dbPTM

HCK_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HCK_MOUSE
UniProt AC	P08103
Protein Name	Tyrosine-protein kinase HCK
Gene Name	Hck
Organism	Mus musculus (Mouse).
Sequence Length	524
Subcellular Localization	Cytoplasmic vesicle, secretory vesicle. Cytoplasm, cytosol. Isoform 1: Membrane Lipid-anchor. Membrane, caveola. Lysosome. Cell projection, podosome membrane Lipid-anchor. Cytoplasm, cytosol. Associated with specialized secretory lysosomes called
Protein Description	Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS (By similarity)..
Protein Sequence	MGGRSSCEDPGCPRSEGRAPRMGCVKSRFLRDGSKASKTEPSANQKGPVYVPDPTSSSKLGPNNSNSMPPGFVEGSEDTIVVALYDYEAIHREDLSFQKGDQMVVLEEAGEWWKARSLATKKEGYIPSNYVARVNSLETEEWFFKGISRKDAERHLLAPGNMLGSFMIRDSETTKGSYSLSVRDFDPQHGDTVKHYKIRTLDSGGFYISPRSTFSSLQELVLHYKKGKDGLCQKLSVPCVSPKPQKPWEKDAWEIPRESLQMEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANLMKSLQHDKLVKLHAVVSQEPIFIVTEFMAKGSLLDFLKSEEGSKQPLPKLIDFSAQISEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARIIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALEHGYRMPRPDNCPEELYNIMIRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGGRSSCED ------CCCCCCCCC	39.97	-
2 (in isoform 2)	Myristoylation	-	39.97	-
3 (in isoform 2)	S-palmitoylation	-	25.62	-
25	Ubiquitination	RAPRMGCVKSRFLRD CCCCCCEEEHHHCCC	5.37	27667366
27	Phosphorylation	PRMGCVKSRFLRDGS CCCCEEEHHHCCCCC	14.10	24719451
34	Phosphorylation	SRFLRDGSKASKTEP HHHCCCCCCCCCCCC	29.36	19144319
37	Phosphorylation	LRDGSKASKTEPSAN CCCCCCCCCCCCCCC	43.79	30635358
39	Phosphorylation	DGSKASKTEPSANQK CCCCCCCCCCCCCCC	51.11	30635358
42	Phosphorylation	KASKTEPSANQKGPV CCCCCCCCCCCCCCE	33.35	30635358
46	Ubiquitination	TEPSANQKGPVYVPD CCCCCCCCCCEECCC	66.06	27667366
50	Phosphorylation	ANQKGPVYVPDPTSS CCCCCCEECCCCCCC	14.92	25159016
55	Phosphorylation	PVYVPDPTSSSKLGP CEECCCCCCCCCCCC	48.93	30635358
56	Phosphorylation	VYVPDPTSSSKLGPN EECCCCCCCCCCCCC	37.69	30635358
57	Phosphorylation	YVPDPTSSSKLGPNN ECCCCCCCCCCCCCC	33.69	30635358
58	Phosphorylation	VPDPTSSSKLGPNNS CCCCCCCCCCCCCCC	31.50	30635358
85	Phosphorylation	DTIVVALYDYEAIHR CEEEEEEECHHHHCH	13.52	-
125	Phosphorylation	LATKKEGYIPSNYVA HCCCCCCCCCCCCEE	15.68	30635358
200	Phosphorylation	VKHYKIRTLDSGGFY EEEEEEEECCCCCEE	38.09	25177544
203	Phosphorylation	YKIRTLDSGGFYISP EEEEECCCCCEEECC	43.88	25367039
207	Phosphorylation	TLDSGGFYISPRSTF ECCCCCEEECCCCCC	12.08	19144319
209	Phosphorylation	DSGGFYISPRSTFSS CCCCEEECCCCCCCC	11.68	25367039
289	Phosphorylation	HTKVAVKTMKPGSMS CCCEEEEECCCCCCC	24.67	30482847
409	Phosphorylation	RIIEDNEYTAREGAK EEECCCCEECCCCCC	16.38	25521595
410	Phosphorylation	IIEDNEYTAREGAKF EECCCCEECCCCCCC	17.04	22499769
460	Phosphorylation	RIPYPGMSNPEVIRA CCCCCCCCCHHHHHH	55.97	29472430
513	Phosphorylation	QSVLDDFYTATESQY HHHHHHHHHHHHHHH	11.49	25367039
514	Phosphorylation	SVLDDFYTATESQYQ HHHHHHHHHHHHHHH	27.39	25367039
516	Phosphorylation	LDDFYTATESQYQQQ HHHHHHHHHHHHHCC	28.50	25367039
518	Phosphorylation	DFYTATESQYQQQP- HHHHHHHHHHHCCC-	29.81	25367039
520	Phosphorylation	YTATESQYQQQP--- HHHHHHHHHCCC---	19.98	19144319

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
29	Y	Phosphorylation	Kinase	HCK	P08103	GPS
50	Y	Phosphorylation	Kinase	HCK	P08103	PSP
388	Y	Phosphorylation	Kinase	HCK	P08103	GPS
409	Y	Phosphorylation	Kinase	HCK	P08103	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HCK_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HCK_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DVL2_MOUSE	Dvl2	physical	19920076
CBL_MOUSE	Cbl	physical	10799548
CBL_MOUSE	Cbl	physical	9890970

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HCK_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; TYR-207 AND TYR-409,AND MASS SPECTROMETRY.	19144319 [Abstract]
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-409, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-409, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Modulation of the catalytic activity of the Src family tyrosinekinase Hck by autophosphorylation at a novel site in the uniquedomain."; Johnson T.M., Williamson N.A., Scholz G., Jaworowski A.,Wettenhall R.E., Dunn A.R., Cheng H.C.; J. Biol. Chem. 275:33353-33364(2000). Cited for: PHOSPHORYLATION AT TYR-50 AND TYR-409, MUTAGENESIS OF TYR-409, ANDENZYME REGULATION.	10934191 [Abstract]