KDM1A_HUMAN - dbPTM
KDM1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM1A_HUMAN
UniProt AC O60341
Protein Name Lysine-specific histone demethylase 1A
Gene Name KDM1A
Organism Homo sapiens (Human).
Sequence Length 852
Subcellular Localization Nucleus .
Protein Description Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7..
Protein Sequence MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
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
19PhosphorylationAAAAAAATGTEAGPG
HHHHHHHHCCCCCCC		39.6527080861
21PhosphorylationAAAAATGTEAGPGTA
HHHHHHCCCCCCCCC		20.5027080861
27PhosphorylationGTEAGPGTAGGSENG
CCCCCCCCCCCCCCC		25.8423312004
27 (in isoform 2)Phosphorylation-25.8427251275
31PhosphorylationGPGTAGGSENGSEVA
CCCCCCCCCCCCCCC		27.2823312004
35PhosphorylationAGGSENGSEVAAQPA
CCCCCCCCCCCCCCC		40.2429496963
45PhosphorylationAAQPAGLSGPAEVGP
CCCCCCCCCCCCCCC		41.6430278072
59PhosphorylationPGAVGERTPRKKEPP
CCCCCCCCCCCCCCC		24.1230278072
59 (in isoform 2)Phosphorylation-24.1227251275
69PhosphorylationKKEPPRASPPGGLAE
CCCCCCCCCCCCCCC		32.6729255136
69 (in isoform 2)Phosphorylation-32.6727251275
80PhosphorylationGLAEPPGSAGPQAGP
CCCCCCCCCCCCCCC		35.5123401153
80 (in isoform 2)Phosphorylation-35.51-
88PhosphorylationAGPQAGPTVVPGSAT
CCCCCCCEECCCCCC		32.9729255136
88 (in isoform 2)Phosphorylation-32.97-
93PhosphorylationGPTVVPGSATPMETG
CCEECCCCCCCCCCC		23.9325850435
95PhosphorylationTVVPGSATPMETGIA
EECCCCCCCCCCCCC		25.5130278072
99PhosphorylationGSATPMETGIAETPE
CCCCCCCCCCCCCCC		27.8630576142
104PhosphorylationMETGIAETPEGRRTS
CCCCCCCCCCCCCCC		20.0225159151
104 (in isoform 2)Phosphorylation-20.0227251275
111PhosphorylationTPEGRRTSRRKRAKV
CCCCCCCCHHHHHHH		28.42-
114"N6,N6-dimethyllysine"GRRTSRRKRAKVEYR
CCCCCHHHHHHHHHH		56.44-
114MethylationGRRTSRRKRAKVEYR
CCCCCHHHHHHHHHH		56.44-
117SumoylationTSRRKRAKVEYREMD
CCHHHHHHHHHHHHH		39.36-
117SumoylationTSRRKRAKVEYREMD
CCHHHHHHHHHHHHH		39.36-
120UbiquitinationRKRAKVEYREMDESL
HHHHHHHHHHHHHHH		18.1723503661
123UbiquitinationAKVEYREMDESLANL
HHHHHHHHHHHHHCC		5.2523503661
126PhosphorylationEYREMDESLANLSED
HHHHHHHHHHCCCHH		28.6322167270
126 (in isoform 2)Phosphorylation-28.63-
131PhosphorylationDESLANLSEDEYYSE
HHHHHCCCHHHHCCH		42.6922167270
131UbiquitinationDESLANLSEDEYYSE
HHHHHCCCHHHHCCH		42.6927667366
131 (in isoform 2)Phosphorylation-42.6927251275
135PhosphorylationANLSEDEYYSEEERN
HCCCHHHHCCHHHHH		25.3122167270
135 (in isoform 2)Phosphorylation-25.31-
136PhosphorylationNLSEDEYYSEEERNA
CCCHHHHCCHHHHHH		13.9322167270
136 (in isoform 2)Phosphorylation-13.93-
137PhosphorylationLSEDEYYSEEERNAK
CCHHHHCCHHHHHHH		37.3222167270
