P08631 (HCK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase HCK
EC=2.7.10.2

Alternative name(s):
Hematopoietic cell kinase
Hemopoietic cell kinase
p59-HCK/p60-HCK
p59Hck
p61Hck

Gene names

Name:

HCK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	526 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. Ref.9 Ref.11 Ref.13 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.32 Ref.34 Ref.37 Ref.38
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.9 Ref.10 Ref.11 Ref.14 Ref.17 Ref.18 Ref.29 Ref.49
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-411 is required for optimal activity. Phosphorylation at Tyr-522 inhibits kinase activity. Inhibited by PP1 and A-770041. Ref.11 Ref.13 Ref.15 Ref.18 Ref.19 Ref.20 Ref.30 Ref.46 Ref.49
Subunit structure	Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with VAV1, WAS and RAPGEF1 By similarity. Interacts (via SH3 domain) with HIV-1 Nef and Vif. This interaction stimulates its tyrosine-kinase activity. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts with ARRB1 and ARRB2. Interacts with ADAM15. Interacts with FASLG. Interacts with CBL. 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. Ref.9 Ref.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.37 Ref.50 Ref.51
Subcellular location	Isoform 1: Lysosome. Membrane; Lipid-anchor. Cell projection › podosome membrane; Lipid-anchor. Cytoplasm › cytosol Ref.12 Ref.14 Ref.25 Ref.26 Ref.29 Ref.31. Note: Associated with specialized secretory lysosomes called azurophil granules. At least half of this isoform is found in the cytoplasm, some of this fraction is myristoylated. Ref.12 Ref.14 Ref.25 Ref.26 Ref.29 Ref.31 Isoform 2: Cell membrane; Lipid-anchor. Membrane › caveola; Lipid-anchor. Cell junction › focal adhesion. Cytoplasm › cytoskeleton. Golgi apparatus. Cytoplasmic vesicle. Lysosome. Nucleus. 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. Ref.12 Ref.14 Ref.25 Ref.26 Ref.29 Ref.31 Cytoplasmic vesicle › secretory vesicle. Cytoplasm › cytosol Ref.12 Ref.14 Ref.25 Ref.26 Ref.29 Ref.31.
Tissue specificity	Detected in monocytes and neutrophils (at protein level). Expressed predominantly in cells of the myeloid and B-lymphoid lineages. Highly expressed in granulocytes. Detected in tonsil. Ref.2 Ref.10 Ref.14
Induction	Up-regulated during myeloid cell differentiation. The highest levels are detected in fully differentiated phagocytes. Up-regulated by IL2. Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.30 Ref.46 Ref.49
Domain	The SH3 domain mediates binding to HIV-1 Nef.
Post-translational modification	Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation by the BCR-ABL fusion protein mediates activation of HCK. Phosphorylation at Tyr-411 increases kinase activity. Phosphorylation at Tyr-522 inhibits kinase activity. Kinase activity is not required for phosphorylation at Tyr-522, suggesting that this site is a target of other kinases. Ref.10 Ref.11 Ref.13 Ref.17 Ref.18 Ref.19 Ref.23 Ref.26 Ref.42 Ref.45 Ref.46 Ubiquitinated by CBL, leading to its degradation via the proteasome. Ref.26 Isoform 2 palmitoylation at position 2 requires prior myristoylation. Palmitoylation at position 3 is required for caveolar localization of isoform 2. Ref.12
Involvement in disease	Aberrant activation of HCK by HIV-1 protein Nef enhances HIV-1 replication and contributes to HIV-1 pathogenicity. Ref.34 Ref.38 Aberrant activation of HCK, e.g. by the BCR-ABL fusion protein, promotes cancer cell proliferation. Ref.34 Ref.38
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 AAA52643.1 differs from that shown. Reason: Frameshift at position 20. The sequence BAF82585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Exocytosis Host-virus interaction 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 Alternative splicing Polymorphism
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Fc-gamma receptor signaling pathway involved in phagocytosis Traceable author statement. Source: Reactome cell adhesion Traceable author statement Ref.39. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response-activating signal transduction Traceable author statement Ref.39. Source: UniProtKB integrin-mediated signaling pathway Traceable author statement Ref.39. Source: UniProtKB interferon-gamma-mediated signaling pathway Traceable author statement Ref.39. Source: UniProtKB leukocyte degranulation Traceable author statement Ref.39. Source: UniProtKB leukocyte migration involved in immune response Traceable author statement Ref.39. Source: UniProtKB lipopolysaccharide-mediated signaling pathway Traceable author statement Ref.39. Source: UniProtKB mesoderm development Traceable author statement Ref.2. Source: ProtInc negative regulation of apoptotic process Inferred from mutant phenotype Ref.31. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from mutant phenotype Ref.17. Source: UniProtKB positive regulation of actin cytoskeleton reorganization Inferred from direct assay Ref.29. Source: UniProtKB positive regulation of actin filament polymerization Traceable author statement Ref.39. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype Ref.17. Source: UniProtKB protein autophosphorylation Inferred from mutant phenotype Ref.17. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype Ref.17Ref.25. Source: UniProtKB regulation of defense response to virus by virus Traceable author statement. Source: Reactome regulation of inflammatory response Traceable author statement Ref.39. Source: UniProtKB regulation of phagocytosis Inferred from mutant phenotype Ref.25. Source: UniProtKB regulation of podosome assembly Inferred from direct assay Ref.29. Source: UniProtKB regulation of sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype Ref.31. Source: UniProtKB respiratory burst after phagocytosis Traceable author statement Ref.39. Source: UniProtKB viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell caveola Inferred from direct assay Ref.12. Source: UniProtKB cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome extrinsic to internal side of plasma membrane Inferred from mutant phenotype Ref.25. Source: UniProtKB focal adhesion Inferred from mutant phenotype Ref.25. Source: UniProtKB lysosome Inferred from direct assay Ref.29. 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 mutant phenotype Ref.17. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	O92972	2	EBI-346340,EBI-710506	From a different organism.
	P27958	5	EBI-346340,EBI-706378	From a different organism.
ELMO1	Q92556	4	EBI-346340,EBI-346417
KHDRBS1	Q07666	2	EBI-346340,EBI-1364
vif	P12504	3	EBI-346340,EBI-779991	From a different organism.
WAS	P42768	9	EBI-346340,EBI-346375
WIPF1	O43516	3	EBI-346340,EBI-346356

