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P08103

- HCK_MOUSE

UniProt

P08103 - HCK_MOUSE

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Protein
Tyrosine-protein kinase HCK
Gene
Hck
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.13 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 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 – 2881ATP By similarity
Active sitei379 – 3791Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2749ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  3. protein binding Source: IntAct
  4. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. defense response to Gram-positive bacterium Source: MGI
  2. exocytosis Source: UniProtKB-KW
  3. inflammatory response Source: UniProtKB-KW
  4. innate immune response Source: UniProtKB-KW
  5. peptidyl-tyrosine phosphorylation Source: UniProtKB
  6. phagocytosis Source: MGI
  7. positive regulation of actin cytoskeleton reorganization Source: UniProtKB
  8. positive regulation of cell proliferation Source: UniProtKB
  9. protein autophosphorylation Source: UniProtKB
  10. regulation of cell shape Source: UniProtKB
  11. regulation of phagocytosis Source: UniProtKB
  12. regulation of podosome assembly Source: UniProtKB
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_196487. 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: Chromosome 2

Organism-specific databases

MGIiMGI:96052. Hck.

Subcellular locationi

Cytoplasmic vesiclesecretory vesicle By similarity. Cytoplasmcytosol By similarity 2 Publications
Isoform 1 : Membrane; Lipid-anchor. Membranecaveola By similarity. Lysosome By similarity. Cell projectionpodosome membrane; Lipid-anchor By similarity. Cytoplasmcytosol By similarity
Note: Associated with specialized secretory lysosomes called azurophil granules. A fraction of this isoform is found in the cytoplasm, some of this fraction is myristoylated By similarity.2 Publications
Isoform 2 : Cell membrane; Lipid-anchor. Membranecaveola; Lipid-anchor By similarity. Cell junctionfocal adhesion By similarity. Cytoplasmcytoskeleton By similarity. Golgi apparatus By similarity. Cytoplasmic vesicle By similarity. Lysosome By similarity. Nucleus By similarity
Note: 20% of this isoform is associated with caveolae. Localization at the cell membrane and at caveolae requires palmitoylation at Cys-3. Colocalizes with the actin cytoskeleton at focal adhesions By similarity.2 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-SubCell
  2. caveola Source: UniProtKB-SubCell
  3. cell projection Source: UniProtKB-KW
  4. cytoskeleton Source: UniProtKB-SubCell
  5. cytosol Source: UniProtKB-SubCell
  6. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  7. focal adhesion Source: UniProtKB-SubCell
  8. lysosome Source: UniProtKB
  9. nucleus Source: UniProtKB-SubCell
  10. transport vesicle Source: UniProtKB-SubCell
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 – 11Removed By similarity
Chaini2 – 524523Tyrosine-protein kinase HCK
PRO_0000024435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Modified residuei50 – 501Phosphotyrosine; by autocatalysis1 Publication
Modified residuei200 – 2001Phosphothreonine By similarity
Modified residuei207 – 2071Phosphotyrosine1 Publication
Modified residuei409 – 4091Phosphotyrosine; by autocatalysis1 Publication
Modified residuei460 – 4601Phosphoserine By 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.

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP08103.
PRIDEiP08103.

PTM databases

PhosphoSiteiP08103.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP08103.
BgeeiP08103.
CleanExiMM_HCK.
GenevestigatoriP08103.

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 RAPGEF1.6 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.

Structurei

3D structure databases

ProteinModelPortaliP08103.
SMRiP08103. Positions 80-524.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 13661SH3
Add
BLAST
Domaini142 – 23998SH2
Add
BLAST
Domaini260 – 513254Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00620000087866.
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. Align

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

MGGRSSCEDP GCPRSEGRAP RMGCVKSRFL RDGSKASKTE PSANQKGPVY    50
VPDPTSSSKL GPNNSNSMPP GFVEGSEDTI VVALYDYEAI HREDLSFQKG 100
DQMVVLEEAG EWWKARSLAT KKEGYIPSNY VARVNSLETE EWFFKGISRK 150
DAERHLLAPG NMLGSFMIRD SETTKGSYSL SVRDFDPQHG DTVKHYKIRT 200
LDSGGFYISP RSTFSSLQEL VLHYKKGKDG LCQKLSVPCV SPKPQKPWEK 250
DAWEIPRESL QMEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF 300
LAEANLMKSL QHDKLVKLHA VVSQEPIFIV TEFMAKGSLL DFLKSEEGSK 350
QPLPKLIDFS AQISEGMAFI EQRNYIHRDL RAANILVSAS LVCKIADFGL 400
ARIIEDNEYT AREGAKFPIK WTAPEAINFG SFTIKSDVWS FGILLMEIVT 450
YGRIPYPGMS NPEVIRALEH GYRMPRPDNC PEELYNIMIR CWKNRPEERP 500
TFEYIQSVLD DFYTATESQY QQQP 524

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:
     2-21: 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).

Show »
Length:504
Mass (Da):57,073
Checksum:iCC4D04E0ABA7DF55
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 2120Missing in isoform 2.
VSP_018859Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
PIRiA27282. TVMSHC.
RefSeqiNP_001165588.1. NM_001172117.1.
NP_034537.2. NM_010407.4. [P08103-1]
UniGeneiMm.715.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS38284.1. [P08103-1 ]
PIRi A27282. TVMSHC.
RefSeqi NP_001165588.1. NM_001172117.1.
NP_034537.2. NM_010407.4. [P08103-1 ]
UniGenei Mm.715.

3D structure databases

ProteinModelPortali P08103.
SMRi P08103. Positions 80-524.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200249. 4 interactions.
IntActi P08103. 5 interactions.
MINTi MINT-4097288.

PTM databases

PhosphoSitei P08103.

Proteomic databases

PaxDbi P08103.
PRIDEi P08103.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000109799 ; ENSMUSP00000105423 ; ENSMUSG00000003283 .
GeneIDi 15162.
KEGGi mmu:15162.
UCSCi uc008nhc.2. mouse. [P08103-1 ]

Organism-specific databases

CTDi 3055.
MGIi MGI:96052. Hck.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00620000087866.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P08103.
KOi K08893.
PhylomeDBi P08103.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_196487. FCGR activation.

Miscellaneous databases

NextBioi 287656.
PROi P08103.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08103.
Bgeei P08103.
CleanExi MM_HCK.
Genevestigatori P08103.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 162 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

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