KYNU_HUMAN - dbPTM
KYNU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KYNU_HUMAN
UniProt AC Q16719
Protein Name Kynureninase {ECO:0000255|HAMAP-Rule:MF_03017}
Gene Name KYNU {ECO:0000255|HAMAP-Rule:MF_03017, ECO:0000312|HGNC:HGNC:6469}
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization Cytoplasm, cytosol .
Protein Description Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity..
Protein Sequence MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLSLVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLMKDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAGQAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKPALVGWFGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMKALRKKSVLLTGYLEYLIKHNYGKDKAATKKPVVNIITPSHVEERGCQLTITFSVPNKDVFQELEKRGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDSAETKN
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
1Acetylation-------MEPSSLEL
-------CCCCCCCC		18.0322814378
4Phosphorylation----MEPSSLELPAD
----CCCCCCCCCHH		33.9620068231
5Phosphorylation---MEPSSLELPADT
---CCCCCCCCCHHH		36.2620068231
12PhosphorylationSLELPADTVQRIAAE
CCCCCHHHHHHHHHH		22.20-
212-HydroxyisobutyrylationQRIAAELKCHPTDER
HHHHHHHCCCCCCCC		23.23-
21AcetylationQRIAAELKCHPTDER
HHHHHHHCCCCCCCC		23.2326051181
21UbiquitinationQRIAAELKCHPTDER
HHHHHHHCCCCCCCC		23.2333845483
30UbiquitinationHPTDERVALHLDEED
CCCCCCEEEECCHHH		8.7621963094
382-HydroxyisobutyrylationLHLDEEDKLRHFREC
EECCHHHHHHHHHHH		51.18-
38UbiquitinationLHLDEEDKLRHFREC
EECCHHHHHHHHHHH		51.1829967540
38AcetylationLHLDEEDKLRHFREC
EECCHHHHHHHHHHH		51.1826051181
64UbiquitinationVDLSLVNKDENAIYF
CCHHHCCCCCCEEEE		59.9629967540
70PhosphorylationNKDENAIYFLGNSLG
CCCCCEEEECCCCCC		7.1327642862
81UbiquitinationNSLGLQPKMVKTYLE
CCCCCCHHHHHHHHH		43.2822817900
84UbiquitinationGLQPKMVKTYLEEEL
CCCHHHHHHHHHHHH		28.1421963094
842-HydroxyisobutyrylationGLQPKMVKTYLEEEL
CCCHHHHHHHHHHHH		28.14-
93AcetylationYLEEELDKWAKIAAY
HHHHHHHHHHHHHHH		62.7727452117
932-HydroxyisobutyrylationYLEEELDKWAKIAAY
HHHHHHHHHHHHHHH		62.77-
93UbiquitinationYLEEELDKWAKIAAY
HHHHHHHHHHHHHHH		62.7721963094
96UbiquitinationEELDKWAKIAAYGHE
HHHHHHHHHHHHCCC		31.5921963094
96UbiquitinationEELDKWAKIAAYGHE
HHHHHHHHHHHHCCC		31.5921890473
106UbiquitinationAYGHEVGKRPWITGD
HHCCCCCCCCCCCCC		61.5433845483
1062-HydroxyisobutyrylationAYGHEVGKRPWITGD
HHCCCCCCCCCCCCC		61.54-
111PhosphorylationVGKRPWITGDESIVG
CCCCCCCCCCHHHHH		34.4120068231
115PhosphorylationPWITGDESIVGLMKD
CCCCCCHHHHHHHHH		27.5820068231
121UbiquitinationESIVGLMKDIVGANE
HHHHHHHHHHCCCCH		49.7129967540
157UbiquitinationKPTPKRYKILLEAKA
CCCCCCEEEHHEEEC		30.8033845483
163UbiquitinationYKILLEAKAFPSDHY
EEEHHEEECCCCCHH		40.9821963094
174PhosphorylationSDHYAIESQLQLHGL
CCHHHHHHHHHHCCC		30.03-
186PhosphorylationHGLNIEESMRMIKPR
CCCCHHHHHHCCCCC		10.01-
247UbiquitinationGQAKGCYVGFDLAHA
CCCCCCEEEEEHHHH		7.7722817900
251UbiquitinationGCYVGFDLAHAVGNV
CCEEEEEHHHHCCCE		3.3422817900
252UbiquitinationCYVGFDLAHAVGNVE
CEEEEEHHHHCCCEE		7.1621963094
276OtherFACWCSYKYLNAGAG
EEEECCCHHHCCCCC		27.28-
276N6-(pyridoxal phosphate)lysineFACWCSYKYLNAGAG
EEEECCCHHHCCCCC		27.28-
293UbiquitinationAGAFIHEKHAHTIKP
HHHHHHHHCCCCCHH		31.7429967540
297PhosphorylationIHEKHAHTIKPALVG
HHHHCCCCCHHHHHH		31.3220068231
297 (in isoform 2)Phosphorylation-31.3224260401
299AcetylationEKHAHTIKPALVGWF