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform 1 (identifier: P08631-1)

Also known as: p60-HCK; p61Hck;

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: P08631-2)

Also known as: p59-HCK; p59Hck;

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

Note: Initiator Met-1 is removed. Myristoylated at Gly-2. S-palmitoylated at Cys-3.

Isoform 3 (identifier: P08631-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     76-76: Missing.

Isoform 4 (identifier: P08631-4)

The sequence of this isoform differs from the canonical sequence as follows:
     76-76: Missing.

Note: Initiates from a CTG codon.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 526

526

Tyrosine-protein kinase HCK

PRO_0000024433

Regions

Domain

78 – 138

61

SH3

Domain

144 – 241

98

SH2

Domain

262 – 515

254

Protein kinase

Nucleotide binding

268 – 276

9

ATP

Sites

Active site

381

1

Proton acceptor

Binding site

290

1

ATP

Amino acid modifications

Modified residue

51

1

Phosphotyrosine; by autocatalysis Ref.26

Modified residue

202

1

Phosphothreonine Ref.36

Modified residue

209

1

Phosphotyrosine By similarity

Modified residue

411

1

Phosphotyrosine; by autocatalysis Ref.19 Ref.26

Modified residue

462

1

Phosphoserine Ref.36

Modified residue

522

1

Phosphotyrosine Ref.19 Ref.26 Ref.42 Ref.45 Ref.46

Lipidation

2

1

N-myristoyl glycine Ref.12

Natural variations

Alternative sequence

1 – 21

21

Missing in isoform 2 and isoform 3.

VSP_018858

Alternative sequence

76

1

Missing in isoform 3 and isoform 4.

VSP_041926

Natural variant

44

1

A → T. Ref.52
Corresponds to variant rs56029200 [ dbSNP | Ensembl ].

VAR_041707

Natural variant

105

1

M → L. Ref.3 Ref.52
Corresponds to variant rs55722810 [ dbSNP | Ensembl ].

VAR_041708

Natural variant

399

1

D → G in an ovarian mucinous carcinoma sample; somatic mutation. Ref.52

VAR_041709

Natural variant

502

1

P → Q.
Corresponds to variant rs17093828 [ dbSNP | Ensembl ].