137 (in isoform 2)Phosphorylation-37.3227251275
141UbiquitinationEYYSEEERNAKAEKE
HHCCHHHHHHHHHHH		52.2423000965
146UbiquitinationEERNAKAEKEKKLPP
HHHHHHHHHHCCCCC		62.1321890473
151UbiquitinationKAEKEKKLPPPPPQA
HHHHHCCCCCCCCCC		13.1023000965
155UbiquitinationEKKLPPPPPQAPPEE
HCCCCCCCCCCCCCC		39.1327667366
166PhosphorylationPPEEENESEPEEPSG
CCCCCCCCCCCCCCC		70.7729255136
166 (in isoform 2)Phosphorylation-70.7720873877
172PhosphorylationESEPEEPSGVEGAAF
CCCCCCCCCCCHHHH		59.7730266825
172 (in isoform 2)Phosphorylation-59.7722210691
181PhosphorylationVEGAAFQSRLPHDRM
CCHHHHHHCCCCCCC		29.3628176443
182 (in isoform 2)Phosphorylation-41.2625247763
183 (in isoform 2)Phosphorylation-5.5225247763
186 (in isoform 2)Phosphorylation-39.8620873877
187MethylationQSRLPHDRMTSQEAA
HHCCCCCCCCHHHHH		27.52115482339
189PhosphorylationRLPHDRMTSQEAACF
CCCCCCCCHHHHHCC		28.3126074081
190PhosphorylationLPHDRMTSQEAACFP
CCCCCCCHHHHHCCH		19.3826074081
192 (in isoform 2)Phosphorylation-37.6920873877
201 (in isoform 2)Phosphorylation-44.7620873877
268AcetylationLINFGIYKRIKPLPT
CEEEEECCCCCCCCC		45.8125953088
268UbiquitinationLINFGIYKRIKPLPT
CEEEEECCCCCCCCC		45.8123000965
271UbiquitinationFGIYKRIKPLPTKKT
EEECCCCCCCCCCCC		44.5323000965
275PhosphorylationKRIKPLPTKKTGKVI
CCCCCCCCCCCCCEE		53.5122964224
276AcetylationRIKPLPTKKTGKVII
CCCCCCCCCCCCEEE		46.5325953088
276UbiquitinationRIKPLPTKKTGKVII
CCCCCCCCCCCCEEE		46.53-
277UbiquitinationIKPLPTKKTGKVIII
CCCCCCCCCCCEEEE		66.06-
280UbiquitinationLPTKKTGKVIIIGSG
CCCCCCCCEEEECCC		35.18-
284UbiquitinationKTGKVIIIGSGVSGL
CCCCEEEECCCHHHH		2.1721963094
288UbiquitinationVIIIGSGVSGLAAAR
EEEECCCHHHHHHHH		4.3723000965
288 (in isoform 2)Ubiquitination-4.37-
290UbiquitinationIIGSGVSGLAAARQL
EECCCHHHHHHHHHH		19.5421963094
291UbiquitinationIGSGVSGLAAARQLQ
ECCCHHHHHHHHHHH		1.9823000965
299PhosphorylationAAARQLQSFGMDVTL
HHHHHHHHCCCCEEE		32.15-
305PhosphorylationQSFGMDVTLLEARDR
HHCCCCEEEEEHHHH		22.74-
322TrimethylationGRVATFRKGNYVADL
CEEEEEECCCEEEEC		47.52-
322MethylationGRVATFRKGNYVADL
CEEEEEECCCEEEEC		47.52-
322UbiquitinationGRVATFRKGNYVADL
CEEEEEECCCEEEEC		47.52-
335PhosphorylationDLGAMVVTGLGGNPM
ECCCEEEECCCCCCH		18.45-
346PhosphorylationGNPMAVVSKQVNMEL
CCCHHHEEHHHCHHH		15.69-
346UbiquitinationGNPMAVVSKQVNMEL
CCCHHHEEHHHCHHH		15.6921963094
347UbiquitinationNPMAVVSKQVNMELA
CCHHHEEHHHCHHHH		46.81-
352UbiquitinationVSKQVNMELAKIKQK
EEHHHCHHHHHHHHH		40.1321963094
355AcetylationQVNMELAKIKQKCPL
HHCHHHHHHHHHCCC		64.1625953088
355UbiquitinationQVNMELAKIKQKCPL
HHCHHHHHHHHHCCC		64.1621906983
355 (in isoform 1)Ubiquitination-64.1621890473
359UbiquitinationELAKIKQKCPLYEAN
