KDM5B_HUMAN - dbPTM
KDM5B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM5B_HUMAN
UniProt AC Q9UGL1
Protein Name Lysine-specific demethylase 5B
Gene Name KDM5B
Organism Homo sapiens (Human).
Sequence Length 1544
Subcellular Localization Nucleus .
Protein Description Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. [PubMed: 24952722]
Protein Sequence MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTVKDAPSRK
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
63UbiquitinationAEQTGICKVRPPPDW
HHHHCCCCCCCCCCC		39.08-
80UbiquitinationPFACDVDKLHFTPRI
CCCCCCCCCCCCHHH		43.65-
80 (in isoform 2)Ubiquitination-43.65-
84PhosphorylationDVDKLHFTPRIQRLN
CCCCCCCCHHHHHHH		10.8324719451
100UbiquitinationLEAQTRVKLNFLDQI
HHHHHHHHHHHHHHH		34.13-
100 (in isoform 2)Ubiquitination-34.13-
109UbiquitinationNFLDQIAKYWELQGS
HHHHHHHHHHHHCCC		53.1521906983
109 (in isoform 1)Ubiquitination-53.1521890473
109 (in isoform 2)Ubiquitination-53.1521890473
110PhosphorylationFLDQIAKYWELQGST
HHHHHHHHHHHCCCC		8.62-
119UbiquitinationELQGSTLKIPHVERK
HHCCCCCCCCCHHHH		55.04-
119 (in isoform 2)Ubiquitination-55.04-
126UbiquitinationKIPHVERKILDLFQL
CCCCHHHHHHHHHHH		33.83-
126 (in isoform 2)Ubiquitination-33.83-
148SumoylationGGFAVVCKDRKWTKI
CCEEEEECCCCCCCC		49.2928112733
148UbiquitinationGGFAVVCKDRKWTKI
CCEEEEECCCCCCCC		49.29-
148 (in isoform 2)Ubiquitination-49.29-
157PhosphorylationRKWTKIATKMGFAPG
CCCCCCCHHCCCCCC		25.66-
158UbiquitinationKWTKIATKMGFAPGK
CCCCCCHHCCCCCCC		28.18-
158 (in isoform 2)Ubiquitination-28.18-
165UbiquitinationKMGFAPGKAVGSHIR
HCCCCCCCCHHHHHH		38.55-
165 (in isoform 2)Ubiquitination-38.55-
182PhosphorylationYERILNPYNLFLSGD
HHHHCCHHHEECCCC		24.3524260401
190PhosphorylationNLFLSGDSLRCLQKP
HEECCCCHHHHCCCC		22.6524260401
196AcetylationDSLRCLQKPNLTTDT
CHHHHCCCCCCCCCC		23.9569587
196UbiquitinationDSLRCLQKPNLTTDT
CHHHHCCCCCCCCCC		23.95-
196 (in isoform 2)Ubiquitination-23.95-
204SumoylationPNLTTDTKDKEYKPH
CCCCCCCCCCCCCCC		70.3928112733
206UbiquitinationLTTDTKDKEYKPHDI
CCCCCCCCCCCCCCC		65.58-
206 (in isoform 2)Ubiquitination-65.58-
208PhosphorylationTDTKDKEYKPHDIPQ
CCCCCCCCCCCCCCC		35.2428555341
209SumoylationDTKDKEYKPHDIPQR
CCCCCCCCCCCCCCC		36.65-
209SumoylationDTKDKEYKPHDIPQR
CCCCCCCCCCCCCCC		36.6528112733
209UbiquitinationDTKDKEYKPHDIPQR
CCCCCCCCCCCCCCC		36.65-
240 (in isoform 2)Phosphorylation-39.1822985185
242SumoylationRAEAMNIKIEPEETT
HHHHHCCCCCCHHCH		35.69-
242SumoylationRAEAMNIKIEPEETT
HHHHHCCCCCCHHCH		35.6928112733
242UbiquitinationRAEAMNIKIEPEETT
HHHHHCCCCCCHHCH		35.69-
248PhosphorylationIKIEPEETTEARTHN
CCCCCHHCHHHHHHH		28.4228152594
249PhosphorylationKIEPEETTEARTHNL
