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Q13882 - PTK6_HUMAN

UniProt

Q13882 - PTK6_HUMAN

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Protein

Protein-tyrosine kinase 6

Gene

PTK6

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

Functioni

Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins: KHDRBS1/SAM68, KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors: STAT3 and STAT5A/B and a variety of signaling molecules: ARHGAP35/p190RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. These proteins include ADAM15, EGFR, ERBB2, ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6 promotes cellular differentiation and apoptosis. In tumors PTK6 contributes to cancer progression by sensitizing cells to mitogenic signals and enhancing proliferation, anchorage-independent survival and migration/invasion. Association with EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and growth through enhancement of EGF-induced signaling via BTK/AKT and PI3 kinase. Contributes to migration and proliferation by contributing to EGF-mediated phosphorylation of ARHGAP35/p190RhoGAP, which promotes association with RASA1/p120RasGAP, inactivating RhoA while activating RAS. EGF stimulation resulted in phosphorylation of PNX/Paxillin by PTK6 and activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. PTK6 activates STAT3 and STAT5B to promote proliferation. Nuclear PTK6 may be important for regulating growth in normal epithelia, while cytoplasmic PTK6 might activate oncogenic signaling pathways.
Isoform 2 inhibits PTK6 phosphorylation and PTK6 association with other tyrosine-phosphorylated proteins.

Catalytic activityi

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

Enzyme regulationi

Activated by EGF, NRG1 and IGF1. Inhibited by SOCS3 to phosphorylate STAT3. Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region. Interaction between Trp-184 within SH2-TK linker region and the catalytic domain appears essential for positive regulation of kinase activity.5 Publications

Kineticsi

  1. KM=83 µM for ATP1 Publication

Vmax=37 nmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei219 – 2191ATPPROSITE-ProRule annotation
Active sitei312 – 3121Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi197 – 2059ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  4. protein serine/threonine kinase activity Source: Ensembl
  5. receptor binding Source: GO_Central

GO - Biological processi

  1. actin cytoskeleton organization Source: GO_Central
  2. cell migration Source: UniProtKB
  3. cellular response to retinoic acid Source: BHF-UCL
  4. innate immune response Source: GO_Central
  5. intestinal epithelial cell differentiation Source: GO_Central
  6. negative regulation of growth Source: Ensembl
  7. negative regulation of protein tyrosine kinase activity Source: UniProtKB
  8. peptidyl-tyrosine autophosphorylation Source: GO_Central
  9. positive regulation of neuron projection development Source: BHF-UCL
  10. protein autophosphorylation Source: UniProtKB
  11. protein phosphorylation Source: ProtInc
  12. regulation of cell proliferation Source: GO_Central
  13. transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
  14. tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  15. tyrosine phosphorylation of Stat5 protein Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
SignaLinkiQ13882.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-tyrosine kinase 6 (EC:2.7.10.2)
Alternative name(s):
Breast tumor kinase
Tyrosine-protein kinase BRK
Gene namesi
Name:PTK6
Synonyms:BRK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9617. PTK6.

Subcellular locationi

Cytoplasm. Nucleus. Cell projection › ruffle. Membrane By similarity
Note: Colocalizes with KHDRBS1, KHDRBS2 or KHDRBS3, within the nucleus. Nuclear localization in epithelial cells of normal prostate but cytoplasmic localization in cancer prostate.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  3. nucleoplasm Source: HPA
  4. nucleus Source: UniProtKB
  5. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441W → A: Strong decrease in STAP2 phosphorylation. Markedly decreased interaction between SH3 domain the linker region. 2 Publications
Mutagenesisi66 – 661Y → A: Decrease in STAP2 phosphorylation. 1 Publication
Mutagenesisi105 – 1051R → L: Decrease in STAP2 phosphorylation. 1 Publication
Mutagenesisi184 – 1841W → A: Abrogates interaction between PTK6-domain kinase and PTK6-linker. Abrogates autophosphorylation and phosphorylation of KHDRBS1. 1 Publication
Mutagenesisi219 – 2191K → M: Abolishes kinase activity and cell transformation, and phosphorylation of STAP2. 3 Publications
Mutagenesisi342 – 3421Y → A: 3-fold lower specific kinase activity. Decrease, but still significant, autophosphorylation. Decrease, but still significant, autophosphorylation; when associated to A-447. 1 Publication
Mutagenesisi447 – 4471Y → F: Decrease in transforming potential and increase in the kinase activity level. Decrease, but still significant, autophosphorylation; when associated to A-342. 3 Publications

