RSBN1_HUMAN - dbPTM
RSBN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSBN1_HUMAN
UniProt AC Q5VWQ0
Protein Name Lysine-specific demethylase 9 {ECO:0000250|UniProtKB:Q80T69}
Gene Name RSBN1
Organism Homo sapiens (Human).
Sequence Length 802
Subcellular Localization Nucleus.
Protein Description Histone demethylase that specifically demethylates dimethylated 'Lys-20' of histone H4 (H4K20me2), thereby modulating chromosome architecture..
Protein Sequence MFISGRRTADKWRAEERLQCPAGSARAALARCADGGAVGPFKCVFVGEMAAQVGAVRVVRAVAAQEEPDKEGKEKPHAGVSPRGVKRQRRSSSGGSQEKRGRPSQEPPLAPPHRRRRSRQHPGPLPPTNAAPTVPGPVEPLLLPPPPPPSLAPAGPAVAAPLPAPSTSALFTFSPLTVSAAGPKHKGHKERHKHHHHRGPDGDPSSCGTDLKHKDKQENGERTGGVPLIKAPKRETPDENGKTQRADDFVLKKIKKKKKKKHREDMRGRRLKMYNKEVQTVCAGLTRISKEILTQGQINSTSGLNKESFRYLKDEQLCRLNLGMQEYRVPQGVQTPFMTHQEHSIRRNFLKTGTKFSNFIHEEHQSNGGALVLHAYMDELSFLSPMEMERFSEEFLALTFSENEKNAAYYALAIVHGAAAYLPDFLDYFAFNFPNTPVKMEILGKKDIETTTISNFHTQVNRTYCCGTYRAGPMRQISLVGAVDEEVGDYFPEFLDMLEESPFLKMTLPWGTLSSLRLQCRSQSDDGPIMWVRPGEQMIPTADMPKSPFKRRRSMNEIKNLQYLPRTSEPREVLFEDRTRAHADHVGQGFDWQSTAAVGVLKAVQFGEWSDQPRITKDVICFHAEDFTDVVQRLQLDLHEPPVSQCVQWVDEAKLNQMRREGIRYARIQLCDNDIYFIPRNVIHQFKTVSAVCSLAWHIRLKQYHPVVEATQNTESNSNMDCGLTGKRELEVDSQCVRIKTESEEACTEIQLLTTASSSFPPASELNLQQDQKTQPIPVLKVESRLDSDQQHNLQEHSTTSV
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
4Phosphorylation----MFISGRRTADK
----CCCCCCCCHHH		18.2524719451
24PhosphorylationRLQCPAGSARAALAR
HHCCCCCCHHHHHHH		19.3825159151
57DimethylationAAQVGAVRVVRAVAA
HHHHCHHHHHHHHHC		22.22-
57MethylationAAQVGAVRVVRAVAA
HHHHCHHHHHHHHHC		22.2224410443
73UbiquitinationEEPDKEGKEKPHAGV
CCCCCCCCCCCCCCC		64.7524816145
75AcetylationPDKEGKEKPHAGVSP
CCCCCCCCCCCCCCC		45.6625953088
81PhosphorylationEKPHAGVSPRGVKRQ
CCCCCCCCCHHHCCC		14.1523401153
91PhosphorylationGVKRQRRSSSGGSQE
HHCCCCCCCCCCCCC		30.9227273156
92PhosphorylationVKRQRRSSSGGSQEK
HCCCCCCCCCCCCCC		31.0628176443
93PhosphorylationKRQRRSSSGGSQEKR
CCCCCCCCCCCCCCC		48.7127273156
96PhosphorylationRRSSSGGSQEKRGRP
CCCCCCCCCCCCCCC		38.4022210691
104PhosphorylationQEKRGRPSQEPPLAP
CCCCCCCCCCCCCCC		45.9025849741
205PhosphorylationRGPDGDPSSCGTDLK
CCCCCCCCCCCCCCC		42.8925627689
206PhosphorylationGPDGDPSSCGTDLKH
CCCCCCCCCCCCCCC		23.1925627689
209PhosphorylationGDPSSCGTDLKHKDK
CCCCCCCCCCCCCCC		42.3525627689
233UbiquitinationVPLIKAPKRETPDEN
CCEEECCCCCCCCCC		68.6624816145
233AcetylationVPLIKAPKRETPDEN
CCEEECCCCCCCCCC		68.6630592075
236PhosphorylationIKAPKRETPDENGKT
EECCCCCCCCCCCCC		39.8228985074
252AcetylationRADDFVLKKIKKKKK
CHHHHHHHHHHHHHH		47.3423749302
252UbiquitinationRADDFVLKKIKKKKK
CHHHHHHHHHHHHHH		47.34-
290SumoylationAGLTRISKEILTQGQ
HHHHHHHHHHHHCCC		46.5328112733
290AcetylationAGLTRISKEILTQGQ
HHHHHHHHHHHHCCC		46.5326051181
290UbiquitinationAGLTRISKEILTQGQ
HHHHHHHHHHHHCCC		46.5329967540
306UbiquitinationNSTSGLNKESFRYLK
CCCCCCCHHHHHHCC		60.8329967540
308PhosphorylationTSGLNKESFRYLKDE
CCCCCHHHHHHCCHH		19.3424719451
311PhosphorylationLNKESFRYLKDEQLC
CCHHHHHHCCHHHHH		18.9824719451
313AcetylationKESFRYLKDEQLCRL
HHHHHHCCHHHHHHH		50.7326051181
313SumoylationKESFRYLKDEQLCRL
HHHHHHCCHHHHHHH		50.7317000644
313SumoylationKESFRYLKDEQLCRL
HHHHHHCCHHHHHHH		50.73-
313UbiquitinationKESFRYLKDEQLCRL
HHHHHHCCHHHHHHH		50.73-
327PhosphorylationLNLGMQEYRVPQGVQ
HCCCCCCCCCCCCCC		10.46-
439SumoylationNFPNTPVKMEILGKK
CCCCCCCEEEECCCC		31.8317000644
439SumoylationNFPNTPVKMEILGKK
CCCCCCCEEEECCCC		31.83-
445AcetylationVKMEILGKKDIETTT
CEEEECCCCCCEECE		43.7725953088
501PhosphorylationFLDMLEESPFLKMTL
