVWEAA 

       490        500        510        520        530        540 
KHDHFDEQGR GHPDEALSYS SMFFPVEVFE NSLSDPGPGK QDDSGQEVPV RAPGVVPVFD 

       550        560        570        580        590        600 
AHNLSVGSDY YIQLEEKSSS NLGLDPPALL TTEVDKLERA GAEEPRTEED FFQSSAHPKE 

       610        620        630        640        650        660 
ASSTEDSRAT SIPGSPFNLF SDLDKADDLP SHQKIFDLME LNGVQADFKP AILSSSLDDP 

       670        680        690        700        710        720 
KDTCQSDKEK PHKLLDQGPL CLSESLLHQD HFDPLSVQEL SENFLFLQEK NLLKGSLTTK 

       730        740        750        760        770        780 
EQVSDLQTEL KNAGFTSALL ESPQRGSESS ELEFLENTLD FPLSQGDTRG QNEGAGVRRH 

       790        800        810        820        830        840 
SGTSPQASPA LLTEEGSPTA PTDPILKPEE TKSFRDVRVP EDSICLELGP DPVTVGVEIP 

       850        860        870        880        890        900 
ATDAKTLDGG NRPPDVTCQS KEALSLTNRH PILVNDITAQ GSVESCLPES RQDLQNEPFS 

       910        920        930        940        950        960 
EDPLSVSSLE KHSEAAETLN QLNSKAAPED AALASALSSD STSQDSLLED SLSTPIPTSE 

       970        980        990       1000       1010       1020 
QSVETPDSLD SVDVREALLE SLGSHTPRKL LPPDKPADSG YETENLESPE WTLHPAPEGT 

      1030       1040       1050       1060       1070       1080 
ADSDAAAAGD SGHSSLPPNP VIVISDAGDG HRGAEGPPQS FTLGPQSSYR DSAYFSDNDS 

      1090       1100       1110       1120       1130       1140 
EPDKKPEEVP GTSANALVLV KGQSPPESVV PEESSDVREG CLEAPQDKPD QSRVSTLQNS 

      1150       1160       1170       1180       1190       1200 
CHSELQETLQ PTPADASRES CPVNDEASSP LSLLNSEPSS CDDLDTQEDR PCTLASTGTN 

      1210       1220       1230       1240       1250       1260 
TNELLAYMSS TLDKSLPSHL ESSKLKEPDI EGKYLGKLCV SGMLDLSEDG MDADEEDENS 

      1270       1280       1290       1300       1310       1320 
DDSDEDLRAF NLHSLSSESE DDTEHPVPII VSNDDGRHLR SLLKPSAAEA IEQLPEDWKK 

      1330       1340       1350       1360       1370       1380 
EKKAVTFFDD VTVYLFDQET PTKELGHCGG EAHGPGPSSP AASSSSPYLG RCMNSESSTD 

      1390       1400       1410       1420       1430       1440 
EEGGGFEWDD DFSPDPFMSK TTSLLGSKPS LQTSKYFSPP PPARSAEQSW PHVSPCSRFS 

      1450       1460       1470 
ISPANIASFS LTHLTDSDIE QGGSSEDGDK D 

« Hide

References

« Hide 'large scale' references
[1]"Structural and functional analysis of the apoptosis-associated tyrosine kinase (AATYK) family."
Tomomura M., Morita N., Yoshikawa F., Konishi A., Akiyama H., Furuichi T., Kamiguchi H.
Neuroscience 148:510-521(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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] OF 1-632 AND 1263-1471.
Strain: C57BL/6J.
Tissue: Spinal cord and Visual cortex.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 410-1471.
Tissue: Brain.
[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] OF 1253-1471.
Strain: C57BL/6.
Tissue: Brain.
[5]"Involvement of BREK, a serine/threonine kinase enriched in brain, in NGF signalling."
Kawa S., Fujimoto J., Tezuka T., Nakazawa T., Yamamoto T.
Genes Cells 9:219-232(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, CHARACTERIZATION, DEVELOPMENTAL STAGE.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781 AND THR-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB288872 mRNA. Translation: BAF64833.1.
AK039738 mRNA. Translation: BAC30433.1.
AK158724 mRNA. Translation: BAE34627.1.
AK129279 mRNA. Translation: BAC98089.2.
BC058653 mRNA. Translation: AAH58653.1.
RefSeqNP_001074578.1. NM_001081109.1.
UniGeneMm.288726.

3D structure databases

ProteinModelPortalQ3TYD6.
SMRQ3TYD6. Positions 136-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ3TYD6. 1 interaction.

PTM databases

PhosphoSiteQ3TYD6.

Proteomic databases

PaxDbQ3TYD6.
PRIDEQ3TYD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041804; ENSMUSP00000048238; ENSMUSG00000038970.
GeneID231876.
KEGGmmu:231876.
UCSCuc009alg.1. mouse.

Organism-specific databases

CTD22853.
MGIMGI:3036247. Lmtk2.
RougeSearch...

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00640000091449.
HOGENOMHOG000252999.
HOVERGENHBG081920.
InParanoidA6BLY9.
KOK08898.
OMANLESPEW.
OrthoDBEOG7HTHG4.
TreeFamTF332280.

Gene expression databases

BgeeQ3TYD6.
CleanExMM_LMTK2.
GenevestigatorQ3TYD6.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio380841.
PROQ3TYD6.
SOURCESearch...

Entry information

Entry nameLMTK2_MOUSE
AccessionPrimary (citable) accession number: Q3TYD6
Secondary accession number(s): A6BLY9 expand/collapse secondary AC list , Q6PDK6, Q6ZPY9, Q8CA34
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot