JADE2_HUMAN - dbPTM
JADE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JADE2_HUMAN
UniProt AC Q9NQC1
Protein Name E3 ubiquitin-protein ligase Jade-2 {ECO:0000303|PubMed:25018020}
Gene Name JADE2
Organism Homo sapiens (Human).
Sequence Length 790
Subcellular Localization
Protein Description Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. [PubMed: 16387653 Acts as a E3 ubiquitin-protein ligase mediating the ubiquitination and subsequent proteasomal degradation of target protein histone demethylase KDM1A]
Protein Sequence MEEKRRKYSISSDNSDTTDSHATSTSASRCSKLPSSTKSGWPRQNEKKPSEVFRTDLITAMKIPDSYQLSPDDYYILADPWRQEWEKGVQVPAGAEAIPEPVVRILPPLEGPPAQASPSSTMLGEGSQPDWPGGSRYDLDEIDAYWLELINSELKEMERPELDELTLERVLEELETLCHQNMARAIETQEGLGIEYDEDVVCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTCALGVQPKCLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAFHVTCAFDHGLEMRTILADNDEVKFKSFCQEHSDGGPRNEPTSEPTEPSQAGEDLEKVTLRKQRLQQLEEDFYELVEPAEVAERLDLAEALVDFIYQYWKLKRKANANQPLLTPKTDEVDNLAQQEQDVLYRRLKLFTHLRQDLERVRNLCYMVTRRERTKHAICKLQEQIFHLQMKLIEQDLCRGLSTSFPIDGTFFNSWLAQSVQITAENMAMSEWPLNNGHREDPAPGLLSEELLQDEETLLSFMRDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGDCPILATPESPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPKVSLHFDTETDGYFSDGEMSDSDVEAEDGGVQRGPREAGAEEVVRMGVLAS
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
8PhosphorylationMEEKRRKYSISSDNS
CCHHHHCCCCCCCCC		14.9323663014
9PhosphorylationEEKRRKYSISSDNSD
CHHHHCCCCCCCCCC		21.0123401153
11 (in isoform 3)Phosphorylation-26.2121406692
11PhosphorylationKRRKYSISSDNSDTT
HHHCCCCCCCCCCCC		26.2125159151
12 (in isoform 3)Phosphorylation-38.8621406692
12PhosphorylationRRKYSISSDNSDTTD
HHCCCCCCCCCCCCC		38.8625159151
15 (in isoform 3)Phosphorylation-41.1321406692
15PhosphorylationYSISSDNSDTTDSHA
CCCCCCCCCCCCCCC		41.1325159151
17PhosphorylationISSDNSDTTDSHATS
CCCCCCCCCCCCCCC		32.1223663014
18PhosphorylationSSDNSDTTDSHATST
CCCCCCCCCCCCCCC		40.2623663014
20PhosphorylationDNSDTTDSHATSTSA
CCCCCCCCCCCCCCH		16.9623663014
23PhosphorylationDTTDSHATSTSASRC
CCCCCCCCCCCHHHH		27.4130108239
24PhosphorylationTTDSHATSTSASRCS
CCCCCCCCCCHHHHH		22.5830108239
25PhosphorylationTDSHATSTSASRCSK
CCCCCCCCCHHHHHC		24.7730108239
26PhosphorylationDSHATSTSASRCSKL
CCCCCCCCHHHHHCC		24.8230108239
28PhosphorylationHATSTSASRCSKLPS
CCCCCCHHHHHCCCC		33.3230108239
31PhosphorylationSTSASRCSKLPSSTK
CCCHHHHHCCCCCCC		35.8016674116
32 (in isoform 3)Acetylation-68.96-
32AcetylationTSASRCSKLPSSTKS
CCHHHHHCCCCCCCC		68.9619608861
38AcetylationSKLPSSTKSGWPRQN
HCCCCCCCCCCCCCC		49.2519608861
75PhosphorylationQLSPDDYYILADPWR
CCCCCCEEEEECHHH		9.1028387310
117PhosphorylationEGPPAQASPSSTMLG
CCCCCCCCCCCCCCC		17.1525850435
119PhosphorylationPPAQASPSSTMLGEG
CCCCCCCCCCCCCCC		35.6325850435
120PhosphorylationPAQASPSSTMLGEGS
CCCCCCCCCCCCCCC		22.6326657352
121PhosphorylationAQASPSSTMLGEGSQ
CCCCCCCCCCCCCCC		22.2825850435
127PhosphorylationSTMLGEGSQPDWPGG
CCCCCCCCCCCCCCC		33.9525850435
135PhosphorylationQPDWPGGSRYDLDEI
CCCCCCCCCCCHHHH		33.3128176443
253UbiquitinationCALGVQPKCLLCPKR
HHCCCCCCEEECCCC		22.03-
259AcetylationPKCLLCPKRGGALKP
CCEEECCCCCCCCCC		63.7825953088
292AcetylationVSIGCPEKMEPITKI
CCCCCCCCCCCCCEE		33.4326051181
298AcetylationEKMEPITKISHIPAS
CCCCCCCEECCCCHH		42.8219608861
318PhosphorylationCSLCKECTGTCIQCS
CCCCHHHHCCEEECC		36.3024719451
336PhosphorylationCVTAFHVTCAFDHGL
CEEEEEHHHHHCCCC		6.9124719451
356UbiquitinationLADNDEVKFKSFCQE
EECCCCEEEHHHHHH		45.05-
358UbiquitinationDNDEVKFKSFCQEHS
CCCCEEEHHHHHHCC		36.58-
374PhosphorylationGGPRNEPTSEPTEPS
CCCCCCCCCCCCCHH		39.27-
381PhosphorylationTSEPTEPSQAGEDLE
CCCCCCHHHCCCCHH		26.8226714015
389UbiquitinationQAGEDLEKVTLRKQR
HCCCCHHHHHHHHHH		48.06-
391PhosphorylationGEDLEKVTLRKQRLQ
CCCHHHHHHHHHHHH		31.73-
445PhosphorylationNANQPLLTPKTDEVD
CCCCCCCCCCCHHHH		30.3520068231
447UbiquitinationNQPLLTPKTDEVDNL
CCCCCCCCCHHHHHH		64.47-
448PhosphorylationQPLLTPKTDEVDNLA
CCCCCCCCHHHHHHH		38.30-
467AcetylationDVLYRRLKLFTHLRQ
HHHHHHHHHHHHHHH		39.4826051181
470PhosphorylationYRRLKLFTHLRQDLE
HHHHHHHHHHHHHHH		30.3620068231
484PhosphorylationERVRNLCYMVTRRER
HHHHHHHHHHHCHHH		9.59-
498AcetylationRTKHAICKLQEQIFH
HHHHHHHHHHHHHHH		47.2826051181
603AcetylationGRTRLPAKKKPPPPP
CCCCCCCCCCCCCCC		60.4325953088
617PhosphorylationPPQDGPGSRTTPDKA
CCCCCCCCCCCCCCC		29.5930576142
619PhosphorylationQDGPGSRTTPDKAPK
CCCCCCCCCCCCCCC		44.3625627689
620PhosphorylationDGPGSRTTPDKAPKK
CCCCCCCCCCCCCCC		28.5128176443
635PhosphorylationTWGQDAGSGKGGQGP
CCCCCCCCCCCCCCC		38.7725159151
637AcetylationGQDAGSGKGGQGPPT
CCCCCCCCCCCCCCC		62.6625953088
652PhosphorylationRKPPRRTSSHLPSSP
CCCCCCCCCCCCCCC		17.6021552520
657PhosphorylationRTSSHLPSSPAAGDC
CCCCCCCCCCCCCCC		56.1421552520
733PhosphorylationDAGMGPPSAVAERPK
CCCCCCCHHHHCCCC		38.2128555341
747PhosphorylationKVSLHFDTETDGYFS
CEEEEEECCCCCCCC		39.5830576142
754PhosphorylationTETDGYFSDGEMSDS
CCCCCCCCCCCCCCC		35.9030576142
761PhosphorylationSDGEMSDSDVEAEDG
CCCCCCCCCCCCCCC		35.9330576142
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 JADE2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JADE2_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 JADE2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ING4_HUMANING4physical
20211142
ZBTB3_HUMANZBTB3physical
20211142
ZN496_HUMANZNF496physical
20211142
GORS2_HUMANGORASP2physical
25416956
ING5_HUMANING5physical
25416956
MYO9A_HUMANMYO9Aphysical
26186194
EAF6_HUMANMEAF6physical
26186194
ING4_HUMANING4physical
26186194
ING5_HUMANING5physical
26186194
MYO5C_HUMANMYO5Cphysical
26186194
ING3_HUMANING3physical
26186194
PI3R4_HUMANPIK3R4physical
26186194
PK3C3_HUMANPIK3C3physical
26186194
GRDN_HUMANCCDC88Aphysical
26186194
CCD93_HUMANCCDC93physical
26186194
KAT7_HUMANKAT7physical
26186194
CP110_HUMANCCP110physical
26186194
CN080_HUMANC14orf80physical
26186194
AASD1_HUMANAARSD1physical
26186194
ING5_HUMANING5physical
21516116
KAT7_HUMANKAT7physical
28514442
ING5_HUMANING5physical
28514442
ING4_HUMANING4physical
28514442
ING3_HUMANING3physical
28514442
PK3C3_HUMANPIK3C3physical
28514442
GRDN_HUMANCCDC88Aphysical
28514442
CN080_HUMANC14orf80physical
28514442
CCD93_HUMANCCDC93physical
28514442
AASD1_HUMANAARSD1physical
28514442
MYO5C_HUMANMYO5Cphysical
28514442
MYO9A_HUMANMYO9Aphysical
28514442
PI3R4_HUMANPIK3R4physical
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 JADE2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-38 AND LYS-298, ANDMASS SPECTROMETRY.
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-38, AND MASSSPECTROMETRY.

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