dbPTM

HCLS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HCLS1_HUMAN
UniProt AC	P14317
Protein Name	Hematopoietic lineage cell-specific protein
Gene Name	HCLS1
Organism	Homo sapiens (Human).
Sequence Length	486
Subcellular Localization	Membrane Peripheral membrane protein . Cytoplasm . Mitochondrion .
Protein Description	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..
Protein Sequence	MWKSVVGHDVSVSVETQGDDWDTDPDFVNDISEKEQRWGAKTIEGSGRTEHINIHQLRNKVSEEHDVLRKKEMESGPKASHGYGGRFGVERDRMDKSAVGHEYVAEVEKHSSQTDAAKGFGGKYGVERDRADKSAVGFDYKGEVEKHTSQKDYSRGFGGRYGVEKDKWDKAALGYDYKGETEKHESQRDYAKGFGGQYGIQKDRVDKSAVGFNEMEAPTTAYKKTTPIEAASSGTRGLKAKFESMAEEKRKREEEEKAQQVARRQQERKAVTKRSPEAPQPVIAMEEPAVPAPLPKKISSEAWPPVGTPPSSESEPVRTSREHPVPLLPIRQTLPEDNEEPPALPPRTLEGLQVEEEPVYEAEPEPEPEPEPEPENDYEDVEEMDRHEQEDEPEGDYEEVLEPEDSSFSSALAGSSGCPAGAGAGAVALGISAVAVYDYQGEGSDELSFDPDDVITDIEMVDEGWWRGRCHGHFGLFPANYVKLLE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	SVVGHDVSVSVETQG CCCCCEEEEEEEECC	18.09	30576142
13	Phosphorylation	VGHDVSVSVETQGDD CCCEEEEEEEECCCC	13.51	28348404
16	Phosphorylation	DVSVSVETQGDDWDT EEEEEEEECCCCCCC	35.38	22817900
23	Phosphorylation	TQGDDWDTDPDFVND ECCCCCCCCHHHHHH	45.22	30576142
32	Phosphorylation	PDFVNDISEKEQRWG HHHHHHCCHHHHHHC	45.54	-
34	Ubiquitination	FVNDISEKEQRWGAK HHHHCCHHHHHHCCE	52.97	-
41	Acetylation	KEQRWGAKTIEGSGR HHHHHCCEECCCCCC	46.20	19608861
41	Acetylation	KEQRWGAKTIEGSGR HHHHHCCEECCCCCC	46.20	-
41	Ubiquitination	KEQRWGAKTIEGSGR HHHHHCCEECCCCCC	46.20	19608861
42	Phosphorylation	EQRWGAKTIEGSGRT HHHHCCEECCCCCCC	24.59	-
46	Phosphorylation	GAKTIEGSGRTEHIN CCEECCCCCCCCCCC	16.59	27080861
49	Phosphorylation	TIEGSGRTEHINIHQ ECCCCCCCCCCCHHH	35.13	27080861
60	Ubiquitination	NIHQLRNKVSEEHDV CHHHHHHHHHHHHHH	40.48	-
60	Ubiquitination	NIHQLRNKVSEEHDV CHHHHHHHHHHHHHH	40.48	29967540
62	Phosphorylation	HQLRNKVSEEHDVLR HHHHHHHHHHHHHHH	38.59	23401153
71	Ubiquitination	EHDVLRKKEMESGPK HHHHHHHHHHHCCCC	56.72	24816145
83	Phosphorylation	GPKASHGYGGRFGVE CCCCCCCCCCCCCCC	15.81	-
96	Acetylation	VERDRMDKSAVGHEY CCCCCCCHHHCCHHH	30.85	25953088
97	Phosphorylation	ERDRMDKSAVGHEYV CCCCCCHHHCCHHHH	24.75	28450419
103	Phosphorylation	KSAVGHEYVAEVEKH HHHCCHHHHHHHHHH	10.17	28674151
111	Phosphorylation	VAEVEKHSSQTDAAK HHHHHHHCCCCHHCC	34.90	29978859
112	Phosphorylation	AEVEKHSSQTDAAKG HHHHHHCCCCHHCCC	36.50	28857561
114	Phosphorylation	VEKHSSQTDAAKGFG HHHHCCCCHHCCCCC	29.56	28857561
118	Ubiquitination	SSQTDAAKGFGGKYG CCCCHHCCCCCCCCC	57.40	29967540
123	Ubiquitination	AAKGFGGKYGVERDR HCCCCCCCCCCCCCC	38.93	-
123	Acetylation	AAKGFGGKYGVERDR HCCCCCCCCCCCCCC	38.93	19608861
123	Ubiquitination	AAKGFGGKYGVERDR HCCCCCCCCCCCCCC	38.93	19608861
124	Phosphorylation	AKGFGGKYGVERDRA CCCCCCCCCCCCCCC	29.67	-
134	Phosphorylation	ERDRADKSAVGFDYK CCCCCCHHCCCCCCC	28.83	29083192
140	Phosphorylation	KSAVGFDYKGEVEKH HHCCCCCCCCCEEEE	20.73	29978859
141	Acetylation	SAVGFDYKGEVEKHT HCCCCCCCCCEEEEC	50.90	25953088
148	Phosphorylation	KGEVEKHTSQKDYSR CCCEEEECCCCCCCC	43.87	28857561
149	Phosphorylation	GEVEKHTSQKDYSRG CCEEEECCCCCCCCC	34.65	23401153
153	Phosphorylation	KHTSQKDYSRGFGGR EECCCCCCCCCCCCC	13.80	22817900
154	Phosphorylation	HTSQKDYSRGFGGRY ECCCCCCCCCCCCCC	35.74	-
155	Methylation	TSQKDYSRGFGGRYG CCCCCCCCCCCCCCC	37.93	115384307
