Z512B_HUMAN - dbPTM
Z512B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Z512B_HUMAN
UniProt AC Q96KM6
Protein Name Zinc finger protein 512B
Gene Name ZNF512B
Organism Homo sapiens (Human).
Sequence Length 892
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MTDPFCVGGRRLPGSSKSGPGKDGSRKEVRLPMLHDPPKMGMPVVRGGQTVPGQAPLCFDPGSPASDKTEGKKKGRPKAENQALRDIPLSLMNDWKDEFKAHSRVKCPNSGCWLEFPSIYGLKYHYQRCQGGAISDRLAFPCPFCEAAFTSKTQLEKHRIWNHMDRPLPASKPGPISRPVTISRPVGVSKPIGVSKPVTIGKPVGVSKPIGISKPVSVGRPMPVTKAIPVTRPVPVTKPVTVSRPMPVTKAMPVTKPITVTKSVPVTKPVPVTKPITVTKLVTVTKPVPVTKPVTVSRPIVVSKPVTVSRPIAISRHTPPCKMVLLTRSENKAPRATGRNSGKKRAADSLDTCPIPPKQARPENGEYGPSSMGQSSAFQLSADTSSGSLSPGSRPSGGMEALKAAGPASPPEEDPERTKHRRKQKTPKKFTGEQPSISGTFGLKGLVKAEDKARVHRSKKQEGPGPEDARKKVPAAPITVSKEAPAPVAHPAPGGPEEQWQRAIHERGEAVCPTCNVVTRKTLVGLKKHMEVCQKLQDALKCQHCRKQFKSKAGLNYHTMAEHSAKPSDAEASEGGEQEERERLRKVLKQMGRLRCPQEGCGAAFSSLMGYQYHQRRCGKPPCEVDSPSFPCTHCGKTYRSKAGHDYHVRSEHTAPPPEEPTDKSPEAEDPLGVERTPSGRVRRTSAQVAVFHLQEIAEDELARDWTKRRMKDDLVPETARLNYTRPGLPTLNPQLLEAWKNEVKEKGHVNCPNDCCEAIYSSVSGLKAHLASCSKGAHLAGKYRCLLCPKEFSSESGVKYHILKTHAENWFRTSADPPPKHRSQDSLVPKKEKKKNLAGGKKRGRKPKERTPEEPVAKLPPRRDDWPPGCRDKGARGSTGRKVGVSKAPEK
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
15PhosphorylationGGRRLPGSSKSGPGK
CCEECCCCCCCCCCC		32.4326437602
16PhosphorylationGRRLPGSSKSGPGKD
CEECCCCCCCCCCCC		36.4326437602
22UbiquitinationSSKSGPGKDGSRKEV
CCCCCCCCCCCCCEE		63.1524816145
36UbiquitinationVRLPMLHDPPKMGMP
EECCCCCCCCCCCCC		58.1824816145
46MethylationKMGMPVVRGGQTVPG
CCCCCEEECCEECCC		43.70115920513
50PhosphorylationPVVRGGQTVPGQAPL
CEEECCEECCCCCCC		31.7626074081
63PhosphorylationPLCFDPGSPASDKTE
CCCCCCCCCCCCCCC		23.7625159151
66PhosphorylationFDPGSPASDKTEGKK
CCCCCCCCCCCCCCC		42.9228450419
69PhosphorylationGSPASDKTEGKKKGR
CCCCCCCCCCCCCCC		55.7728450419
78UbiquitinationGKKKGRPKAENQALR
CCCCCCCHHHHHHHH		67.9529967540
124PhosphorylationPSIYGLKYHYQRCQG
CCCEEEEEHHHCCCC		15.71-
126PhosphorylationIYGLKYHYQRCQGGA
CEEEEEHHHCCCCCC		8.44-
171PhosphorylationMDRPLPASKPGPISR
CCCCCCCCCCCCCCC		37.1320363803
177PhosphorylationASKPGPISRPVTISR
CCCCCCCCCCEEECC		33.3920363803
207PhosphorylationIGKPVGVSKPIGISK
CCCCCCCCCCCCCCC		27.1332645325
231PhosphorylationVTKAIPVTRPVPVTK
CCCCCCCCCCCCCCC		24.7320860994
231O-linked_GlycosylationVTKAIPVTRPVPVTK
CCCCCCCCCCCCCCC		24.7330059200