Organism-specific databases

PharmGKBiPA33960.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Protein-tyrosine kinase 6PRO_0000088133Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphotyrosine; by autocatalysis
Modified residuei61 – 611Phosphotyrosine; by autocatalysis
Modified residuei66 – 661Phosphotyrosine; by autocatalysis
Modified residuei114 – 1141Phosphotyrosine; by autocatalysis1 Publication
Modified residuei342 – 3421Phosphotyrosine; by autocatalysis1 Publication
Modified residuei351 – 3511Phosphotyrosine; by autocatalysis1 Publication
Modified residuei447 – 4471Phosphotyrosine1 Publication

Post-translational modificationi

Autophosphorylated. Autophosphorylation of Tyr-342 leads to an increase of kinase activity. Tyr-447 binds to the SH2 domain when phosphorylated and negatively regulates kinase activity.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13882.
PaxDbiQ13882.
PRIDEiQ13882.

PTM databases

PhosphoSiteiQ13882.

Expressioni

Tissue specificityi

Epithelia-specific. Very high level in colon and high levels in small intestine and prostate, and low levels in some fetal tissues. Not expressed in breast or ovarian tissue but expressed in high percentage of breast and ovarian cancers. Also overexpressed in some metastatic melanomas, lymphomas, colon cancers, squamous cell carcinomas and prostate cancers. Also found in melanocytes. Not expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Isoform 2 is present in prostate epithelial cell lines derived from normal prostate and prostate adenocarcinomas, as well as in a variety of cell lines.4 Publications

Gene expression databases

BgeeiQ13882.
CleanExiHS_PTK6.
GenevestigatoriQ13882.

Organism-specific databases

HPAiCAB032952.
HPA036070.
HPA036071.

Interactioni

Subunit structurei

Interacts with GAP-A.p65 (By similarity). Interacts (via SH3 and SH2 domains) with KHDRBS1. Interacts (via SH3 and SH2 domains) with phosphorylated IRS4. Interacts with ADAM15. Interacts (via SH3 domain) with SFPQ. Interacts with EGFR and ERBB2. Interacts with STAP2. Interacts with PNX. Interacts with SFPQ. Interacts with PTK/ATK. Interacts with CTNNB1.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1383632,EBI-1383632
ERBB2P046262EBI-1383632,EBI-641062
GAB1Q134806EBI-1383632,EBI-517684
KITP107214EBI-1383632,EBI-1379503
SFPQP232465EBI-1383632,EBI-355453

Protein-protein interaction databases

BioGridi111720. 20 interactions.
DIPiDIP-39785N.
IntActiQ13882. 10 interactions.
MINTiMINT-1494499.
STRINGi9606.ENSP00000217185.

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 143Combined sources
Beta strandi35 – 406Combined sources
Beta strandi45 – 506Combined sources
Beta strandi56 – 627Combined sources
Turni64 – 663Combined sources
Beta strandi67 – 704Combined sources
Helixi85 – 928Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi137 – 1404Combined sources
Beta strandi143 – 1475Combined sources
Helixi148 – 15710Combined sources
Beta strandi162 – 1643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJANMR-A75-174[»]
2KGTNMR-A1-72[»]
ProteinModelPortaliQ13882.
SMRiQ13882. Positions 1-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13882.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 7262SH3PROSITE-ProRule annotationAdd
BLAST
Domaini78 – 17093SH2PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 445255Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni171 – 19020LinkerAdd
BLAST

Domaini

The SH3 domain plays a major role in substrate interactions. The SH2 domain of PTK6 plays a role in protein-protein interactions, but is likely more important for the regulation of catalytic activity.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. BRK/PTK6/SIK subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ13882.
KOiK08894.
OMAiVRHYKIW.
OrthoDBiEOG73BVCD.
PhylomeDBiQ13882.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13882-1) [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
MVSRDQAHLG PKYVGLWDFK SRTDEELSFR AGDVFHVARK EEQWWWATLL 
        60         70         80         90        100
DEAGGAVAQG YVPHNYLAER ETVESEPWFF GCISRSEAVR RLQAEGNATG 
       110        120        130        140        150
AFLIRVSEKP SADYVLSVRD TQAVRHYKIW RRAGGRLHLN EAVSFLSLPE 
       160        170        180        190        200
LVNYHRAQSL SHGLRLAAPC RKHEPEPLPH WDDWERPREE FTLCRKLGSG 
       210        220        230        240        250
YFGEVFEGLW KDRVQVAIKV ISRDNLLHQQ MLQSEIQAMK KLRHKHILAL 
       260        270        280        290        300
YAVVSVGDPV YIITELMAKG SLLELLRDSD EKVLPVSELL DIAWQVAEGM 
       310        320        330        340        350
CYLESQNYIH RDLAARNILV GENTLCKVGD FGLARLIKED VYLSHDHNIP 
       360        370        380        390        400
YKWTAPEALS RGHYSTKSDV WSFGILLHEM FSRGQVPYPG MSNHEAFLRV 
       410        420        430        440        450
DAGYRMPCPL ECPPSVHKLM LTCWCRDPEQ RPCFKALRER LSSFTSYENP 