VAR_033836

Experimental info

Mutagenesis

3

1

G → C: Slight palmitoylation, cytoplasmic and caveolar localization; in isoform 1;. Ref.12 Ref.25

Mutagenesis

3

1

G → S: Abolishes palmitoylation and localization at the cell membrane. Ref.12 Ref.25

Mutagenesis

23

1

G → A: Myristoylation and palmitoylation are abolished, leading to entirely cytoplasmic localization; in isoform 2. Ref.12

Mutagenesis

24

1

C → S: Palmitoylation is abolished, some cytoplasmic and no calveolar localization; in isoform 2. Ref.12

Mutagenesis

290

1

K → E: Loss of kinase activity. Ref.26

Mutagenesis

305

1

E → A: Loss of kinase activity. Ref.19

Mutagenesis

381

1

D → E: Loss of kinase activity. Ref.29

Mutagenesis

411

1

Y → A: Reduced catalytic activity and higher affinity for target peptides. Ref.19

Mutagenesis

522

1

Y → F: Constitutively activated kinase, leading to cellular transformation. Ref.17 Ref.26

Sequence conflict

24

1

C → S in AAA52643. Ref.1

Sequence conflict

69

1

N → D in BAF82585. Ref.3

Sequence conflict

144

1

W → R in BAB15482. Ref.3

Sequence conflict

168

1

F → Y in BAF82585. Ref.3

Sequence conflict

378

1

I → T in AAI13855. Ref.6

Sequence conflict

488

1

N → S in BAF82585. Ref.3

Secondary structure

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526

Helix Strand Turn

Details...