161	Phosphorylation	SRGFGGRYGVEKDKW CCCCCCCCCCCCCCC	28.88	29978859
165	Ubiquitination	GGRYGVEKDKWDKAA CCCCCCCCCCCCHHH	63.30	24816145
165	Acetylation	GGRYGVEKDKWDKAA CCCCCCCCCCCCHHH	63.30	26822725
170	Ubiquitination	VEKDKWDKAALGYDY CCCCCCCHHHCCCCC	34.15	29967540
175	Phosphorylation	WDKAALGYDYKGETE CCHHHCCCCCCCCCC	19.56	28796482
177	Phosphorylation	KAALGYDYKGETEKH HHHCCCCCCCCCCCC	16.65	28796482
181	Phosphorylation	GYDYKGETEKHESQR CCCCCCCCCCCHHHH	60.03	29978859
186	Phosphorylation	GETEKHESQRDYAKG CCCCCCHHHHHHHHC	30.18	29978859
190	Phosphorylation	KHESQRDYAKGFGGQ CCHHHHHHHHCCCCC	16.64	29978859
192	Acetylation	ESQRDYAKGFGGQYG HHHHHHHHCCCCCCC	48.85	19608861
192	Ubiquitination	ESQRDYAKGFGGQYG HHHHHHHHCCCCCCC	48.85	19608861
198	Phosphorylation	AKGFGGQYGIQKDRV HHCCCCCCCCCCCCC	21.33	28674151
202	Ubiquitination	GGQYGIQKDRVDKSA CCCCCCCCCCCCHHH	45.65	24816145
204	Acetylation	QYGIQKDRVDKSAVG CCCCCCCCCCHHHCC	45.64	19608861
204	Ubiquitination	QYGIQKDRVDKSAVG CCCCCCCCCCHHHCC	45.64	24816145
208	Phosphorylation	QKDRVDKSAVGFNEM CCCCCCHHHCCCCCC	24.59	27251275
212	Ubiquitination	VDKSAVGFNEMEAPT CCHHHCCCCCCCCCC	5.86	27667366
219	Phosphorylation	FNEMEAPTTAYKKTT CCCCCCCCCCCCCCC	30.98	29978859
220	Phosphorylation	NEMEAPTTAYKKTTP CCCCCCCCCCCCCCC	27.25	29978859
220	Ubiquitination	NEMEAPTTAYKKTTP CCCCCCCCCCCCCCC	27.25	24816145
222	Phosphorylation	MEAPTTAYKKTTPIE CCCCCCCCCCCCCHH	15.78	28674151
223	Acetylation	EAPTTAYKKTTPIEA CCCCCCCCCCCCHHH	40.97	25953088
224	Acetylation	APTTAYKKTTPIEAA CCCCCCCCCCCHHHH	44.98	22361441
232	Phosphorylation	TTPIEAASSGTRGLK CCCHHHHHCCCHHHH	36.03	28857561
235	Phosphorylation	IEAASSGTRGLKAKF HHHHHCCCHHHHHHH	24.42	28857561
239	Ubiquitination	SSGTRGLKAKFESMA HCCCHHHHHHHHHHH	52.97	-
241	Ubiquitination	GTRGLKAKFESMAEE CCHHHHHHHHHHHHH	48.34	24816145
241	Acetylation	GTRGLKAKFESMAEE CCHHHHHHHHHHHHH	48.34	19608861
249	Ubiquitination	FESMAEEKRKREEEE HHHHHHHHHHHHHHH	55.51	27667366
257	Ubiquitination	RKREEEEKAQQVARR HHHHHHHHHHHHHHH	55.57	24816145
272	Phosphorylation	QQERKAVTKRSPEAP HHHHHHHHCCCCCCC	26.12	23401153
275	Phosphorylation	RKAVTKRSPEAPQPV HHHHHCCCCCCCCCE	28.75	28674151
285	Sulfoxidation	APQPVIAMEEPAVPA CCCCEEEECCCCCCC	4.05	21406390
299	Phosphorylation	APLPKKISSEAWPPV CCCCCCCCCCCCCCC	30.88	23401153
300	Phosphorylation	PLPKKISSEAWPPVG CCCCCCCCCCCCCCC	34.50	28787133
308	Phosphorylation	EAWPPVGTPPSSESE CCCCCCCCCCCCCCC	32.06	23401153
311	Phosphorylation	PPVGTPPSSESEPVR CCCCCCCCCCCCCCC	48.19	28348404
311	O-linked_Glycosylation	PPVGTPPSSESEPVR CCCCCCCCCCCCCCC	48.19	27655845
312	Phosphorylation	PVGTPPSSESEPVRT CCCCCCCCCCCCCCC	51.41	28348404
312	O-linked_Glycosylation	PVGTPPSSESEPVRT CCCCCCCCCCCCCCC	51.41	27655845
314	O-linked_Glycosylation	GTPPSSESEPVRTSR CCCCCCCCCCCCCCC	49.50	27655845
314	Phosphorylation	GTPPSSESEPVRTSR CCCCCCCCCCCCCCC	49.50	28348404
319	Phosphorylation	SESEPVRTSREHPVP CCCCCCCCCCCCCCC	32.16	30108239
320	Phosphorylation	ESEPVRTSREHPVPL CCCCCCCCCCCCCCC	25.71	30108239
333	Phosphorylation	PLLPIRQTLPEDNEE CCCCCCCCCCCCCCC	34.14	27080861
360	Phosphorylation	QVEEEPVYEAEPEPE EEEEECCCCCCCCCC	21.82	28796482
378	Phosphorylation	EPEPENDYEDVEEMD CCCCCCCCCCHHHHH	26.13	22679023
397	Phosphorylation	EDEPEGDYEEVLEPE CCCCCCCHHHHCCCC	25.50	22679023
481	Phosphorylation	FGLFPANYVKLLE-- CCCCCHHHHHHCC--	10.89	29978859

