Reviewed, UniProtKB/Swiss-Prot P08631 (HCK_HUMAN)

Names and origin

Protein names

Recommended name:
    Tyrosine-protein kinase HCK
    EC=2.7.10.2
Alternative name(s):
    Hemopoietic cell kinase
    p59-HCK/p60-HCK

Gene names

Name:

HCK

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May serve as part of a signaling pathway coupling the Fc receptor to the activation of the respiratory burst. May also contribute to neutrophil migration and may regulate the degranulation process of neutrophils.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	May interact (via SH3 domain) with HIV-1 Nef and Vif. This interaction would stimulates its tyrosine-kinase activity. Interacts (via SH3 domain) with HEV ORF3 protein. Ref.8 Ref.9 Ref.10
Subcellular location	Isoform p59-HCK: Membrane; Lipid-anchor. Isoform p60-HCK: Membrane; Lipid-anchor. Cytoplasm.
Tissue specificity	Expressed predominantly in cells of the myeloid and B-lymphoid lineages.
Domain	The SH3 domain mediates binding to HIV-1 Nef.
Post-translational modification	Isoform p59-HCK contains a N-myristoyl glycine at position 3 By similarity. Isoform p59-HCK contains a S-palmitoyl cysteine at position 3 By similarity.
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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative initiation Polymorphism
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mesoderm development Ref.2 Traceable author statement. Source: ProtInc protein amino acid phosphorylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 binding Ref.9 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	O92972	2	EBI-346340,EBI-710506	From a different organism.
	P26660	1	EBI-346340,EBI-706322	From a different organism.
	P27958	5	EBI-346340,EBI-706378	From a different organism.
	Q9UDG1	1	EBI-346340,EBI-346967
	Q9WMX2	1	EBI-346340,EBI-710918	From a different organism.
ASAP1	Q9ULH1	1	EBI-346340,EBI-346622
C2orf44	Q9H6R7	1	EBI-346340,EBI-346906
CD2AP	Q9Y5K6	1	EBI-346340,EBI-298152
DNM2	P50570	1	EBI-346340,EBI-346547
ELMO1	Q92556	4	EBI-346340,EBI-346417
EVL	Q9UI08	1	EBI-346340,EBI-346653
HNRNPK	P61978	1	EBI-346340,EBI-304185
INPP5D	Q92835	1	EBI-346340,EBI-1380477
KHDRBS1	Q07666	2	EBI-346340,EBI-1364
LCP2	Q13094	1	EBI-346340,EBI-346946
PIK3R1	P27986	1	EBI-346340,EBI-79464
PIK3R2	O00459	1	EBI-346340,EBI-346930
SF3B3	Q15393	1	EBI-346340,EBI-346977
SH3BP1	Q9Y3L3	1	EBI-346340,EBI-346869
SH3KBP1	Q96B97	1	EBI-346340,EBI-346595
SOS1	Q07889	1	EBI-346340,EBI-297487
TSG101	Q99816	1	EBI-346340,EBI-346882
vif	P12504	3	EBI-346340,EBI-779991	From a different organism.
WAS	P42768	2	EBI-346340,EBI-346375
WIPF1	O43516	3	EBI-346340,EBI-346356

Alternative products

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

Isoform p60-HCK (identifier: P08631-1)

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.

Isoform p59-HCK (identifier: P08631-2)

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 3 (By similarity). Contains a S-palmitoyl cysteine at position 4 (By similarity).

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 526

525

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

209

1

Phosphotyrosine Ref.12

Modified residue

411

1

Phosphotyrosine; by autocatalysis By similarity

Lipidation

2

1

N-myristoyl glycine By similarity

Natural variations

Alternative sequence

1 – 21

21

Missing in isoform p59-HCK.

VSP_018858

Natural variant

44

1

A → T Ref.18

VAR_041707

Natural variant

105

1

M → L Ref.18

VAR_041708

Natural variant

399

1

D → G in an ovarian mucinous carcinoma sample; somatic mutation. Ref.18

VAR_041709

Natural variant

502

1

P → Q: dbSNP rs17093828.

