RNZ2_HUMAN - dbPTM
RNZ2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNZ2_HUMAN
UniProt AC Q9BQ52
Protein Name Zinc phosphodiesterase ELAC protein 2
Gene Name ELAC2
Organism Homo sapiens (Human).
Sequence Length 826
Subcellular Localization Mitochondrion . Nucleus . Mainly mitochondrial.
Protein Description Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA..
Protein Sequence MWALCSLLRSAAGRTMSQGRTISQAPARRERPRKDPLRHLRTREKRGPSGCSGGPNTVYLQVVAAGSRDSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPPQLEKYLEAIKIFSGPLKGIELAVRPHSAPEYEDETMTVYQIPIHSEQRRGKHQPWQSPERPLSRLSPERSSDSESNENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNFLVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVECPDESFIQPICENATFQRYQGKADAPVALVVHMAPASVLVDSRYQQWMERFGPDTQHLVLNENCASVHNLRSHKIQTQLNLIHPDIFPLLTSFRCKKEGPTLSVPMVQGECLLKYQLRPRREWQRDAIITCNPEEFIVEALQLPNFQQSVQEYRRSAQDGPAPAEKRSQYPEIIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQVDRVLGTLAAVFVSHLHADHHTGLPSILLQRERALASLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCLVRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYAKVPLFSPNFSEKVGVAFDHMKVCFGDFPTMPKLIPPLKALFAGDIEEMEERREKRELRQVRAALLSRELAGGLEDGEPQQKRAHTEEPQAKKVRAQ
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
6O-linked_Glycosylation--MWALCSLLRSAAG
--CHHHHHHHHHHCC		31.1530379171
28MethylationTISQAPARRERPRKD
CCCCCCCCCCCCCCC		39.68-
52PhosphorylationKRGPSGCSGGPNTVY
CCCCCCCCCCCCEEE		50.7628258704
57PhosphorylationGCSGGPNTVYLQVVA
CCCCCCCEEEEEEEE		17.4228258704
58 (in isoform 2)Ubiquitination-5.9621890473
67PhosphorylationLQVVAAGSRDSGAAL
EEEEEECCCCCCEEE		28.3428258704
99MethylationQRLMQEHKLKVARLD
HHHHHHHCCHHHHCC		49.6123644510
101MethylationLMQEHKLKVARLDNI
HHHHHCCHHHHCCCE		38.3623644510
101UbiquitinationLMQEHKLKVARLDNI
HHHHHCCHHHHCCCE		38.36-
104 (in isoform 3)Ubiquitination-45.6321890473
123 (in isoform 3)Ubiquitination-16.5221890473
135UbiquitinationLKETGLPKCVLSGPP
EHHHCCCCCHHCCCH		41.8521890473
135UbiquitinationLKETGLPKCVLSGPP
EHHHCCCCCHHCCCH		41.85-
139PhosphorylationGLPKCVLSGPPQLEK
CCCCCHHCCCHHHHH		28.9330108239
146UbiquitinationSGPPQLEKYLEAIKI
CCCHHHHHHHHHHHH		64.82-
152AcetylationEKYLEAIKIFSGPLK
HHHHHHHHHHCCCCC		44.7590917
152UbiquitinationEKYLEAIKIFSGPLK
HHHHHHHHHHCCCCC		44.7521890473
152 (in isoform 1)Ubiquitination-44.7521890473
166 (in isoform 2)Ubiquitination-20.0121890473
181PhosphorylationEDETMTVYQIPIHSE
CCCCEEEEEEECCCH		7.4928064214
185 (in isoform 2)Ubiquitination-6.2821890473
188 (in isoform 2)Ubiquitination-33.6621890473
193UbiquitinationHSEQRRGKHQPWQSP
CCHHCCCCCCCCCCC		36.94-
199PhosphorylationGKHQPWQSPERPLSR
CCCCCCCCCCCCHHH		25.5122167270
199 (in isoform 3)Ubiquitination-25.5121890473
205PhosphorylationQSPERPLSRLSPERS
CCCCCCHHHCCCCCC		33.5823927012
208PhosphorylationERPLSRLSPERSSDS
CCCHHHCCCCCCCCC		24.4929255136
212PhosphorylationSRLSPERSSDSESNE
HHCCCCCCCCCCCCC		36.5129255136
213PhosphorylationRLSPERSSDSESNEN
HCCCCCCCCCCCCCC		51.9129255136
215PhosphorylationSPERSSDSESNENEP
CCCCCCCCCCCCCCC		44.8929255136
217PhosphorylationERSSDSESNENEPHL
