HCK HCK proto-oncogene, Src family tyrosine kinase [Homo sapiens (human)] - Gene

Summary

Official Symbol: HCKprovided by HGNC
Official Full Name: HCK proto-oncogene, Src family tyrosine kinaseprovided by HGNC
Primary source: HGNC:HGNC:4840
See related: Ensembl:ENSG00000101336 MIM:142370; AllianceGenome:HGNC:4840
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: JTK9; AIPCV; p59Hck; p61Hck
Summary: The protein encoded by this gene is a member of the Src family of tyrosine kinases. This protein is primarily hemopoietic, particularly in cells of the myeloid and B-lymphoid lineages. It may help couple the Fc receptor to the activation of the respiratory burst. In addition, it may play a role in neutrophil migration and in the degranulation of neutrophils. Multiple isoforms with different subcellular distributions are produced due to both alternative splicing and the use of alternative translation initiation codons, including a non-AUG (CUG) codon. [provided by RefSeq, Feb 2010]
Expression: Broad expression in appendix (RPKM 55.1), spleen (RPKM 40.9) and 14 other tissues See more
Orthologs: mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 20q11.21

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	20	NC_000020.11 (32052242..32101856)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	20	NC_060944.1 (33776868..33826471)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	20	NC_000020.10 (30640045..30689659)

Chromosome 20 - NC_000020.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

HCK Promotes High-Grade Serous Ovarian Cancer Tumorigenesis through CD44 and NOTCH3 Signaling.
Title: HCK Promotes High-Grade Serous Ovarian Cancer Tumorigenesis through CD44 and NOTCH3 Signaling.
A new role for the SRC family kinase HCK as a driver of SYK activation in MYD88 mutated lymphomas.
Title: A new role for the SRC family kinase HCK as a driver of SYK activation in MYD88 mutated lymphomas.
Kinase-deficient BTK mutants confer ibrutinib resistance through activation of the kinase HCK.
Title: Kinase-deficient BTK mutants confer ibrutinib resistance through activation of the kinase HCK.
HCK is a Potential Prognostic Biomarker that Correlates with Immune Cell Infiltration in Acute Myeloid Leukemia.
Title: HCK is a Potential Prognostic Biomarker that Correlates with Immune Cell Infiltration in Acute Myeloid Leukemia.
miR-181b and miR-204 suppress the VSMC proliferation and migration by downregulation of HCK.
Title: miR-181b and miR-204 suppress the VSMC proliferation and migration by downregulation of HCK.
HCK maintains the self-renewal of leukaemia stem cells via CDK6 in AML.
Title: HCK maintains the self-renewal of leukaemia stem cells via CDK6 in AML.
Nucleotide binding domain and leucine-rich repeat pyrin domain-containing protein 12: characterization of its binding to hematopoietic cell kinase.
Title: Nucleotide binding domain and leucine-rich repeat pyrin domain-containing protein 12: characterization of its binding to hematopoietic cell kinase.
HCK can serve as novel prognostic biomarker and therapeutic target for Breast Cancer patients.
Title: HCK can serve as novel prognostic biomarker and therapeutic target for Breast Cancer patients.
Selective targeting of the inactive state of hematopoietic cell kinase (Hck) with a stable curcumin derivative.
Title: Selective targeting of the inactive state of hematopoietic cell kinase (Hck) with a stable curcumin derivative.
Identification of the SRC-family tyrosine kinase HCK as a therapeutic target in mantle cell lymphoma.
Title: Identification of the SRC-family tyrosine kinase HCK as a therapeutic target in mantle cell lymphoma.

Submit: New GeneRIF Correction See all GeneRIFs (59)

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Autoinflammation with pulmonary and cutaneous vasculitis MedGen: C5830371 OMIM: 620296 GeneReviews: Not available	not available

EBI GWAS Catalog

Description
Host-microbe interactions have shaped the genetic architecture of inflammatory bowel disease. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