Beta strand

82 – 87

6

Beta strand

93 – 96

4

Beta strand

104 – 109

6

Beta strand

114 – 119

6

Turn

120 – 122

3

Beta strand

125 – 129

5

Helix

130 – 132

3

Beta strand

133 – 135

3

Helix

136 – 138

3

Helix

139 – 141

3

Beta strand

145 – 148

4

Helix

151 – 159

9

Beta strand

168 – 172

5

Beta strand

174 – 176

3

Beta strand

179 – 188

10

Turn

189 – 191

3

Beta strand

192 – 202

11

Beta strand

204 – 206

3

Beta strand

208 – 214

7

Beta strand

216 – 218

3

Helix

219 – 226

8

Beta strand

233 – 235

3

Turn

252 – 255

4

Helix

259 – 261

3

Beta strand

262 – 269

8

Beta strand

272 – 281

10

Turn

282 – 284

3

Beta strand

285 – 292

8

Helix

299 – 309

11

Beta strand

320 – 324

5

Beta strand

326 – 328

3

Beta strand

330 – 333

4

Helix

341 – 346

6

Helix

348 – 351

4

Helix

355 – 374

20

Helix

384 – 386

3

Beta strand

387 – 389

3

Beta strand

395 – 397

3

Helix

402 – 405

4

Helix

409 – 412

4

Beta strand

416 – 419

4

Helix

421 – 423

3

Helix

426 – 431

6

Helix

436 – 451

16

Turn

452 – 454

3

Beta strand

457 – 460

4

Helix

463 – 472

10

Helix

484 – 493

10

Helix

498 – 500

3

Helix

504 – 512

9

Beta strand

514 – 518

5

Beta strand

521 – 523

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (p60-HCK) (p61Hck) [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 847E877A0A641725	FASTA	526	59,600
	10 20 30 40 50 60 MGGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV YVPDPTSTIK 70 80 90 100 110 120 PGPNSHNSNT PGIREAGSED IIVVALYDYE AIHHEDLSFQ KGDQMVVLEE SGEWWKARSL 130 140 150 160 170 180 ATRKEGYIPS NYVARVDSLE TEEWFFKGIS RKDAERQLLA PGNMLGSFMI RDSETTKGSY 190 200 210 220 230 240 SLSVRDYDPR QGDTVKHYKI RTLDNGGFYI SPRSTFSTLQ ELVDHYKKGN DGLCQKLSVP 250 260 270 280 290 300 CMSSKPQKPW EKDAWEIPRE SLKLEKKLGA GQFGEVWMAT YNKHTKVAVK TMKPGSMSVE 310 320 330 340 350 360 AFLAEANVMK TLQHDKLVKL HAVVTKEPIY IITEFMAKGS LLDFLKSDEG SKQPLPKLID 370 380 390 400 410 420 FSAQIAEGMA FIEQRNYIHR DLRAANILVS ASLVCKIADF GLARVIEDNE YTAREGAKFP 430 440 450 460 470 480 IKWTAPEAIN FGSFTIKSDV WSFGILLMEI VTYGRIPYPG MSNPEVIRAL ERGYRMPRPE 490 500 510 520 NCPEELYNIM MRCWKNRPEE RPTFEYIQSV LDDFYTATES QYQQQP
	Isoform 2 (p59-HCK) (p59Hck) [UniParc]. Checksum: 4F1EC1E8F3EDF9CA	FASTA	505	57,312
	10 20 30 40 50 60 MGCMKSKFLQ VGGNTFSKTE TSASPHCPVY VPDPTSTIKP GPNSHNSNTP GIREAGSEDI 70 80 90 100 110 120 IVVALYDYEA IHHEDLSFQK GDQMVVLEES GEWWKARSLA TRKEGYIPSN YVARVDSLET 130 140 150 160 170 180 EEWFFKGISR KDAERQLLAP GNMLGSFMIR DSETTKGSYS LSVRDYDPRQ GDTVKHYKIR 190 200 210 220 230 240 TLDNGGFYIS PRSTFSTLQE LVDHYKKGND GLCQKLSVPC MSSKPQKPWE KDAWEIPRES 250 260 270 280 290 300 LKLEKKLGAG QFGEVWMATY NKHTKVAVKT MKPGSMSVEA FLAEANVMKT LQHDKLVKLH 310 320 330 340 350 360 AVVTKEPIYI ITEFMAKGSL LDFLKSDEGS KQPLPKLIDF SAQIAEGMAF IEQRNYIHRD 370 380 390 400 410 420 LRAANILVSA SLVCKIADFG LARVIEDNEY TAREGAKFPI KWTAPEAINF GSFTIKSDVW 430 440 450 460 470 480 SFGILLMEIV TYGRIPYPGM SNPEVIRALE RGYRMPRPEN CPEELYNIMM RCWKNRPEER 490 500 PTFEYIQSVL DDFYTATESQ YQQQP
	Isoform 3 [UniParc]. Checksum: C07FF5B8D3C1B862	FASTA	504	57,241
	10 20 30 40 50 60 MGCMKSKFLQ VGGNTFSKTE TSASPHCPVY VPDPTSTIKP GPNSHNSNTP GIREGSEDII 70 80 90 100 110 120 VVALYDYEAI HHEDLSFQKG DQMVVLEESG EWWKARSLAT RKEGYIPSNY VARVDSLETE 130 140 150 160 170 180 EWFFKGISRK DAERQLLAPG NMLGSFMIRD SETTKGSYSL SVRDYDPRQG DTVKHYKIRT 190 200 210 220 230 240 LDNGGFYISP RSTFSTLQEL VDHYKKGNDG LCQKLSVPCM SSKPQKPWEK DAWEIPRESL 250 260 270 280 290 300 KLEKKLGAGQ FGEVWMATYN KHTKVAVKTM KPGSMSVEAF LAEANVMKTL QHDKLVKLHA 310 320 330 340 350 360 VVTKEPIYII TEFMAKGSLL DFLKSDEGSK QPLPKLIDFS AQIAEGMAFI EQRNYIHRDL 370 380 390 400 410 420 RAANILVSAS LVCKIADFGL ARVIEDNEYT AREGAKFPIK WTAPEAINFG SFTIKSDVWS 430 440 450 460 470 480 FGILLMEIVT YGRIPYPGMS NPEVIRALER GYRMPRPENC PEELYNIMMR CWKNRPEERP 490 500 TFEYIQSVLD DFYTATESQY QQQP
	Isoform 4 [UniParc]. Checksum: 803967415A2F57FC	FASTA	525	59,529
	10 20 30 40 50 60 MGGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV YVPDPTSTIK 70 80 90 100 110 120 PGPNSHNSNT PGIREGSEDI IVVALYDYEA IHHEDLSFQK GDQMVVLEES GEWWKARSLA 130 140 150 160 170 180 TRKEGYIPSN YVARVDSLET EEWFFKGISR KDAERQLLAP GNMLGSFMIR DSETTKGSYS 190 200 210 220 230 240 LSVRDYDPRQ GDTVKHYKIR TLDNGGFYIS PRSTFSTLQE LVDHYKKGND GLCQKLSVPC 250 260 270 280 290 300 MSSKPQKPWE KDAWEIPRES LKLEKKLGAG QFGEVWMATY NKHTKVAVKT MKPGSMSVEA 310 320 330 340 350 360 FLAEANVMKT LQHDKLVKLH AVVTKEPIYI ITEFMAKGSL LDFLKSDEGS KQPLPKLIDF 370 380 390 400 410 420 SAQIAEGMAF IEQRNYIHRD LRAANILVSA SLVCKIADFG LARVIEDNEY TAREGAKFPI 430 440 450 460 470 480 KWTAPEAINF GSFTIKSDVW SFGILLMEIV TYGRIPYPGM SNPEVIRALE RGYRMPRPEN 490 500 510 520 CPEELYNIMM RCWKNRPEER PTFEYIQSVL DDFYTATESQ YQQQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells." Quintrell N., Lebo R., Varmus H., Bishop J.M., Pettenati M.J., le Beau M.M., Diaz M.O., Rowley J.D. Mol. Cell. Biol. 7:2267-2275(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin." Ziegler S.F., Marth J.D., Lewis D.B., Perlmutter R.M. Mol. Cell. Biol. 7:2276-2285(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), VARIANT LEU-105. Tissue: Corpus callosum and Ileal mucosa.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: B-cell and Lymph.
