HIP1_YEAST - dbPTM
HIP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIP1_YEAST
UniProt AC P06775
Protein Name Histidine permease
Gene Name HIP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 603
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description High-affinity permease for histidine..
Protein Sequence MPRNPLKKEYWADVVDGFKPATSPAFENEKESTTFVTELTSKTDSAFPLSSKDSPGINQTTNDITSSDRFRRNEDTEQEDINNTNLSKDLSVRHLLTLAVGGAIGTGLYVNTGAALSTGGPASLVIDWVIISTCLFTVINSLGELSAAFPVVGGFNVYSMRFIEPSFAFAVNLNYLAQWLVLLPLELVAASITIKYWNDKINSDAWVAIFYATIALANMLDVKSFGETEFVLSMIKILSIIGFTILGIVLSCGGGPHGGYIGGKYWHDPGAFVGHSSGTQFKGLCSVFVTAAFSYSGIEMTAVSAAESKNPRETIPKAAKRTFWLITASYVTILTLIGCLVPSNDPRLLNGSSSVDAASSPLVIAIENGGIKGLPSLMNAIILIAVVSVANSAVYACSRCMVAMAHIGNLPKFLNRVDKRGRPMNAILLTLFFGLLSFVAASDKQAEVFTWLSALSGLSTIFCWMAINLSHIRFRQAMKVQERSLDELPFISQTGVKGSWYGFIVLFLVLIASFWTSLFPLGGSGASAESFFEGYLSFPILIVCYVGHKLYTRNWTLMVKLEDMDLDTGRKQVDLTLRREEMRIERETLAKRSFVTRFLHFWC
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
19UbiquitinationADVVDGFKPATSPAF
HHHCCCCCCCCCCCC
38.9923749301
22PhosphorylationVDGFKPATSPAFENE
CCCCCCCCCCCCCCC
43.7121440633
23PhosphorylationDGFKPATSPAFENEK
CCCCCCCCCCCCCCC
19.1427717283
30UbiquitinationSPAFENEKESTTFVT
CCCCCCCCCCCEEEE
69.4223749301
37PhosphorylationKESTTFVTELTSKTD
CCCCEEEEECCCCCC
22.5327017623
40PhosphorylationTTFVTELTSKTDSAF
CEEEEECCCCCCCCC
23.1921440633
41PhosphorylationTFVTELTSKTDSAFP
EEEEECCCCCCCCCC
46.3021440633
42UbiquitinationFVTELTSKTDSAFPL
EEEECCCCCCCCCCC
51.6323749301
45PhosphorylationELTSKTDSAFPLSSK
ECCCCCCCCCCCCCC
36.7223749301
50PhosphorylationTDSAFPLSSKDSPGI
CCCCCCCCCCCCCCC
35.2623749301
51PhosphorylationDSAFPLSSKDSPGIN
CCCCCCCCCCCCCCC
48.4423749301
52UbiquitinationSAFPLSSKDSPGINQ
CCCCCCCCCCCCCCC
59.8723749301
54PhosphorylationFPLSSKDSPGINQTT
CCCCCCCCCCCCCCC
28.8517330950
60PhosphorylationDSPGINQTTNDITSS
CCCCCCCCCCCCCCC
24.0729688323
61PhosphorylationSPGINQTTNDITSSD
CCCCCCCCCCCCCCC
22.5629688323
65PhosphorylationNQTTNDITSSDRFRR
CCCCCCCCCCCCHHC
25.6623749301
66PhosphorylationQTTNDITSSDRFRRN
CCCCCCCCCCCHHCC
30.4921440633
67PhosphorylationTTNDITSSDRFRRNE
CCCCCCCCCCHHCCC
24.9323749301
76PhosphorylationRFRRNEDTEQEDINN
CHHCCCCCCCHHHCC
33.1321551504
88UbiquitinationINNTNLSKDLSVRHL
HCCCCCCHHHCHHHH
66.8923749301
576PhosphorylationGRKQVDLTLRREEMR
CCEEEEHHHHHHHHH
17.4715665377
603S-palmitoylationTRFLHFWC-------
HHHHHHCC-------
3.8016751107

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 HIP1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HIP1_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 HIP1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
C1TC_YEASTADE3genetic
12684846
TAT1_YEASTTAT1genetic
9473505
SAM3_YEASTSAM3genetic
16269340
LHS1_YEASTLHS1genetic
16269340
PRA1_YEASTYIP3genetic
16269340
GLO3_YEASTGLO3genetic
16269340
CFAH_HUMANCFHphysical
17959597
SHR3_YEASTSHR3physical
16093310
MKAR_YEASTIFA38physical
16093310
ELO2_YEASTELO2physical
16093310
STE24_YEASTSTE24physical
16093310
ELO3_YEASTELO3physical
16093310
ERP4_YEASTERP4physical
16093310

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HIP1_YEAST

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Related Literatures of Post-Translational Modification

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