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
16	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
23	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
222	Y	Phosphorylation	Kinase	FGR	P09769	Uniprot
222	Y	Phosphorylation	Kinase	FGR	Q6P6U0	PSP
222	Y	Phosphorylation	Kinase	LYN	P07948	PSP
222	Y	Phosphorylation	Kinase	LYN	Q07014	PSP
378	Y	Phosphorylation	Kinase	FES	P07332	Uniprot
378	Y	Phosphorylation	Kinase	SYK	P43405	Uniprot
378	Y	Phosphorylation	Kinase	LYN	P07948	PhosphoELM
378	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
397	Y	Phosphorylation	Kinase	FES	P07332	Uniprot
397	Y	Phosphorylation	Kinase	FGR	P09769	PhosphoELM
397	Y	Phosphorylation	Kinase	SYK	P43405	Uniprot
397	Y	Phosphorylation	Kinase	LYN	P07948	PhosphoELM
397	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HCLS1_HUMAN !!

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 HCLS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH24A_HUMAN	SH2D4A	physical	16189514
ARP3_HUMAN	ACTR3	physical	12534372
FGR_HUMAN	FGR	physical	10066823
M4K1_HUMAN	MAP4K1	physical	10233887
CD79A_HUMAN	CD79A	physical	7927516
ZBT25_HUMAN	ZBTB25	physical	20211142
LZTR1_HUMAN	LZTR1	physical	20211142
NEMO_HUMAN	IKBKG	physical	20211142
GO45_HUMAN	BLZF1	physical	20211142
SSBP3_HUMAN	SSBP3	physical	20211142
TRI29_HUMAN	TRIM29	physical	20211142
SH24A_HUMAN	SH2D4A	physical	25416956
KCNA3_HUMAN	KCNA3	physical	25739456
SNX1_HUMAN	SNX1	physical	28514442
SNX5_HUMAN	SNX5	physical	28514442

Drug and Disease Associations

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

Regulatory Network of HCLS1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-123; LYS-192 ANDLYS-241, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND THR-308, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-103 AND SER-275, ANDMASS SPECTROMETRY.	16094384 [Abstract]
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198, AND MASSSPECTROMETRY.	12522270 [Abstract]
"Molecular features underlying the sequential phosphorylation of HS1protein and its association with c-Fgr protein-tyrosine kinase."; Brunati A.M., Donella-Deana A., James P., Quadroni M., Contri A.,Marin O., Pinna L.A.; J. Biol. Chem. 274:7557-7564(1999). Cited for: PHOSPHORYLATION AT TYR-222 AND TYR-397, MASS SPECTROMETRY, ANDINTERACTION WITH FGR.	10066823 [Abstract]
"SH2 domains mediate the sequential phosphorylation of HS1 protein byp72syk and Src-related protein tyrosine kinases."; Ruzzene M., Brunati A.M., Marin O., Donella-Deana A., Pinna L.A.; Biochemistry 35:5327-5332(1996). Cited for: PHOSPHORYLATION AT TYR-222 AND TYR-397, AND PHOSPHORYLATION BY SYK;LYN; FYN AND FGR.	8611520 [Abstract]