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Protein

Leukocyte tyrosine kinase receptor

Gene

LTK

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

Functioni

Orphan receptor with a tyrosine-protein kinase activity. The exact function of this protein is not known. Studies with chimeric proteins (replacing its extracellular region with that of several known growth factor receptors, such as EGFR and CSFIR) demonstrate its ability to promote growth and specifically neurite outgrowth, and cell survival. Signaling appears to involve the PI3 kinase pathway. Involved in regulation of the secretory pathway involving endoplasmic reticulum (ER) export sites (ERESs) and ER to Golgi transport.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei544 – 5441ATPPROSITE-ProRule annotation
Active sitei643 – 6431Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi516 – 5249ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase activity Source: UniProtKB
  3. protein tyrosine kinase activity Source: ProtInc
  4. transmembrane receptor protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. cellular response to retinoic acid Source: BHF-UCL
  3. negative regulation of apoptotic process Source: UniProtKB
  4. peptidyl-tyrosine phosphorylation Source: GOC
  5. phosphatidylinositol 3-kinase signaling Source: UniProtKB
  6. positive regulation of cardiac muscle cell apoptotic process Source: UniProtKB
  7. positive regulation of neuron projection development Source: BHF-UCL
  8. protein phosphorylation Source: UniProtKB
  9. signal transduction Source: ProtInc
  10. transmembrane receptor protein tyrosine kinase signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
SignaLinkiP29376.

Names & Taxonomyi

Protein namesi
Recommended name:
Leukocyte tyrosine kinase receptor (EC:2.7.10.1)
Alternative name(s):
Protein tyrosine kinase 1
Gene namesi
Name:LTK
Synonyms:TYK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:6721. LTK.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 424408ExtracellularSequence AnalysisAdd
BLAST
Transmembranei425 – 44925HelicalSequence AnalysisAdd
BLAST
Topological domaini450 – 864415CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. membrane Source: UniProtKB
  3. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Genetic variations in LTK that cause up-regulation of the PI3K pathway may possibly contribute to susceptibility to abnormal proliferation of self-reactive B-cells and, therefore, to systemic lupus erythematosus (SLE). SLE is a chronic, inflammatory and often febrile multisystemic disorder of connective tissue, thought to represent a failure of the regulatory mechanisms of the autoimmune system.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi544 – 5441K → M: Loss of interaction with PLCG1, PI3-kinase subunit p85, Ras GTPase-activating protein and RAF1. 1 Publication
Mutagenesisi750 – 7501G → E: Increases autophosphorylation and interaction with PI3-kinase subunit p85 (demonstrated with chimeric EGFR-LTK). 1 Publication
Mutagenesisi753 – 7531Y → F: Abolishes interaction with PI3-kinase subunit p85, impairs PI3 kinase activity and leads to apoptosis (demonstrated with chimeric EGFR-LTK). 1 Publication
Mutagenesisi862 – 8621Y → F: Impairs phosphorylation of CBLC (demonstrated with chimeric EGFR-LTK). 1 Publication

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

PharmGKBiPA30483.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 864848Leukocyte tyrosine kinase receptorPRO_0000016738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
Modified residuei676 – 6761Phosphotyrosine; by autocatalysisBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP29376.
PRIDEiP29376.

PTM databases

PhosphoSiteiP29376.

Expressioni

Tissue specificityi

Expressed in non-hematopoietic cell lines and T- and B-cell lines.1 Publication

Gene expression databases

BgeeiP29376.
CleanExiHS_LTK.
ExpressionAtlasiP29376. baseline and differential.
GenevestigatoriP29376.

Organism-specific databases

HPAiHPA059545.

Interactioni

Subunit structurei

Homodimer when bound to ligand (Probable). Part of a complex including LTK, TNK2 and GRB2, in which GRB2 promotes LTK recruitment by TNK2.Curated

Protein-protein interaction databases

BioGridi110236. 7 interactions.
IntActiP29376. 3 interactions.
MINTiMINT-6744900.
STRINGi9606.ENSP00000263800.

Structurei

3D structure databases

ProteinModelPortaliP29376.
SMRiP29376. Positions 465-793.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini510 – 786277Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000231766.
HOVERGENiHBG052371.
InParanoidiP29376.
KOiK05118.
OMAiAEGGQGC.
OrthoDBiEOG7GN2KT.
PhylomeDBiP29376.
TreeFamiTF351636.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR026984. LTK.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PANTHERiPTHR24416:SF138. PTHR24416:SF138. 1 hit.
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform Lambda P2 (identifier: P29376-1) [UniParc]FASTAAdd to basket

