P08103 (HCK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Hck

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.23 Ref.24
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.10
Enzyme regulation	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. Ref.10 Ref.12
Subunit structure	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. Ref.8 Ref.11 Ref.13 Ref.14 Ref.15 Ref.24
Subcellular location	Cytoplasmic vesicle › secretory vesicle By similarity. Cytoplasm › cytosol By similarity. Isoform 1: Membrane; Lipid-anchor. Membrane › caveola By similarity. Lysosome By similarity. Cell projection › podosome membrane; Lipid-anchor By similarity. Cytoplasm › cytosol 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. Ref.5 Ref.11 Isoform 2: Cell membrane; Lipid-anchor. Membrane › caveola; Lipid-anchor By similarity. Cell junction › focal adhesion By similarity. Cytoplasm › cytoskeleton 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. Ref.5 Ref.11
Tissue specificity	Expressed predominantly in cells of the myeloid and B-lymphoid lineages.
Post-translational modification	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. Ref.12 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.
Disruption phenotype	No visible phenotype, but macrophages have impaired phagocytosis. Mice lacking both HCK and FGR are extremely sensitive to infections by L.monocytogenes. Ref.6 Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.
Sequence caution	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.

Ontologies

Keywords
Biological process	Exocytosis Immunity Inflammatory response Innate immunity Phagocytosis
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoplasmic vesicle Cytoskeleton Golgi apparatus Lysosome Membrane Nucleus
Coding sequence diversity	Alternative initiation
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to Gram-positive bacterium Inferred from genetic interaction Ref.6. Source: MGI exocytosis Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB phagocytosis Inferred from mutant phenotype Ref.6. Source: MGI positive regulation of actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB regulation of phagocytosis Inferred from sequence or structural similarity. Source: UniProtKB regulation of podosome assembly Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell caveola Inferred from electronic annotation. Source: UniProtKB-SubCell cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to internal side of plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell transport vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-6248894,EBI-6248894
WAS	P42768	3	EBI-6248894,EBI-346375	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform 1 (identifier: P08103-1)

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.

Note: Initiates from a CTG codon.

Isoform 2 (identifier: P08103-2)

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).

