dbPTM

BYST_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BYST_HUMAN
UniProt AC	Q13895
Protein Name	Bystin
Gene Name	BYSL
Organism	Homo sapiens (Human).
Sequence Length	437
Subcellular Localization	Cytoplasm . Nucleus, nucleolus . Associated with 40S ribosomal subunits.
Protein Description	Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. May be required for trophinin-dependent regulation of cell adhesion during implantation of human embryos..
Protein Sequence	MPKFKAARGVGGQEKHAPLADQILAGNAVRAGVREKRRGRGTGEAEEEYVGPRLSRRILQQARQQQEELEAEHGTGDKPAAPRERTTRLGPRMPQDGSDDEDEEWPTLEKAATMTAAGHHAEVVVDPEDERAIEMFMNKNPPARRTLADIIMEKLTEKQTEVETVMSEVSGFPMPQLDPRVLEVYRGVREVLSKYRSGKLPKAFKIIPALSNWEQILYVTEPEAWTAAAMYQATRIFASNLKERMAQRFYNLVLLPRVRDDVAEYKRLNFHLYMALKKALFKPGAWFKGILIPLCESGTCTLREAIIVGSIITKCSIPVLHSSAAMLKIAEMEYSGANSIFLRLLLDKKYALPYRVLDALVFHFLGFRTEKRELPVLWHQCLLTLVQRYKADLATDQKEALLELLRLQPHPQLSPEIRRELQSAVPRDVEDVPITVE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MPKFKAARGV -----CCCCCCCCCC	59.19	24816145
5	Methylation	---MPKFKAARGVGG ---CCCCCCCCCCCC	47.46	-
8	Methylation	MPKFKAARGVGGQEK CCCCCCCCCCCCCCC	45.23	-
15	Acetylation	RGVGGQEKHAPLADQ CCCCCCCCCCCHHHH	36.86	21466224
15	Ubiquitination	RGVGGQEKHAPLADQ CCCCCCCCCCCHHHH	36.86	19608861
30	Methylation	ILAGNAVRAGVREKR HHHCHHHHHCHHCHH	24.18	-
38	Methylation	AGVREKRRGRGTGEA HCHHCHHCCCCCCCC	50.67	-
40	Methylation	VREKRRGRGTGEAEE HHCHHCCCCCCCCHH	37.37	24129315
42	Phosphorylation	EKRRGRGTGEAEEEY CHHCCCCCCCCHHHH	30.41	21945579
49	Phosphorylation	TGEAEEEYVGPRLSR CCCCHHHHHHHHHHH	17.62	21945579
55	Phosphorylation	EYVGPRLSRRILQQA HHHHHHHHHHHHHHH	22.31	25159151
75	Phosphorylation	ELEAEHGTGDKPAAP HHHHHHCCCCCCCCC	44.08	22210691
78	Acetylation	AEHGTGDKPAAPRER HHHCCCCCCCCCCCC	37.59	25953088
78	Ubiquitination	AEHGTGDKPAAPRER HHHCCCCCCCCCCCC	37.59	29967540
86	Phosphorylation	PAAPRERTTRLGPRM CCCCCCCCCCCCCCC	16.12	26074081
87	Phosphorylation	AAPRERTTRLGPRMP CCCCCCCCCCCCCCC	30.07	29496963
98	Phosphorylation	PRMPQDGSDDEDEEW CCCCCCCCCCCCCCC	50.61	22167270
107	Phosphorylation	DEDEEWPTLEKAATM CCCCCCCHHHHHHHH	48.93	22167270
113	Phosphorylation	PTLEKAATMTAAGHH CHHHHHHHHHHCCCC	21.66	26074081
139	Ubiquitination	AIEMFMNKNPPARRT HHHHHHCCCCCHHHH	60.07	24816145
152	Sulfoxidation	RTLADIIMEKLTEKQ HHHHHHHHHHHHHCC	3.67	21406390
154	Ubiquitination	LADIIMEKLTEKQTE HHHHHHHHHHHCCHH	43.24	21906983
154	2-Hydroxyisobutyrylation	LADIIMEKLTEKQTE HHHHHHHHHHHCCHH	43.24	-
154	Acetylation	LADIIMEKLTEKQTE HHHHHHHHHHHCCHH	43.24	27452117
156	Phosphorylation	DIIMEKLTEKQTEVE HHHHHHHHHCCHHHH	52.80	28188228
158	Ubiquitination	IMEKLTEKQTEVETV HHHHHHHCCHHHHHH	58.23	22817900
160	Phosphorylation	EKLTEKQTEVETVMS HHHHHCCHHHHHHHH	53.73	21712546
164	Phosphorylation	EKQTEVETVMSEVSG HCCHHHHHHHHHHCC	27.04	21712546
167	Phosphorylation	TEVETVMSEVSGFPM HHHHHHHHHHCCCCC	30.43	21712546
170	Phosphorylation	ETVMSEVSGFPMPQL HHHHHHHCCCCCCCC	30.57	21712546
185	Phosphorylation	DPRVLEVYRGVREVL CHHHHHHHHHHHHHH	7.71	28634298
186	Methylation	PRVLEVYRGVREVLS HHHHHHHHHHHHHHH	42.16	-
194	Ubiquitination	GVREVLSKYRSGKLP HHHHHHHHHHCCCCC	40.29	29967540