CCCCHHCHHHHHHHH		30.8128152594
253PhosphorylationEETTEARTHNLRRRM
HHCHHHHHHHHHHHC		23.3628152594
264PhosphorylationRRRMGCPTPKCENEK
HHHCCCCCCCCCCHH		39.1827251275
270 (in isoform 2)Phosphorylation-28.2725690035
274SumoylationCENEKEMKSSIKQEP
CCCHHHHHHHHCCCC		41.9928112733
278SumoylationKEMKSSIKQEPIERK
HHHHHHHCCCCCCCC		51.02-
278SumoylationKEMKSSIKQEPIERK
HHHHHHHCCCCCCCC		51.0228112733
278UbiquitinationKEMKSSIKQEPIERK
HHHHHHHCCCCCCCC		51.02-
314 (in isoform 2)Ubiquitination-2.35-
329 (in isoform 2)Ubiquitination-18.76-
331 (in isoform 2)Ubiquitination-54.11-
355UbiquitinationKGDWRCPKCLAQECS
CCCCCCCHHHHHHCC		45.57-
363UbiquitinationCLAQECSKPQEAFGF
HHHHHCCCHHHHHCH		63.48-
378PhosphorylationEQAARDYTLRTFGEM
HHHHHHHHHHHHHHH		17.6624719451
390UbiquitinationGEMADAFKSDYFNMP
HHHHHHHHHCCCCCC		44.10-
391 (in isoform 2)Ubiquitination-30.96-
399 (in isoform 2)Ubiquitination-12.97-
408UbiquitinationVPTELVEKEFWRLVS
CCHHHHHHHHHHHHH		51.21-
415PhosphorylationKEFWRLVSTIEEDVT
HHHHHHHHCCCCCCE		28.41-
426 (in isoform 2)Ubiquitination-11.85-
429 (in isoform 2)Phosphorylation-4.6527642862
444UbiquitinationGFPVRDGKIKLSPEE
CCCCCCCCEECCHHH		40.74-
444 (in isoform 2)Ubiquitination-40.74-
457PhosphorylationEEEEYLDSGWNLNNM
HHHHHHHCCCCCCCC		43.01-
476PhosphorylationQSVLAHITADICGMK
HHHHHHHHHHHHCCC		14.38-
535UbiquitinationEQLENVMKKLAPELF
HHHHHHHHHHCHHHH		40.11-
572 (in isoform 2)Ubiquitination-26.40-
635UbiquitinationSHDEMICKMASKADV
CCCHHHHHHCCCCCH		26.95-
639UbiquitinationMICKMASKADVLDVV
HHHHHCCCCCHHHEE		38.78-
663UbiquitinationAIMIEDEKALRETVR
CHHHCCHHHHHHHHH		66.11-
671UbiquitinationALRETVRKLGVIDSE
HHHHHHHHHCCCCHH		45.30-
671 (in isoform 2)Ubiquitination-45.30-
675 (in isoform 2)Ubiquitination-4.59-
699 (in isoform 2)Ubiquitination-3.05-
707 (in isoform 2)Ubiquitination-20.55-
729UbiquitinationLCSCPPYKYKLRYRY
HHCCCCCCEEEEEEE		41.50-
730PhosphorylationCSCPPYKYKLRYRYT
HCCCCCCEEEEEEEE		14.93-
730 (in isoform 2)Ubiquitination-14.93-
734PhosphorylationPYKYKLRYRYTLDDL
CCCEEEEEEEEHHHH		20.5725884760
736PhosphorylationKYKLRYRYTLDDLYP
CEEEEEEEEHHHHHH		11.6125884760
742PhosphorylationRYTLDDLYPMMNALK
EEEHHHHHHHHHHHH		8.9725884760
749UbiquitinationYPMMNALKLRAESYN
HHHHHHHHHHHHHHH		33.25-
765 (in isoform 2)Ubiquitination-12.90-
769SumoylationVNEALEAKINKKKSL
HHHHHHHHCCCCCCH		37.1228112733
769UbiquitinationVNEALEAKINKKKSL
HHHHHHHHCCCCCCH		37.12-
774UbiquitinationEAKINKKKSLVSFKA
HHHCCCCCCHHHHHH		51.11-
780UbiquitinationKKSLVSFKALIEESE
CCCHHHHHHHHHHHH		34.47-
785 (in isoform 2)Ubiquitination-45.03-
789UbiquitinationLIEESEMKKFPDNDL
HHHHHHHHCCCCCHH		47.40-
790UbiquitinationIEESEMKKFPDNDLL