Go to the top of the page Help

Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	HIV-1 gp120 downregulates the expression of HCK proto-oncogene, Src family tyrosine kinase (HCK) in human B cells	PubMed
Nef	nef	HIV-1 Nef binds HCK without affecting SH2-tail interaction and impacts local dynamics near the HCK active site; these changes are reversed in the presence of a selective inhibitor of the Nef-HCK complex	PubMed
	nef	HIV-1 Nef activates HCK via HCK SH3 domain displacement NOT via dephosphorylation or release from the SH2 domain	PubMed
	nef	The PXXP motif (65-82) and C-terminal proline residues 147 and 150 of HIV-1 Nef interacts with the SH3 domain of Hck; the single amino acid residue 96 in the Hck SH3 domain determines its high affinity in binding to Nef	PubMed
	nef	HIV-1-mediated effects on podosomes and migration involve Nef-HCK interaction, and HCK-mediated phosphorylation of WASP at podosomes	PubMed
	nef	The HIV-1 Nef EEEE(65) targeting motif enables the Nef PXXP(75) motif to bind and activate a trans-Golgi network-localized tyrosine kinase Hck	PubMed
	nef	Mutations P72G, V74I, P75G, and R77K in the PXXPXR motif of HIV-1 Nef abolish the binding between Nef and Hck	PubMed
	nef	Small molecule compounds, which inhibit the SH3 domain of HIV-1 Nef binding to Hck, significantly reduce Nef-mediated viral infectivity enhancement	PubMed
	nef	Mutation of the PXXP motif in HIV-1 Nef abolishes the interaction of Nef with Hck in transgenic mice, resulting in the delayed development of an AIDS-like disease in the mice	PubMed
	nef	SH3-dependent activation of Hck by HIV-1 Nef binding or by SH2-kinase linker mutation does not modulate tail tyrosine phosphorylation in vivo	PubMed
	nef	The Interaction of HIV-1 Nef with the SH3 domain of Hck regulates the effects of Nef on Hck tyrosine kinase activation	PubMed
	nef	Structure analyses reveal that an RT loop region (residues 90-108) in the Hck SH3 domain binds to the PXXP motif (residues 69-78) of HIV-1 Nef; proline residues substituted by alanine in the PXXP motif abolish its binding to Hck	PubMed
	nef	HIV-1 Nef induces accumulation of Hck at the recycling endosomes and the trans-Golgi network by blocking the anterograde transport of Hck to the plasma membrane	PubMed
	nef	HIV-1 Nef associates with Hck in HIV-1 virions derived from 293T cells and primary monocyte-derived macrophages	PubMed
	nef	Molecular modeling has identified three residues in the core region of Nef from HIV-1 SF2 (Ala83, His116, and Tyr120) that are required for Hck recruitment and activation	PubMed
	nef	HIV-1 Nef activates endogenous Hck in the granulocyte-macrophage colony-stimulating factor-dependent human myeloid cell line, TF-1, resulting in TF-1 cytokine-independence and Stat 3 activation	PubMed
	nef	The Nef-HCK complex involves the Nef PXXPXR motif intercalating with the HCK SH3 surface residues Tyr-90, Tyr-92, Trp-118, Pro-133, and Tyr-136	PubMed
	nef	HCK SH2 kinase linker residues Pro250 and Pro253 make stable hydrophobic contacts with SH3 domain residues Tyr90, Trp118, and Tyr136 to stabilize the HIV-1 Nef dimer interface	PubMed
	nef	The binding of HIV-1 Nef to the SH3 domain of Hck is required for Nef/activated PAK2 complex formation. A new locus GFP/F (G67, F68, P69 and F90) of Nef is involved in the Nef/activated PAK2 complex formation	PubMed
	nef	Diaminoquinoxaline benzenesulfonamide (DQBS) treatment reduces the amount of both HCK and the p85 regulatory subunit of PI3K associated with HIV-1 Nef and completely blocks Nef-dependent activation of ZAP-70	PubMed
	nef	The Nef/hnRNPK/PKC-delta/Hck protein complex activates Pak2 activity but inhibits Pak1 activity, which induces paxillin phosphorylation on Ser272/274 and regulates paxillin/TACE association and secretion	PubMed