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

« Hide

        10         20         30         40         50
MGCWGQLLVW FGAAGAILCS SPGSQETFLR SSPLPLASPS PRDPKVSAPP
60 70 80 90 100
SILEPASPLN SPGTEGSWLF STCGASGRHG PTQTQCDGAY AGTSVVVTVG
110 120 130 140 150
AAGQLRGVQL WRVPGPGQYL ISAYGAAGGK GAKNHLSRAH GVFVSAIFSL
160 170 180 190 200
GLGESLYILV GQQGEDACPG GSPESQLVCL GESRAVEEHA AMDGSEGVPG
210 220 230 240 250
SRRWAGGGGG GGGATYVFRV RAGELEPLLV AAGGGGRAYL RPRDRGRTQA
260 270 280 290 300
SPEKLENRSE APGSGGRGGA AGGGGGWTSR APSPQAGRSL QEGAEGGQGC
310 320 330 340 350
SEAWATLGWA AAGGFGGGGG ACTAGGGGGG YRGGDASETD NLWADGEDGV
360 370 380 390 400
SFIHPSSELF LQPLAVTENH GEVEIRRHLN CSHCPLRDCQ WQAELQLAEC
410 420 430 440 450
LCPEGMELAV DNVTCMDLHK PPGPLVLMVA VVATSTLSLL MVCGVLILVK
460 470 480 490 500
QKKWQGLQEM RLPSPELELS KLRTSAIRTA PNPYYCQVGL GPAQSWPLPP
510 520 530 540 550
GVTEVSPANV TLLRALGHGA FGEVYEGLVI GLPGDSSPLQ VAIKTLPELC
560 570 580 590 600
SPQDELDFLM EALIISKFRH QNIVRCVGLS LRATPRLILL ELMSGGDMKS
610 620 630 640 650
FLRHSRPHLG QPSPLVMRDL LQLAQDIAQG CHYLEENHFI HRDIAARNCL
660 670 680 690 700
LSCAGPSRVA KIGDFGMARD IYRASYYRRG DRALLPVKWM PPEAFLEGIF
710 720 730 740 750
TSKTDSWSFG VLLWEIFSLG YMPYPGRTNQ EVLDFVVGGG RMDPPRGCPG
760 770 780 790 800
PVYRIMTQCW QHEPELRPSF ASILERLQYC TQDPDVLNSL LPMELGPTPE
810 820 830 840 850
EEGTSGLGNR SLECLRPPQP QELSPEKLKS WGGSPLGPWL SSGLKPLKSR
860
GLQPQNLWNP TYRS
Length:864
Mass (Da):91,681
Last modified:April 3, 2007 - v3
Checksum:i0617F378AA04298E
GO
Isoform Lambda P1 (identifier: P29376-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-170: G → VAAASGDGAAPAPGARAAWGPGERAFLGAGSPAQRGEAPGPRRFPPPLPAG
     171-864: Missing.

Show »
Length:220
Mass (Da):21,952
Checksum:iEC71C9296310B1AA
GO
Isoform Lambda P3 (identifier: P29376-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     448-448: L → GTKRLAGTVDSRLLLSSELGWVSAAGSRRQ
     449-864: Missing.

Show »
Length:477
Mass (Da):48,354
Checksum:i55867ECA5C4A4CF4
GO
Isoform 2 (identifier: P29376-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-334: Missing.

Show »
Length:803
Mass (Da):86,213
Checksum:i3877888B402CE78A
GO
Isoform 5 (identifier: P29376-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-334: Missing.
     449-544: VKQKKWQGLQ...DSSPLQVAIK → GGAWPGPVLASATRCHRGFPSQCYSAQ

Show »
Length:734
Mass (Da):78,714
Checksum:iAAB41D3555D6DF93
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061R → G in BAG59451 (PubMed:14702039).Curated
Sequence conflicti220 – 2201V → L in CAA43113 (PubMed:1655406).Curated
Sequence conflicti449 – 4491V → GTKRLAGTVDSRLLLSM in CAA36460 (PubMed:2320375).Curated
Sequence conflicti652 – 6543SCA → MR in CAA36460 (PubMed:2320375).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421R → Q.2 Publications
Corresponds to variant rs2305030 [ dbSNP | Ensembl ].
VAR_031569
Natural varianti384 – 3841C → R.1 Publication
Corresponds to variant rs55683312 [ dbSNP | Ensembl ].
VAR_046106
Natural varianti535 – 5351D → N.1 Publication
Corresponds to variant rs35932273 [ dbSNP | Ensembl ].
VAR_046107
Natural varianti569 – 5691R → S.1 Publication
Corresponds to variant rs148513655 [ dbSNP | Ensembl ].
VAR_046108
Natural varianti673 – 6731R → Q.1 Publication
Corresponds to variant rs55876255 [ dbSNP | Ensembl ].
VAR_046109
Natural varianti745 – 7451P → S.1 Publication
Corresponds to variant rs55900837 [ dbSNP | Ensembl ].
VAR_046110
Natural varianti763 – 7631E → K May possibly contribute to susceptibility to systemic lupus erythematosus; increases autophosphorylation and interaction with PI3-kinase subunit p85. 1 Publication
Corresponds to variant rs76282169 [ dbSNP | Ensembl ].
VAR_065465
Natural varianti838 – 8381P → S.1 Publication
Corresponds to variant rs56367146 [ dbSNP | Ensembl ].
VAR_046111

