KDM2A_HUMAN - dbPTM
KDM2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM2A_HUMAN
UniProt AC Q9Y2K7
Protein Name Lysine-specific demethylase 2A
Gene Name KDM2A
Organism Homo sapiens (Human).
Sequence Length 1162
Subcellular Localization Nucleus, nucleoplasm . Punctate expression throughout the nucleoplasm and enriched in the perinucleolar region. Specifically nucleates at CpG islands where it's presence results in chromatin depleted in H3K36me2.
Protein Description Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis..
Protein Sequence MEPEEERIRYSQRLRGTMRRRYEDDGISDDEIEGKRTFDLEEKLHTNKYNANFVTFMEGKDFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTVNDVKMCVGSRRMVDVMDVNTQKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLENMVQRPSTVDFIDWVDNMWPRHLKESQTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDFGGTSVWYHIHQGGKVFWLIPPTAHNLELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYTFVIPSGWIHAVYTPTDTLVFGGNFLHSFNIPMQLKIYNIEDRTRVPNKFRYPFYYEMCWYVLERYVYCITNRSHLTKEFQKESLSMDLELNGLESGNGDEEAVDREPRRLSSRRSVLTSPVANGVNLDYDGLGKTCRSLPSLKKTLAGDSSSDCSRGSHNGQVWDPQCAPRKDRQVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWPKRDKLKFPTRPKVRVPTIPITKPHTMKPAPRLTPVRPAAASPIVSGARRRRVRCRKCKACVQGECGVCHYCRDMKKFGGPGRMKQSCVLRQCLAPRLPHSVTCSLCGEVDQNEETQDFEKKLMECCICNEIVHPGCLQMDGEGLLNEELPNCWECPKCYQEDSSEKAQKRKMEESDEEAVQAKVLRPLRSCDEPLTPPPHSPTSMLQLIHDPVSPRGMVTRSSPGAGPSDHHSASRDERFKRRQLLRLQATERTMVREKENNPSGKKELSEVEKAKIRGSYLTVTLQRPTKELHGTSIVPKLQAITASSANLRHSPRVLVQHCPARTPQRGDEEGLGGEEEEEEEEEEEDDSAEEGGAARLNGRGSWAQDGDESWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKIDLSRCKAIVPQALSGIIKRQPVSLDLSWTNISKKQLTWLVNRLPGLKDLLLAGCSWSAVSALSTSSCPLLRTLDLRWAVGIKDPQIRDLLTPPADKPGQDNRSKLRNMTDFRLAGLDITDATLRLIIRHMPLLSRLDLSHCSHLTDQSSNLLTAVGSSTRYSLTELNMAGCNKLTDQTLIYLRRIANVTLIDLRGCKQITRKACEHFISDLSINSLYCLSDEKLIQKIS
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
10PhosphorylationPEEERIRYSQRLRGT
HHHHHHHHHHHHHHH		13.5426074081
11PhosphorylationEEERIRYSQRLRGTM
HHHHHHHHHHHHHHH		10.0426074081
17PhosphorylationYSQRLRGTMRRRYED
HHHHHHHHHHHHCCC		10.8926074081
21 (in isoform 5)Phosphorylation-28.9125159151
22PhosphorylationRGTMRRRYEDDGISD
HHHHHHHCCCCCCCH		23.1529632367
28PhosphorylationRYEDDGISDDEIEGK
HCCCCCCCHHHCCCC		44.5329255136
30 (in isoform 5)Phosphorylation-52.57-
36 (in isoform 5)Phosphorylation-52.02-
43UbiquitinationRTFDLEEKLHTNKYN
EEECHHHHHCCCCCC		35.87-
79UbiquitinationLRDPLIFKNSDGLGI
CCCCEEEECCCCCCC		48.8521890473
81PhosphorylationDPLIFKNSDGLGIKM
CCEEEECCCCCCCCC		33.3822210691
104PhosphorylationDVKMCVGSRRMVDVM
HEEHHHCCCCEEEEE		9.0522210691
115PhosphorylationVDVMDVNTQKGIEMT
EEEEECCCCHHHHEH		31.3523532336
180PhosphorylationWPRHLKESQTESTNA
CHHHHCCCCCCCCHH		40.5930576142
182PhosphorylationRHLKESQTESTNAIL
HHHCCCCCCCCHHHH		40.9830576142
185PhosphorylationKESQTESTNAILEMQ
CCCCCCCCHHHHHHC		23.5730576142
193PhosphorylationNAILEMQYPKVQKYC
HHHHHHCCHHHHHHE		12.0530576142