HHHHHHHHCCCEECC		32.5829967540
363PhosphorylationIKQKCPLYEANGQAV
HHHHCCCEECCCCCC		9.7227642862
372UbiquitinationANGQAVPKEKDEMVE
CCCCCCCHHHHHHHH		71.4529967540
374UbiquitinationGQAVPKEKDEMVEQE
CCCCCHHHHHHHHHH		66.1821906983
374 (in isoform 1)Ubiquitination-66.1821890473
375 (in isoform 2)Ubiquitination-50.7621890473
377SulfoxidationVPKEKDEMVEQEFNR
CCHHHHHHHHHHHHH		6.0321406390
398 (in isoform 2)Ubiquitination-10.4121890473
421UbiquitinationVVIQLQEKHVKDEQI
HHHHHHHHCCCHHHH		40.5123503661
424SumoylationQLQEKHVKDEQIEHW
HHHHHCCCHHHHHHH		56.09-
424SumoylationQLQEKHVKDEQIEHW
HHHHHCCCHHHHHHH		56.09-
424UbiquitinationQLQEKHVKDEQIEHW
HHHHHCCCHHHHHHH		56.0921906983
424 (in isoform 1)Ubiquitination-56.0921890473
432AcetylationDEQIEHWKKIVKTQE
HHHHHHHHHHHHCHH		34.237972565
432UbiquitinationDEQIEHWKKIVKTQE
HHHHHHHHHHHHCHH		34.2321906983
432 (in isoform 1)Ubiquitination-34.2321890473
433AcetylationEQIEHWKKIVKTQEE
HHHHHHHHHHHCHHH		47.767972575
433UbiquitinationEQIEHWKKIVKTQEE
HHHHHHHHHHHCHHH		47.76-
436AcetylationEHWKKIVKTQEELKE
HHHHHHHHCHHHHHH		48.227972585
436UbiquitinationEHWKKIVKTQEELKE
HHHHHHHHCHHHHHH		48.2229967540
441UbiquitinationIVKTQEELKELLNKM
HHHCHHHHHHHHHHH		5.2723503661
442SumoylationVKTQEELKELLNKMV
HHCHHHHHHHHHHHH		49.98-
442SumoylationVKTQEELKELLNKMV
HHCHHHHHHHHHHHH		49.9828112733
442UbiquitinationVKTQEELKELLNKMV
HHCHHHHHHHHHHHH		49.9823000965
442 (in isoform 1)Ubiquitination-49.9821890473
443UbiquitinationKTQEELKELLNKMVN
HCHHHHHHHHHHHHC		71.7323000965
444UbiquitinationTQEELKELLNKMVNL
CHHHHHHHHHHHHCH		6.4523503661
445UbiquitinationQEELKELLNKMVNLK
HHHHHHHHHHHHCHH		6.4123503661
447UbiquitinationELKELLNKMVNLKEK
HHHHHHHHHHCHHHH		44.1623000965
447 (in isoform 1)Ubiquitination-44.1621890473
448UbiquitinationLKELLNKMVNLKEKI
HHHHHHHHHCHHHHH		2.0533845483
448 (in isoform 2)Ubiquitination-2.0521890473
449UbiquitinationKELLNKMVNLKEKIK
HHHHHHHHCHHHHHH		8.9523000965
4522-HydroxyisobutyrylationLNKMVNLKEKIKELH
HHHHHCHHHHHHHHH		52.32-
452SumoylationLNKMVNLKEKIKELH
HHHHHCHHHHHHHHH		52.32-
452UbiquitinationLNKMVNLKEKIKELH
HHHHHCHHHHHHHHH		52.3223000965
454UbiquitinationKMVNLKEKIKELHQQ
HHHCHHHHHHHHHHH		58.45-
456UbiquitinationVNLKEKIKELHQQYK
HCHHHHHHHHHHHHH		66.3527667366
456 (in isoform 2)Ubiquitination-66.3521890473
460UbiquitinationEKIKELHQQYKEASE
HHHHHHHHHHHHHHC		62.0129967540
462UbiquitinationIKELHQQYKEASEVK
HHHHHHHHHHHHCCC		12.2923000965
463UbiquitinationKELHQQYKEASEVKP
HHHHHHHHHHHCCCC		42.3332015554
466PhosphorylationHQQYKEASEVKPPRD
HHHHHHHHCCCCCCC		43.9729116813
466UbiquitinationHQQYKEASEVKPPRD
HHHHHHHHCCCCCCC		43.9723000965
466 (in isoform 2)Ubiquitination-43.9721890473