HHHHHHHCCCCCHHH		61.90-
809UbiquitinationLVTQDAEKCASVAQQ
HHHCCHHHHHHHHHH		36.50-
810 (in isoform 2)Ubiquitination-2.28-
812PhosphorylationQDAEKCASVAQQLLN
CCHHHHHHHHHHHHC		27.7024719451
816 (in isoform 2)Ubiquitination-37.87-
821UbiquitinationAQQLLNGKRQTRYRS
HHHHHCCCCCCCCCC		40.01-
825 (in isoform 2)Ubiquitination-19.27-
826 (in isoform 2)Ubiquitination-16.71-
832AcetylationRYRSGGGKSQNQLTV
CCCCCCCCCCCCCCH		52.7423749302
832UbiquitinationRYRSGGGKSQNQLTV
CCCCCCCCCCCCCCH		52.7421906983
832 (in isoform 1)Ubiquitination-52.7421890473
845 (in isoform 2)Ubiquitination-5.33-
857 (in isoform 2)Ubiquitination-16.18-
859PhosphorylationLPCVLSQTPLLKDLL
HHHHHHCCHHHHHHH		16.7224719451
868 (in isoform 2)Ubiquitination-32.9221890473
932PhosphorylationQACLDPSSLTLDDMR
HHHCCCHHCCHHHHH		30.6622210691
934PhosphorylationCLDPSSLTLDDMRRL
HCCCHHCCHHHHHHH		30.0422210691
956UbiquitinationAPYSAVEKAMARLQE
CCHHHHHHHHHHHHH		36.5421906983
956 (in isoform 1)Ubiquitination-36.5421890473
974UbiquitinationVSEHWDDKAKSLLKA
HHHHCCHHHHHHHHH		56.06-
976UbiquitinationEHWDDKAKSLLKARP
HHCCHHHHHHHHHCC		47.58-
977PhosphorylationHWDDKAKSLLKARPR
HCCHHHHHHHHHCCC		43.7424719451
980UbiquitinationDKAKSLLKARPRHSL
HHHHHHHHHCCCCCH		47.87-
986PhosphorylationLKARPRHSLNSLATA
HHHCCCCCHHHHHHH		30.4430266825
989PhosphorylationRPRHSLNSLATAVKE
CCCCCHHHHHHHHHH		25.3630266825
992PhosphorylationHSLNSLATAVKEIEE
CCHHHHHHHHHHHHH		36.9627732954
992 (in isoform 2)Ubiquitination-36.9621890473
995UbiquitinationNSLATAVKEIEEIPA
HHHHHHHHHHHHCCC		50.97-
1010 (in isoform 2)Ubiquitination-6.67-
1011UbiquitinationLPNGAALKDSVQRAR
CCCCHHHHHHHHHHH		43.1421906983
1011 (in isoform 1)Ubiquitination-43.1421890473
1012 (in isoform 2)Ubiquitination-55.69-
1016 (in isoform 2)Ubiquitination-29.45-
1031 (in isoform 2)Ubiquitination-30.35-
1047 (in isoform 2)Ubiquitination-28.2821890473
1055PhosphorylationSIPVHLNSLPRLETL
CCCCCHHHCCCHHHH		46.2220860994
1102UbiquitinationDIGLLGLKRKQRKLK
CHHHHCHHHHHHHCC		56.61-
1107AcetylationGLKRKQRKLKEPLPN
CHHHHHHHCCCCCCC		62.517221493
1119PhosphorylationLPNGKKKSTKLESLS
CCCCCCCCCHHHCHH		39.3926670566
1120PhosphorylationPNGKKKSTKLESLSD
CCCCCCCCHHHCHHH		48.8326670566
1121SumoylationNGKKKSTKLESLSDL
CCCCCCCHHHCHHHH		58.30-
1121SumoylationNGKKKSTKLESLSDL
CCCCCCCHHHCHHHH		58.30-
1121UbiquitinationNGKKKSTKLESLSDL
CCCCCCCHHHCHHHH		58.30-
1126PhosphorylationSTKLESLSDLERALT
CCHHHCHHHHHHHHH		49.80-
1135PhosphorylationLERALTESKETASAM
HHHHHHHCHHHHHHH		30.47-
1136UbiquitinationERALTESKETASAMA
HHHHHHCHHHHHHHH		53.5021906983
1136 (in isoform 1)Ubiquitination-53.5021890473
1138 (in isoform 2)Ubiquitination-29.64-