T
Length:451
Mass (Da):51,834
Last modified:November 1, 1996 - v1
Checksum:iCDCAC0EE242E1BD7
GO
Isoform 2 (identifier: Q13882-2) [UniParc]FASTAAdd to Basket

Also known as: ALT-PTK6, deltam5

The sequence of this isoform differs from the canonical sequence as follows:
     78-134: WFFGCISRSE...RHYKIWRRAG → AGHAGCAALQ...AGRALPEARA
     135-451: Missing.

Show »
Length:134
Mass (Da):14,465
Checksum:i7F350D1F4D13EBE9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161L → F in a renal papillary sample; somatic mutation. 1 Publication
VAR_041760
Natural varianti436 – 4361A → T.1 Publication
Corresponds to variant rs56145017 [ dbSNP | Ensembl ].		VAR_041761

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei78 – 13457WFFGC…WRRAG → AGHAGCAALQDLAACRGPAA PERGGVLPQPARACELPQGP EPVPRPAAGRALPEARA in isoform 2. 2 PublicationsVSP_042066Add
BLAST
Alternative sequencei135 – 451317Missing in isoform 2. 2 PublicationsVSP_042067Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78549 mRNA. Translation: CAA55295.1.
U61412
, U61406, U61407, U61408, U61409, U61410, U61411 Genomic DNA. Translation: AAC34935.1.
AK315232 mRNA. Translation: BAG37660.1.
AK301364 mRNA. Translation: BAG62908.1. Sequence problems.
AL121829 Genomic DNA. Translation: CAC15525.1.
BC035843 mRNA. Translation: AAH35843.1.
CCDSiCCDS13524.1. [Q13882-1]
CCDS74750.1. [Q13882-2]
PIRiS49016.
RefSeqiNP_001243287.1. NM_001256358.1. [Q13882-2]
NP_005966.1. NM_005975.3. [Q13882-1]
UniGeneiHs.51133.

Genome annotation databases

EnsembliENST00000217185; ENSP00000217185; ENSG00000101213. [Q13882-2]
ENST00000542869; ENSP00000442460; ENSG00000101213. [Q13882-1]
GeneIDi5753.
KEGGihsa:5753.
UCSCiuc002yfg.4. human. [Q13882-1]
uc011aay.3. human. [Q13882-2]

Polymorphism databases

DMDMi8928302.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78549 mRNA. Translation: CAA55295.1.
U61412
, U61406, U61407, U61408, U61409, U61410, U61411 Genomic DNA. Translation: AAC34935.1.
AK315232 mRNA. Translation: BAG37660.1.
AK301364 mRNA. Translation: BAG62908.1. Sequence problems.
AL121829 Genomic DNA. Translation: CAC15525.1.
BC035843 mRNA. Translation: AAH35843.1.
CCDSiCCDS13524.1. [Q13882-1]
CCDS74750.1. [Q13882-2]
PIRiS49016.
RefSeqiNP_001243287.1. NM_001256358.1. [Q13882-2]
NP_005966.1. NM_005975.3. [Q13882-1]
UniGeneiHs.51133.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJANMR-A75-174[»]
2KGTNMR-A1-72[»]
ProteinModelPortaliQ13882.
SMRiQ13882. Positions 1-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111720. 20 interactions.
DIPiDIP-39785N.
IntActiQ13882. 10 interactions.
MINTiMINT-1494499.
STRINGi9606.ENSP00000217185.

Chemistry

BindingDBiQ13882.
ChEMBLiCHEMBL4601.
DrugBankiDB05294. Vandetanib.
GuidetoPHARMACOLOGYi2182.

PTM databases

PhosphoSiteiQ13882.

Polymorphism databases

DMDMi8928302.

Proteomic databases

MaxQBiQ13882.
PaxDbiQ13882.
PRIDEiQ13882.

