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Protein

Tyrosine-protein kinase HCK

Gene

Hck

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 found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Subject to autoinhibition, mediated by intramolecular interactions involving the SH2 and SH3 domains. Kinase activity is also regulated by phosphorylation at regulatory tyrosine residues. Phosphorylation at Tyr-409 is required for optimal activity. Phosphorylation at Tyr-520 inhibits kinase activity. Inhibited by PP1.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei288 – 2881ATPPROSITE-ProRule annotation
Active sitei379 – 3791Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2749ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Exocytosis, Immunity, Inflammatory response, Innate immunity, Phagocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_333749. FCGR activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase HCK (EC:2.7.10.2)
Alternative name(s):
B-cell/myeloid kinase
Short name:
BMK
Hematopoietic cell kinase
Hemopoietic cell kinase
p56-HCK/p59-HCK
Gene namesi
Name:Hck
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:96052. Hck.

Subcellular locationi

Isoform 1 :
Isoform 2 :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Lysosome, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype, but macrophages have impaired phagocytosis. Mice lacking both HCK and FGR are extremely sensitive to infections by L.monocytogenes.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi409 – 4091Y → F: Reduced autophosphorylation. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 524523Tyrosine-protein kinase HCKPRO_0000024435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei50 – 501Phosphotyrosine; by autocatalysis1 Publication
Modified residuei200 – 2001PhosphothreonineBy similarity
Modified residuei207 – 2071Phosphotyrosine1 Publication
Modified residuei409 – 4091Phosphotyrosine; by autocatalysis1 Publication
Modified residuei460 – 4601PhosphoserineBy similarity
Modified residuei520 – 5201Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation at Tyr-409 increases kinase activity. Phosphorylation at Tyr-520 inhibits kinase activity. Kinase activity is not required for phosphorylation at Tyr-520, suggesting that this site may be a target of other kinases.1 Publication
Ubiquitinated by CBL, leading to its degradation via the proteasome.
Isoform 2 palmitoylation at position 2 requires prior myristoylation. Palmitoylation at position 3 is required for caveolar localization of isoform 2 (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP08103.
PaxDbiP08103.
PRIDEiP08103.

PTM databases

PhosphoSiteiP08103.

Expressioni

Tissue specificityi

Expressed predominantly in cells of the myeloid and B-lymphoid lineages.

Gene expression databases

BgeeiP08103.
CleanExiMM_HCK.
ExpressionAtlasiP08103. baseline and differential.
GenevisibleiP08103. MM.

Interactioni

Subunit structurei

Interacts with ADAM15. Interacts with FASLG. Interacts with ARRB1 and ARRB2. Interacts with FCGR1A; the interaction may be indirect. Interacts with IL6ST. Interacts (via SH3 domain) with ELMO1. Interacts (via SH3 domain) with TP73. Interacts with YAP1. Interacts with ABL1 and ITGB1, and thereby recruits ABL1 to activated ITGB1 (By similarity). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with CBL. Interacts with VAV1, WAS and RAPGEF1. Interacts (via SH3 domain) with C2orf44 (By similarity).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
WASP427683EBI-6248894,EBI-346375From a different organism.

Protein-protein interaction databases

BioGridi200249. 4 interactions.
IntActiP08103. 5 interactions.
MINTiMINT-4097288.
STRINGi10090.ENSMUSP00000003370.

Structurei

3D structure databases

ProteinModelPortaliP08103.
SMRiP08103. Positions 80-524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 13661SH3PROSITE-ProRule annotationAdd
BLAST
Domaini142 – 23998SH2PROSITE-ProRule annotationAdd
BLAST
Domaini260 – 513254Protein 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.
InParanoidiP08103.
KOiK08893.
PhylomeDBiP08103.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P08103-1) [UniParc]FASTAAdd to basket