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei170 – 1701G → VAAASGDGAAPAPGARAAWG PGERAFLGAGSPAQRGEAPG PRRFPPPLPAG in isoform Lambda P1. CuratedVSP_002946
Alternative sequencei171 – 864694Missing in isoform Lambda P1. CuratedVSP_002947Add
BLAST
Alternative sequencei274 – 33461Missing in isoform 2 and isoform 5. 2 PublicationsVSP_035109Add
BLAST
Alternative sequencei448 – 4481L → GTKRLAGTVDSRLLLSSELG WVSAAGSRRQ in isoform Lambda P3. CuratedVSP_002948
Alternative sequencei449 – 864416Missing in isoform Lambda P3. CuratedVSP_002949Add
BLAST
Alternative sequencei449 – 54496VKQKK…QVAIK → GGAWPGPVLASATRCHRGFP SQCYSAQ in isoform 5. 1 PublicationVSP_044521Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16105 mRNA. Translation: BAA03679.1.
X60702 mRNA. Translation: CAA43113.1.
AK296892 mRNA. Translation: BAG59451.1.
AC016134 Genomic DNA. No translation available.
AC087721 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92496.1.
X52213 mRNA. Translation: CAA36460.1.
CCDSiCCDS10077.1. [P29376-1]
CCDS10078.1. [P29376-4]
CCDS45237.1. [P29376-5]
PIRiA48266.
RefSeqiNP_001129157.1. NM_001135685.1. [P29376-5]
NP_002335.2. NM_002344.5. [P29376-1]
NP_996844.1. NM_206961.3. [P29376-4]
UniGeneiHs.434481.

Genome annotation databases

EnsembliENST00000263800; ENSP00000263800; ENSG00000062524. [P29376-1]
ENST00000355166; ENSP00000347293; ENSG00000062524. [P29376-4]
ENST00000453182; ENSP00000392196; ENSG00000062524. [P29376-5]
GeneIDi4058.
KEGGihsa:4058.
UCSCiuc001zoa.3. human. [P29376-1]
uc001zob.3. human. [P29376-4]
uc010ucx.1. human. [P29376-5]

Polymorphism databases

DMDMi143811416.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16105 mRNA. Translation: BAA03679.1.
X60702 mRNA. Translation: CAA43113.1.
AK296892 mRNA. Translation: BAG59451.1.
AC016134 Genomic DNA. No translation available.
AC087721 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92496.1.
X52213 mRNA. Translation: CAA36460.1.
CCDSiCCDS10077.1. [P29376-1]
CCDS10078.1. [P29376-4]
CCDS45237.1. [P29376-5]
PIRiA48266.
RefSeqiNP_001129157.1. NM_001135685.1. [P29376-5]
NP_002335.2. NM_002344.5. [P29376-1]
NP_996844.1. NM_206961.3. [P29376-4]
UniGeneiHs.434481.

3D structure databases

ProteinModelPortaliP29376.
SMRiP29376. Positions 465-793.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110236. 7 interactions.
IntActiP29376. 3 interactions.
MINTiMINT-6744900.
STRINGi9606.ENSP00000263800.

Chemistry

BindingDBiP29376.
ChEMBLiCHEMBL5627.
GuidetoPHARMACOLOGYi1838.

PTM databases

PhosphoSiteiP29376.

Polymorphism databases

DMDMi143811416.

Proteomic databases

PaxDbiP29376.
PRIDEiP29376.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263800; ENSP00000263800; ENSG00000062524. [P29376-1]
ENST00000355166; ENSP00000347293; ENSG00000062524. [P29376-4]
ENST00000453182; ENSP00000392196; ENSG00000062524. [P29376-5]
GeneIDi4058.
KEGGihsa:4058.
UCSCiuc001zoa.3. human. [P29376-1]
uc001zob.3. human. [P29376-4]
uc010ucx.1. human. [P29376-5]

Organism-specific databases

CTDi4058.
GeneCardsiGC15M041795.
H-InvDBHIX0038138.
HGNCiHGNC:6721. LTK.
HPAiHPA059545.
MIMi151520. gene.
neXtProtiNX_P29376.
PharmGKBiPA30483.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000231766.
HOVERGENiHBG052371.
InParanoidiP29376.
KOiK05118.
OMAiAEGGQGC.
OrthoDBiEOG7GN2KT.
PhylomeDBiP29376.
TreeFamiTF351636.

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
SignaLinkiP29376.