467UbiquitinationQQYKEASEVKPPRDI
HHHHHHHCCCCCCCC		62.7021890473
469SumoylationYKEASEVKPPRDITA
HHHHHCCCCCCCCCH		45.3028112733
469UbiquitinationYKEASEVKPPRDITA
HHHHHCCCCCCCCCH		45.3029967540
471UbiquitinationEASEVKPPRDITAEF
HHHCCCCCCCCCHHH		40.6421890473
471 (in isoform 2)Ubiquitination-40.6421890473
472UbiquitinationASEVKPPRDITAEFL
HHCCCCCCCCCHHHH		57.3923000965
476UbiquitinationKPPRDITAEFLVKSK
CCCCCCCHHHHHHCC		13.0823000965
480UbiquitinationDITAEFLVKSKHRDL
CCCHHHHHHCCCCCH		8.8127667366
481UbiquitinationITAEFLVKSKHRDLT
CCHHHHHHCCCCCHH		56.8021906983
481 (in isoform 1)Ubiquitination-56.8021890473
487UbiquitinationVKSKHRDLTALCKEY
HHCCCCCHHHHHHHH		2.8132015554
490 (in isoform 2)Phosphorylation-3.4527251275
492UbiquitinationRDLTALCKEYDELAE
CCHHHHHHHHHHHHH		61.2229967540
493UbiquitinationDLTALCKEYDELAET
CHHHHHHHHHHHHHH		58.1629967540
503AcetylationELAETQGKLEEKLQE
HHHHHHCHHHHHHHH		42.8026051181
503UbiquitinationELAETQGKLEEKLQE
HHHHHHCHHHHHHHH		42.80PubMed
503 (in isoform 1)Ubiquitination-42.8021890473
505UbiquitinationAETQGKLEEKLQELE
HHHHCHHHHHHHHHH		57.4832015554
505 (in isoform 2)Ubiquitination-57.4821890473
507UbiquitinationTQGKLEEKLQELEAN
HHCHHHHHHHHHHHC		46.2029967540
516UbiquitinationQELEANPPSDVYLSS
HHHHHCCCCCEECCH		42.8629967540
527UbiquitinationYLSSRDRQILDWHFA
ECCHHHHHHHEEECC		44.9029967540
527 (in isoform 2)Ubiquitination-44.9021890473
531UbiquitinationRDRQILDWHFANLEF
HHHHHHEEECCCCEE		5.7629967540
585SumoylationLAEGLDIKLNTAVRQ
HHCCCCEECCHHHHH		35.04-
585UbiquitinationLAEGLDIKLNTAVRQ
HHCCCCEECCHHHHH		35.0421963094
588PhosphorylationGLDIKLNTAVRQVRY
CCCEECCHHHHHHEE		36.65-
591UbiquitinationIKLNTAVRQVRYTAS
EECCHHHHHHEECCC		27.1521963094
605UbiquitinationSGCEVIAVNTRSTSQ
CCCEEEEEECCCCCC		5.3021963094
609UbiquitinationVIAVNTRSTSQTFIY
EEEEECCCCCCCEEE		30.3021963094
611PhosphorylationAVNTRSTSQTFIYKC
EEECCCCCCCEEEEC		28.5923917254
611UbiquitinationAVNTRSTSQTFIYKC
EEECCCCCCCEEEEC		28.5921963094
617UbiquitinationTSQTFIYKCDAVLCT
CCCCEEEECCEEEEC		22.33-
631UbiquitinationTLPLGVLKQQPPAVQ
CCCCCHHCCCCCCCE		44.47-
647UbiquitinationVPPLPEWKTSAVQRM
CCCCCCCCCHHHHHC		30.8221906983
647 (in isoform 1)Ubiquitination-30.8221890473
653UbiquitinationWKTSAVQRMGFGNLN
CCCHHHHHCCCCCCC		22.1621963094
661UbiquitinationMGFGNLNKVVLCFDR
CCCCCCCCEEEEEEE		36.57-
667UbiquitinationNKVVLCFDRVFWDPS
CCEEEEEEEEECCCC		44.8521963094
671UbiquitinationLCFDRVFWDPSVNLF
EEEEEEECCCCCCEE		17.4721963094
671 (in isoform 2)Ubiquitination-17.4721890473
673UbiquitinationFDRVFWDPSVNLFGH
EEEEECCCCCCEECC		30.6721963094
683PhosphorylationNLFGHVGSTTASRGE
CEECCCCCCCCCCCC		22.84-
687PhosphorylationHVGSTTASRGELFLF