237O-linked_GlycosylationVTRPVPVTKPVTVSR
CCCCCCCCCCEEECC		24.4630059200
237PhosphorylationVTRPVPVTKPVTVSR
CCCCCCCCCCEEECC		24.4620068231
241PhosphorylationVPVTKPVTVSRPMPV
CCCCCCEEECCCCCC		22.6920068231
243PhosphorylationVTKPVTVSRPMPVTK
CCCCEEECCCCCCCC		22.6924719451
249PhosphorylationVSRPMPVTKAMPVTK
ECCCCCCCCCCCCCC		13.7620068231
255O-linked_GlycosylationVTKAMPVTKPITVTK
CCCCCCCCCCEEEEE		25.8230059200
255PhosphorylationVTKAMPVTKPITVTK
CCCCCCCCCCEEEEE		25.8218452278
256AcetylationTKAMPVTKPITVTKS
CCCCCCCCCEEEEEC		34.3626051181
259PhosphorylationMPVTKPITVTKSVPV
CCCCCCEEEEECCEE		30.5627251275
261PhosphorylationVTKPITVTKSVPVTK
CCCCEEEEECCEECC		14.6727251275
263PhosphorylationKPITVTKSVPVTKPV
CCEEEEECCEECCCC		23.4526074081
263O-linked_GlycosylationKPITVTKSVPVTKPV
CCEEEEECCEECCCC		23.4530059200
267PhosphorylationVTKSVPVTKPVPVTK
EEECCEECCCCCCCC		24.4626074081
267O-linked_GlycosylationVTKSVPVTKPVPVTK
EEECCEECCCCCCCC		24.4630059200
268AcetylationTKSVPVTKPVPVTKP
EECCEECCCCCCCCC		44.2326051181
273PhosphorylationVTKPVPVTKPITVTK
ECCCCCCCCCEEEEE		25.6526074081
273O-linked_GlycosylationVTKPVPVTKPITVTK
ECCCCCCCCCEEEEE		25.6530059200
274AcetylationTKPVPVTKPITVTKL
CCCCCCCCCEEEEEE		34.3626051181
277PhosphorylationVPVTKPITVTKLVTV
CCCCCCEEEEEEEEE		30.5626074081
279PhosphorylationVTKPITVTKLVTVTK
CCCCEEEEEEEEECC		15.2626074081
297PhosphorylationVTKPVTVSRPIVVSK
CCCCEEECCCEEECC		23.9924719451
304AcetylationSRPIVVSKPVTVSRP
CCCEEECCCEEECCC		31.7125825284
309PhosphorylationVSKPVTVSRPIAISR
ECCCEEECCCEEECC		23.9924719451
327PhosphorylationPCKMVLLTRSENKAP
CCEEEEEECCCCCCC		28.1729214152
329PhosphorylationKMVLLTRSENKAPRA
EEEEEECCCCCCCCC		40.0425159151
332AcetylationLLTRSENKAPRATGR
EEECCCCCCCCCCCC		56.5725953088
337O-linked_GlycosylationENKAPRATGRNSGKK
CCCCCCCCCCCCCCC		37.6430059200
367PhosphorylationARPENGEYGPSSMGQ
CCCCCCCCCCCCCCC		35.4224275569
370PhosphorylationENGEYGPSSMGQSSA
CCCCCCCCCCCCCCC		28.7024275569
371PhosphorylationNGEYGPSSMGQSSAF
CCCCCCCCCCCCCCE		30.0224275569
393PhosphorylationSGSLSPGSRPSGGME
CCCCCCCCCCCCHHH		44.3922210691
396PhosphorylationLSPGSRPSGGMEALK
CCCCCCCCCHHHHHH		47.0422210691
409PhosphorylationLKAAGPASPPEEDPE
HHHCCCCCCCCCCHH		44.0929255136
436PhosphorylationKFTGEQPSISGTFGL
CCCCCCCCCCCCCCC		29.1328555341
438PhosphorylationTGEQPSISGTFGLKG
CCCCCCCCCCCCCCC		35.8028555341
448SumoylationFGLKGLVKAEDKARV