1144PhosphorylationETASAMATLGEARLR
HHHHHHHHHHHHHHH		23.39-
1154 (in isoform 2)Ubiquitination-41.28-
1157 (in isoform 2)Ubiquitination-47.68-
1158PhosphorylationREMEALQSLRLANEG
HHHHHHHHHHHHCCC		19.1223186163
1166UbiquitinationLRLANEGKLLSPLQD
HHHHCCCCCCCCCCC		39.8221906983
1166 (in isoform 1)Ubiquitination-39.8221890473
1169PhosphorylationANEGKLLSPLQDVDI
HCCCCCCCCCCCCCE		33.7227251275
1172 (in isoform 2)Ubiquitination-52.6521890473
1183UbiquitinationIKICLCQKAPAAPMI
EEEEEECCCCCCCEE		56.17-
1202 (in isoform 2)Ubiquitination-9.6821890473
1219 (in isoform 2)Ubiquitination-27.69-
1226UbiquitinationPHCRRSEKPPLEKIL
CCCCCCCCCCHHHHH		53.86-
1238PhosphorylationKILPLLASLQRIRVR
HHHHHHHHHCCCEEC		25.6327251275
1262 (in isoform 2)Ubiquitination-7.33-
1276UbiquitinationLLSSGNLKFVQDRVG
HHHCCCCEECCCCCC		47.7121890473
1276 (in isoform 1)Ubiquitination-47.7121890473
1289PhosphorylationVGSGLLYSRWQASAG
CCCCCEEHHHCCCCC		27.3224719451
1294PhosphorylationLYSRWQASAGQVSDT
EEHHHCCCCCCCCCC		20.1723898821
1299PhosphorylationQASAGQVSDTNKVSQ
CCCCCCCCCCCCCCC		30.7223898821
1301PhosphorylationSAGQVSDTNKVSQPP
CCCCCCCCCCCCCCC		29.4523898821
1312 (in isoform 2)Ubiquitination-16.8121890473
1328PhosphorylationNRTSYLHSPFSTGRS
CCCCCCCCCCCCCCC		25.6625159151
1331PhosphorylationSYLHSPFSTGRSCIP
CCCCCCCCCCCCCCC		33.0823186163
1332PhosphorylationYLHSPFSTGRSCIPL
CCCCCCCCCCCCCCC		36.6723186163
1367PhosphorylationLPEIQELYQTLLAKP
HHHHHHHHHHHHCCC		9.9426074081
1369PhosphorylationEIQELYQTLLAKPSP
HHHHHHHHHHCCCCC		15.3526074081
1375PhosphorylationQTLLAKPSPAQQTDR
HHHHCCCCCCCCCCC		31.9626074081
1380PhosphorylationKPSPAQQTDRSSPVR
CCCCCCCCCCCCCCC		22.6926074081
1383PhosphorylationPAQQTDRSSPVRPSS
CCCCCCCCCCCCCCC		41.6323401153
1384PhosphorylationAQQTDRSSPVRPSSE
CCCCCCCCCCCCCCC		28.4525159151
1389PhosphorylationRSSPVRPSSEKNDCC
CCCCCCCCCCCCCCC		40.3330576142
1390PhosphorylationSSPVRPSSEKNDCCR
CCCCCCCCCCCCCCC		56.1030576142
1392UbiquitinationPVRPSSEKNDCCRGK
CCCCCCCCCCCCCCC		61.09-
1405PhosphorylationGKRDGINSLERKLKR
CCCCCHHHHHHHHHH		29.6823401153
1419 (in isoform 2)Phosphorylation-4.3321406692
1420PhosphorylationRLEREGLSSERWERV
HHHHCCCCHHHHHHH		40.8023898821
1420 (in isoform 2)Phosphorylation-40.8021406692
1428 (in isoform 2)Ubiquitination-47.26-
1444UbiquitinationKIKLSHPKDMNNFKL
CCCCCCCCCCCCCCC		65.27-
1450SumoylationPKDMNNFKLERERSY
CCCCCCCCCCHHHHH		52.11-
1450SumoylationPKDMNNFKLERERSY
CCCCCCCCCCHHHHH		52.1128112733
1450UbiquitinationPKDMNNFKLERERSY
CCCCCCCCCCHHHHH		52.11-
1456PhosphorylationFKLERERSYELVRSA
CCCCHHHHHHHHHHH		20.4329276005
1457PhosphorylationKLERERSYELVRSAE
CCCHHHHHHHHHHHH		21.3629978859