195	Phosphorylation	VREVLSKYRSGKLPK HHHHHHHHHCCCCCH	13.46	23532336
197	Phosphorylation	EVLSKYRSGKLPKAF HHHHHHHCCCCCHHH	36.87	23532336
220	Phosphorylation	WEQILYVTEPEAWTA CEEEEEECCHHHHHH	32.06	24719451
226	Phosphorylation	VTEPEAWTAAAMYQA ECCHHHHHHHHHHHH	17.29	24719451
231	Phosphorylation	AWTAAAMYQATRIFA HHHHHHHHHHHHHHH	7.11	24719451
242	Ubiquitination	RIFASNLKERMAQRF HHHHHCHHHHHHHHH	47.74	21963094
250	Phosphorylation	ERMAQRFYNLVLLPR HHHHHHHHHHCCHHH	15.13	28152594
265	Phosphorylation	VRDDVAEYKRLNFHL CCCCHHHHHHHCHHH	7.53	24248375
266	Ubiquitination	RDDVAEYKRLNFHLY CCCHHHHHHHCHHHH	41.75	24816145
277	Acetylation	FHLYMALKKALFKPG HHHHHHHHHHHCCCC	26.85	25953088
282	Ubiquitination	ALKKALFKPGAWFKG HHHHHHCCCCCCCCC	43.31	29967540
282	Acetylation	ALKKALFKPGAWFKG HHHHHHCCCCCCCCC	43.31	26051181
322	Phosphorylation	CSIPVLHSSAAMLKI CCCCCCCCCHHHHHH	19.94	24260401
332	Sulfoxidation	AMLKIAEMEYSGANS HHHHHHHHHCCCCCH	4.30	28183972
349	Ubiquitination	LRLLLDKKYALPYRV HHHHHCCCCCCCHHH	35.11	24816145
349	2-Hydroxyisobutyrylation	LRLLLDKKYALPYRV HHHHHCCCCCCCHHH	35.11	-
389	Phosphorylation	LLTLVQRYKADLATD HHHHHHHHHHCCCCC	8.08	28152594
390	Ubiquitination	LTLVQRYKADLATDQ HHHHHHHHHCCCCCH	37.30	24816145
395	Phosphorylation	RYKADLATDQKEALL HHHHCCCCCHHHHHH	46.38	28152594
398	Sumoylation	ADLATDQKEALLELL HCCCCCHHHHHHHHH	48.00	-
398	Ubiquitination	ADLATDQKEALLELL HCCCCCHHHHHHHHH	48.00	21906983
398	Sumoylation	ADLATDQKEALLELL HCCCCCHHHHHHHHH	48.00	-
414	Phosphorylation	LQPHPQLSPEIRREL HCCCCCCCHHHHHHH	18.42	20873877

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
Oops, there are no upstream regulatory protein records of BYST_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
K2C8_HUMAN	KRT8	physical	9560222
TROP_HUMAN	TRO	physical	9560222
TROAP_HUMAN	TROAP	physical	9560222
TRI37_HUMAN	TRIM37	physical	16189514
A4_HUMAN	APP	physical	21832049
NEP1_HUMAN	EMG1	physical	22939629
WDR3_HUMAN	WDR3	physical	22939629
PNO1_HUMAN	PNO1	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
KC1E_HUMAN	CSNK1E	physical	22939629
KC1D_HUMAN	CSNK1D	physical	22939629
HERC1_HUMAN	HERC1	physical	22863883
PNO1_HUMAN	PNO1	physical	22863883
RS26_HUMAN	RPS26	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
PHC2_HUMAN	PHC2	physical	25416956
EMD_HUMAN	EMD	physical	25416956
EPS8_HUMAN	EPS8	physical	25416956
GOGA2_HUMAN	GOLGA2	physical	25416956
K1H1_HUMAN	KRT31	physical	25416956
TRI18_HUMAN	MID1	physical	25416956
TRI37_HUMAN	TRIM37	physical	25416956
TRI27_HUMAN	TRIM27	physical	25416956
TRIP6_HUMAN	TRIP6	physical	25416956
UBE2H_HUMAN	UBE2H	physical	25416956
ZBT14_HUMAN	ZBTB14	physical	25416956
AIMP2_HUMAN	AIMP2	physical	25416956
COIL_HUMAN	COIL	physical	25416956
STX11_HUMAN	STX11	physical	25416956
CDC23_HUMAN	CDC23	physical	25416956
PNMA1_HUMAN	PNMA1	physical	25416956
FXR2_HUMAN	FXR2	physical	25416956
TRAF4_HUMAN	TRAF4	physical	25416956
MYOME_HUMAN	PDE4DIP	physical	25416956
TNIP1_HUMAN	TNIP1	physical	25416956
IKZF1_HUMAN	IKZF1	physical	25416956
DDX17_HUMAN	DDX17	physical	25416956
PNMA2_HUMAN	PNMA2	physical	25416956
TRIM1_HUMAN	MID2	physical	25416956
MTUS2_HUMAN	MTUS2	physical	25416956