CCCCCEEEHHHHHHH		51.61-
448SumoylationFGLKGLVKAEDKARV
CCCCCEEEHHHHHHH		51.61-
459MethylationKARVHRSKKQEGPGP
HHHHHHCCCCCCCCH		59.43116253495
481PhosphorylationPAAPITVSKEAPAPV
CCCCEEECCCCCCCC		19.0120860994
482AcetylationAAPITVSKEAPAPVA
CCCEEECCCCCCCCC		54.2626051181
557PhosphorylationKSKAGLNYHTMAEHS
HHHHCCCHHHHHHHC		12.0528555341
559PhosphorylationKAGLNYHTMAEHSAK
HHCCCHHHHHHHCCC		14.0228555341
561UbiquitinationGLNYHTMAEHSAKPS
CCCHHHHHHHCCCCC		16.7124816145
562UbiquitinationLNYHTMAEHSAKPSD
CCHHHHHHHCCCCCC		27.7924816145
564PhosphorylationYHTMAEHSAKPSDAE
HHHHHHHCCCCCCCC		29.5028555341
611PhosphorylationAFSSLMGYQYHQRRC
HHHHHHHHHHHHHHC		7.61-
613PhosphorylationSSLMGYQYHQRRCGK
HHHHHHHHHHHHCCC		7.46-
627PhosphorylationKPPCEVDSPSFPCTH
CCCCCCCCCCCCCCC		27.8521712546
629PhosphorylationPCEVDSPSFPCTHCG
CCCCCCCCCCCCCCC		45.8628555341
651PhosphorylationGHDYHVRSEHTAPPP
CCCEECCCCCCCCCC		32.4225849741
654PhosphorylationYHVRSEHTAPPPEEP
EECCCCCCCCCCCCC		36.4926074081
662PhosphorylationAPPPEEPTDKSPEAE
CCCCCCCCCCCCCCC		60.3823401153
665PhosphorylationPEEPTDKSPEAEDPL
CCCCCCCCCCCCCCC		30.6823401153
677PhosphorylationDPLGVERTPSGRVRR
CCCCCCCCCCCCCCC		14.3225849741
679PhosphorylationLGVERTPSGRVRRTS
CCCCCCCCCCCCCCC		38.3228102081
685PhosphorylationPSGRVRRTSAQVAVF
CCCCCCCCCCEEEEE		20.1820068231
686PhosphorylationSGRVRRTSAQVAVFH
CCCCCCCCCEEEEEE		18.2026055452
761PhosphorylationNDCCEAIYSSVSGLK
HHHHHHHHHHHHHHH		11.27-
765PhosphorylationEAIYSSVSGLKAHLA
HHHHHHHHHHHHHHH		40.1121712546
815PhosphorylationAENWFRTSADPPPKH
HHHCCCCCCCCCCCC		26.8128555341
824PhosphorylationDPPPKHRSQDSLVPK
CCCCCCCCCCCCCCH		37.7528555341
834AcetylationSLVPKKEKKKNLAGG
CCCCHHHHHCCCCCC		77.3190839
835AcetylationLVPKKEKKKNLAGGK
CCCHHHHHCCCCCCC		48.24130047
836AcetylationVPKKEKKKNLAGGKK
CCHHHHHCCCCCCCC		69.1626210075
842AcetylationKKNLAGGKKRGRKPK
HCCCCCCCCCCCCCC		38.0826210075
843AcetylationKNLAGGKKRGRKPKE
CCCCCCCCCCCCCCC		64.4626210075
852PhosphorylationGRKPKERTPEEPVAK
CCCCCCCCCCCCHHC		35.8223401153
873UbiquitinationDWPPGCRDKGARGST
CCCCCCCCCCCCCCC		58.7924816145
888AcetylationGRKVGVSKAPEK---
CCCCCCCCCCCC---		66.6025953088
892UbiquitinationGVSKAPEK-------
CCCCCCCC-------		65.6624816145
906Ubiquitination---------------------
---------------------		24816145
