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P29376 (LTK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. 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:
Leukocyte tyrosine kinase receptor

EC=2.7.10.1
Alternative name(s):
Protein tyrosine kinase 1
Gene names
Name:LTK
Synonyms:TYK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length864 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.12 Ref.14

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.10

Subunit structure

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

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in non-hematopoietic cell lines and T- and B-cell lines. Ref.7

Involvement in disease

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.

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseSystemic lupus erythematosus
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from direct assay Ref.10. Source: UniProtKB

cellular response to retinoic acid

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Traceable author statement Ref.1. Source: GOC

phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of cardiac muscle cell apoptotic process

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

protein phosphorylation

Inferred from direct assay Ref.9. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

membrane

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Inferred from direct assay Ref.10. Source: UniProtKB

protein tyrosine kinase activity

Traceable author statement Ref.1. Source: ProtInc

transmembrane receptor protein tyrosine kinase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

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

Note: Additional isoforms seem to exist.
Isoform Lambda P2 (identifier: P29376-1)

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 Lambda P1 (identifier: P29376-2)

The sequence of this isoform differs from the canonical sequence as follows:
     170-170: G → VAAASGDGAAPAPGARAAWGPGERAFLGAGSPAQRGEAPGPRRFPPPLPAG
     171-864: Missing.
Isoform Lambda P3 (identifier: P29376-3)

The sequence of this isoform differs from the canonical sequence as follows:
     448-448: L → GTKRLAGTVDSRLLLSSELGWVSAAGSRRQ
     449-864: Missing.
Isoform 2 (identifier: P29376-4)

The sequence of this isoform differs from the canonical sequence as follows:
     274-334: Missing.
Isoform 5 (identifier: P29376-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 864848Leukocyte tyrosine kinase receptor
PRO_0000016738

Regions

Topological domain17 – 424408Extracellular Potential
Transmembrane425 – 44925Helical; Potential
Topological domain450 – 864415Cytoplasmic Potential
Domain510 – 786277Protein kinase
Nucleotide binding516 – 5249ATP By similarity

Sites

Active site6431Proton acceptor By similarity
Binding site5441ATP By similarity

Amino acid modifications

Modified residue6761Phosphotyrosine; by autocatalysis By similarity
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1701G → VAAASGDGAAPAPGARAAWG PGERAFLGAGSPAQRGEAPG PRRFPPPLPAG in isoform Lambda P1.
VSP_002946
Alternative sequence171 – 864694Missing in isoform Lambda P1.
VSP_002947
Alternative sequence274 – 33461Missing in isoform 2 and isoform 5.
VSP_035109
Alternative sequence4481L → GTKRLAGTVDSRLLLSSELG WVSAAGSRRQ in isoform Lambda P3.
VSP_002948
Alternative sequence449 – 864416Missing in isoform Lambda P3.
VSP_002949
Alternative sequence449 – 54496VKQKK…QVAIK → GGAWPGPVLASATRCHRGFP SQCYSAQ in isoform 5.
VSP_044521
Natural variant421R → Q. Ref.1 Ref.15
Corresponds to variant rs2305030 [ dbSNP | Ensembl ].
VAR_031569
Natural variant3841C → R. Ref.15
Corresponds to variant rs55683312 [ dbSNP | Ensembl ].
VAR_046106
Natural variant5351D → N. Ref.15
Corresponds to variant rs35932273 [ dbSNP | Ensembl ].
VAR_046107
Natural variant5691R → S. Ref.15
Corresponds to variant rs148513655 [ dbSNP | Ensembl ].
VAR_046108
Natural variant6731R → Q. Ref.15
Corresponds to variant rs55876255 [ dbSNP | Ensembl ].
VAR_046109
Natural variant7451P → S. Ref.15
Corresponds to variant rs55900837 [ dbSNP | Ensembl ].
VAR_046110
Natural variant7631E → K May possibly contribute to susceptibility to systemic lupus erythematosus; increases autophosphorylation and interaction with PI3-kinase subunit p85. Ref.11
Corresponds to variant rs76282169 [ dbSNP | Ensembl ].
VAR_065465
Natural variant8381P → S. Ref.15
Corresponds to variant rs56367146 [ dbSNP | Ensembl ].
VAR_046111

Experimental info

Mutagenesis5441K → M: Loss of interaction with PLCG1, PI3-kinase subunit p85, Ras GTPase-activating protein and RAF1. Ref.8
Mutagenesis7501G → E: Increases autophosphorylation and interaction with PI3-kinase subunit p85 (demonstrated with chimeric EGFR-LTK). Ref.11
Mutagenesis7531Y → F: Abolishes interaction with PI3-kinase subunit p85, impairs PI3 kinase activity and leads to apoptosis (demonstrated with chimeric EGFR-LTK). Ref.9
Mutagenesis8621Y → F: Impairs phosphorylation of CBLC (demonstrated with chimeric EGFR-LTK). Ref.9
Sequence conflict1061R → G in BAG59451. Ref.3
Sequence conflict2201V → L in CAA43113. Ref.2
Sequence conflict4491V → GTKRLAGTVDSRLLLSM in CAA36460. Ref.6
Sequence conflict652 – 6543SCA → MR in CAA36460. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform Lambda P2 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: 0617F378AA04298E

FASTA86491,681
        10         20         30         40         50         60 
MGCWGQLLVW FGAAGAILCS SPGSQETFLR SSPLPLASPS PRDPKVSAPP SILEPASPLN 