NECA2_HUMAN	NECAB2	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
CDA7L_HUMAN	CDCA7L	physical	25416956
ZF64A_HUMAN	ZFP64	physical	25416956
ZF64B_HUMAN	ZFP64	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
GMCL1_HUMAN	GMCL1	physical	25416956
CC136_HUMAN	CCDC136	physical	25416956
HMBX1_HUMAN	HMBOX1	physical	25416956
VP37B_HUMAN	VPS37B	physical	25416956
C102B_HUMAN	CCDC102B	physical	25416956
CCD33_HUMAN	CCDC33	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
CEP44_HUMAN	CEP44	physical	25416956
DOCK8_HUMAN	DOCK8	physical	25416956
TEKT1_HUMAN	TEKT1	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
LMBL3_HUMAN	L3MBTL3	physical	25416956
LTV1_HUMAN	LTV1	physical	25416956
CA094_HUMAN	C1orf94	physical	25416956
KRA42_HUMAN	KRTAP4-2	physical	25416956
LONF1_HUMAN	LONRF1	physical	25416956
MR1L1_HUMAN	MRFAP1L1	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
RALYL_HUMAN	RALYL	physical	25416956
MIPO1_HUMAN	MIPOL1	physical	25416956
OLIG3_HUMAN	OLIG3	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
BEND7_HUMAN	BEND7	physical	25416956
CE57L_HUMAN	CEP57L1	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
ZBT8A_HUMAN	ZBTB8A	physical	25416956
RL26L_HUMAN	RPL26L1	physical	26186194
LTV1_HUMAN	LTV1	physical	26186194
RS3_HUMAN	RPS3	physical	26186194
RRP12_HUMAN	RRP12	physical	26186194
DDX10_HUMAN	DDX10	physical	26186194
RBM19_HUMAN	RBM19	physical	26186194
NOP14_HUMAN	NOP14	physical	26186194
UT14A_HUMAN	UTP14A	physical	26186194
TSR1_HUMAN	TSR1	physical	26186194
PARN_HUMAN	PARN	physical	26186194
F207A_HUMAN	FAM207A	physical	26186194
NOP9_HUMAN	NOP9	physical	26186194
DHYS_HUMAN	DHPS	physical	26186194
NOC4L_HUMAN	NOC4L	physical	26186194
KRR1_HUMAN	KRR1	physical	26186194
DDX18_HUMAN	DDX18	physical	26186194
SRFB1_HUMAN	SRFBP1	physical	26186194
DHX36_HUMAN	DHX36	physical	26186194
NOB1_HUMAN	NOB1	physical	26186194
DDX3X_HUMAN	DDX3X	physical	26344197
FBRL_HUMAN	FBL	physical	26344197
NOB1_HUMAN	NOB1	physical	26344197
PNO1_HUMAN	PNO1	physical	26344197
RPAC1_HUMAN	POLR1C	physical	26344197
PWP2_HUMAN	PWP2	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
TNPO1_HUMAN	TNPO1	physical	26344197
TNPO2_HUMAN	TNPO2	physical	26344197
TSR2_HUMAN	TSR2	physical	26344197
WDR12_HUMAN	WDR12	physical	26344197
WDR89_HUMAN	WDR89	physical	26344197
TRIP6_HUMAN	TRIP6	physical	21516116
TRAF4_HUMAN	TRAF4	physical	21516116
DHYS_HUMAN	DHPS	physical	28514442
PARN_HUMAN	PARN	physical	28514442
NOP14_HUMAN	NOP14	physical	28514442
NOC4L_HUMAN	NOC4L	physical	28514442
LTV1_HUMAN	LTV1	physical	28514442
SRFB1_HUMAN	SRFBP1	physical	28514442
RRP12_HUMAN	RRP12	physical	28514442
F207A_HUMAN	FAM207A	physical	28514442
NOB1_HUMAN	NOB1	physical	28514442
RBM19_HUMAN	RBM19	physical	28514442
NOP9_HUMAN	NOP9	physical	28514442
DHX36_HUMAN	DHX36	physical	28514442
DDX10_HUMAN	DDX10	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
RS3_HUMAN	RPS3	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 BYST_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-15, 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-98 AND SER-167, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.	17081983 [Abstract]