Also known as: p59-HCK

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
MGGRSSCEDP GCPRSEGRAP RMGCVKSRFL RDGSKASKTE PSANQKGPVY
60 70 80 90 100
VPDPTSSSKL GPNNSNSMPP GFVEGSEDTI VVALYDYEAI HREDLSFQKG
110 120 130 140 150
DQMVVLEEAG EWWKARSLAT KKEGYIPSNY VARVNSLETE EWFFKGISRK
160 170 180 190 200
DAERHLLAPG NMLGSFMIRD SETTKGSYSL SVRDFDPQHG DTVKHYKIRT
210 220 230 240 250
LDSGGFYISP RSTFSSLQEL VLHYKKGKDG LCQKLSVPCV SPKPQKPWEK
260 270 280 290 300
DAWEIPRESL QMEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF
310 320 330 340 350
LAEANLMKSL QHDKLVKLHA VVSQEPIFIV TEFMAKGSLL DFLKSEEGSK
360 370 380 390 400
QPLPKLIDFS AQISEGMAFI EQRNYIHRDL RAANILVSAS LVCKIADFGL
410 420 430 440 450
ARIIEDNEYT AREGAKFPIK WTAPEAINFG SFTIKSDVWS FGILLMEIVT
460 470 480 490 500
YGRIPYPGMS NPEVIRALEH GYRMPRPDNC PEELYNIMIR CWKNRPEERP
510 520
TFEYIQSVLD DFYTATESQY QQQP
Note: Initiates from a CTG codon.
Length:524
Mass (Da):59,129
Last modified:January 23, 2007 - v4
Checksum:iDF72FD69B38C9706
GO
Isoform 2 (identifier: P08103-2) [UniParc]FASTAAdd to basket

Also known as: p56-HCK

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Note: Initiator Met-1 is removed. Contains a N-myristoyl glycine at position 2 (By similarity). Contains a S-palmitoyl cysteine at position 3 (By similarity).By similarity
Show »
Length:503
Mass (Da):56,942
Checksum:i29E004E0ABA7DF40
GO

Sequence cautioni

The sequence AAA37305.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAE29054.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAE29445.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAE29787.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAE33532.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence BAE38133.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAA68544.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform 2. CuratedVSP_018859Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00487 mRNA. Translation: CAA68544.1. Sequence problems.
J03023 mRNA. Translation: AAA37305.1. Sequence problems.
AK149736 mRNA. Translation: BAE29054.1. Sequence problems.
AK150290 mRNA. Translation: BAE29445.1. Sequence problems.
AK150709 mRNA. Translation: BAE29787.1. Sequence problems.
AK155975 mRNA. Translation: BAE33532.1. Sequence problems.
AK165315 mRNA. Translation: BAE38133.1. Sequence problems.
BC010478 mRNA. Translation: AAH10478.2.
CCDSiCCDS38284.1. [P08103-1]
CCDS50756.1. [P08103-2]
PIRiA27282. TVMSHC.
RefSeqiNP_001165588.1. NM_001172117.1. [P08103-2]
NP_034537.2. NM_010407.4. [P08103-1]
UniGeneiMm.715.

Genome annotation databases

EnsembliENSMUST00000109799; ENSMUSP00000105423; ENSMUSG00000003283. [P08103-2]
ENSMUST00000189688; ENSMUSP00000141030; ENSMUSG00000003283. [P08103-2]
GeneIDi15162.
KEGGimmu:15162.
UCSCiuc008nhc.2. mouse. [P08103-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00487 mRNA. Translation: CAA68544.1. Sequence problems.
J03023 mRNA. Translation: AAA37305.1. Sequence problems.
AK149736 mRNA. Translation: BAE29054.1. Sequence problems.
AK150290 mRNA. Translation: BAE29445.1. Sequence problems.
AK150709 mRNA. Translation: BAE29787.1. Sequence problems.
AK155975 mRNA. Translation: BAE33532.1. Sequence problems.
AK165315 mRNA. Translation: BAE38133.1. Sequence problems.
BC010478 mRNA. Translation: AAH10478.2.
CCDSiCCDS38284.1. [P08103-1]
CCDS50756.1. [P08103-2]
PIRiA27282. TVMSHC.
RefSeqiNP_001165588.1. NM_001172117.1. [P08103-2]
NP_034537.2. NM_010407.4. [P08103-1]
UniGeneiMm.715.

3D structure databases

ProteinModelPortaliP08103.
SMRiP08103. Positions 80-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200249. 4 interactions.
IntActiP08103. 5 interactions.
MINTiMINT-4097288.
STRINGi10090.ENSMUSP00000003370.

PTM databases

PhosphoSiteiP08103.

Proteomic databases

MaxQBiP08103.
PaxDbiP08103.
PRIDEiP08103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000109799; ENSMUSP00000105423; ENSMUSG00000003283. [P08103-2]
ENSMUST00000189688; ENSMUSP00000141030; ENSMUSG00000003283. [P08103-2]
GeneIDi15162.
KEGGimmu:15162.
UCSCiuc008nhc.2. mouse. [P08103-1]

Organism-specific databases

CTDi3055.
MGIiMGI:96052. Hck.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP08103.
KOiK08893.
PhylomeDBiP08103.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_333749. FCGR activation.

Miscellaneous databases

NextBioi287656.
PROiP08103.
SOURCEiSearch...