        70         80         90        100        110        120 
SPGTEGSWLF STCGASGRHG PTQTQCDGAY AGTSVVVTVG AAGQLRGVQL WRVPGPGQYL 

       130        140        150        160        170        180 
ISAYGAAGGK GAKNHLSRAH GVFVSAIFSL GLGESLYILV GQQGEDACPG GSPESQLVCL 

       190        200        210        220        230        240 
GESRAVEEHA AMDGSEGVPG SRRWAGGGGG GGGATYVFRV RAGELEPLLV AAGGGGRAYL 

       250        260        270        280        290        300 
RPRDRGRTQA SPEKLENRSE APGSGGRGGA AGGGGGWTSR APSPQAGRSL QEGAEGGQGC 

       310        320        330        340        350        360 
SEAWATLGWA AAGGFGGGGG ACTAGGGGGG YRGGDASETD NLWADGEDGV SFIHPSSELF 

       370        380        390        400        410        420 
LQPLAVTENH GEVEIRRHLN CSHCPLRDCQ WQAELQLAEC LCPEGMELAV DNVTCMDLHK 

       430        440        450        460        470        480 
PPGPLVLMVA VVATSTLSLL MVCGVLILVK QKKWQGLQEM RLPSPELELS KLRTSAIRTA 

       490        500        510        520        530        540 
PNPYYCQVGL GPAQSWPLPP GVTEVSPANV TLLRALGHGA FGEVYEGLVI GLPGDSSPLQ 

       550        560        570        580        590        600 
VAIKTLPELC SPQDELDFLM EALIISKFRH QNIVRCVGLS LRATPRLILL ELMSGGDMKS 

       610        620        630        640        650        660 
FLRHSRPHLG QPSPLVMRDL LQLAQDIAQG CHYLEENHFI HRDIAARNCL LSCAGPSRVA 

       670        680        690        700        710        720 
KIGDFGMARD IYRASYYRRG DRALLPVKWM PPEAFLEGIF TSKTDSWSFG VLLWEIFSLG 

       730        740        750        760        770        780 
YMPYPGRTNQ EVLDFVVGGG RMDPPRGCPG PVYRIMTQCW QHEPELRPSF ASILERLQYC 

       790        800        810        820        830        840 
TQDPDVLNSL LPMELGPTPE EEGTSGLGNR SLECLRPPQP QELSPEKLKS WGGSPLGPWL 

       850        860 
SSGLKPLKSR GLQPQNLWNP TYRS 

« Hide

Isoform Lambda P1 [UniParc].

Checksum: EC71C9296310B1AA
Show »

FASTA22021,952
Isoform Lambda P3 [UniParc].

Checksum: 55867ECA5C4A4CF4
Show »

FASTA47748,354
Isoform 2 [UniParc].

Checksum: 3877888B402CE78A
Show »

FASTA80386,213
Isoform 5 [UniParc].

Checksum: AAB41D3555D6DF93
Show »

FASTA73478,714

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10077.1. [P29376-1]
CCDS10078.1. [P29376-4]
CCDS45237.1. [P29376-5]
PIRA48266.
RefSeqNP_001129157.1. NM_001135685.1. [P29376-5]
NP_002335.2. NM_002344.5. [P29376-1]
NP_996844.1. NM_206961.3. [P29376-4]
UniGeneHs.434481.

3D structure databases

ProteinModelPortalP29376.
SMRP29376. Positions 465-793.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110236. 7 interactions.
IntActP29376. 2 interactions.
MINTMINT-6744900.
STRING9606.ENSP00000263800.

Chemistry

BindingDBP29376.
ChEMBLCHEMBL5627.
GuidetoPHARMACOLOGY1838.

PTM databases

PhosphoSiteP29376.

Polymorphism databases

DMDM143811416.

Proteomic databases

PaxDbP29376.
PRIDEP29376.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263800; ENSP00000263800; ENSG00000062524. [P29376-1]
ENST00000355166; ENSP00000347293; ENSG00000062524. [P29376-4]
ENST00000453182; ENSP00000392196; ENSG00000062524. [P29376-5]
GeneID4058.
KEGGhsa:4058.
UCSCuc001zoa.3. human. [P29376-1]
uc001zob.3. human. [P29376-4]
uc010ucx.1. human. [P29376-5]

Organism-specific databases

CTD4058.
GeneCardsGC15M041795.
H-InvDBHIX0038138.
HGNCHGNC:6721. LTK.
HPAHPA059545.
MIM151520. gene.
neXtProtNX_P29376.
PharmGKBPA30483.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231766.
HOVERGENHBG052371.
InParanoidP29376.
KOK05118.
OMAAEGGQGC.
OrthoDBEOG7GN2KT.
PhylomeDBP29376.
TreeFamTF351636.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP29376.

Gene expression databases

ArrayExpressP29376.
BgeeP29376.
CleanExHS_LTK.
GenevestigatorP29376.

Family and domain databases

InterProIPR011009. 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]
PANTHERPTHR24416:SF138. PTHR24416:SF138. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Other

GeneWikiLeukocyte_receptor_tyrosine_kinase.
GenomeRNAi4058.
NextBio15900.
PROP29376.
SOURCESearch...

Entry information

Entry nameLTK_HUMAN
AccessionPrimary (citable) accession number: P29376
Secondary accession number(s): A6NNJ8, B4DL89, E9PFX4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 152 of the entry and version 3 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

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

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