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 524	524	Tyrosine-protein kinase HCK		PRO_0000024435
Regions
	Domain	76 – 136	61	SH3
	Domain	142 – 239	98	SH2
	Domain	260 – 513	254	Protein kinase
	Nucleotide binding	266 – 274	9	ATP By similarity
Sites
	Active site	379	1	Proton acceptor By similarity
	Binding site	288	1	ATP By similarity
Amino acid modifications
	Modified residue	34	1	Phosphoserine Ref.21
	Modified residue	50	1	Phosphotyrosine; by autocatalysis Ref.12
	Modified residue	200	1	Phosphothreonine By similarity
	Modified residue	207	1	Phosphotyrosine Ref.21
	Modified residue	409	1	Phosphotyrosine; by autocatalysis Ref.12 Ref.20 Ref.21 Ref.22
	Modified residue	460	1	Phosphoserine By similarity
	Modified residue	520	1	Phosphotyrosine By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity
Natural variations
	Alternative sequence	1 – 21	21	Missing in isoform 2.		VSP_018859
Experimental info
	Mutagenesis	409	1	Y → F: Reduced autophosphorylation. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p59-HCK) [UniParc]. Last modified January 23, 2007. Version 4. Checksum: DF72FD69B38C9706	FASTA	524	59,129
	10 20 30 40 50 60 MGGRSSCEDP GCPRSEGRAP RMGCVKSRFL RDGSKASKTE PSANQKGPVY VPDPTSSSKL 70 80 90 100 110 120 GPNNSNSMPP GFVEGSEDTI VVALYDYEAI HREDLSFQKG DQMVVLEEAG EWWKARSLAT 130 140 150 160 170 180 KKEGYIPSNY VARVNSLETE EWFFKGISRK DAERHLLAPG NMLGSFMIRD SETTKGSYSL 190 200 210 220 230 240 SVRDFDPQHG DTVKHYKIRT LDSGGFYISP RSTFSSLQEL VLHYKKGKDG LCQKLSVPCV 250 260 270 280 290 300 SPKPQKPWEK DAWEIPRESL QMEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF 310 320 330 340 350 360 LAEANLMKSL QHDKLVKLHA VVSQEPIFIV TEFMAKGSLL DFLKSEEGSK QPLPKLIDFS 370 380 390 400 410 420 AQISEGMAFI EQRNYIHRDL RAANILVSAS LVCKIADFGL ARIIEDNEYT AREGAKFPIK 430 440 450 460 470 480 WTAPEAINFG SFTIKSDVWS FGILLMEIVT YGRIPYPGMS NPEVIRALEH GYRMPRPDNC 490 500 510 520 PEELYNIMIR CWKNRPEERP TFEYIQSVLD DFYTATESQY QQQP
	Isoform 2 (p56-HCK) [UniParc]. Checksum: 29E004E0ABA7DF40	FASTA	503	56,942
	10 20 30 40 50 60 MGCVKSRFLR DGSKASKTEP SANQKGPVYV PDPTSSSKLG PNNSNSMPPG FVEGSEDTIV 70 80 90 100 110 120 VALYDYEAIH REDLSFQKGD QMVVLEEAGE WWKARSLATK KEGYIPSNYV ARVNSLETEE 130 140 150 160 170 180 WFFKGISRKD AERHLLAPGN MLGSFMIRDS ETTKGSYSLS VRDFDPQHGD TVKHYKIRTL 190 200 210 220 230 240 DSGGFYISPR STFSSLQELV LHYKKGKDGL CQKLSVPCVS PKPQKPWEKD AWEIPRESLQ 250 260 270 280 290 300 MEKKLGAGQF GEVWMATYNK HTKVAVKTMK PGSMSVEAFL AEANLMKSLQ HDKLVKLHAV 310 320 330 340 350 360 VSQEPIFIVT EFMAKGSLLD FLKSEEGSKQ PLPKLIDFSA QISEGMAFIE QRNYIHRDLR 370 380 390 400 410 420 AANILVSASL VCKIADFGLA RIIEDNEYTA REGAKFPIKW TAPEAINFGS FTIKSDVWSF 430 440 450 460 470 480 GILLMEIVTY GRIPYPGMSN PEVIRALEHG YRMPRPDNCP EELYNIMIRC WKNRPEERPT 490 500 FEYIQSVLDD FYTATESQYQ QQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the mouse hck gene." Klemsz M.J., McKercher S.R., Maki R.A. Nucleic Acids Res. 15:9600-9600(1987) [PubMed] [Europe PMC] [Abstract] 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]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-409, MASS SPECTROMETRY. Tissue: Brain.
[21]	"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 SER-34; TYR-207 AND TYR-409, MASS SPECTROMETRY. Tissue: Macrophage.
[22]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-409, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[23]	"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.
[24]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00129487. IPI00760068.
PIR	TVMSHC. A27282.
RefSeq	NP_001165588.1. NM_001172117.1. NP_034537.2. NM_010407.4.
UniGene	Mm.715.
3D structure databases
ProteinModelPortal	P08103.
SMR	P08103. Positions 80-524.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08103. 3 interactions.
MINT	MINT-4097288.
PTM databases
PhosphoSite	P08103.
Proteomic databases
PaxDb	P08103.
PRIDE	P08103.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000109799; ENSMUSP00000105423; ENSMUSG00000003283.
GeneID	15162.
KEGG	mmu:15162.
UCSC	uc008nhc.2. mouse.
Organism-specific databases
CTD	3055.
MGI	MGI:96052. Hck.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00620000087866.
HOGENOM	HOG000233858.
HOVERGEN	HBG008761.
InParanoid	P08103.
KO	K08893.
Enzyme and pathway databases
BRENDA	2.7.10.2. 3474.
Gene expression databases
ArrayExpress	P08103.
Bgee	P08103.
CleanEx	MM_HCK.
Genevestigator	P08103.
GermOnline	ENSMUSG00000003283. Mus musculus.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_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]
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	287656.
SOURCE	Search...

Entry information

Entry name

HCK_MOUSE

Accession

Primary (citable) accession number: P08103
Secondary accession number(s): Q0VH03, Q3UD17

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 148 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program