SMYD2_HUMAN - dbPTM
SMYD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMYD2_HUMAN
UniProt AC Q9NRG4
Protein Name N-lysine methyltransferase SMYD2
Gene Name SMYD2
Organism Homo sapiens (Human).
Sequence Length 433
Subcellular Localization Cytoplasm, cytosol. Nucleus.
Protein Description Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'..
Protein Sequence MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
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
35PhosphorylationQVGDLLFSCPAYAYV
ECCCHHCCCCEEEEE		21.11-
44PhosphorylationPAYAYVLTVNERGNH
CEEEEEEEEECCCCC		15.96-
64UbiquitinationTRKEGLSKCGRCKQA
ECCCCHHHCCCCCEE		45.8324816145
80UbiquitinationYCNVECQKEDWPMHK
EECCEECCCCCCCCE		70.1129967540
127UbiquitinationPERTPSEKLLAVKEF
CCCCCHHHHHHHHHH		53.8129967540
132UbiquitinationSEKLLAVKEFESHLD
HHHHHHHHHHHHHHH		51.5929967540
145UbiquitinationLDKLDNEKKDLIQSD
HHHHHHHHHHHHHHH		58.82-
146UbiquitinationDKLDNEKKDLIQSDI
HHHHHHHHHHHHHHH		52.14-
281UbiquitinationKAKVEIRKLSDPPKA
HCEEEEEECCCCCHH		58.9924816145
283PhosphorylationKVEIRKLSDPPKAEA
EEEEEECCCCCHHHH		51.6230266825
312UbiquitinationFRRAKHYKSPSELLE
HHHHCCCCCHHHHHH		56.4629967540
313PhosphorylationRRAKHYKSPSELLEI
HHHCCCCCHHHHHHH		26.8822673903
315PhosphorylationAKHYKSPSELLEICE
HCCCCCHHHHHHHHH		48.2222673903
324PhosphorylationLLEICELSQEKMSSV
HHHHHHHCHHHHHHH		17.6322673903
329PhosphorylationELSQEKMSSVFEDSN
HHCHHHHHHHHCCCC		34.1224043423
330PhosphorylationLSQEKMSSVFEDSNV
HCHHHHHHHHCCCCH		27.5924043423
335PhosphorylationMSSVFEDSNVYMLHM
HHHHHCCCCHHHHHH		22.4624043423
338PhosphorylationVFEDSNVYMLHMMYQ
HHCCCCHHHHHHHHH		9.7524043423
344PhosphorylationVYMLHMMYQAMGVCL
HHHHHHHHHHHCHHH		5.8824043423
352PhosphorylationQAMGVCLYMQDWEGA
HHHCHHHHCCCHHHH		6.3924043423
362PhosphorylationDWEGALQYGQKIIKP
CHHHHHHHHHEECCC		23.5224043423
377PhosphorylationYSKHYPLYSLNVASM
CCCCCCCCCHHHHHH		13.4522817900
398MethylationLYMGLEHKAAGEKAL
HHHCCCCHHHHHHHH		30.47115980821
418UbiquitinationIMEVAHGKDHPYISE
HHHHHCCCCCCCHHH		42.8929967540
427UbiquitinationHPYISEIKQEIESH-
CCCHHHHHHHHHCC-		37.5129967540
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 SMYD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMYD2_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 SMYD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSK3B_HUMANGSK3Bphysical
17353931
E41L3_HUMANEPB41L3physical
17353931
CLAP2_HUMANCLASP2physical
17353931
AKA11_HUMANAKAP11physical
17353931
CDC37_HUMANCDC37physical
17353931
IF2B1_HUMANIGF2BP1physical
17353931
AXIN1_HUMANAXIN1physical
17353931
P53_HUMANTP53physical
17108971
P53_HUMANTP53physical
18065756
E41L3_HUMANEPB41L3physical
18065756
HS90A_HUMANHSP90AA1physical
18065756
RB_HUMANRB1physical
20870719
HS90A_HUMANHSP90AA1physical
22028380
H32_HUMANHIST2H3Cphysical
21678921
ESR1_HUMANESR1physical
24101509
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
There are no disease associations of PTM sites.
Regulatory Network of SMYD2_HUMAN

loading...

Related Literatures of Post-Translational Modification

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