SETMR_HUMAN - dbPTM
SETMR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SETMR_HUMAN
UniProt AC Q53H47
Protein Name Histone-lysine N-methyltransferase SETMAR {ECO:0000305}
Gene Name SETMAR {ECO:0000312|HGNC:HGNC:10762}
Organism Homo sapiens (Human).
Sequence Length 684
Subcellular Localization Nucleus . Chromosome . Recruited on damaged DNA at sites of double-strand breaks.
Protein Description Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. [PubMed: 16332963]
Protein Sequence MFAEAAKTTRPCGMAEFKEKPEAPTEQLDVACGQENLPVGAWPPGAAPAPFQYTPDHVVGPGADIDPTQITFPGCICVKTPCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFECNVLCRCSDHCRNRVVQKGLQFHFQVFKTHKKGWGLRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDSNYIIAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEPNLLMIPVRIDSMVPKLALFAAKDIVPEEELSYDYSGRYLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFDSSLYCPVEKSNISCGNEKEPSMCGSAPSVFPSCKRLTLETMKMMLDKKQIRAIFLFEFKMGRKAAETTRNINNAFGPGTANERTVQWWFKKFCKGDESLEDEERSGRPSEVDNDQLRAIIEADPLTTTREVAEELNVNHSTVVRHLKQIGKVKKLDKWVPHELTENQKNRRFEVSSSLILRNHNEPFLDRIVTCDEKWILYDNRRRSAQWLDQEEAPKHFPKPILHPKKVMVTIWWSAAGLIHYSFLNPGETITSEKYAQEIDEMNQKLQRLQLALVNRKGPILLHDNARPHVAQPTLQKLNELGYEVLPHPPYSPDLLPTNYHVFKHLNNFLQGKRFHNQQDAENAFQEFVESQSTDFYATGINQLISRWQKCVDCNGSYFD
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
100PhosphorylationGENYDDNSCLRDIGS
CCCCCCCCCCCCCCC		38.6229116813
107PhosphorylationSCLRDIGSGGKYAEP
CCCCCCCCCCCCCCC		8.9129116813
110AcetylationRDIGSGGKYAEPVFE
CCCCCCCCCCCCEEE		20.8625953088
252AcetylationALFAAKDIVPEEELS
HHHHHCCCCCHHHHC		27.1619608861
275UbiquitinationNLTVSEDKERLDHGK
EEEECCCHHHCCCCC		11.49-
330AcetylationMCGSAPSVFPSCKRL
CCCCCCCCCHHHHHH		28.69-
335MethylationPSVFPSCKRLTLETM
CCCCHHHHHHCHHHH		42.49-
335AcetylationPSVFPSCKRLTLETM
CCCCHHHHHHCHHHH		42.49-
335"N6,N6-dimethyllysine"PSVFPSCKRLTLETM
CCCCHHHHHHCHHHH		42.49-
338PhosphorylationFPSCKRLTLETMKMM
CHHHHHHCHHHHHHH		4.3924076635
341PhosphorylationCKRLTLETMKMMLDK
HHHHCHHHHHHHCCH		1.9024076635
343AcetylationRLTLETMKMMLDKKQ
HHCHHHHHHHCCHHH		3.0820167786
348AcetylationTMKMMLDKKQIRAIF
HHHHHCCHHHHHHHE		8.3520167786
353 (in isoform 2)Phosphorylation-20.0828634120
378AcetylationNINNAFGPGTANERT
CCHHCCCCCCCCHHH		31.08-
379UbiquitinationINNAFGPGTANERTV
CHHCCCCCCCCHHHH		46.66-
382UbiquitinationAFGPGTANERTVQWW
CCCCCCCCHHHHHHH		72.95-
391AcetylationRTVQWWFKKFCKGDE
HHHHHHHHHHCCCCC		65.5519608861
395AcetylationWWFKKFCKGDESLED
HHHHHHCCCCCCCCC		32.5826051181
395UbiquitinationWWFKKFCKGDESLED
HHHHHHCCCCCCCCC		32.58-
410PhosphorylationEERSGRPSEVDNDQL
HHHCCCCCCCCHHHH		17.2025159151
442PhosphorylationELNVNHSTVVRHLKQ
HCCCCHHHHHHHHHH		65.9824719451
448AcetylationSTVVRHLKQIGKVKK
HHHHHHHHHHCCCEE		17.707370207
485MethylationSLILRNHNEPFLDRI
HHHHCCCCCCCHHEE		26.70-
498MethylationRIVTCDEKWILYDNR
EEEEECCCEEEEECC		11.1318790802
498UbiquitinationRIVTCDEKWILYDNR
EEEEECCCEEEEECC		11.13-
498"N6,N6-dimethyllysine"RIVTCDEKWILYDNR
EEEEECCCEEEEECC		11.13-
508PhosphorylationLYDNRRRSAQWLDQE
EEECCHHHCHHCCHH		11.8319664994
523UbiquitinationEAPKHFPKPILHPKK
HCCCCCCCCCCCCCC		3.59-
535UbiquitinationPKKVMVTIWWSAAGL
CCCEEEEEECCCHHH		6.59-
569UbiquitinationEIDEMNQKLQRLQLA
HHHHHHHHHHHHHHH		15.96-
624UbiquitinationPDLLPTNYHVFKHLN
CCCCCCCHHHHHHHH		38.64-
637UbiquitinationLNNFLQGKRFHNQQD
HHHHHCCCCCCCHHH		40.59-
661UbiquitinationESQSTDFYATGINQL
HHCCCCHHHHHHHHH		29.30-
674UbiquitinationQLISRWQKCVDCNGS
HHHHHHHHHHCCCCC		-
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
508SPhosphorylationKinaseCHK1O14757
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
508SPhosphorylation

19690332
508SPhosphorylation

19690332
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 SETMR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SETMR_HUMANSETMARphysical
16169070
TOP2A_HUMANTOP2Aphysical
18790802
XRCC4_HUMANXRCC4physical
18773976
TOP2A_HUMANTOP2Aphysical
19458360
PCNA_HUMANPCNAphysical
20457750
RAD9A_HUMANRAD9Aphysical
20457750
SETMR_HUMANSETMARphysical
20416268
PRP19_HUMANPRPF19physical
20416268
DOC2A_HUMANDOC2Aphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
SETX_HUMANSETXphysical
28514442
PCBP1_HUMANPCBP1physical
28514442
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 SETMR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-325 AND THR-328, ANDMASS SPECTROMETRY.

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