THNS1_HUMAN - dbPTM
THNS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THNS1_HUMAN
UniProt AC Q8IYQ7
Protein Name Threonine synthase-like 1
Gene Name THNSL1
Organism Homo sapiens (Human).
Sequence Length 743
Subcellular Localization
Protein Description
Protein Sequence MLHFNRCHHLKKITQKCFSSIHVKTDKHAQRFLSRTFALAELRKSWYSTHSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGSNPMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKTDRIVGQNSGTSMKDLLKFRRQYYKKWYDARVFCESGASPEEVADKVLNAIKRYQDVDSETFISTRHVWPEDCEQKVSAKFFSEAVIEGLASDGGLFVPAKEFPKLSCGEWKSLVGATYVERAQILLERCIHPADIPAARLGEMIETAYGENFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHCIPPSCNYMILVATSGDTGSAVLNGFSRLNKNDKQRIAVVAFFPENGVSDFQKAQIIGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTGFLTVEYGTILSSANSINWGRLLPQVVYHASAYLDLVSQGFISFGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNHVLTDFIKTGHYDLRERKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNRLESQHHFQIEKALVEKLQQDFVADWCSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQDKTCPVIISSTAHYSKFAPAIMQALKIKEINETSSSQLYLLGSYNALPPLHEALLERTKQQEKMEYQVCAADMNVLKSHVEQLVQNQFI
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
45PhosphorylationALAELRKSWYSTHSL
HHHHHHHHHHHHCCE		25.4729083192
47PhosphorylationAELRKSWYSTHSLVG
HHHHHHHHHHCCEEC		15.6929083192
48PhosphorylationELRKSWYSTHSLVGD
HHHHHHHHHCCEECC		17.2429083192
49PhosphorylationLRKSWYSTHSLVGDK
HHHHHHHHCCEECCC		10.3729083192
51PhosphorylationKSWYSTHSLVGDKNI
HHHHHHCCEECCCEE		25.4929083192
56AcetylationTHSLVGDKNIILMGP
HCCEECCCEEEEECC		44.0812654933
68AcetylationMGPPGAGKTTVGRII
ECCCCCCHHHHHHHH		40.2512654945
69PhosphorylationGPPGAGKTTVGRIIG
CCCCCCHHHHHHHHH		26.2923532336
70PhosphorylationPPGAGKTTVGRIIGQ
CCCCCHHHHHHHHHH		25.1723532336
98PhosphorylationLEKTWNMSVSEKLQD
HHHHCCCCHHHHHHH		21.1928857561
183UbiquitinationQNSGTSMKDLLKFRR
CCCCCCHHHHHHHHH		45.02-
183SuccinylationQNSGTSMKDLLKFRR
CCCCCCHHHHHHHHH		45.0223954790
183AcetylationQNSGTSMKDLLKFRR
CCCCCCHHHHHHHHH		45.0225953088
192PhosphorylationLLKFRRQYYKKWYDA
HHHHHHHHHHHHCCC		18.5526657352
193PhosphorylationLKFRRQYYKKWYDAR
HHHHHHHHHHHCCCC		9.5826657352
197PhosphorylationRQYYKKWYDARVFCE
HHHHHHHCCCCCCCC		14.4926657352
228PhosphorylationKRYQDVDSETFISTR
HHHCCCCCCCEEEEC		38.08-
245AcetylationWPEDCEQKVSAKFFS
CCHHHCHHHHHHHHC		18.8325038526
281UbiquitinationKLSCGEWKSLVGATY
CCCCCCHHHHHCCHH		29.6119608861
281SuccinylationKLSCGEWKSLVGATY
CCCCCCHHHHHCCHH		29.6123954790
281AcetylationKLSCGEWKSLVGATY
CCCCCCHHHHHCCHH		29.6119608861
351N6-(pyridoxal phosphate)lysineHGPTGSFKDLSLQLM
CCCCCCHHHHHHHHH		60.50-
351OtherHGPTGSFKDLSLQLM
CCCCCCHHHHHHHHH		60.50-
417UbiquitinationNGVSDFQKAQIIGSQ
CCCCHHHHHEECCEE		42.10-
559PhosphorylationRERKLAQTFSPSIDI
HHHHHHHHCCCCHHH		22.0720068231
561PhosphorylationRKLAQTFSPSIDILK
HHHHHHCCCCHHHHH		22.5620068231
563PhosphorylationLAQTFSPSIDILKSS
HHHHCCCCHHHHHCC		31.5220068231
596PhosphorylationELFNRLESQHHFQIE
HHHHHHHHHHCHHHH		39.13-
604AcetylationQHHFQIEKALVEKLQ
HHCHHHHHHHHHHHH		48.9625038526
652MethylationVAKVVADRVQDKTCP
HHHHHHHHHCCCCCC		20.47115918409
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 THNS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THNS1_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 THNS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of THNS1_HUMAN !!
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
DB00156L-Threonine
Regulatory Network of THNS1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-281, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory