KMT5A_HUMAN - dbPTM
KMT5A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KMT5A_HUMAN
UniProt AC Q9NQR1
Protein Name N-lysine methyltransferase KMT5A {ECO:0000305}
Gene Name KMT5A {ECO:0000312|HGNC:HGNC:29489}
Organism Homo sapiens (Human).
Sequence Length 393
Subcellular Localization Nucleus. Chromosome. Specifically localizes to mitotic chromosomes. Colocalized with SIRT2 at mitotic foci. Associates with chromosomes during mitosis
association is increased in a H(2)O(2)-induced oxidative stress-dependent manner. Associates with
Protein Description Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration..
Protein Sequence MGEGGAAAALVAAAAAAAAAAAAVVAGQRRRRLGRRARCHGPGRAAGGKMSKPCAVEAAAAAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSPNKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDARKGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
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
25 (in isoform 2)Phosphorylation-22210691
55PhosphorylationGKMSKPCAVEAAAAA
CCCCCCHHHHHHHHH		-
59PhosphorylationKPCAVEAAAAAVAAT
CCHHHHHHHHHHHHC		20068231
83PhosphorylationRGPGRPRTDGENVFT
CCCCCCCCCCCCCCC		28555341
96PhosphorylationFTGQSKIYSYMSPNK
CCCCCEEEECCCCCC		23663014
97PhosphorylationTGQSKIYSYMSPNKC
CCCCEEEECCCCCCC		23663014
98PhosphorylationGQSKIYSYMSPNKCS
CCCEEEECCCCCCCC		23663014
100PhosphorylationSKIYSYMSPNKCSGM
CEEEECCCCCCCCCC		25159151
105PhosphorylationYMSPNKCSGMRFPLQ
CCCCCCCCCCCCCCC		23663014
110SumoylationKCSGMRFPLQEENSV
CCCCCCCCCCCCCCC		-
116PhosphorylationFPLQEENSVTHHEVK
CCCCCCCCCCCEEEE		25627689
118PhosphorylationLQEENSVTHHEVKCQ
CCCCCCCCCEEEEEC		25627689
121AcetylationENSVTHHEVKCQGKP
CCCCCCEEEEECCCC		-
131SumoylationCQGKPLAGIYRKREE
ECCCCCCEEHHCHHH		-
140PhosphorylationYRKREEKRNAGNAVR
HHCHHHHHHHHHHHH		24719451
151SumoylationNAVRSAMKSEEQKIK
HHHHHHHHCHHHHHH		-
151SumoylationNAVRSAMKSEEQKIK
HHHHHHHHCHHHHHH		-
162AcetylationQKIKDARKGPLVPFP
HHHHHHHCCCCCCCC		62154809
172SumoylationLVPFPNQKSEAAEPP
CCCCCCCCCCCCCCC		-
172SumoylationLVPFPNQKSEAAEPP
CCCCCCCCCCCCCCC		-
172AcetylationLVPFPNQKSEAAEPP
CCCCCCCCCCCCCCC		23468428
173PhosphorylationVPFPNQKSEAAEPPK
CCCCCCCCCCCCCCC		24732914
180UbiquitinationSEAAEPPKTPPSSCD
CCCCCCCCCCCCCCC		-
181PhosphorylationEAAEPPKTPPSSCDS
CCCCCCCCCCCCCCC		23401153
184PhosphorylationEPPKTPPSSCDSTNA
CCCCCCCCCCCCCHH		24732914
185PhosphorylationPPKTPPSSCDSTNAA
CCCCCCCCCCCCHHH		24732914
188PhosphorylationTPPSSCDSTNAAIAK
CCCCCCCCCHHHHHH		24732914
189PhosphorylationPPSSCDSTNAAIAKQ
CCCCCCCCHHHHHHH		24732914
191PhosphorylationSSCDSTNAAIAKQAL
CCCCCCHHHHHHHHH		-
195UbiquitinationSTNAAIAKQALKKPI
CCHHHHHHHHHCCCC		-
195 (in isoform 2)Ubiquitination-21906983
204UbiquitinationALKKPIKGKQAPRKK
HHCCCCCCCCCCCHH		-
204 (in isoform 2)Ubiquitination-21906983
214UbiquitinationAPRKKAQGKTQQNRK
CCCHHCCCCCHHHHC		-
214 (in isoform 2)Ubiquitination-21906983
216PhosphorylationRKKAQGKTQQNRKLT
CHHCCCCCHHHHCCC		24043423