CCCCCCCCCCCCCCC		54.0929255136
229PhosphorylationPHLPHGVSQRRGVRD
CCCCCCHHHCCCCCC		23.6723401153
237PhosphorylationQRRGVRDSSLVVAFI
HCCCCCCHHHHHHHH		18.2730576142
238PhosphorylationRRGVRDSSLVVAFIC
CCCCCCHHHHHHHHH		29.4930576142
245GlutathionylationSLVVAFICKLHLKRG
HHHHHHHHHHHHHCC		2.8722555962
258UbiquitinationRGNFLVLKAKEMGLP
CCCEEEEEHHHHCCC		50.35-
260UbiquitinationNFLVLKAKEMGLPVG
CEEEEEHHHHCCCCC		46.8021906983
260 (in isoform 1)Ubiquitination-46.8021890473
262SulfoxidationLVLKAKEMGLPVGTA
EEEEHHHHCCCCCHH		7.0521406390
279AcetylationAPIIAAVKDGKSITH
HHHHHHHHCCCCCCC		56.9123954790
279UbiquitinationAPIIAAVKDGKSITH
HHHHHHHHCCCCCCC		56.9121906983
279 (in isoform 1)Ubiquitination-56.9121890473
282UbiquitinationIAAVKDGKSITHEGR
HHHHHCCCCCCCCCH		49.1421906983
282 (in isoform 1)Ubiquitination-49.1421890473
332UbiquitinationTFQRYQGKADAPVAL
CHHHHCCCCCCCEEE		27.80-
359 (in isoform 3)Ubiquitination-41.7321890473
370 (in isoform 3)Ubiquitination-9.2921890473
382 (in isoform 2)Ubiquitination-32.0921890473
384UbiquitinationVHNLRSHKIQTQLNL
HHHHHHCCHHHHHHH		37.44-
401 (in isoform 2)Ubiquitination-33.2421890473
407UbiquitinationLTSFRCKKEGPTLSV
HHCEECCCCCCCEEE		72.09-
421GlutathionylationVPMVQGECLLKYQLR
EEEECCEEEEEEECC		7.4422555962
424UbiquitinationVQGECLLKYQLRPRR
ECCEEEEEEECCCCC		20.29-
439 (in isoform 3)Ubiquitination-3.7321890473
466PhosphorylationSVQEYRRSAQDGPAP
HHHHHHHHCCCCCCC		22.6824144214
476UbiquitinationDGPAPAEKRSQYPEI
CCCCCHHHHHCCCEE		60.5021906983
476 (in isoform 1)Ubiquitination-60.5021890473
478UbiquitinationPAPAEKRSQYPEIIF
CCCHHHHHCCCEEEE		45.1721890473
478PhosphorylationPAPAEKRSQYPEIIF
CCCHHHHHCCCEEEE		45.1724144214
480PhosphorylationPAEKRSQYPEIIFLG
CHHHHHCCCEEEEEC		12.2228188228
488PhosphorylationPEIIFLGTGSAIPMK
CEEEEECCCCCCCEE		30.0628188228
490PhosphorylationIIFLGTGSAIPMKIR
EEEECCCCCCCEEEE		23.9028188228
495UbiquitinationTGSAIPMKIRNVSAT
CCCCCCEEEEEEEEE		32.9121890473
495 (in isoform 1)Ubiquitination-32.9121890473
500PhosphorylationPMKIRNVSATLVNIS
CEEEEEEEEEEEEEC		21.0526074081
502PhosphorylationKIRNVSATLVNISPD
EEEEEEEEEEEECCC		24.5926074081
507PhosphorylationSATLVNISPDTSLLL
EEEEEEECCCCCEEE		16.1226074081
510PhosphorylationLVNISPDTSLLLDCG
EEEECCCCCEEEECC		25.3426074081
511PhosphorylationVNISPDTSLLLDCGE
EEECCCCCEEEECCC		25.1326074081
520PhosphorylationLLDCGEGTFGQLCRH
EEECCCCHHHHHHHH		21.9326074081
528PhosphorylationFGQLCRHYGDQVDRV
HHHHHHHHHHHHHHH		11.75-
554UbiquitinationLHADHHTGLPSILLQ
HHHCCCCCCCHHHHH		31.1021890473
571AcetylationRALASLGKPLHPLLV
HHHHHCCCCCCEEEE		50.1026051181
571UbiquitinationRALASLGKPLHPLLV
HHHHHCCCCCCEEEE		50.1021890473
571 (in isoform 1)Ubiquitination-50.1021890473
608AcetylationHISMIPAKCLQEGAE
HHHCCCHHHHHCCCC		30.0825953088
608UbiquitinationHISMIPAKCLQEGAE
HHHCCCHHHHHCCCC		30.08-
617PhosphorylationLQEGAEISSPAVERL
HHCCCCCCCHHHHHH		23.0529396449
618PhosphorylationQEGAEISSPAVERLI
HCCCCCCCHHHHHHH		23.6525159151
627PhosphorylationAVERLISSLLRTCDL
HHHHHHHHHHHHCCH		25.1624719451
646AcetylationTCLVRHCKHAFGCAL
HHHHHHCHHHHCCEE		31.6626051181
