HSL7_YEAST - dbPTM
HSL7_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSL7_YEAST
UniProt AC P38274
Protein Name Protein arginine N-methyltransferase HSL7 {ECO:0000305|PubMed:10903903}
Gene Name HSL7 {ECO:0000303|PubMed:8647431}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 827
Subcellular Localization Bud neck . Associates with the septin ring of the bud neck during cell division.
Protein Description S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that can catalyze both the mono- and symmetric (type II) dimethylation of the guanidino nitrogens of arginine residues in target proteins. [PubMed: 18515076 Involved in the control of the cell cycle at the G2/M (mitosis) transition. Cooperates with HSL1 to hyperphosphorylate SWE1, thereby targeting SWE1 for polyubiquitination and subsequent degradation]
Protein Sequence MHSNVFVGVKPGFNHKQHSKKSRFLENVSSHSPELPSNYDYVLLPITTPRYKEIVGQVFKDFQRQSIQNWKPLQIPEPQLQDICIPPFNVKKLDNDDTPSYIGLLSSWLELESRDPNVRDLGLKVLLNECKYARFVGINKLILAPPRDLSNLQLYGQMIYRLLQNRIVFAAPALTISISLPLYEDSDPLATWELWNTVRKQCEYHPSLTISLALPRTRTPSYVLNRWLAEPVSCLLVSSSIFASNQYDYPVLHKFNQNLILKFQKVNGDSQILGNELCVILHGMEKYANNVKGGESAYLEYINYLLKKGDKVLNSNSNHQFLLQEDSRIMPPLKPHSDNLLNSTYLTFEKDLVKYDLYESAILEALQDLAPRASAKRPLVILVAGAGRGPLVDRTFKIISMLFMDSKVSIIAIEKNPQAYLYLQKRNFDCWDNRVKLIKEDMTKWQINEPSEKRIQIDLCISELLGSFGCNELSPECLWSIEKYHSHNDTIFIPRSYSSYIAPISSPLFYQKLSQTNRSLEAPWIVHRVPYCILSSRVNEVWRFEHPMAQKDTVQDEDDFTVEFSQSSLNEFKIKHRGEIHGFIGFFSANLYNNIFLSTLPNDSTVRLKFSEETLMNTRREENLIKKCDHTPNMTSWSPIIFPLKQPISFIDDSELSVLMSRIHSDTEQKVWYEWSLESFIYLMLSNYTSAVTAASMTIPRSIVTDDTKTLAHNRHYSATTNQKLDNQIDLDQDIENEEEQGFLSNLETGWQSVQDIHGLSETAKPDHLDSINKPMFDLKSTKALEPSNELPRHEDLEEDVPEVHVRVKTSVSTLHNVCGRAFSLPL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
22PhosphorylationHKQHSKKSRFLENVS
CCHHCHHHHHHHHHH		31.8124961812
29PhosphorylationSRFLENVSSHSPELP
HHHHHHHHHCCCCCC		33.6422369663
30PhosphorylationRFLENVSSHSPELPS
HHHHHHHHCCCCCCC		24.5721440633
32PhosphorylationLENVSSHSPELPSNY
HHHHHHCCCCCCCCC		23.2422369663
315PhosphorylationKGDKVLNSNSNHQFL
HCCEECCCCCCCCEE		37.1627017623
317PhosphorylationDKVLNSNSNHQFLLQ
CEECCCCCCCCEEEC		35.1923749301
327PhosphorylationQFLLQEDSRIMPPLK
CEEECCCCCCCCCCC		23.9723749301
400PhosphorylationDRTFKIISMLFMDSK
HHHHHHHHHHHCCCC		16.9527017623
409PhosphorylationLFMDSKVSIIAIEKN
HHCCCCEEEEEEECC		16.4127017623
420PhosphorylationIEKNPQAYLYLQKRN
EECCHHHEEEEECCC		7.2227017623
422PhosphorylationKNPQAYLYLQKRNFD
CCHHHEEEEECCCCC		8.3927017623
512UbiquitinationSSPLFYQKLSQTNRS
CCHHHHHHHHHCCCC		38.4323749301
614PhosphorylationRLKFSEETLMNTRRE
EEEECHHHHHHCHHH		27.5318515076
649PhosphorylationFPLKQPISFIDDSEL
EECCCCCEECCHHHH		23.8819684113
657PhosphorylationFIDDSELSVLMSRIH
ECCHHHHHHHHHHHC		14.7819684113
702PhosphorylationASMTIPRSIVTDDTK
HHCCCCCHHCCCCCC		18.9623749301
705PhosphorylationTIPRSIVTDDTKTLA
CCCCHHCCCCCCHHH		26.8728889911
708PhosphorylationRSIVTDDTKTLAHNR
CHHCCCCCCHHHCCC		28.8328889911
710PhosphorylationIVTDDTKTLAHNRHY
HCCCCCCHHHCCCCC		31.1328889911
718PhosphorylationLAHNRHYSATTNQKL
HHCCCCCCCCCCCHH		17.0217287358
720PhosphorylationHNRHYSATTNQKLDN
CCCCCCCCCCCHHHH		21.9721440633
721PhosphorylationNRHYSATTNQKLDNQ
CCCCCCCCCCHHHHC		35.0621551504
753PhosphorylationNLETGWQSVQDIHGL
CHHHHHCCHHHHCCC		18.4228889911
788PhosphorylationSTKALEPSNELPRHE
CCCCCCCCCCCCCCC		33.2927017623
813PhosphorylationVRVKTSVSTLHNVCG
EEEECCHHHHHHHCC		25.6421440633
814PhosphorylationRVKTSVSTLHNVCGR
EEECCHHHHHHHCCC		29.8528889911
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 HSL7_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSL7_YEAST !!