212 (in isoform 2)Ubiquitination-22.5021890473
386PhosphorylationDREPRRLSSRRSVLT
CCCCCCHHHCCHHHC		21.7117081983
387PhosphorylationREPRRLSSRRSVLTS
CCCCCHHHCCHHHCC		35.9817081983
390PhosphorylationRRLSSRRSVLTSPVA
CCHHHCCHHHCCCCC		21.9925159151
393PhosphorylationSSRRSVLTSPVANGV
HHCCHHHCCCCCCCC		28.9124732914
394PhosphorylationSRRSVLTSPVANGVN
HCCHHHCCCCCCCCC		17.1425159151
404PhosphorylationANGVNLDYDGLGKTC
CCCCCCCCCCCCHHH		18.3124732914
409AcetylationLDYDGLGKTCRSLPS
CCCCCCCHHHHCCHH		49.8723749302
413PhosphorylationGLGKTCRSLPSLKKT
CCCHHHHCCHHHCHH		46.94-
416PhosphorylationKTCRSLPSLKKTLAG
HHHHCCHHHCHHHCC		59.1023401153
425PhosphorylationKKTLAGDSSSDCSRG
CHHHCCCCCCCCCCC		30.7228348404
426PhosphorylationKTLAGDSSSDCSRGS
HHHCCCCCCCCCCCC		34.6328348404
427PhosphorylationTLAGDSSSDCSRGSH
HHCCCCCCCCCCCCC		46.7328348404
476UbiquitinationESLPLHKKCVPTGIE
HCCCCCCCCCCCCCC		29.71-
505SumoylationELANSDPKLALTGVP
HHHCCCCCHHHCCCC		51.9228112733
505SumoylationELANSDPKLALTGVP
HHHCCCCCHHHCCCC		51.92-
518UbiquitinationVPIVQWPKRDKLKFP
CCCCCCCCCCCCCCC		70.9821890473
518 (in isoform 3)Ubiquitination-70.9821890473
518 (in isoform 1)Ubiquitination-70.9821890473
526PhosphorylationRDKLKFPTRPKVRVP
CCCCCCCCCCCCCCC		63.84-
534PhosphorylationRPKVRVPTIPITKPH
CCCCCCCCCCCCCCC		36.2117924679
550PhosphorylationMKPAPRLTPVRPAAA
CCCCCCCCCCCCCCC		22.4829255136
558PhosphorylationPVRPAAASPIVSGAR
CCCCCCCCCCCCCHH		15.5029255136
562PhosphorylationAAASPIVSGARRRRV
CCCCCCCCCHHCCCC		27.7030266825
603PhosphorylationGPGRMKQSCVLRQCL
CCCHHHHHHHHHHHH		10.7328555341
632PhosphorylationEVDQNEETQDFEKKL
CCCCCCCCHHHHHHH		27.5317525332
637AcetylationEETQDFEKKLMECCI
CCCHHHHHHHHHHHC		51.7226051181
692PhosphorylationQKRKMEESDEEAVQA
HHHHHHHCHHHHHHH		36.7029255136
700UbiquitinationDEEAVQAKVLRPLRS
HHHHHHHHHHHCCCC		25.39-
700AcetylationDEEAVQAKVLRPLRS
HHHHHHHHHHHCCCC		25.3926051181
707PhosphorylationKVLRPLRSCDEPLTP
HHHHCCCCCCCCCCC		33.3330266825
713PhosphorylationRSCDEPLTPPPHSPT
CCCCCCCCCCCCCCC		44.4529255136
718PhosphorylationPLTPPPHSPTSMLQL
CCCCCCCCCCCHHHH		35.3329255136
720PhosphorylationTPPPHSPTSMLQLIH
CCCCCCCCCHHHHHC		29.7729255136
721PhosphorylationPPPHSPTSMLQLIHD
CCCCCCCCHHHHHCC		22.3729255136
731PhosphorylationQLIHDPVSPRGMVTR
HHHCCCCCCCCCCCC		17.8023927012
737PhosphorylationVSPRGMVTRSSPGAG
CCCCCCCCCCCCCCC		18.8830576142
739PhosphorylationPRGMVTRSSPGAGPS
CCCCCCCCCCCCCCC		31.3623401153
740PhosphorylationRGMVTRSSPGAGPSD
CCCCCCCCCCCCCCC		24.8623401153
746PhosphorylationSSPGAGPSDHHSASR
CCCCCCCCCCCCCCC		48.9724732914
750PhosphorylationAGPSDHHSASRDERF
CCCCCCCCCCCCHHH		25.2324732914
752PhosphorylationPSDHHSASRDERFKR
CCCCCCCCCCHHHHH		43.1924732914
768PhosphorylationQLLRLQATERTMVRE
HHHHHHHHHHHHHHH		17.0322210691
781PhosphorylationREKENNPSGKKELSE
HHHHCCCCCCCCHHH		66.4229214152
791AcetylationKELSEVEKAKIRGSY
CCHHHHHHHHHCCCE		61.2212655761
797PhosphorylationEKAKIRGSYLTVTLQ
HHHHHCCCEEEEEEE		13.71-