HHHHHHHCCCCEEEC		16.1524719451
514PhosphorylationTLPWGTLSSLRLQCR
ECCCCCHHHHEEEEE		27.4530301811
515PhosphorylationLPWGTLSSLRLQCRS
CCCCCHHHHEEEEEC		22.1825954137
522PhosphorylationSLRLQCRSQSDDGPI
HHEEEEECCCCCCCE		41.4823090842
524PhosphorylationRLQCRSQSDDGPIMW
EEEEECCCCCCCEEE		38.6327080861
541PhosphorylationPGEQMIPTADMPKSP
CCCCCCCCCCCCCCH		25.1028450419
547PhosphorylationPTADMPKSPFKRRRS
CCCCCCCCHHCCCCC		29.6929255136
554PhosphorylationSPFKRRRSMNEIKNL
CHHCCCCCHHHHHCC		24.9322617229
559 (in isoform 1)Ubiquitination-45.4821890473
559AcetylationRRSMNEIKNLQYLPR
CCCHHHHHCCCCCCC		45.4812656573
559UbiquitinationRRSMNEIKNLQYLPR
CCCHHHHHCCCCCCC		45.4822817900
563PhosphorylationNEIKNLQYLPRTSEP
HHHHCCCCCCCCCCC		23.1130576142
567PhosphorylationNLQYLPRTSEPREVL
CCCCCCCCCCCCEEH		35.1929449344
568PhosphorylationLQYLPRTSEPREVLF
CCCCCCCCCCCEEHH		47.0528555341
704PhosphorylationWHIRLKQYHPVVEAT
HHHHHHHHCCEEEEE		13.4024719451
714PhosphorylationVVEATQNTESNSNMD
EEEEECCCCCCCCCC		30.8524719451
716PhosphorylationEATQNTESNSNMDCG
EEECCCCCCCCCCCC		43.4527251275
718PhosphorylationTQNTESNSNMDCGLT
ECCCCCCCCCCCCCC		42.6927251275
727AcetylationMDCGLTGKRELEVDS
CCCCCCCCEEEEECC		37.1525953088
734PhosphorylationKRELEVDSQCVRIKT
CEEEEECCEEEEEEE		30.5624719451
740SumoylationDSQCVRIKTESEEAC
CCEEEEEEECCHHHC		35.3617000644
740SumoylationDSQCVRIKTESEEAC
CCEEEEEEECCHHHC		35.36-
781SumoylationTQPIPVLKVESRLDS
CCCCCEEEEEECCCH		44.1617000644
781SumoylationTQPIPVLKVESRLDS
CCCCCEEEEEECCCH		44.16-
784PhosphorylationIPVLKVESRLDSDQQ
CCEEEEEECCCHHHC		40.9228555341
788PhosphorylationKVESRLDSDQQHNLQ
EEEECCCHHHCCCHH		41.7428555341
799PhosphorylationHNLQEHSTTSV----
CCHHHCCCCCC----		25.6228348404
800PhosphorylationNLQEHSTTSV-----
CHHHCCCCCC-----		30.4328348404
801PhosphorylationLQEHSTTSV------
HHHCCCCCC------		26.3928348404
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 RSBN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSBN1_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 RSBN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPTN4_HUMANSPTBN4physical
28514442
ZN317_HUMANZNF317physical
28514442
SETD2_HUMANSETD2physical
28514442
CD11B_HUMANCDK11Bphysical
28514442
CDC16_HUMANCDC16physical
28514442
SET1A_HUMANSETD1Aphysical
28514442
ZCH18_HUMANZC3H18physical
28514442
RL36L_HUMANRPL36ALphysical
28514442
CXXC1_HUMANCXXC1physical
28514442
CEBPZ_HUMANCEBPZphysical
28514442
UBF1_HUMANUBTFphysical
28514442
LIN41_HUMANTRIM71physical
28514442
RBM34_HUMANRBM34physical
28514442
CDC27_HUMANCDC27physical
28514442
AFF4_HUMANAFF4physical
28514442
TYDP2_HUMANTDP2physical
28514442
PININ_HUMANPNNphysical
28514442
RL26L_HUMANRPL26L1physical
28514442
ZN629_HUMANZNF629physical
28514442
BBX_HUMANBBXphysical
28514442
EEPD1_HUMANEEPD1physical
28514442
ZN512_HUMANZNF512physical
28514442
DDX51_HUMANDDX51physical
28514442
RRP5_HUMANPDCD11physical
28514442
GBB4_HUMANGNB4physical
28514442
NUFP1_HUMANNUFIP1physical
28514442
RBMX2_HUMANRBMX2physical
28514442
NOL6_HUMANNOL6physical
28514442
DHX37_HUMANDHX37physical
28514442
TEX10_HUMANTEX10physical
28514442
UBP7_HUMANUSP7physical
28514442
RRP8_HUMANRRP8physical
28514442
GLYR1_HUMANGLYR1physical
28514442
ZN865_HUMANZNF865physical
28514442
DDX52_HUMANDDX52physical
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 RSBN1_HUMAN

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Related Literatures of Post-Translational Modification

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