[7]	"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), ALTERNATIVE INITIATION. Tissue: Bone marrow.
[8]	"The genomic locus of the human hemopoietic-specific cell protein tyrosine kinase (PTK)-encoding gene (HCK) confirms conservation of exon-intron structure among human PTKs of the src family." Hradetzky D., Strebhardt K., Ruesamen-Waigmann H. Gene 113:275-280(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-526. Tissue: Spleen.
[9]	"Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells." Ghazizadeh S., Bolen J.B., Fleit H.B. J. Biol. Chem. 269:8878-8884(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCGR2A, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF FCGR2A.
[10]	"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn." Wang A.V., Scholl P.R., Geha R.S. J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION.
[11]	"The Fc gamma RI receptor signals through the activation of hck and MAP kinase." Durden D.L., Kim H.M., Calore B., Liu Y. J. Immunol. 154:4039-4047(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN FCGR1A SIGNALING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION.
[12]	"Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae." Robbins S.M., Quintrell N.A., Bishop J.M. Mol. Cell. Biol. 15:3507-3515(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, MYRISTOYLATION, PALMITOYLATION, MUTAGENESIS OF GLY-3; GLY-23 AND CYS-24.
[13]	"Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines." Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N., de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B. Exp. Hematol. 25:1367-1377(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH IL6ST.
[14]	"Hck is activated by opsonized zymosan and A23187 in distinct subcellular fractions of human granulocytes." Welch H., Maridonneau-Parini I. J. Biol. Chem. 272:102-109(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[15]	"SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1." Briggs S.D., Sharkey M., Stevenson M., Smithgall T.E. J. Biol. Chem. 272:17899-17902(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH HIV-1 NEF.
[16]	"The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr." Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B., Hallek M. J. Biol. Chem. 272:33260-33270(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF BCR, INTERACTION WITH BCR-ABL.
[17]	"The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase." Howlett C.J., Bisson S.A., Resek M.E., Tigley A.W., Robbins S.M. Biochem. Biophys. Res. Commun. 257:129-138(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CBL PHOSPHORYLATION; CELL PROLIFERATION AND REGULATION OF CELL SHAPE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-522, INTERACTION WITH CBL.
[18]	"IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck." Bosco M.C., Curiel R.E., Zea A.H., Malabarba M.G., Ortaldo J.R., Espinoza-Delgado I. J. Immunol. 164:4575-4585(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN IL2 SIGNALING, CATALYTIC ACTIVITY, INDUCTION, ENZYME REGULATION, PHOSPHORYLATION.
[19]	"Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand." Porter M., Schindler T., Kuriyan J., Miller W.T. J. Biol. Chem. 275:2721-2726(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-411 AND TYR-522, MASS SPECTROMETRY, ENZYME REGULATION, MUTAGENESIS OF GLU-305 AND TYR-411.
[20]	"Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI." Barlic J., Andrews J.D., Kelvin A.A., Bosinger S.E., DeVries M.E., Xu L., Dobransky T., Feldman R.D., Ferguson S.S., Kelvin D.J. Nat. Immunol. 1:227-233(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN IL8-MEDIATED DEGRANULATION, ENZYME REGULATION, INTERACTION WITH ARRB1 AND ARRB2.
[21]	"The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein." Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C., Olive D., Collette Y., Vigne R., Decroly E. J. Biol. Chem. 276:16885-16893(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 VIF.