Protocols and materials databases

DNASUi5753.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217185; ENSP00000217185; ENSG00000101213. [Q13882-2]
ENST00000542869; ENSP00000442460; ENSG00000101213. [Q13882-1]
GeneIDi5753.
KEGGihsa:5753.
UCSCiuc002yfg.4. human. [Q13882-1]
uc011aay.3. human. [Q13882-2]

Organism-specific databases

CTDi5753.
GeneCardsiGC20M062159.
HGNCiHGNC:9617. PTK6.
HPAiCAB032952.
HPA036070.
HPA036071.
MIMi602004. gene.
neXtProtiNX_Q13882.
PharmGKBiPA33960.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ13882.
KOiK08894.
OMAiVRHYKIW.
OrthoDBiEOG73BVCD.
PhylomeDBiQ13882.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
SignaLinkiQ13882.

Miscellaneous databases

EvolutionaryTraceiQ13882.
GeneWikiiPTK6.
GenomeRNAii5753.
NextBioi22386.
PROiQ13882.
SOURCEiSearch...

Gene expression databases

BgeeiQ13882.
CleanExiHS_PTK6.
GenevestigatoriQ13882.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterisation of cDNAs encoding a novel non-receptor tyrosine kinase, brk, expressed in human breast tumours."
    Mitchell P.J., Barker K.T., Martindale J.E., Kamalati T., Lowe P.N., Page M.J., Gusterson B.A., Crompton M.R.
    Oncogene 9:2383-2390(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary tumor.
  2. "Characterisation and chromosome mapping of the human non receptor tyrosine kinase gene, brk."
    Mitchell P.J., Barker K.T., Shipley J., Crompton M.R.
    Oncogene 15:1497-1502(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  3. "Exon-intron structure of the human PTK6 gene demonstrates that PTK6 constitutes a distinct family of non-receptor tyrosine kinase."
    Lee H.-Y., Kim M., Lee K.-H., Kang K.-N., Lee S.-T.
    Mol. Cells 8:401-407(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Melanocyte.
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Urinary bladder.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Blood.
  7. "Brk, a breast tumor-derived non-receptor protein-tyrosine kinase, sensitizes mammary epithelial cells to epidermal growth factor."
    Kamalati T., Jolin H.E., Mitchell P.J., Barker K.T., Jackson L.E., Dean C.J., Page M.J., Gusterson B.A., Crompton M.R.
    J. Biol. Chem. 271:30956-30963(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH EGFR, MUTAGENESIS OF LYS-219 AND TYR-447.
  8. "Loss of expression of receptor tyrosine kinase family genes PTK7 and SEK in metastatic melanoma."
    Easty D.J., Mitchell P.J., Patel K., Florenes V.A., Spritz R.A., Bennett D.C.
    Int. J. Cancer 71:1061-1065(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "A novel adaptor-like protein which is a substrate for the non-receptor tyrosine kinase, BRK."
    Mitchell P.J., Sara E.A., Crompton M.R.
    Oncogene 19:4273-4282(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STAP2, MUTAGENESIS OF TRP-44; TYR-66; ARG-105 AND LYS-219.
  10. "Sik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding ability."
    Derry J.J., Richard S., Valderrama Carvajal H., Ye X., Vasioukhin V., Cochrane A.W., Chen T., Tyner A.L.
    Mol. Cell. Biol. 20:6114-6126(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KHDRBS1.
  11. "Regulation of the nonreceptor tyrosine kinase Brk by autophosphorylation and by autoinhibition."
    Qiu H., Miller W.T.
    J. Biol. Chem. 277:34634-34641(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-342; TYR-351 AND TYR-447, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-342 AND TYR-447, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Altered localization and activity of the intracellular tyrosine kinase BRK/Sik in prostate tumor cells."
    Derry J.J., Prins G.S., Ray V., Tyner A.L.
    Oncogene 22:4212-4220(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. "The nuclear tyrosine kinase BRK/Sik phosphorylates and inhibits the RNA-binding activities of the Sam68-like mammalian proteins SLM-1 and SLM-2."
    Haegebarth A., Heap D., Bie W., Derry J.J., Richard S., Tyner A.L.
    J. Biol. Chem. 279:54398-54404(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-219 AND TYR-447, PHOSPHORYLATION.
  14. "Brk activates rac1 and promotes cell migration and invasion by phosphorylating paxillin."
    Chen H.Y., Shen C.H., Tsai Y.T., Lin F.C., Huang Y.P., Chen R.H.
    Mol. Cell. Biol. 24:10558-10572(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, FUNCTION IN PHOSPHORYLATION OF PXN, SUBCELLULAR LOCATION, INTERACTION WITH PXN.
  15. "Differential expression of the non-receptor tyrosine kinase BRK in oral squamous cell carcinoma and normal oral epithelium."
    Petro B.J., Tan R.C., Tyner A.L., Lingen M.W., Watanabe K.
