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UniProtKB/Swiss-Prot entry P08103


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HCK_MOUSE
Primary accession number P08103
Secondary accession numbers Q0VH03 Q3UD17
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 4, 2008 (Entry version 102)
Name and origin of the protein
Protein name Tyrosine-protein kinase HCK
Synonyms EC 2.7.10.2
Hemopoietic cell kinase
p56-HCK/p59-HCK
B-cell/myeloid kinase
BMK
Gene name
Name: Hck
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P59-HCK).
STRAIN=ICR;
TISSUE=Macrophage;
DOI=10.1093/nar/15.22.9600; PubMed=3684607 [NCBI, ExPASy, EBI, Israel, Japan]
Klemsz M.J., McKercher S.R., Maki R.A.;
"Nucleotide sequence of the mouse hck gene.";
Nucleic Acids Res. 15:9600-9600(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P59-HCK).
TISSUE=Macrophage;
PubMed=3317404 [NCBI, ExPASy, EBI, Israel, Japan]
Holtzman D.A., Cook W.D., Dunn A.R.;
"Isolation and sequence of a cDNA corresponding to a src-related gene expressed in murine hemopoietic cells.";
Proc. Natl. Acad. Sci. U.S.A. 84:8325-8329(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P59-HCK).
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone marrow macrophage, and Spleen;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P59-HCK).
STRAIN=FVB/N;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM P59-HCK), SUBCELLULAR LOCATION, AND ALTERNATIVE INITIATION.
PubMed=1875927 [NCBI, ExPASy, EBI, Israel, Japan]
Lock P., Ralph S., Stanley E., Boulet I., Ramsay R., Dunn A.R.;
"Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization.";
Mol. Cell. Biol. 11:4363-4370(1991).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-409, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00487; CAA68544.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03023; AAA37305.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK149736; BAE29054.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK150290; BAE29445.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK150709; BAE29787.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK155975; BAE33532.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK165315; BAE38133.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010478; AAH10478.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A27282; TVMSHC.
RefSeq NP_034537.2; -.
UniGene Mm.715
3D structure databases
HSSP P08631; 1AD5. [HSSP ENTRY / PDB]
SMR P08103; 80-524.
ModBase P08103.
PTM databases
PhosphoSite P08103; -.
Organism-specific databases
MGI MGI:96052; Hck.
Gene expression databases
ArrayExpress P08103; -.
CleanEx MM_HCK; -.
GermOnline ENSMUSG00000003283; Mus musculus.
Ontologies
GO
GO:0050830; Biological process: defense response to Gram-positive bacterium (inferred from genetic interaction from MGI).
GO:0006909; Biological process: phagocytosis (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
IPR001452; SH3.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 1.
Pfam PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P08103.
ProtoNet P08103.
Genome annotation databases
Ensembl ENSMUSG00000003283; Mus musculus. [Contig view]
GeneID 15162; -.
KEGG mmu:15162; -.
Phylogenomic databases
HOGENOM P08103; -.
HOVERGEN P08103; -.
Other
NextBio 287656; -.
SOURCE Hck; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative initiation; ATP-binding; Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   524  523     Tyrosine-protein kinase HCK. PRO_0000024435
DOMAIN   76   136  61     SH3. 
DOMAIN   142   239  98     SH2. 
DOMAIN   260   513  254     Protein kinase. 
NP_BIND   266   274  9     ATP (By similarity). 
ACT_SITE   379   379        Proton acceptor (By similarity). 
BINDING   288   288        ATP (By similarity). 
MOD_RES   207   207        Phosphotyrosine (By similarity). 
MOD_RES   409   409        Phosphotyrosine; by autocatalysis (By similarity). 
LIPID   2     2        N-myristoyl glycine (By similarity). 
VAR_SEQ   1    21        Missing (in isoform p56-HCK). VSP_018859
Sequence information
Length: 524 AA [This is the length of the unprocessed precursor] Molecular weight: 59129 Da [This is the MW of the unprocessed precursor] CRC64: DF72FD69B38C9706 [This is a checksum on the sequence]
        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 

P08103 in FASTA format

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View entry in raw text format (no links)
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