[22]	"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK." Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D. J. Biol. Chem. 276:42389-42400(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[23]	"The Src family kinase Hck couples BCR/ABL to STAT5 activation in myeloid leukemia cells." Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A., Wilson M., Smithgall T.E., Skorski T. EMBO J. 21:5766-5774(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS EFFECTOR OF THE BCR-ABL FUSION PROTEIN IN PHOSPHORYLATION OF STAT5B, INTERACTION WITH STAT5B AND THE BCR-ABL FUSION PROTEIN, PHOSPHORYLATION.
[24]	"Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases." Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G., Edwards D.R. J. Biol. Chem. 277:4999-5007(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADAM15, FUNCTION IN PHOSPHORYLATION OF ADAM15.
[25]	"p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner." Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I. J. Biol. Chem. 277:21007-21016(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), MUTAGENESIS OF GLY-3.
[26]	"Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation." Howlett C.J., Robbins S.M. Oncogene 21:1707-1716(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL PROLIFERATION, UBIQUITINATION, PHOSPHORYLATION AT TYR-51; TYR-411 AND TYR-522, SUBCELLULAR LOCATION, INTERACTION WITH CBL (ISOFORM 2), MUTAGENESIS OF LYS-290 AND TYR-522.
[27]	"Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation and survival of multiple myeloma cells." Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P., Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C. J. Biol. Chem. 279:21658-21665(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN IL6 SIGNALING CASCADE AND IN PHOSPHORYLATION OF GAB1 AND GAB2.
[28]	"Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck." Yokoyama N., deBakker C.D., Zappacosta F., Huddleston M.J., Annan R.S., Ravichandran K.S., Miller W.T. Biochemistry 44:8841-8849(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ELMO1, INTERACTION WITH ELMO1.
[29]	"Activation of the lysosome-associated p61Hck isoform triggers the biogenesis of podosomes." Cougoule C., Carreno S., Castandet J., Labrousse A., Astarie-Dequeker C., Poincloux R., Le Cabec V., Maridonneau-Parini I. Traffic 6:682-694(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-381.
[30]	"HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction." Trible R.P., Emert-Sedlak L., Smithgall T.E. J. Biol. Chem. 281:27029-27038(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 NEF, ENZYME REGULATION.
[31]	"Regulation of p73 by Hck through kinase-dependent and independent mechanisms." Paliwal P., Radha V., Swarup G. BMC Mol. Biol. 8:45-45(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION AND INHIBITION OF TP73 ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TP73 AND YAP1.
[32]	"Inhibition of IL-6-dependent growth of myeloma cells by an acidic peptide repressing the gp130-mediated activation of Src family kinases." Hausherr A., Tavares R., Schaffer M., Obermeier A., Miksch C., Mitina O., Ellwart J., Hallek M., Krause G. Oncogene 26:4987-4998(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH IL6ST.
[33]	"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening." Voss M., Lettau M., Janssen O. BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FASLG.
[34]	"The oncogenic activity of the Src family kinase Hck requires the cooperative action of the plasma membrane- and lysosome-associated isoforms." Poincloux R., Al Saati T., Maridonneau-Parini I., Le Cabec V. Eur. J. Cancer 45:321-327(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REORGANIZATION OF ACTIN CYTOSKELETON AND CELL PROLIFERATION, ROLE IN DISEASE.
[35]	"Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins." Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K. J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADAM15.
[36]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND SER-462, MASS SPECTROMETRY.
[37]	"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 ABL1-MEDIATED CELL MIGRATION, IDENTIFICATION IN A COMPLEX WITH ITGB1 AND WITH ABL1.
[38]	"Expression of a Src family kinase in chronic myelogenous leukemia cells induces resistance to imatinib in a kinase-dependent manner." Pene-Dumitrescu T., Smithgall T.E. J. Biol. Chem. 285:21446-21457(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN DISEASE, FUNCTION IN PHOSPHORYLATION OF THE BCR-ABL FUSION PROTEIN.
[39]	"Hematopoietic cell kinase (Hck) isoforms and phagocyte duties - from signaling and actin reorganization to migration and phagocytosis." Guiet R., Poincloux R., Castandet J., Marois L., Labrousse A., Le Cabec V., Maridonneau-Parini I. Eur. J. Cell Biol. 87:527-542(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN PHAGOCYTOSIS AND SUBSTRATES.
