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HS1 (human)

Overview HS1 Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression. Associates with the SH2 and SH3 domains of LCK. Binding to he LCK SH3 domain occurs constitutively, while binding to the LCK SH2 domain occurs only upon TCR stimulation. A similar binding pattern was observed with LYN, but not with FYN in which the FYN SH2 region associates upon TCR stimulation but the FYN SH3 region does not associate regardless of TCR stimulation. Directly associates with HAX1, through binding to its C-terminal region. Interacts with HS1BP3. Interacts with FES/FPS. Interacts (via SH2 domain) with FGR. Forms a multiprotein complex with LYN and ANKRD54. Expressed only in tissues and cells of hematopoietic origin. Note: This description may include information from UniProtKB. Protein type: Adaptor/scaffold; Motility/polarity/chemotaxis Cellular Component: mitochondrion; cytoplasm; plasma membrane; nucleus Molecular Function: DNA binding; protein complex binding; SH3 domain binding; transcription factor activity Biological Process: positive regulation of tyrosine phosphorylation of STAT protein; regulation of transcription, DNA-dependent; positive regulation of cell proliferation; response to hormone stimulus; erythrocyte differentiation Reference #:  P14317 (UniProtKB) Alt. Names/Synonyms: cortactin-like; CTTNL; HCLS1; Hematopoietic cell-specific LYN substrate 1; Hematopoietic lineage cell-specific protein; HS1; LckBP1; p75 Gene Symbols: HCLS1 Molecular weight: 54,014 Da Basal Isoelectric point: 4.74  Predict pI for various phosphorylation states CST Pathways:  B Cell Receptor Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below HS1

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	Sites Implicated In
apoptosis, altered: Y378‑p, Y397‑p cell adhesion, altered: Y397‑p cell motility, altered: Y378‑p cytoskeletal reorganization: Y378‑p, Y397‑p transcription, altered: Y378‑p, Y397‑p intracellular localization: Y378‑p, Y397‑p molecular association, regulation: Y378‑p, Y397‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
1	0		T16-p	DVSVSVEtQGDDWDt
1	13		T23-p	tQGDDWDtDPDFVND
0	2		S32-p	PDFVNDIsEkEQRWG
0	1		K34-u	FVNDIsEkEQRWGAk
0	1		K41-a	kEQRWGAktIEGSGR
0	8		T42-p	EQRWGAktIEGSGRT
0	1		K60-u	NIHQLRNkVSEEHDV
0	4		Y83-p	GPKASHGyGGRFGVE
0	1		S97-p	ERDRMDKsAVGHEyV
0	133		Y103-p	KsAVGHEyVAEVEKH
0	1		K123-a	AAKGFGGkyGVERDR
0	26		Y124-p	AKGFGGkyGVERDRA
0	3		S134-p	ERDRADKsAVGFDyk
0	97		Y140-p	KsAVGFDykGEVEKH
0	1		K141-a	sAVGFDykGEVEKHT
0	12		Y153-p	KHTSQKDysRGFGGR
0	6		S154-p	HTSQKDysRGFGGRy
0	3		Y161-p	sRGFGGRyGVEKDKW
0	165		Y175-p	WDKAALGyDyKGEtE
0	118		Y177-p	KAALGyDyKGEtEKH
0	1		T181-p	GyDyKGEtEKHEsQR
0	1		S186-p	GEtEKHEsQRDyAkG
0	1		D189	EKHEsQRDyAkGFGG
0	56		Y190-p	KHEsQRDyAkGFGGQ
0	1		K192-a	EsQRDyAkGFGGQyG
0	276		Y198-p	AkGFGGQyGIQKDRV
0	2		S208-p	QKDRVDKsAVGFNEM
3	141		Y222-p	MEAPTTAykkTTPIE
0	2		K223-a	EAPTTAykkTTPIEA
0	1		K224-a	APTTAykkTTPIEAA
0	1		K239-u	SSGTRGLkAkFESMA
0	1		K241-a	GTRGLkAkFESMAEE
0	26		S275-p	RKAVTKRsPEAPQPV
0	4		T308-p	EAWPPVGtPPSSESE
0	5		H323	PVRTSREHPVPLLPI
0	1		L327	SREHPVPLLPIRQtL
0	1		I330	HPVPLLPIRQtLPED
0	4		T333-p	PLLPIRQtLPEDNEE
0	20		Y360-p	QVEEEPVyEAEPEPE
0	1		P374	EPEPEPEPENDyEDV
7	39		Y378-p	EPEPENDyEDVEEMD
8	9		Y397-p	EDEPEGDyEEVLEPE
0	3		Y481-p	FGLFPANyVKLLE__

	mouse
T16	DVSVSVETQGDDWDT
T23	TQGDDWDTDPDFVND
S32	PDFVNDISEKEQRWG
K34	FVNDISEKEQRWGAK
K41	KEQRWGAKTIEGSGR
T42	EQRWGAKTIEGSGRT
K60	NIHQLRNKVSEEHDI
Y83	GPKASHGYGGRFGVE
S97	ERDRMDKSAVGHEyV
Y103-p	KSAVGHEyVADVEKH
K123	AARGFGGKYGVERDR
Y124	ARGFGGKYGVERDRA
S134	ERDRADKSAVGFDyK
Y140-p	KSAVGFDyKGEVEKH
K141	SAVGFDyKGEVEKHA
Y153-p	KHASQKDySHGFGGR
S154	HASQKDySHGFGGRY
Y161	SHGFGGRYGVEKDKR
Y175-p	RDKAALGyDyKGETE
Y177-p	KAALGyDyKGETEKH
T181	GyDyKGETEKHESQR
S186	GETEKHESQRdYAKG
D189-ca	EKHESQRdYAKGFGG
Y190	KHESQRdYAKGFGGQ
K192	ESQRdYAKGFGGQyG
Y198-p	AKGFGGQyGIQKDRV
S208	QKDRVDKSAVGFNEM
Y222-p	MEAPTTAyKKTTPIE
K223	EAPTTAyKKTTPIEA
K224	APTTAyKKTTPIEAA
K239	SSGARGLKAKFESLA
K241	GARGLKAKFESLAEE
S275	RKAVVKMSREVQQPS
S308	EVWPPAESHLPPESQ
Y323-p	PVRSRREyPVPsLPt
S327-p	RREyPVPsLPtRQsP
T330-p	yPVPsLPtRQsPLQN
S333-p	PsLPtRQsPLQNHLE
Y364-p	QVVEEPVyEAAPELE
T384-p	DYEPEPEtEPDyEDV
Y388-p	EPEtEPDyEDVGELD
Y405-p	DEDAEGDyEDVLEPE
Y482	FGLFPANYVKLL___

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