	nef	The Nef/hnRNPK/PKC-delta/Hck protein complex increases paxillin phosphorylation at position Y118 and activates and secrets TACE through Erk1/2 activation	PubMed
	nef	The first 18 amino acids (SH4 domain) of Hck, including the myristoylation site (G2), are required for the HIV-1 Nef-induced accumulation of Hck at the recycling endosomes and the trans-Golgi network	PubMed
	nef	The HIV-1 Nef highly conserved valine-glycine-phenylalanine amino acid triplet (VGF) motif is required for the physical interaction of the adjacent proline-rich motif with Hck	PubMed
	nef	In promonocytic cells, Nef/Hck complex recruits the ZAP-70 homolog Syk to downregulate MHC-I	PubMed
	nef	Nef/Hck complex recruits and phosphorylates the tyrosine kinase ZAP-70, which binds class I PI3K to trigger MHC-I downregulation in primary CD4+ T cells	PubMed
	nef	PACS-1S278A mutant blocks the association of Nef with Hck on the cell membrane, while wild-type PACS-1 has no effect	PubMed
	nef	HIV-1 Nef binds Hck and induces skewed Golgi-localization of Hck, which leads to Fms maturation arrest	PubMed
	nef	HIV-1 Nef-induced activation of p61Hck is required for the formation of multinucleated giant cells (MGCs), which is dependent on lysosomal proteins including vacuolar adenosine triphosphatase and proteases participated in Nef-induced MGCs	PubMed
	nef	The primary M-group HIV-1 Nef proteins (from A, B, C, F, G, H, J, and K subtypes) strongly activate HCK in cells	PubMed
	nef	HIV-1 Nef causes the FMS N-glycosylation defect and induces relocalization of the GM130 by activating the p56Hck/MEK/ERK/GRASP65 phosphorylation cascade in the Golgi	PubMed
	nef	The interaction of SIV Nef with human Hck is not mediated via conserved proline-rich motifs, which are known to mediate HIV-1 Nef binding to the Hck SH3 domain; instead, SIV Nef binds the Hck SH2 domain	PubMed
	nef	Hck binds to HIV-1 subtype B and E Nef proteins with equal affinity, but has weaker binding to HIV-2 subtype A Nef and no binding to HIV-2 subtype B Nef	PubMed
	nef	Peptides derived from the Hck SH3 domain with high affinity binding to HIV-1 Nef inhibit SH3-dependent Nef functions, such as association with PAK2 and induction of NFAT	PubMed
	nef	A dominant-negative mutant protein derived from Hck, (composed of the N-terminal region, SH2, and SH3 domains) interacts with HIV-1 Nef and inhibits Nef-induced downregulation of MHC class I	PubMed
	nef	HIV-1 Nef increases the amount of intracellular stored Ca2+ in myelomonocytic cells through binding to Hck	PubMed
	nef	HIV-1 Nef-induced aberrant molecular formation between Hck and M-CSF receptor inhibits M-CSF bioactivities in monocytes/macrophages	PubMed
	nef	In Rat-2 fibroblasts co-expressing Hck and a Nef fusion protein with the hormone-binding domain of estrogen receptor (Nef-ER), 4-hydroxytamoxifen treatment induces Nef-ER oligomerization, leading to Hck kinase activation and cellular transformation	PubMed
	nef	HIV-1 Nef alleles (HIV-1 SF2, LAI and Consensus) bind and activate Hck, while HIV-1 ELI Nef fails to bind to the Hck SH3 domain in vitro and does not cooperate with Hck in fibroblast transformation	PubMed
	nef	Induction of AP-1 by HIV-1 Nef is a specific feature of human and murine macrophage cell lines that requires signal transduction events involving Hck and MAPK	PubMed
Vif	vif	The interaction of Hck with HIV-1 Vif affects Vif oligomerization in living cells	PubMed
	vif	Vif binds specifically to the Src homology 3 domain of Hck, represses the kinase activity of Hck, and suppresses negative effects of Hck on HIV-1 replication	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Markers