[40]	"Protein tyrosine kinases in neutrophil activation and recruitment." Zarbock A., Ley K. Arch. Biochem. Biophys. 510:112-119(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN NEUTROPHIL FUNCTION AND SIGNALING.
[41]	"Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase." Zhang W., Smithgall T.E., Gmeiner W.H. FEBS Lett. 406:131-135(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 140-245.
[42]	"Crystal structure of the Src family tyrosine kinase Hck." Sicheri F., Moarefi I., Kuriyan J. Nature 385:602-609(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-526 IN COMPLEX WITH CALCIUM, PHOSPHORYLATION AT TYR-522.
[43]	"RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef." Arold S., O'Brien R., Franken P., Strub M.-P., Hoh F., Dumas C., Ladbury J.E. Biochemistry 37:14683-14691(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 81-137.
[44]	"Solution structure of the human Hck SH3 domain and identification of its ligand binding site." Horita D.A., Baldisseri D.M., Zhang W., Altieri A.S., Smithgall T.E., Gmeiner W.H., Byrd R.A. J. Mol. Biol. 278:253-265(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 72-143.
[45]	"Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor." Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., Kuriyan J. Mol. Cell 3:639-648(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 81-522 IN COMPLEX WITH THE PYRAZOLO PYRIMIDINE-TYPE INHIBITOR PP1, PHOSPHORYLATION AT TYR-522.
[46]	"Discovery of A-770041, a src-family selective orally active lck inhibitor that prevents organ allograft rejection." Burchat A., Borhani D.W., Calderwood D.J., Hirst G.C., Li B., Stachlewitz R.F. Bioorg. Med. Chem. Lett. 16:118-122(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 81-522 IN COMPLEXES WITH INHIBITORS A-420983; A-641359 AND A-770041, ENZYME REGULATION, PHOSPHORYLATION AT TYR-522.
[47]	"The development of 2-benzimidazole substituted pyrimidine based inhibitors of lymphocyte specific kinase (Lck)." Sabat M., VanRens J.C., Laufersweiler M.J., Brugel T.A., Maier J., Golebiowski A., De B., Easwaran V., Hsieh L.C., Walter R.L., Mekel M.J., Evdokimov A., Janusz M.J. Bioorg. Med. Chem. Lett. 16:5973-5977(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 247-513 IN COMPLEX WITH INHIBITOR PG-1009247.
[48]	"Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes." Schmidt H., Hoffmann S., Tran T., Stoldt M., Stangler T., Wiesehan K., Willbold D. J. Mol. Biol. 365:1517-1532(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 61-140 IN COMPLEX WITH PROLINE-RICH SYNTHETIC PEPTIDE.
[49]	"Crystal structure of the Src family kinase Hck SH3-SH2 linker regulatory region supports an SH3-dominant activation mechanism." Alvarado J.J., Betts L., Moroco J.A., Smithgall T.E., Yeh J.I. J. Biol. Chem. 285:35455-35461(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 72-256, ENZYME REGULATION, CATALYTIC ACTIVITY.
[50]	"Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef." Breuer S., Schievink S.I., Schulte A., Blankenfeldt W., Fackler O.T., Geyer M. PLoS ONE 6:E20033-E20033(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 79-138 IN COMPLEX WITH HIV-1 NEF, INTERACTION WITH HIV-1 NEF.
[51]	"Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly." Horenkamp F.A., Breuer S., Schulte A., Lulf S., Weyand M., Saksela K., Geyer M. Traffic 12:867-877(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 79-138 IN COMPLEX WITH HIV-1 NEF, INTERACTION WITH HIV-1 NEF.
[52]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-44; LEU-105 AND GLY-399.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16591 mRNA. Translation: AAA52643.1. Frameshift.
M16592 mRNA. Translation: AAA52644.1.
AK026432 mRNA. Translation: BAB15482.1.
AK289896 mRNA. Translation: BAF82585.1. Different initiation.
AK298726 mRNA. Translation: BAG60878.1.
AL353092, AL049539 Genomic DNA. Translation: CAI19694.1.
AL353092, AL049539 Genomic DNA. Translation: CAI19695.1.
AL049539, AL353092 Genomic DNA. Translation: CAI22966.1.
AL049539, AL353092 Genomic DNA. Translation: CAI22967.1.
CH471077 Genomic DNA. Translation: EAW76392.1.
CH471077 Genomic DNA. Translation: EAW76393.1.
BC014435 mRNA. Translation: AAH14435.2.
BC094847 mRNA. Translation: AAH94847.2.
BC108930 mRNA. Translation: AAI08931.2.
BC108931 mRNA. Translation: AAI08932.2.
BC113854 mRNA. Translation: AAI13855.2.
BC114463 mRNA. Translation: AAI14464.2.
X58741, X58742, X58743 Genomic DNA. Translation: CAA41565.2.