CCCCCCCCCCCEEHH		38.43-
732AcetylationGRCLAILKGIFGSSA
HHHHHHHHHHHCCCC		43.7926051181
732UbiquitinationGRCLAILKGIFGSSA
HHHHHHHHHHHCCCC		43.79-
744UbiquitinationSSAVPQPKETVVSRW
CCCCCCCCCCEEEEE		61.8523000965
744 (in isoform 1)Ubiquitination-61.8521890473
746PhosphorylationAVPQPKETVVSRWRA
CCCCCCCCEEEEEEC		32.1320068231
750UbiquitinationPKETVVSRWRADPWA
CCCCEEEEEECCCCC		18.4523000965
764UbiquitinationARGSYSYVAAGSSGN
CCCCEEEEECCCCCC		2.1223000965
768UbiquitinationYSYVAAGSSGNDYDL
EEEEECCCCCCCCCC		30.2823000965
768 (in isoform 2)Ubiquitination-30.2821890473
770UbiquitinationYVAAGSSGNDYDLMA
EEECCCCCCCCCCCC		32.5023000965
807PhosphorylationGEHTIRNYPATVHGA
CCCCHHCCCHHHHHH		5.6128152594
810PhosphorylationTIRNYPATVHGALLS
CHHCCCHHHHHHHHH		14.4528152594
817PhosphorylationTVHGALLSGLREAGR
HHHHHHHHHHHHHHH		36.3124719451
834PhosphorylationDQFLGAMYTLPRQAT
HHHHHHHHCCCCCCC		12.4626074081
835PhosphorylationQFLGAMYTLPRQATP
HHHHHHHCCCCCCCC		19.7326074081
838MethylationGAMYTLPRQATPGVP
HHHHCCCCCCCCCCC		41.7197816407
841PhosphorylationYTLPRQATPGVPAQQ
HCCCCCCCCCCCCCC		16.5528348404
849PhosphorylationPGVPAQQSPSM----
CCCCCCCCCCC----		13.5825159151
851PhosphorylationVPAQQSPSM------
CCCCCCCCC------		42.2330266825
873 (in isoform 2)Phosphorylation-27251275
875 (in isoform 2)Phosphorylation-27251275
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
126SPhosphorylationKinasePLK1P53350
PSP
131SPhosphorylationKinaseCSNK2A1P68400
GPS
137SPhosphorylationKinaseCSNK2A1P68400
GPS
683SPhosphorylationKinaseGSK3BP49841
PSP
687SPhosphorylationKinaseCSNK1A1P48729
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM1A_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 KDM1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HM20B_HUMANHMG20Bphysical
12032298
PF21A_HUMANPHF21Aphysical
15325272
ZN217_HUMANZNF217physical
12493763
ZMYM3_HUMANZMYM3physical
12493763
ZMYM2_HUMANZMYM2physical
12493763
GSE1_HUMANGSE1physical
12493763
GTF2I_HUMANGTF2Iphysical
12493763
KDM1A_HUMANKDM1Aphysical
12493763
PF21A_HUMANPHF21Aphysical
12493763
HM20B_HUMANHMG20Bphysical
12493763
HDAC1_HUMANHDAC1physical
12493763
HDAC2_HUMANHDAC2physical
12493763
HDAC1_HUMANHDAC1physical
11171972
RCOR1_HUMANRCOR1physical
11171972
SIN3A_HUMANSIN3Aphysical
11171972
MIC60_HUMANIMMTphysical
16169070
CC90B_HUMANCCDC90Bphysical
16169070
U119A_HUMANUNC119physical
16169070
SETB1_HUMANSETDB1physical
16169070
GDF9_HUMANGDF9physical
16169070
NSD2_HUMANWHSC1physical
18156491
PRDM1_HUMANPRDM1physical
19124609
H31_HUMANHIST1H3Aphysical
16956976
RCOR1_HUMANRCOR1physical
16885027
P53_HUMANTP53physical
18573881
ESCO2_HUMANESCO2physical
18501190