798PhosphorylationKAKIRGSYLTVTLQR
HHHHCCCEEEEEEEC		14.8222210691
800PhosphorylationKIRGSYLTVTLQRPT
HHCCCEEEEEEECCC		11.8322210691
802PhosphorylationRGSYLTVTLQRPTKE
CCCEEEEEEECCCCH		16.3728555341
807PhosphorylationTVTLQRPTKELHGTS
EEEEECCCCHHCCCC		39.0622210691
813PhosphorylationPTKELHGTSIVPKLQ
CCCHHCCCCCHHCHH		12.4428555341
814PhosphorylationTKELHGTSIVPKLQA
CCHHCCCCCHHCHHH		26.6128555341
818AcetylationHGTSIVPKLQAITAS
CCCCCHHCHHHHHCC		42.1925953088
823PhosphorylationVPKLQAITASSANLR
HHCHHHHHCCCCCCC		24.4124732914
825PhosphorylationKLQAITASSANLRHS
CHHHHHCCCCCCCCC		22.7227696853
826PhosphorylationLQAITASSANLRHSP
HHHHHCCCCCCCCCC		20.7927696853
832PhosphorylationSSANLRHSPRVLVQH
CCCCCCCCCEEEEEE		14.1525159151
844PhosphorylationVQHCPARTPQRGDEE
EEECCCCCCCCCCCC		26.3626055452
869PhosphorylationEEEEEDDSAEEGGAA
HHHHCCCCHHHCCCC		50.3230175587
883PhosphorylationARLNGRGSWAQDGDE
CCCCCCCCCCCCCCC		20.2026055452
927AcetylationWYKWCCDKRLWTKID
HHHHHCCCCCCCCCC		35.1626051181
932UbiquitinationCDKRLWTKIDLSRCK
CCCCCCCCCCHHHHH		23.73-
936PhosphorylationLWTKIDLSRCKAIVP
CCCCCCHHHHHHHHH		31.7030301811
951AcetylationQALSGIIKRQPVSLD
HHHHHHHHCCCEEEE		42.9625953088
951UbiquitinationQALSGIIKRQPVSLD
HHHHHHHHCCCEEEE		42.96-
988PhosphorylationDLLLAGCSWSAVSAL
HHHHCCCCHHHHHHH		24.13-
1015UbiquitinationLRWAVGIKDPQIRDL
CCHHCCCCCHHHHHH		58.38-
1024PhosphorylationPQIRDLLTPPADKPG
HHHHHHCCCCCCCCC		34.2327050516
1029UbiquitinationLLTPPADKPGQDNRS
HCCCCCCCCCCCCHH		53.83-
1029AcetylationLLTPPADKPGQDNRS
HCCCCCCCCCCCCHH		53.8325953088
1094PhosphorylationAVGSSTRYSLTELNM
HHCCCCCCCCEECCC		14.2320068231
1095PhosphorylationVGSSTRYSLTELNMA
HCCCCCCCCEECCCC		26.0620068231
1097PhosphorylationSSTRYSLTELNMAGC
CCCCCCCEECCCCCC		32.2721955146
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
550TPhosphorylationKinaseCDK2P24941
PSP
632TPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM2A_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 KDM2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF65_HUMANRELAphysical
20080798
H32_HUMANHIST2H3Cphysical
21251613
SKP1_HUMANSKP1physical
15070733
H31T_HUMANHIST3H3physical
16362057
UB2G2_HUMANUBE2G2physical
21988832
RB_HUMANRB1physical
25029110
E2F1_HUMANE2F1physical
25029110
IPP2_HUMANPPP1R2physical
26344197
STAG2_HUMANSTAG2physical
26344197
SKP1_HUMANSKP1physical
17463251
ATM_HUMANATMphysical
25823024
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 KDM2A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-550; SER-558;SER-692 AND SER-869, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-394; THR-550;SER-558; SER-692; THR-713; SER-718; SER-721; SER-731; SER-832; THR-844AND SER-869, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550; SER-558; THR-713;SER-718; THR-720; SER-731; SER-739 AND SER-740, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-534, AND MASSSPECTROMETRY.

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