VAR_033836

Experimental info

Sequence conflict

24

1

C → S in AAA52643. Ref.1

Sequence conflict

76

1

Missing in CAI19695. Ref.4

Sequence conflict

76

1

Missing in CAI22967. Ref.4

Sequence conflict

76

1

Missing in AAI13855. Ref.5

Sequence conflict

144

1

W → R in BAB15482. Ref.3

Sequence conflict

378

1

I → T in AAI13855. Ref.5

Secondary structure

1

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526

Helix Strand Turn

Details...

Beta strand

82 – 87

6

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

139 – 141

3

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

208 – 214

7

Beta strand

216 – 218

3

Helix

219 – 226

8

Beta strand

233 – 235

3

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

Helix

463 – 472

10

Helix

484 – 493

10

Helix

498 – 500

3

Helix

504 – 512

9

Beta strand

514 – 518

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform p60-HCK [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 p59-HCK. 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

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: 3496523] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P60-HCK).
[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: 3453117] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P59-HCK).
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P60-HCK). Tissue: 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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P60-HCK). Tissue: B-cell and Lymph.
[6]	"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: 1875927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM P60-HCK), ALTERNATIVE INITIATION. Tissue: Bone marrow.
[7]	"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: 1572549] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-526. Tissue: Spleen.
[8]	"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: 9218412] [Abstract] Cited for: INTERACTION WITH HIV-1 NEF.
[9]	"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: 11278465] [Abstract] Cited for: INTERACTION WITH HIV-1 VIF.
[10]	"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: 11518702] [Abstract] Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-411, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-209, MASS SPECTROMETRY.
[13]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-411, MASS SPECTROMETRY. Tissue: Platelet.
[14]	"Crystal structure of the Src family tyrosine kinase Hck." Sicheri F., Moarefi I., Kuriyan J. Nature 385:602-609(1997) [PubMed: 9024658] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-526.
[15]	"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: 9778343] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 81-137.
[16]	"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: 9571048] [Abstract] Cited for: STRUCTURE BY NMR OF 78-138.
[17]	"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: 9109402] [Abstract] Cited for: STRUCTURE BY NMR OF 139-245.
[18]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-44; LEU-105 AND GLY-399.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M16591 mRNA. Translation: AAA52643.1. Frameshift.
M16592 mRNA. Translation: AAA52644.1.
AK026432 mRNA. Translation: BAB15482.1.
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.
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. Different initiation.
BC114463 mRNA. Translation: AAI14464.2.
X58741, X58742, X58743 Genomic DNA. Translation: CAA41565.2.

IPI

IPI00029769.
IPI00646510.

PIR

TVHUHC. A27811.
A41263.

RefSeq

NP_002101.2.

UniGene

Hs.655210

3D structure databases

PDBPDBe

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	[»]
4HCK	NMR	-	A	72-143	[»]
5HCK	NMR	-	A	72-143	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1051N.

IntAct

P08631. 32 interactions.

PTM databases

PhosphoSite

P08631.

Proteomic databases

PRIDE

P08631.

Genome annotation databases

Ensembl

ENSG00000101336. Homo sapiens. [Contig view]

GeneID

3055.

KEGG

hsa:3055.

Organism-specific databases

GeneCards

GC20P030103.

H-InvDB

HIX0015721.

HGNC

HGNC:4840. HCK.

HPA

CAB005195.

MIM

142370. gene.

PharmGKB

PA29216.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P08631.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.

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_6185. HIV Infection.

Gene expression databases

ArrayExpress

P08631.

Bgee

P08631.

GermOnline

ENSG00000101336. Homo sapiens.

Family and domain databases

InterPro

IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00109. TYRKINASE.

ProDom

PD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

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 Resources

NextBio

12093.

SOURCE

Search...

Entry information

Entry name

HCK_HUMAN

Accession

Primary (citable) accession number: P08631
Secondary accession number(s): 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:	June 16, 2009
This is version 134 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)