HCK (e-PCR)
- UniSTS:253721

D20S512E (e-PCR)
- UniSTS:150311

D20S727 (e-PCR)
- UniSTS:62512

SGC34341 (e-PCR)
- UniSTS:45621

RH92890 (e-PCR)
- UniSTS:90960

336XG5 (e-PCR)
- UniSTS:13699

RH45427 (e-PCR)
- UniSTS:81800

AL031189 (e-PCR)
- UniSTS:21946

G09843 (e-PCR)
- UniSTS:65997

SHGC-112528 (e-PCR)
- UniSTS:168682

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables histone H2AXY142 kinase activity	IEA Inferred from Electronic Annotation more info
enables histone H3Y41 kinase activity	IEA Inferred from Electronic Annotation more info
enables lipid binding	EXP Inferred from Experiment more info	PubMed
enables non-membrane spanning protein tyrosine kinase activity	IBA Inferred from Biological aspect of Ancestor more info
enables phosphotyrosine residue binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein tyrosine kinase activity	EXP Inferred from Experiment more info	PubMed
enables protein tyrosine kinase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein tyrosine kinase activity	TAS Traceable Author Statement more info
enables signaling receptor binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in Fc-gamma receptor signaling pathway involved in phagocytosis	TAS Traceable Author Statement more info
involved_in cell adhesion	TAS Traceable Author Statement more info	PubMed
involved_in cell differentiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in cell surface receptor protein tyrosine kinase signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
involved_in cytokine-mediated signaling pathway	TAS Traceable Author Statement more info	PubMed
involved_in inflammatory response	IEA Inferred from Electronic Annotation more info
involved_in innate immune response-activating signaling pathway	TAS Traceable Author Statement more info	PubMed
involved_in integrin-mediated signaling pathway	TAS Traceable Author Statement more info	PubMed
involved_in intracellular signal transduction	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in leukocyte degranulation	TAS Traceable Author Statement more info	PubMed
involved_in leukocyte migration involved in immune response	TAS Traceable Author Statement more info	PubMed
involved_in lipopolysaccharide-mediated signaling pathway	TAS Traceable Author Statement more info	PubMed
involved_in mesoderm development	TAS Traceable Author Statement more info	PubMed
involved_in negative regulation of apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of inflammatory response to antigenic stimulus	TAS Traceable Author Statement more info
involved_in peptidyl-tyrosine phosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of actin filament polymerization	TAS Traceable Author Statement more info	PubMed
involved_in positive regulation of cell population proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein autophosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein phosphorylation	TAS Traceable Author Statement more info	PubMed
involved_in regulation of DNA-binding transcription factor activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of actin cytoskeleton organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of cell shape	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of inflammatory response	TAS Traceable Author Statement more info	PubMed
involved_in regulation of phagocytosis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of podosome assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in respiratory burst after phagocytosis	TAS Traceable Author Statement more info	PubMed
involved_in type II interferon-mediated signaling pathway	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
colocalizes_with actin filament	IDA Inferred from Direct Assay more info	PubMed
located_in caveola	IDA Inferred from Direct Assay more info	PubMed
located_in cell projection	IEA Inferred from Electronic Annotation more info
located_in cytoplasmic side of plasma membrane	IMP Inferred from Mutant Phenotype more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	TAS Traceable Author Statement more info
located_in focal adhesion	IMP Inferred from Mutant Phenotype more info	PubMed
located_in intracellular membrane-bounded organelle	IDA Inferred from Direct Assay more info
located_in lysosome	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IDA Inferred from Direct Assay more info
located_in transport vesicle	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: tyrosine-protein kinase HCK

Names: hematopoietic cell kinase; hemopoietic cell kinase; p59-HCK/p60-HCK

NP_001165600.1

EC 2.7.10.2

NP_001165601.1

EC 2.7.10.2

NP_001165602.1

EC 2.7.10.2

NP_001165603.1

EC 2.7.10.2

NP_001165604.1

EC 2.7.10.2

NP_002101.2

EC 2.7.10.2

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_029471.1 RefSeqGene

Range

5055..54669

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001172129.3 → NP_001165600.1 tyrosine-protein kinase HCK isoform b

See identical proteins and their annotated locations for NP_001165600.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes two isoforms due to the use of alternative translation initiation codons, as demonstrated in PMIDs 1875927 and 7791757. The longer isoform (a, also known as p61HCK) is derived from an upstream non-AUG (CUG) start codon, while the shorter isoform (b, also known as p59HCK) is derived from a downstream AUG start codon. The shorter isoform (b) is represented in this RefSeq. Both variants 1 and 4 encode isoform b.

Source sequence(s)

AL049539, AW139272, BC114463, DA465978

Consensus CDS

CCDS54455.1

UniProtKB/TrEMBL

J3KPD6

Related

ENSP00000429848.1, ENST00000520553.5

Conserved Domains (3) summary

cd10363
Location:119 → 222

SH2_Src_HCK; Src homology 2 (SH2) domain found in HCK

cl17036
Location:61 → 116

SH3; Src Homology 3 domain superfamily

cl21453
Location:233 → 503

PKc_like; Protein Kinases, catalytic domain
NM_001172130.3 → NP_001165601.1 tyrosine-protein kinase HCK isoform c

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses an alternate in-frame splice site in the 5' coding region, compared to variant 1. This variant encodes two isoforms due to the use of alternative translation initiation codons, as demonstrated in PMIDs 1875927 and 7791757. The longer isoform (c) is derived from an upstream non-AUG (CUG) start codon, while the shorter isoform (d) is derived from a downstream AUG start codon. The longer isoform (c) is represented in this RefSeq, but it is overall shorter, compared to isoform a.