1486 (in isoform 2)Ubiquitination-4.47-
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
1328SPhosphorylationKinaseCDK1P06493
PSP
1456SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM5B_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 KDM5B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOXG1_HUMANFOXG1physical
12657635
PAX9_HUMANPAX9physical
12657635
CAC1H_HUMANCACNA1Hphysical
19336002
CDC20_HUMANCDC20physical
19336002
PCX1_HUMANPCNXphysical
19336002
SMRC2_HUMANSMARCC2physical
19336002
DGKQ_HUMANDGKQphysical
19336002
CAC1A_HUMANCACNA1Aphysical
19336002
NR4A3_HUMANNR4A3physical
19336002
BMP2K_HUMANBMP2Kphysical
19336002
VGLL3_HUMANVGLL3physical
19336002
CDX2_HUMANCDX2physical
19336002
CBX4_HUMANCBX4physical
19336002
SLIK3_HUMANSLITRK3physical
19336002
AXIN2_HUMANAXIN2physical
19336002
FOXC2_HUMANFOXC2physical
19336002
ONEC2_HUMANONECUT2physical
19336002
MAF_HUMANMAFphysical
19336002
ELF4_HUMANELF4physical
19336002
S39A6_HUMANSLC39A6physical
19336002
BRD4_HUMANBRD4physical
19336002
RNF43_HUMANRNF43physical
19336002
RB15B_HUMANRBM15Bphysical
19336002
PRD13_HUMANPRDM13physical
19336002
TF2AA_HUMANGTF2A1physical
19336002
DBNL_HUMANDBNLphysical
19336002
T121B_HUMANCECR6physical
19336002
RHBT2_HUMANRHOBTB2physical
19336002
TAF2_HUMANTAF2physical
19336002
SHOX2_HUMANSHOX2physical
19336002
ARI1B_HUMANARID1Bphysical
19336002
HXA1_HUMANHOXA1physical
19336002
NMDE2_HUMANGRIN2Bphysical
19336002
MEOX2_HUMANMEOX2physical
19336002
RB_HUMANRB1physical
16645588
ANDR_HUMANARphysical
18048344
FOXG1_HUMANFOXG1physical
17973255
PAX9_HUMANPAX9physical
17973255
RBTN2_HUMANLMO2physical
17973255
KLF10_HUMANKLF10physical
20863814
HDAC1_HUMANHDAC1physical
21502505
RB_HUMANRB1physical
21980403
CHD3_HUMANCHD3physical
21937684
KDM1A_HUMANKDM1Aphysical
21937684
MTA2_HUMANMTA2physical
21937684
MTA3_HUMANMTA3physical
21937684
HDAC1_HUMANHDAC1physical
21937684
HDAC2_HUMANHDAC2physical
21937684
RBBP7_HUMANRBBP7physical
21937684
RBBP4_HUMANRBBP4physical
21937684
MBD2_HUMANMBD2physical
21937684
MBD3_HUMANMBD3physical
21937684
PAX9_HUMANPAX9physical
17373667
HDAC1_HUMANHDAC1physical
17373667
HDAC4_HUMANHDAC4physical
17373667
HDAC5_HUMANHDAC5physical
17373667
HDAC7_HUMANHDAC7physical
17373667
MYC_HUMANMYCphysical
22371483
AP2C_HUMANTFAP2Cphysical
22371483
CDX2_HUMANCDX2physical
23202735
CBX4_HUMANCBX4physical
23970103
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 KDM5B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1405, 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-1383 AND SER-1384, ANDMASS SPECTROMETRY.

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