IPI

IPI00029769.
IPI00646510.

PIR

TVHUHC. A27811.
A41263.

RefSeq

NP_001165600.1. NM_001172129.1.
NP_001165601.1. NM_001172130.1.
NP_001165602.1. NM_001172131.1.
NP_001165604.1. NM_001172133.1.
NP_002101.2. NM_002110.3.

UniGene

Hs.655210.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AD5	X-ray	2.60	A/B	79-526	[»]
1BU1	X-ray	2.60	A/B/C/D/E/F	81-137	[»]
1QCF	X-ray	2.00	A	81-522	[»]
2C0I	X-ray	2.30	A/B	81-522	[»]
2C0O	X-ray	2.85	A/B	81-522	[»]
2C0T	X-ray	2.15	A/B	81-522	[»]
2HCK	X-ray	3.00	A/B	79-526	[»]
2HK5	X-ray	2.00	A	247-513	[»]
2OI3	NMR	-	A	61-140	[»]
2OJ2	NMR	-	A	61-140	[»]
3HCK	NMR	-	A	140-245	[»]
3NHN	X-ray	2.61	A	72-256	[»]
3RBB	X-ray	2.35	B/D	79-138	[»]
3REA	X-ray	2.00	B/D	79-138	[»]
3REB	X-ray	3.45	B/D	79-138	[»]
4HCK	NMR	-	A	72-143	[»]
5HCK	NMR	-	A	72-143	[»]

ProteinModelPortal

P08631.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1051N.

IntAct

P08631. 32 interactions.

MINT

MINT-135300.

PTM databases

PhosphoSite

P08631.

Polymorphism databases

DMDM

20141296.

Proteomic databases

PaxDb

P08631.

PRIDE

P08631.

Protocols and materials databases

DNASU

3055.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000518730; ENSP00000427757; ENSG00000101336.
ENST00000520553; ENSP00000429848; ENSG00000101336.
ENST00000538448; ENSP00000441169; ENSG00000101336.

GeneID

3055.

KEGG

hsa:3055.

UCSC

uc002wxh.3. human.

Organism-specific databases

CTD

3055.

GeneCards

GC20P030641.

HGNC

HGNC:4840. HCK.

HPA

CAB005195.

MIM

142370. gene.

neXtProt

NX_P08631.

PharmGKB

PA29216.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

InParanoid

P08631.

KO

K08893.

OrthoDB

EOG4N04DP.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
amb2_neutrophils_pathway. amb2 Integrin signaling.
pi3kcipathway. Class I PI3K signaling events.
epha_fwdpathway. EPHA forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
glypican_1pathway. Glypican 1 network.
il6_7pathway. IL6-mediated signaling events.
pdgfrbpathway. PDGFR-beta signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
ptp1bpathway. Signaling events mediated by PTP1B.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_116125. Disease.
REACT_6900. Immune System.

SignaLink

P08631.

Gene expression databases

ArrayExpress

P08631.

Bgee

P08631.

Genevestigator

P08631.

GermOnline

ENSG00000101336. Homo sapiens.

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

BindingDB

P08631.

ChEMBL

CHEMBL3234.

ChiTaRS

HCK. human.

EvolutionaryTrace

P08631.

GenomeRNAi

3055.

NextBio

12093.

SOURCE

Search...

Entry information

Entry name

HCK_HUMAN

Accession

Primary (citable) accession number: P08631
Secondary accession number(s): A8K1I1 , B4DQB6, E1P5M2, Q29RX1, Q2VPE2, Q504R5, Q5T7K1, Q5T7K2, Q96CC0, Q9H5Y5, Q9NUA4, Q9UMJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 181 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.