Source sequence(s)

AK289896, AL049539, AW139272, BC113854, DA465978

Consensus CDS

CCDS54453.1

UniProtKB/TrEMBL

H0Y3C5

Related

ENSP00000365022.3, ENST00000375862.7

Conserved Domains (4) summary

cd10363
Location:139 → 242

SH2_Src_HCK; Src homology 2 (SH2) domain found in HCK

pfam07714
Location:261 → 510

Pkinase_Tyr; Protein tyrosine kinase

cl17036
Location:81 → 136

SH3; Src Homology 3 domain superfamily

cl21453
Location:253 → 523

PKc_like; Protein Kinases, catalytic domain
NM_001172131.3 → NP_001165602.1 tyrosine-protein kinase HCK isoform d

See identical proteins and their annotated locations for NP_001165602.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses an alternate in-frame splice site in the 5' coding region, compared to variant 1. This variant encodes two isoforms due to the use of alternative translation initiation codons, as demonstrated in PMIDs 1875927 and 7791757. The longer isoform (c) is derived from an upstream non-AUG (CUG) start codon, while the shorter isoform (d) is derived from a downstream AUG start codon. The shorter isoform (d) is represented in this RefSeq, and is overall shorter, compared to isoform a.

Source sequence(s)

AK289896, AL049539, AW139272, BC113854, DA465978

Consensus CDS

CCDS54456.1

UniProtKB/TrEMBL

H0Y3C5

Related

ENSP00000427757.1, ENST00000518730.5

Conserved Domains (4) summary

cd10363
Location:118 → 221

SH2_Src_HCK; Src homology 2 (SH2) domain found in HCK

pfam07714
Location:240 → 489

Pkinase_Tyr; Protein tyrosine kinase

cl17036
Location:60 → 115

SH3; Src Homology 3 domain superfamily

cl21453
Location:232 → 502

PKc_like; Protein Kinases, catalytic domain
NM_001172132.3 → NP_001165603.1 tyrosine-protein kinase HCK isoform e

See identical proteins and their annotated locations for NP_001165603.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) differs in its 5' UTR and uses an alternate AUG translation start codon, compared to variant 1. The encoded isoform (e) has a distinct and shorter N-terminus, compared to isoform a.

Source sequence(s)

AK290928, AL049539

UniProtKB/TrEMBL

A8K4G3, J3KPD6

Conserved Domains (4) summary

cd10363
Location:120 → 223

SH2_Src_HCK; Src homology 2 (SH2) domain found in HCK

pfam07714
Location:242 → 491

Pkinase_Tyr; Protein tyrosine kinase

cl17036
Location:62 → 117

SH3; Src Homology 3 domain superfamily

cl21453
Location:234 → 504

PKc_like; Protein Kinases, catalytic domain
NM_001172133.3 → NP_001165604.1 tyrosine-protein kinase HCK isoform b

See identical proteins and their annotated locations for NP_001165604.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) differs in its 5' UTR and uses the downstream AUG start codon, compared to variant 1, resulting in an isoform (b) that is shorter at the N-terminus, compared to isoform a. Both variants 1 and 4 encode isoform b.

Source sequence(s)

AK298726, AL049539, AW139272

Consensus CDS

CCDS54455.1

UniProtKB/TrEMBL

J3KPD6

Related

ENSP00000486627.1, ENST00000629881.2

Conserved Domains (3) summary

cd10363
Location:119 → 222

SH2_Src_HCK; Src homology 2 (SH2) domain found in HCK

cl17036
Location:61 → 116

SH3; Src Homology 3 domain superfamily

cl21453
Location:233 → 503

PKc_like; Protein Kinases, catalytic domain
NM_002110.5 → NP_002101.2 tyrosine-protein kinase HCK isoform a

See identical proteins and their annotated locations for NP_002101.2

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes two isoforms due to the use of alternative translation initiation codons, as demonstrated in PMIDs 1875927 and 7791757. The longer isoform (a, also known as p61HCK) is derived from an upstream non-AUG (CUG) start codon, while the shorter isoform (b, also known as p59HCK) is derived from a downstream AUG start codon. The longer isoform (a) is represented in this RefSeq.

Source sequence(s)

AL049539, AW139272, BC114463, DA465978

Consensus CDS

CCDS33460.1

UniProtKB/Swiss-Prot

A8K1I1, B4DQB6, E1P5M2, P08631, Q29RX1, Q2VPE2, Q504R5, Q5T7K1, Q5T7K2, Q96CC0, Q9H5Y5, Q9NUA4, Q9UMJ5

UniProtKB/TrEMBL

J3KPD6

Related

ENSP00000365012.3, ENST00000375852.5

Conserved Domains (4) summary

cd10363
Location:140 → 243

SH2_Src_HCK; Src homology 2 (SH2) domain found in HCK

pfam07714
Location:262 → 511

Pkinase_Tyr; Protein tyrosine kinase

cl17036
Location:82 → 137

SH3; Src Homology 3 domain superfamily

cl21453
Location:254 → 524

PKc_like; Protein Kinases, catalytic domain