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Protein

Tyrosine-protein kinase FRK

Gene

Frk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-receptor tyrosine-protein kinase that negatively regulates cell proliferation. Positively regulates PTEN protein stability through phosphorylation of PTEN on 'Tyr-336', which in turn prevents its ubiquitination and degradation, possibly by reducing its binding to NEDD4. May function as a tumor suppressor (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei269 – 2691ATPPROSITE-ProRule annotation
Active sitei361 – 3611Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi247 – 2559ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase FRK (EC:2.7.10.2)
Alternative name(s):
Beta-cell Src-homology tyrosine kinase
Short name:
BSK
FYN-related kinase
Intestine tyrosine kinase
Gene namesi
Name:Frk
Synonyms:Bsk, Iyk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:103265. Frk.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Predominantly found in the nucleus, with a small fraction found in the cell periphery.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are viable and do not show any histological abnormalities in epithelial tissues or develop any pathological and/or metabolic disorders associated with the failure of epithelial organs.1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Tyrosine-protein kinase FRKPRO_0000260826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei185 – 1851PhosphothreonineBy similarity
Modified residuei394 – 3941Phosphotyrosine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ922K9.
PaxDbiQ922K9.
PRIDEiQ922K9.

PTM databases

PhosphoSiteiQ922K9.

Expressioni

Tissue specificityi

Expressed in intestinal tract, fetal and adult islets of Langerhans, kidney, liver and lung.2 Publications

Gene expression databases

BgeeiQ922K9.
CleanExiMM_FRK.
GenevisibleiQ922K9. MM.

Interactioni

Subunit structurei

Interacts (via the SH3-domain) with PTEN. Interacts with RB1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019913.

Structurei

Secondary structure

1
512
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 587Combined sources
Beta strandi63 – 675Combined sources
Beta strandi76 – 805Combined sources
Beta strandi83 – 919Combined sources
Beta strandi103 – 1086Combined sources
Turni109 – 1113Combined sources
Beta strandi112 – 1143Combined sources
Helixi116 – 1205Combined sources
Beta strandi122 – 1243Combined sources
Helixi130 – 1378Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi153 – 1575Combined sources
Beta strandi159 – 1679Combined sources
Beta strandi169 – 1768Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi182 – 1854Combined sources
Beta strandi188 – 1925Combined sources
Helixi193 – 2008Combined sources
Beta strandi205 – 2095Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8JNMR-A52-115[»]
2DLYNMR-A113-220[»]
ProteinModelPortaliQ922K9.
SMRiQ922K9. Positions 49-223, 232-498.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922K9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 11776SH3PROSITE-ProRule annotationAdd
BLAST
Domaini123 – 21593SH2PROSITE-ProRule annotationAdd
BLAST
Domaini241 – 498258Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC 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.
InParanoidiQ922K9.
KOiK08892.
OMAiKNLRHPK.
OrthoDBiEOG7GTT2V.
PhylomeDBiQ922K9.
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.
PF00018. SH3_1. 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]

Sequencei

Sequence statusi: Complete.

Q922K9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSVCVRLWA YLQPFLPCWS QEADKSVVIE NPGAFCPPEA PRSQEPERSH
60 70 80 90 100
GQYFVALFDY QARTAEDLSF RAGDKLQVLD TSHEGWWLAR HLEKKGTGLG
110 120 130 140 150
QQLQGYIPSN YVAEDRSLQA EPWFFGAIKR ADAEKQLLYS ENQTGAFLIR
160 170 180 190 200
ESESQKGDFS LSVLDEGVVK HYRIRRLDEG GFFLTRRKVF STLNEFVNYY
210 220 230 240 250
TTTSDGLCVK LEKPCLKIQV PTPFDLSYKT ADQWEIDRNS IQLLKRLGSG
260 270 280 290 300
QFGEVWEGLW NNTTPVAVKT LKPGSMDPND FLREAQIMKS LRHPKLIQLY
310 320 330 340 350
AVCTLEDPIY IITELMRHGS LQEYLQNDGG SKIHLIQQVD MAAQVASGMA
360 370 380 390 400
YLESQNYIHR DLAARNVLVG EHNIYKVADF GLARVFKVDN EDIYESKHEI
410 420 430 440 450
KLPVKWTAPE AIRTNKFSIK SDVWSFGILL YEIITYGKMP YSGMTGAQVI
460 470 480 490 500
QMLSQNYRLP QPSNCPQQFY SIMLECWNVE PKQRPTFETL HWKLEDYFET
510
DCSYSDTNNF IN
Length:512
Mass (Da):58,844
Last modified:January 23, 2007 - v3
Checksum:iB79A0BC07B9EC5F8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541S → T in CAA88658 (PubMed:7733928).Curated
Sequence conflicti237 – 2371D → H in CAA88658 (PubMed:7733928).Curated
Sequence conflicti335 – 3351L → F in CAA88658 (PubMed:7733928).Curated
Sequence conflicti335 – 3351L → F in AAA65197 (PubMed:7835707).Curated
Sequence conflicti509 – 5091N → K in CAA88658 (PubMed:7733928).Curated
Sequence conflicti509 – 5091N → K in AAA65197 (PubMed:7835707).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48757 mRNA. Translation: CAA88658.1.
L36132 mRNA. Translation: AAA65197.1.
AK028855 mRNA. Translation: BAC26155.1.
AK052614 mRNA. Translation: BAC35063.1.
AK166379 mRNA. Translation: BAE38741.1.
BC007137 mRNA. Translation: AAH07137.1.
CCDSiCCDS23781.1.
PIRiI49552.
RefSeqiNP_001153016.1. NM_001159544.1.
NP_034367.2. NM_010237.3.
XP_006512597.1. XM_006512534.2.
XP_006512598.1. XM_006512535.2.
XP_006512599.1. XM_006512536.2.
UniGeneiMm.332432.