Miscellaneous databases

GeneWikiiLeukocyte_receptor_tyrosine_kinase.
GenomeRNAii4058.
NextBioi15900.
PROiP29376.
SOURCEiSearch...

Gene expression databases

BgeeiP29376.
CleanExiHS_LTK.
ExpressionAtlasiP29376. baseline and differential.
GenevestigatoriP29376.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR026984. LTK.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PANTHERiPTHR24416:SF138. PTHR24416:SF138. 1 hit.
PfamiPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Differently spliced cDNAs of human leukocyte tyrosine kinase receptor tyrosine kinase predict receptor proteins with and without a tyrosine kinase domain and a soluble receptor protein."
    Toyoshima H., Kozutsumi H., Maru Y., Hagiwara K., Furaya A., Mioh H., Hanai N., Takaku F., Yazaki Y., Hirai H.
    Proc. Natl. Acad. Sci. U.S.A. 90:5404-5408(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-42.
    Tissue: Placenta.
  2. "The ltk gene encodes a novel receptor-type protein tyrosine kinase."
    Krolewski J.J., Dalla-Favera R.
    EMBO J. 10:2911-2919(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  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] (ISOFORM 5).
    Tissue: Tongue.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Human ltk: gene structure and preferential expression in human leukemic cells."
    Maru Y., Hirai H., Takaku F.
    Oncogene Res. 5:199-204(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 416-864.
  7. "Identification and chromosomal mapping of new human tyrosine kinase genes."
    Krolewski J.J., Lee R., Eddy R., Shows T.B., Dalla-Favera R.
    Oncogene 5:277-282(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 608-716, TISSUE SPECIFICITY.
  8. "Human ltk receptor tyrosine kinase binds to PLC-gamma 1, PI3-K, GAP and Raf-1 in vivo."
    Kozutsumi H., Toyoshima H., Hagiwara K., Yazaki Y., Hirai H.
    Oncogene 9:2991-2998(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MUTAGENESIS OF LYS-544.
  9. "The phosphatidylinositol 3' kinase pathway is required for the survival signal of leukocyte tyrosine kinase."
    Ueno H., Honda H., Nakamoto T., Yamagata T., Sasaki K., Miyagawa K., Mitani K., Yazaki Y., Hirai H.
    Oncogene 14:3067-3072(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION, MUTAGENESIS OF TYR-753 AND TYR-862.
  10. "Heart-specific activation of LTK results in cardiac hypertrophy, cardiomyocyte degeneration and gene reprogramming in transgenic mice."
    Honda H., Harada K., Komuro I., Terasaki F., Ueno H., Tanaka Y., Kawamura K., Yazaki Y., Hirai H.
    Oncogene 18:3821-3830(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  11. "Gain-of-function polymorphism in mouse and human Ltk: implications for the pathogenesis of systemic lupus erythematosus."
    Li N., Nakamura K., Jiang Y., Tsurui H., Matsuoka S., Abe M., Ohtsuji M., Nishimura H., Kato K., Kawai T., Atsumi T., Koike T., Shirai T., Ueno H., Hirose S.
    Hum. Mol. Genet. 13:171-179(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO SYSTEMIC LUPUS ERYTHEMATOSUS, VARIANT LYS-763, CHARACTERIZATION OF VARIANT LYS-763, AUTOPHOSPHORYLATION, MUTAGENESIS OF GLY-750.
  12. "Expression of a chimeric CSF1R-LTK mediates ligand-dependent neurite outgrowth."
    Yamada S., Nomura T., Takano K., Fujita S., Miyake M., Miyake J.
    NeuroReport 19:1733-1738(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION.
  13. "Cytoplasmic ACK1 interaction with multiple receptor tyrosine kinases is mediated by Grb2: an analysis of ACK1 effects on Axl signaling."
    Pao-Chun L., Chan P.M., Chan W., Manser E.
    J. Biol. Chem. 284:34954-34963(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB2 AND TNK2.
  14. "MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening."
    Farhan H., Wendeler M.W., Mitrovic S., Fava E., Silberberg Y., Sharan R., Zerial M., Hauri H.P.
    J. Cell Biol. 189:997-1011(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF THE SECRETORY PATHWAY.
  15. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-42; ARG-384; ASN-535; SER-569; GLN-673; SER-745 AND SER-838.

Entry informationi

Entry nameiLTK_HUMAN
AccessioniPrimary (citable) accession number: P29376
Secondary accession number(s): A6NNJ8, B4DL89, E9PFX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: April 3, 2007
Last modified: January 7, 2015
This is version 155 of the entry and version 3 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

Miscellaneous

Transgenic mice expressing human LTK show specific activation (tyrosine phosphorylation, kinase activity, membrane localization and homooligomerization) in heart combined with cardiac hypertrophy, cardiomyocyte degeneration.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.