221UbiquitinationGKTQQNRKLTDFYPV
CCCHHHHCCCCCHHC		-
223PhosphorylationTQQNRKLTDFYPVRR
CHHHHCCCCCHHCCC		24043423
226 (in isoform 2)Ubiquitination-21906983
226PhosphorylationNRKLTDFYPVRRSSR
HHCCCCCHHCCCCCC		24043423
226UbiquitinationNRKLTDFYPVRRSSR
HHCCCCCHHCCCCCC		-
231PhosphorylationDFYPVRRSSRKSKAE
CCHHCCCCCCCCHHH		23882029
232PhosphorylationFYPVRRSSRKSKAEL
CHHCCCCCCCCHHHH		23882029
234UbiquitinationPVRRSSRKSKAELQS
HCCCCCCCCHHHHHH		-
236UbiquitinationRRSSRKSKAELQSEE
CCCCCCCHHHHHHHH		21906983
236 (in isoform 1)Ubiquitination-21906983
245 (in isoform 1)Ubiquitination-21906983
245UbiquitinationELQSEERKRIDELIE
HHHHHHHHHHHHHHH		21906983
255 (in isoform 1)Ubiquitination-21906983
255UbiquitinationDELIESGKEEGMKID
HHHHHHCHHCCCEEE		21906983
260UbiquitinationSGKEEGMKIDLIDGK
HCHHCCCEEEEECCC		-
267UbiquitinationKIDLIDGKGRGVIAT
EEEEECCCCCEEEEE		21906983
267 (in isoform 1)Ubiquitination-21906983
275UbiquitinationGRGVIATKQFSRGDF
CCEEEEEEEECCCCE		-
278O-linked_GlycosylationVIATKQFSRGDFVVE
EEEEEEECCCCEEEE		30620550
301UbiquitinationTDAKKREALYAQDPS
CCHHHHHHHHCCCCC		-
308UbiquitinationALYAQDPSTGCYMYY
HHHCCCCCCCCCHHH		-
341 (in isoform 2)Ubiquitination-21906983
341UbiquitinationLGRLINHSKCGNCQT
HHHHHHHHCCCCCCC		-
342UbiquitinationGRLINHSKCGNCQTK
HHHHHHHCCCCCCCE		-
349UbiquitinationKCGNCQTKLHDIDGV
CCCCCCCEEECCCCC		-
351UbiquitinationGNCQTKLHDIDGVPH
CCCCCEEECCCCCCE		-
375PhosphorylationAAGEELLYDYGDRSK
HHCCCHHCCCCCCCC		28796482
377PhosphorylationGEELLYDYGDRSKAS
CCCHHCCCCCCCCCC		28796482
381PhosphorylationLYDYGDRSKASIEAH
HCCCCCCCCCCHHCC		-
382 (in isoform 1)Ubiquitination-21906983
382UbiquitinationYDYGDRSKASIEAHP
CCCCCCCCCCHHCCC		2190698
392UbiquitinationIEAHPWLKH------
HHCCCCCCC------		-
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
100SPhosphorylationKinaseCDK1P06493
PSP
-KUbiquitinationE3 ubiquitin ligaseDTLQ9NZJ0
PMID:21035370
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
172KAcetylation

23468428
172KAcetylation

23468428
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 KMT5A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBBP4_HUMANRBBP4physical
12351676
EZH2_HUMANEZH2physical
12351676
SUZ12_HUMANSUZ12physical
12351676
EED_HUMANEEDphysical
12351676
AEBP2_HUMANAEBP2physical
12351676
PCNA_HUMANPCNAphysical
18319261
PCNA_HUMANPCNAphysical
18166648
DTL_HUMANDTLphysical
20932472
DDB1_HUMANDDB1physical
20932471
P53_HUMANTP53physical
17707234
PCNA_HUMANPCNAphysical
21035370
TP53B_HUMANTP53BP1physical
21035370
FZR1_HUMANFZR1physical
20966048
UBC9_HUMANUBE2Iphysical
21829513
TWST1_HUMANTWIST1physical
21983900
PCNA_HUMANPCNAphysical
22556262
LEF1_HUMANLEF1physical
21282610
TF7L2_HUMANTCF7L2physical
21282610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KMT5A_HUMAN

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Related Literatures of Post-Translational Modification

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