H31_HUMANHIST1H3Aphysical
16223729
RREB1_HUMANRREB1physical
16140033
ZMYM2_HUMANZMYM2physical
16140033
ZN217_HUMANZNF217physical
16140033
PF21A_HUMANPHF21Aphysical
16140033
RCOR1_HUMANRCOR1physical
16140033
HDAC1_HUMANHDAC1physical
16140033
CTBP1_HUMANCTBP1physical
16140033
HM20A_HUMANHMG20Aphysical
16140033
HM20B_HUMANHMG20Bphysical
16140033
H31_HUMANHIST1H3Aphysical
16140033
ZMYM3_HUMANZMYM3physical
16079794
ZMYM2_HUMANZMYM2physical
16079794
ZN516_HUMANZNF516physical
16079794
GSE1_HUMANGSE1physical
16079794
ZN217_HUMANZNF217physical
16079794
PF21A_HUMANPHF21Aphysical
16079794
RCOR1_HUMANRCOR1physical
16079794
HDAC1_HUMANHDAC1physical
16079794
HDAC2_HUMANHDAC2physical
16079794
CTBP1_HUMANCTBP1physical
16079794
HM20B_HUMANHMG20Bphysical
16079794
H31_HUMANHIST1H3Aphysical
16079794
RB_HUMANRB1physical
18216119
HDAC1_HUMANHDAC1physical
11102443
HDAC2_HUMANHDAC2physical
11102443
RCOR1_HUMANRCOR1physical
11102443
P53_HUMANTP53physical
17805299
H32_HUMANHIST2H3Cphysical
17687328
HDAC1_HUMANHDAC1physical
17634443
MBD2_HUMANMBD2physical
17634443
ESR1_HUMANESR1physical
17289570
EP300_HUMANEP300physical
17289570
PELP1_HUMANPELP1physical
20448663
E2F1_HUMANE2F1physical
20603083
ESCO1_HUMANESCO1physical
20331966
H31_HUMANHIST1H3Aphysical
20228790
RCOR1_HUMANRCOR1physical
20164337
HDAC2_HUMANHDAC2physical
20164337
HDAC1_HUMANHDAC1physical
20856864
RCOR1_HUMANRCOR1physical
21142040
MYPT1_HUMANPPP1R12Aphysical
21115810
CHD3_HUMANCHD3physical
19703393
HDAC1_HUMANHDAC1physical
19703393
HDAC2_HUMANHDAC2physical
19703393
MTA1_HUMANMTA1physical
19703393
MTA2_HUMANMTA2physical
19703393
MTA3_HUMANMTA3physical
19703393
MBD3_HUMANMBD3physical
19703393
SNAI1_HUMANSNAI1physical
20389281
RCOR1_HUMANRCOR1physical
20389281
TAL1_HUMANTAL1physical
19497860
MEF2D_MOUSEMef2dphysical
20833138
RCOR1_HUMANRCOR1physical
22143567
HDAC1_HUMANHDAC1physical
22143567
E2F1_HUMANE2F1physical
21320024
CHD3_HUMANCHD3physical
21937684
KDM1A_HUMANKDM1Aphysical
21937684
MTA2_HUMANMTA2physical
21937684
MTA3_HUMANMTA3physical
21937684
HDAC1_HUMANHDAC1physical
21937684
HDAC2_HUMANHDAC2physical
21937684
RBBP7_HUMANRBBP7physical
21937684
RBBP4_HUMANRBBP4physical
21937684
MBD3_HUMANMBD3physical
21937684
STAT3_HUMANSTAT3physical
21098664
DNMT1_HUMANDNMT1physical
22278882
YETS4_HUMANYEATS4physical
22068108
NR2C2_HUMANNR2C2physical
21670149
NR2C1_HUMANNR2C1physical
21670149
DNMT1_HUMANDNMT1physical
21670149
RCOR1_HUMANRCOR1physical
21670149
HDAC1_HUMANHDAC1physical
21670149
HDAC2_HUMANHDAC2physical
21670149
MTA2_HUMANMTA2physical
21670149
MTA1_HUMANMTA1physical
21670149
CHD4_HUMANCHD4physical
21670149
RBBP4_HUMANRBBP4physical