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 HSL7_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSL1_YEASTHSL1physical
10490648
SWE1_YEASTSWE1physical
10490648
HSL1_YEASTHSL1physical
11408575
SWE1_YEASTSWE1physical
12388757
SWE1_YEASTSWE1physical
10490630
SWE1_YEASTSWE1physical
11408575
APP1_YEASTAPP1physical
11489916
HSL7_YEASTHSL7physical
11408575
H2A1_YEASTHTA1physical
12925763
ZDS1_YEASTZDS1genetic
8647431
GCN5_YEASTGCN5genetic
16951088
SPT7_YEASTSPT7genetic
16951088
ESA1_YEASTESA1genetic
16951088
SIN3_YEASTSIN3genetic
16951088
RPD3_YEASTRPD3genetic
16951088
SET1_YEASTSET1genetic
16951088
SWE1_YEASTSWE1genetic
16951088
CG22_YEASTCLB2genetic
16571676
STE20_YEASTSTE20genetic
10411908
MOB2_YEASTMOB2genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
NSE1_YEASTNSE1genetic
27708008
NUM1_YEASTNUM1genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
CDC27_YEASTCDC27genetic
27708008
CND2_YEASTBRN1genetic
27708008
APC11_YEASTAPC11genetic
27708008
CDC7_YEASTCDC7genetic
27708008
CDC48_YEASTCDC48genetic
27708008
CDC53_YEASTCDC53genetic
27708008
DBF4_YEASTDBF4genetic
27708008
SLU7_YEASTSLU7genetic
27708008
CDC37_YEASTCDC37genetic
27708008
ERF3_YEASTSUP35genetic
27708008
CDC1_YEASTCDC1genetic
27708008
GPI8_YEASTGPI8genetic
27708008
COG3_YEASTCOG3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
CAK1_YEASTCAK1genetic
27708008
ACT_YEASTACT1genetic
27708008
RPN11_YEASTRPN11genetic
27708008
SAD1_YEASTSAD1genetic
27708008
RPN12_YEASTRPN12genetic
27708008
SLD3_YEASTSLD3genetic
27708008
CDC20_YEASTCDC20genetic
27708008
MCE1_YEASTCEG1genetic
27708008
GPI10_YEASTGPI10genetic
27708008
ZPR1_YEASTZPR1genetic
27708008
DNA2_YEASTDNA2genetic
27708008
CDC23_YEASTCDC23genetic
27708008
GPI16_YEASTGPI16genetic
27708008
CTF8_YEASTCTF8genetic
27708008
MOB1_YEASTMOB1genetic
27708008
STS1_YEASTSTS1genetic
27708008
RFC2_YEASTRFC2genetic
27708008
CDC16_YEASTCDC16genetic
27708008
PRS7_YEASTRPT1genetic
27708008
SN114_YEASTSNU114genetic
27708008
MCM5_YEASTMCM5genetic
27708008
SC61A_YEASTSEC61genetic
27708008
CDC91_YEASTGAB1genetic
27708008
PDS5_YEASTPDS5genetic
27708008
VTI1_YEASTVTI1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
NOP2_YEASTNOP2genetic
27708008
MED4_YEASTMED4genetic
27708008
APC5_YEASTAPC5genetic
27708008
PRS10_YEASTRPT4genetic
27708008
DEP1_YEASTDEP1genetic
27708008
LTE1_YEASTLTE1genetic
27708008
SHE1_YEASTSHE1genetic
27708008
DCC1_YEASTDCC1genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
MBP1_YEASTMBP1genetic
27708008
CG23_YEASTCLB3genetic
27708008
NBP2_YEASTNBP2genetic
27708008
UME6_YEASTUME6genetic
27708008
MNN10_YEASTMNN10genetic
27708008
MSN5_YEASTMSN5genetic
27708008
CEM1_YEASTCEM1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
SDS3_YEASTSDS3genetic
27708008
MGA2_YEASTMGA2genetic
27708008
DPOD3_YEASTPOL32genetic
27708008
NFU1_YEASTNFU1genetic
27708008
RT109_YEASTRTT109genetic
27708008
ENV10_YEASTENV10genetic
27708008
CSF1_YEASTCSF1genetic
27708008
ALAM_YEASTALT1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
MMS22_YEASTMMS22genetic
27708008
MPIP_YEASTMIH1genetic
27708008
CTF18_YEASTCTF18genetic
27708008
MGR3_YEASTMGR3genetic
27708008
ZDS1_YEASTZDS1genetic
27708008
FKH2_YEASTFKH2genetic
27708008
ASE1_YEASTASE1genetic
27708008
VAM10_YEASTVAM10genetic
27708008
RUD3_YEASTRUD3genetic
27708008
SUR1_YEASTSUR1genetic
27708008
YME1_YEASTYME1genetic
27708008
THP3_YEASTTHP3genetic
27708008
CG22_YEASTCLB2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSL7_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; THR-614; THR-708AND SER-718, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718, AND MASSSPECTROMETRY.

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