    Oral Oncol. 40:1040-1047(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  16. "Regulated association of protein kinase B/Akt with breast tumor kinase."
    Zhang P., Ostrander J.H., Faivre E.J., Olsen A., Fitzsimmons D., Lange C.A.
    J. Biol. Chem. 280:1982-1991(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BTK, INTERACTION WITH BTK.
  17. "An intramolecular interaction between SH2-kinase linker and kinase domain is essential for the catalytic activity of protein-tyrosine kinase-6."
    Kim H.I.E., Lee S.T.
    J. Biol. Chem. 280:28973-28980(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TRP-184, ENZYME REGULATION.
  18. "Tyrosine phosphorylation of sam68 by breast tumor kinase regulates intranuclear localization and cell cycle progression."
    Lukong K.E., Larocque D., Tyner A.L., Richard S.
    J. Biol. Chem. 280:38639-38647(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF KHDRBS1.
  19. "Interaction between Brk kinase and insulin receptor substrate-4."
    Qiu H., Zappacosta F., Su W., Annan R.S., Miller W.T.
    Oncogene 24:5656-5664(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRS4, ENZYME REGULATION.
  20. "Expression and oncogenic role of Brk (PTK6/Sik) protein tyrosine kinase in lymphocytes."
    Kasprzycka M., Majewski M., Wang Z.J., Ptasznik A., Wysocka M., Zhang Q., Marzec M., Gimotty P., Crompton M.R., Wasik M.A.
    Am. J. Pathol. 168:1631-1641(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  21. "Identification of STAT3 as a specific substrate of breast tumor kinase."
    Liu L., Gao Y., Qiu H., Miller W.T., Poli V., Reich N.C.
    Oncogene 25:4904-4912(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF STAT3, ENZYME REGULATION.
  22. "Molecular dissection of the interaction between the SH3 domain and the SH2-Kinase Linker region in PTK6."
    Kim H.I.E., Jung J., Lee E.S., Kim Y.C., Lee W., Lee S.T.
    Biochem. Biophys. Res. Commun. 362:829-834(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, MUTAGENESIS OF TRP-44.
  23. "Signal transducer and activator of transcription 5b: a new target of breast tumor kinase/protein tyrosine kinase 6."
    Weaver A.M., Silva C.M.
    Breast Cancer Res. 9:R79-R79(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF STAT5B.
  24. "Breast tumor kinase phosphorylates p190RhoGAP to regulate rho and ras and promote breast carcinoma growth, migration, and invasion."
    Shen C.H., Chen H.Y., Lin M.S., Li F.Y., Chang C.C., Kuo M.L., Settleman J., Chen R.H.
    Cancer Res. 68:7779-7787(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ARHGAP35.
  25. "Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
    Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
    Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADAM15.
  26. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: INTERACTION WITH ERBB2.
  28. "BRK phosphorylates PSF promoting its cytoplasmic localization and cell cycle arrest."
    Lukong K.E., Huot M.E., Richard S.
    Cell. Signal. 21:1415-1422(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFPQ.
  29. "Building a better understanding of the intracellular tyrosine kinase PTK6 - BRK by BRK."
    Brauer P.M., Tyner A.L.
    Biochim. Biophys. Acta 1806:66-73(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  30. "Identification of beta-catenin as a target of the intracellular tyrosine kinase PTK6."
    Palka-Hamblin H.L., Gierut J.J., Bie W., Brauer P.M., Zheng Y., Asara J.M., Tyner A.L.
    J. Cell Sci. 123:236-245(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION OF CTNNB1, INTERACTION WITH CTNNB1.
  31. "The alternative splice variant of protein tyrosine kinase 6 negatively regulates growth and enhances PTK6-mediated inhibition of beta-catenin."
    Brauer P.M., Zheng Y., Evans M.D., Dominguez-Brauer C., Peehl D.M., Tyner A.L.
    PLoS ONE 6:E14789-E14789(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), INTERACTION (ISOFORM 2) WITH KHDRBS1 AND CTNNB1.
  32. "Solution structure and backbone dynamics of the non-receptor protein-tyrosine kinase-6 Src homology 2 domain."
    Hong E., Shin J., Kim H.I., Lee S.T., Lee W.
    J. Biol. Chem. 279:29700-29708(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 75-174.
  33. "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] PHE-16 AND THR-436.
+Additional computationally mapped references.

Entry informationi

Entry nameiPTK6_HUMAN
AccessioniPrimary (citable) accession number: Q13882
Secondary accession number(s): B2RCR3, B4DW46, Q58F01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: February 4, 2015
This is version 160 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.