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 Z512B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Z512B_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 Z512B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPT5H_HUMANSUPT5Hphysical
15231748
DDX3X_HUMANDDX3Xphysical
15231748
ANR28_HUMANANKRD28physical
15231748
HTSF1_HUMANHTATSF1physical
15231748
TOM1_HUMANTOM1physical
15231748
ANKL2_HUMANANKLE2physical
15231748
CD123_HUMANCDC123physical
15231748
PR15A_HUMANPPP1R15Aphysical
15231748
GLRX3_HUMANGLRX3physical
15231748
TOX4_HUMANTOX4physical
15231748
BRD1_HUMANBRD1physical
15231748
VWF_HUMANVWFphysical
15231748
YES_HUMANYES1physical
15231748
PTPRF_HUMANPTPRFphysical
15231748
XRCC6_HUMANXRCC6physical
15231748
PLCG2_HUMANPLCG2physical
15231748
TGM2_HUMANTGM2physical
15231748
MYH10_HUMANMYH10physical
15231748
VHL_HUMANVHLphysical
15231748
ATRX_HUMANATRXphysical
15231748
VPS41_HUMANVPS41physical
15231748
LAMB2_HUMANLAMB2physical
15231748
CTBP2_HUMANCTBP2physical
15231748
SPTB2_HUMANSPTBN1physical
15231748
XPC_HUMANXPCphysical
15231748
APLP2_HUMANAPLP2physical
15231748
KLF10_HUMANKLF10physical
15231748
OS9_HUMANOS9physical
15231748
DCTN1_HUMANDCTN1physical
15231748
SMAD1_HUMANSMAD1physical
15231748
RS27A_HUMANRPS27Aphysical
15231748
LITD1_HUMANL1TD1physical
15231748
MYOME_HUMANPDE4DIPphysical
15231748
KDM3B_HUMANKDM3Bphysical
15231748
PEG10_HUMANPEG10physical
15231748
PB1_HUMANPBRM1physical
15231748
AP1G1_HUMANAP1G1physical
15231748
PIAS4_HUMANPIAS4physical
15231748
DVL3_HUMANDVL3physical
15231748
VPS35_HUMANVPS35physical
15231748
NIBL1_HUMANFAM129Bphysical
15231748
LZTS2_HUMANLZTS2physical
15231748
CAB45_HUMANSDF4physical
15231748
TRAF4_HUMANTRAF4physical
15231748
BTBD2_HUMANBTBD2physical
15231748
PAPP2_HUMANPAPPA2physical
15231748
TNKS2_HUMANTNKS2physical
15231748
HEYL_HUMANHEYLphysical
15231748
RNC_HUMANDROSHAphysical
15231748
ZHANG_HUMANCREBZFphysical
15231748
I36RA_HUMANIL36RNphysical
15231748
ZMYM2_HUMANZMYM2physical
15231748
KMT2B_HUMANKMT2Bphysical
15231748
INVS_HUMANINVSphysical
15231748
KDM2A_HUMANKDM2Aphysical
15231748
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 Z512B_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-686, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-665 ANDTHR-852, 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-409, AND MASSSPECTROMETRY.

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