HHCCCCCHHHHHHHH		25.9526051181
299UbiquitinationEKHAHTIKPALVGWF
HHCCCCCHHHHHHHH		25.9533845483
311PhosphorylationGWFGHELSTRFKMDN
HHHCCCHHHCCCCCC		17.9820068231
312PhosphorylationWFGHELSTRFKMDNK
HHCCCHHHCCCCCCC		53.3920068231
319UbiquitinationTRFKMDNKLQLIPGV
HCCCCCCCCCCCCCC		33.0933845483
327S-palmitoylationLQLIPGVCGFRISNP
CCCCCCCCCEEECCC		5.4529575903
331UbiquitinationPGVCGFRISNPPILL
CCCCCEEECCCCEEE		4.3321963094
361PhosphorylationMKALRKKSVLLTGYL
HHHHHHHHHHHHHHH		22.4920068231
365PhosphorylationRKKSVLLTGYLEYLI
HHHHHHHHHHHHHHH		21.4420068231
367PhosphorylationKSVLLTGYLEYLIKH
HHHHHHHHHHHHHHC		7.3620068231
370PhosphorylationLLTGYLEYLIKHNYG
HHHHHHHHHHHCCCC		15.9020068231
373UbiquitinationGYLEYLIKHNYGKDK
HHHHHHHHCCCCCCC		24.1733845483
3782-HydroxyisobutyrylationLIKHNYGKDKAATKK
HHHCCCCCCCCCCCC		45.77-
378UbiquitinationLIKHNYGKDKAATKK
HHHCCCCCCCCCCCC		45.7729967540
380UbiquitinationKHNYGKDKAATKKPV
HCCCCCCCCCCCCCE		43.3322817900
384UbiquitinationGKDKAATKKPVVNII
CCCCCCCCCCEEEEE		50.8022817900
385UbiquitinationKDKAATKKPVVNIIT
CCCCCCCCCEEEEEC		38.3921963094
392PhosphorylationKPVVNIITPSHVEER
CCEEEEECHHHHHHC		18.2329083192
394PhosphorylationVVNIITPSHVEERGC
EEEEECHHHHHHCCC		31.3629083192
420UbiquitinationDVFQELEKRGVVCDK
HHHHHHHHCCCCCCC		68.0529967540
420AcetylationDVFQELEKRGVVCDK
HHHHHHHHCCCCCCC		68.0527452117
427UbiquitinationKRGVVCDKRNPNGIR
HCCCCCCCCCCCCEE		49.2833845483
451PhosphorylationFHDVYKFTNLLTSIL
HHHHHHHHHHHHHHH		22.3220068231
455PhosphorylationYKFTNLLTSILDSAE
HHHHHHHHHHHHHHH		19.5220068231
456PhosphorylationKFTNLLTSILDSAET
HHHHHHHHHHHHHHC		22.5620068231
460PhosphorylationLLTSILDSAETKN--
HHHHHHHHHHCCC--		25.2620068231
463PhosphorylationSILDSAETKN-----
HHHHHHHCCC-----		35.2920068231
464UbiquitinationILDSAETKN------
HHHHHHCCC------		52.7621963094
464AcetylationILDSAETKN------
HHHHHHCCC------		52.7619809797
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 KYNU_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KYNU_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 KYNU_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPM3_HUMANTPM3physical
22939629
SMRD2_HUMANSMARCD2physical
22939629
COIL_HUMANCOILphysical
22939629
S23IP_HUMANSEC23IPphysical
22939629
PO210_HUMANNUP210physical
22939629
PALM2_HUMANPALM2physical
22939629
SPSY_HUMANSMSphysical
22939629
PPM1G_HUMANPPM1Gphysical
22939629
P4R3B_HUMANSMEK2physical
22939629
SSU72_HUMANSSU72physical
22939629
SIR1_HUMANSIRT1physical
22939629
SGTA_HUMANSGTAphysical
22939629
CNDP2_HUMANCNDP2physical
22863883
LDHA_HUMANLDHAphysical
22863883
NDRG1_HUMANNDRG1physical
22863883
PEPD_HUMANPEPDphysical
22863883
KS6A1_HUMANRPS6KA1physical
22863883
ADK_HUMANADKphysical
26344197
ASSY_HUMANASS1physical
26344197
COF1_HUMANCFL1physical
26344197
DEST_HUMANDSTNphysical
26344197
ETFA_HUMANETFAphysical
26344197
FUBP1_HUMANFUBP1physical
26344197
GLRX1_HUMANGLRXphysical
26344197
MEMO1_HUMANMEMO1physical
26344197
PPIA_HUMANPPIAphysical
26344197
SERC_HUMANPSAT1physical
26344197
SPRE_HUMANSPRphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
236800Hydroxykynureninuria (HYXKY)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00160L-Alanine
Regulatory Network of KYNU_HUMAN

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Related Literatures of Post-Translational Modification

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