Gene expression databases

BgeeiP08103.
CleanExiMM_HCK.
ExpressionAtlasiP08103. baseline and differential.
GenevisibleiP08103. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: ICR.
    Tissue: Macrophage.
  2. "Isolation and sequence of a cDNA corresponding to a src-related gene expressed in murine hemopoietic cells."
    Holtzman D.A., Cook W.D., Dunn A.R.
    Proc. Natl. Acad. Sci. U.S.A. 84:8325-8329(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Macrophage.
  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] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow macrophage and Spleen.
  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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. "Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization."
    Lock P., Ralph S., Stanley E., Boulet I., Ramsay R., Dunn A.R.
    Mol. Cell. Biol. 11:4363-4370(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM 1), SUBCELLULAR LOCATION, IDENTIFICATION OF ISOFORM 2, ALTERNATIVE INITIATION.
  6. "Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity."
    Lowell C.A., Soriano P., Varmus H.E.
    Genes Dev. 8:387-398(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. "Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions."
    Lowell C.A., Fumagalli L., Berton G.
    J. Cell Biol. 133:895-910(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of vav in macrophages: evidence for involvement of the hck tyrosine kinase."
    English B.K., Orlicek S.L., Mei Z., Meals E.A.
    J. Leukoc. Biol. 62:859-864(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VAV1.
  9. "Impaired integrin-mediated signal transduction, altered cytoskeletal structure and reduced motility in Hck/Fgr deficient macrophages."
    Suen P.W., Ilic D., Caveggion E., Berton G., Damsky C.H., Lowell C.A.
    J. Cell Sci. 112:4067-4078(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck."
    Mocsai A., Ligeti E., Lowell C.A., Berton G.
    J. Immunol. 162:1120-1126(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  11. "Hck enhances the adherence of lipopolysaccharide-stimulated macrophages via Cbl and phosphatidylinositol 3-kinase."
    Scholz G., Cartledge K., Dunn A.R.
    J. Biol. Chem. 275:14615-14623(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CBL, SUBCELLULAR LOCATION, INTERACTION WITH CBL.
  12. "Modulation of the catalytic activity of the Src family tyrosine kinase Hck by autophosphorylation at a novel site in the unique domain."
    Johnson T.M., Williamson N.A., Scholz G., Jaworowski A., Wettenhall R.E., Dunn A.R., Cheng H.C.
    J. Biol. Chem. 275:33353-33364(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-50 AND TYR-409, MUTAGENESIS OF TYR-409, ENZYME REGULATION.
  13. "Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein."
    Cory G.O., Garg R., Cramer R., Ridley A.J.
    J. Biol. Chem. 277:45115-45121(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF WAS, INTERACTION WITH WAS.
  14. "Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain."
    Shivakrupa R., Radha V., Sudhakar C., Swarup G.
    J. Biol. Chem. 278:52188-52194(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAPGEF1, FUNCTION IN REGULATION OF APOPTOSIS.
  15. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
    Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
    Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT3.
  16. "CpG DNA enhances macrophage cell spreading by promoting the Src-family kinase-mediated phosphorylation of paxillin."
    Achuthan A., Elsegood C., Masendycz P., Hamilton J.A., Scholz G.M.
    Cell. Signal. 18:2252-2261(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "The Src family kinase Hck regulates mast cell activation by suppressing an inhibitory Src family kinase Lyn."
    Hong H., Kitaura J., Xiao W., Horejsi V., Ra C., Lowell C.A., Kawakami Y., Kawakami T.
    Blood 110:2511-2519(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Regulation of myeloproliferation and M2 macrophage programming in mice by Lyn/Hck, SHIP, and Stat5."
    Xiao W., Hong H., Kawakami Y., Lowell C.A., Kawakami T.
    J. Clin. Invest. 118:924-934(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Myeloid Src kinases regulate phagocytosis and oxidative burst in pneumococcal meningitis by activating NADPH oxidase."
    Paul R., Obermaier B., Van Ziffle J., Angele B., Pfister H.W., Lowell C.A., Koedel U.
    J. Leukoc. Biol. 84:1141-1150(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207 AND TYR-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Three-dimensional migration of macrophages requires Hck for podosome organization and extracellular matrix proteolysis."
    Cougoule C., Le Cabec V., Poincloux R., Al Saati T., Mege J.L., Tabouret G., Lowell C.A., Laviolette-Malirat N., Maridonneau-Parini I.
    Blood 115:1444-1452(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
    Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
    FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MYELOID CELL MIGRATION, INTERACTION WITH ABL1.

Entry informationi

Entry nameiHCK_MOUSE
AccessioniPrimary (citable) accession number: P08103
Secondary accession number(s): Q0VH03, Q3UD17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 170 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. 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.