670GlutathionylationYSGDTMPCEALVRMG
ECCCCCCHHHHHHCC		3.1222555962
678UbiquitinationEALVRMGKDATLLIH
HHHHHCCCCEEEEEE		34.54-
688PhosphorylationTLLIHEATLEDGLEE
EEEEEEEECCCCCCH		27.91-
701PhosphorylationEEEAVEKTHSTTSQA
CHHHHHHCCCCHHHH		13.93-
714UbiquitinationQAISVGMRMNAEFIM
HHHHHHHHCCCEEEE		14.8521890473
729PhosphorylationLNHFSQRYAKVPLFS
HHHHHHHCCCCCCCC		11.7923322592
731UbiquitinationHFSQRYAKVPLFSPN
HHHHHCCCCCCCCCC		35.1421890473
731 (in isoform 1)Ubiquitination-35.1421890473
736PhosphorylationYAKVPLFSPNFSEKV
CCCCCCCCCCHHHCC		26.9812515253
740PhosphorylationPLFSPNFSEKVGVAF
CCCCCCHHHCCCEEC		43.0529255136
742UbiquitinationFSPNFSEKVGVAFDH
CCCCHHHCCCEECCC		42.9921906983
742 (in isoform 1)Ubiquitination-42.9921890473
751UbiquitinationGVAFDHMKVCFGDFP
CEECCCCEEECCCCC		32.22-
753GlutathionylationAFDHMKVCFGDFPTM
ECCCCEEECCCCCCC		2.3522555962
762UbiquitinationGDFPTMPKLIPPLKA
CCCCCCCCCCHHHHH		48.50-
768AcetylationPKLIPPLKALFAGDI
CCCCHHHHHHHCCCH		49.1425953088
768UbiquitinationPKLIPPLKALFAGDI
CCCCHHHHHHHCCCH		49.14-
778SulfoxidationFAGDIEEMEERREKR
HCCCHHHHHHHHHHH		4.1521406390
796PhosphorylationQVRAALLSRELAGGL
HHHHHHHHHHHHHCC		25.2628555341
811UbiquitinationEDGEPQQKRAHTEEP
CCCCCHHHHCCCCCH		46.432190698
811 (in isoform 1)Ubiquitination-46.4321890473
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 RNZ2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNZ2_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 RNZ2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOXH1_HUMANFOXH1physical
16636667
ARI1_HUMANARIH1physical
22863883
FEN1_HUMANFEN1physical
22863883
SYHC_HUMANHARSphysical
22863883
IPO7_HUMANIPO7physical
22863883
NRDC_HUMANNRD1physical
22863883
PFD1_HUMANPFDN1physical
22863883
PP2AB_HUMANPPP2CBphysical
22863883
SYSC_HUMANSARSphysical
22863883
SNX5_HUMANSNX5physical
22863883
TNPO3_HUMANTNPO3physical
22863883
TSN_HUMANTSNphysical
22863883
WDR4_HUMANWDR4physical
22863883
CKAP5_HUMANCKAP5physical
26344197
DDX5_HUMANDDX5physical
26344197
DJC17_HUMANDNAJC17physical
26344197
EIF2D_HUMANEIF2Dphysical
26344197
IF6_HUMANEIF6physical
26344197
FERM2_HUMANFERMT2physical
26344197
GLRX5_HUMANGLRX5physical
26344197
GORS2_HUMANGORASP2physical
26344197
SYHC_HUMANHARSphysical
26344197
HNRPF_HUMANHNRNPFphysical
26344197
HNRH1_HUMANHNRNPH1physical
26344197
HNRPK_HUMANHNRNPKphysical
26344197
HCD2_HUMANHSD17B10physical
26344197
KIF2C_HUMANKIF2Cphysical
26344197
PFKAM_HUMANPFKMphysical
26344197
PFKAP_HUMANPFKPphysical
26344197
PUF60_HUMANPUF60physical
26344197
ZNHI2_HUMANZNHIT2physical
26344197
UBAC1_HUMANUBAC1physical
28514442
RN123_HUMANRNF123physical
28514442
MRRP1_HUMANTRMT10Cphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614731Prostate cancer, hereditary, 2 (HPC2)
615440Combined oxidative phosphorylation deficiency 17 (COXPD17)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNZ2_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-199, 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-199, AND MASSSPECTROMETRY.

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