21670149
HDAC3_HUMANHDAC3physical
21670149
TIF1B_HUMANTRIM28physical
21670149
RCOR1_HUMANRCOR1physical
21602794
SMRC1_HUMANSMARCC1physical
22939629
TIM50_HUMANTIMM50physical
22939629
KINH_HUMANKIF5Bphysical
22939629
UBE3C_HUMANUBE3Cphysical
22939629
NADAP_HUMANSLC4A1APphysical
22939629
SUH_HUMANRBPJphysical
23022380
NOTC1_HUMANNOTCH1physical
23022380
H32_HUMANHIST2H3Cphysical
15620353
HDAC2_HUMANHDAC2physical
21258344
HDAC1_HUMANHDAC1physical
21258344
HM20B_HUMANHMG20Bphysical
21258344
HM20A_HUMANHMG20Aphysical
21258344
GSE1_HUMANGSE1physical
21258344
RCOR3_HUMANRCOR3physical
21258344
RCOR1_HUMANRCOR1physical
21258344
MCAT_HUMANSLC25A20physical
23178685
HDAC3_HUMANHDAC3physical
23752268
RN168_HUMANRNF168physical
24217620
RCOR1_HUMANRCOR1physical
24217620
KDM1A_HUMANKDM1Aphysical
23455924
WASC3_HUMANCCDC53physical
25416956
TRI39_HUMANTRIM39physical
25416956
TRI54_HUMANTRIM54physical
25416956
KLC3_HUMANKLC3physical
25416956
UBP28_HUMANUSP28physical
24075993
H31_HUMANHIST1H3Aphysical
20389281
CSK22_HUMANCSNK2A2physical
25999347
PPM1D_HUMANPPM1Dphysical
25999347
RN168_HUMANRNF168physical
25999347
TP53B_HUMANTP53BP1physical
25999347
CSN2_HUMANCOPS2physical
26344197
HDAC1_HUMANHDAC1physical
26344197
HDAC2_HUMANHDAC2physical
26344197
RCOR1_HUMANRCOR1physical
26344197
RCOR3_HUMANRCOR3physical
26344197
TRI39_HUMANTRIM39physical
21516116
NMI_HUMANNMIphysical
21516116
ZBED1_HUMANZBED1physical
21516116
BMAL1_HUMANARNTLphysical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
CAVN1_HUMANPTRFphysical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CCD93_HUMANCCDC93physical
27173435
VPS50_HUMANCCDC132physical
27173435
RCOR1_HUMANRCOR1physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
DZIP3_HUMANDZIP3physical
27173435
VPS53_HUMANVPS53physical
27173435
PSMD9_HUMANPSMD9physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
GOGA5_HUMANGOLGA5physical
27173435
TUFT1_HUMANTUFT1physical
27173435
YETS4_HUMANYEATS4physical
27173435
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 KDM1A_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 THR-104; SER-131; SER-137AND SER-166, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-137, ANDMASS 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-80; THR-104; SER-126;SER-131; SER-137; SER-166 AND SER-849, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-137, ANDMASS SPECTROMETRY.
"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 SER-166, AND MASSSPECTROMETRY.
"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-166, AND MASSSPECTROMETRY.

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