Genome annotation databases

EnsembliENSMUST00000019913; ENSMUSP00000019913; ENSMUSG00000019779.
ENSMUST00000170771; ENSMUSP00000130289; ENSMUSG00000019779.
GeneIDi14302.
KEGGimmu:14302.
UCSCiuc007euy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48757 mRNA. Translation: CAA88658.1.
L36132 mRNA. Translation: AAA65197.1.
AK028855 mRNA. Translation: BAC26155.1.
AK052614 mRNA. Translation: BAC35063.1.
AK166379 mRNA. Translation: BAE38741.1.
BC007137 mRNA. Translation: AAH07137.1.
CCDSiCCDS23781.1.
PIRiI49552.
RefSeqiNP_001153016.1. NM_001159544.1.
NP_034367.2. NM_010237.3.
XP_006512597.1. XM_006512534.2.
XP_006512598.1. XM_006512535.2.
XP_006512599.1. XM_006512536.2.
UniGeneiMm.332432.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8JNMR-A52-115[»]
2DLYNMR-A113-220[»]
ProteinModelPortaliQ922K9.
SMRiQ922K9. Positions 49-223, 232-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000019913.

PTM databases

PhosphoSiteiQ922K9.

Proteomic databases

MaxQBiQ922K9.
PaxDbiQ922K9.
PRIDEiQ922K9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019913; ENSMUSP00000019913; ENSMUSG00000019779.
ENSMUST00000170771; ENSMUSP00000130289; ENSMUSG00000019779.
GeneIDi14302.
KEGGimmu:14302.
UCSCiuc007euy.2. mouse.

Organism-specific databases

CTDi2444.
MGIiMGI:103265. Frk.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiQ922K9.
KOiK08892.
OMAiKNLRHPK.
OrthoDBiEOG7GTT2V.
PhylomeDBiQ922K9.
TreeFamiTF351634.

Miscellaneous databases

EvolutionaryTraceiQ922K9.
NextBioi285723.
PROiQ922K9.
SOURCEiSearch...

Gene expression databases

BgeeiQ922K9.
CleanExiMM_FRK.
GenevisibleiQ922K9. MM.

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.
PF00018. SH3_1. 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. "iyk, a novel intracellular protein tyrosine kinase differentially expressed in the mouse mammary gland and intestine."
    Thuveson M., Albrecht D., Zuercher G., Andres A., Ziemiecki A.
    Biochem. Biophys. Res. Commun. 209:582-589(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Mammary gland.
  2. "Cloning of BSK, a murine FRK homologue with a specific pattern of tissue distribution."
    Oberg-Welsh C., Welsh M.
    Gene 152:239-242(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "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.
    , 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].
    Strain: C57BL/6J.
    Tissue: Kidney, Mammary gland and Skin.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "Characterization of mice deficient in the Src family nonreceptor tyrosine kinase Frk/rak."
    Chandrasekharan S., Qiu T.H., Alkharouf N., Brantley K., Mitchell J.B., Liu E.T.
    Mol. Cell. Biol. 22:5235-5247(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. "The tyrosine kinase FRK/RAK participates in cytokine-induced islet cell cytotoxicity."
    Welsh M., Welsh C., Ekman M., Dixelius J., Hagerkvist R., Anneren C., Akerblom B., Mahboobi S., Chandrasekharan S., Liu E.T.
    Biochem. J. 382:261-268(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-394.
  7. "Solution structure of the SH3 and SH2 domains of FYN-related kinase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 50-220.

Entry informationi

Entry nameiFRK_MOUSE
AccessioniPrimary (citable) accession number: Q922K9
Secondary accession number(s): Q61364, Q61745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. 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.