dbPTM

RNZ_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RNZ_YEAST
UniProt AC	P36159
Protein Name	Ribonuclease Z
Gene Name	TRZ1
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	838
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA..
Protein Sequence	MFTFIPITHPTSDTKHPLLLVQSAHGEKYFFGKIGEGSQRSLTENKIRISKLKDIFLTGELNWSDIGGLPGMILTIADQGKSNLVLHYGNDILNYIVSTWRYFVFRFGIDLNDHIMKDKEVYKDKIIAVKSFNVLKNGGEDRLGVFDSFQKGVLRSIVAKMFPKHAPTDRYDPSSDPHLNVELPDLDAKVEVSTNYEISFSPVRGKFKVEEAIKLGVPKGPLFAKLTKGQTITLDNGIVVTPEQVLENERHFAKVLILDIPDDLYLNAFVEKFKDYDCAELGMVYYFLGDEVTINDNLFAFIDIFEKNNYGKVNHMISHNKISPNTISFFGSALTTLKLKALQVNNYNLPKTDRVFSKDFYDRFDTPLSRGTSMCKSQEEPLNTIIEKDNIHIFSQNKTVTFEPFRMNEEPMKCNINGEVADFSWQEIFEEHVKPLEFPLADVDTVINNQLHVDNFNNSAEKKKHVEIITLGTGSALPSKYRNVVSTLVKVPFTDADGNTINRNIMLDAGENTLGTIHRMFSQLAVKSIFQDLKMIYLSHLHADHHLGIISVLNEWYKYNKDDETSYIYVVTPWQYHKFVNEWLVLENKEILKRIKYISCEHFINDSFVRMQTQSVPLAEFNEILKENSNQESNRKLELDRDSSYRDVDLIRQMYEDLSIEYFQTCRAIHCDWAYSNSITFRMDENNEHNTFKVSYSGDTRPNIEKFSLEIGYNSDLLIHEATLENQLLEDAVKKKHCTINEAIGVSNKMNARKLILTHFSQRYPKLPQLDNNIDVMAREFCFAFDSMIVDYEKIGEQQRIFPLLNKAFVEEKEEEEDVDDVESVQDLEVKLKKHKKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
148	Phosphorylation	DRLGVFDSFQKGVLR CCCCCCHHHHHHHHH	20.36	30377154
151	Acetylation	GVFDSFQKGVLRSIV CCCHHHHHHHHHHHH	49.31	24489116
174	Phosphorylation	PTDRYDPSSDPHLNV CCCCCCCCCCCCCCC	44.46	21551504
175	Phosphorylation	TDRYDPSSDPHLNVE CCCCCCCCCCCCCCC	61.62	21551504
225	Acetylation	PKGPLFAKLTKGQTI CCCCCEEECCCCCEE	49.72	24489116
369	Phosphorylation	DRFDTPLSRGTSMCK HHCCCCCCCCCCCCC	29.84	27017623
481	Phosphorylation	GSALPSKYRNVVSTL CCCCCHHHHCCCCEE	16.26	27017623
486	Phosphorylation	SKYRNVVSTLVKVPF HHHHCCCCEEEECCC	16.25	27017623
528	Phosphorylation	FSQLAVKSIFQDLKM HHHHHHHHHHHHHHH	23.26	19779198
551	Phosphorylation	DHHLGIISVLNEWYK CCCHHHHHHHHHHHC	20.73	19779198
644	Phosphorylation	LELDRDSSYRDVDLI CCCCCCCCHHHHHHH	28.60	30377154
736	Ubiquitination	LEDAVKKKHCTINEA HHHHHHHCCCCHHHH	37.89	17644757
749	Ubiquitination	EAIGVSNKMNARKLI HHHCCCCHHCHHHHH	26.48	17644757
824	Phosphorylation	EDVDDVESVQDLEVK CCCCCCCHHHHHHHH	25.56	22369663

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 RNZ_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RNZ_YEAST !!

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 RNZ_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUC1_YEAST	NUC1	physical	14690591
YMY9_YEAST	YMR099C	physical	14690591
NAP1_YEAST	NAP1	physical	14759368
RNZ_YEAST	TRZ1	physical	14759368
NUC1_YEAST	NUC1	physical	11805826
NUC1_YEAST	NUC1	physical	16429126
RSA3_YEAST	RSA3	genetic	19061648
CGR1_YEAST	CGR1	genetic	19061648
NU120_YEAST	NUP120	genetic	19061648
MRT4_YEAST	MRT4	genetic	19061648
SYMM_YEAST	MSM1	genetic	19061648
LSM7_YEAST	LSM7	genetic	19061648
FBRL_YEAST	NOP1	physical	24249226
MDHM_YEAST	MDH1	physical	24249226
NUC1_YEAST	NUC1	physical	28899942

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RNZ_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824, AND MASSSPECTROMETRY.	18407956 [Abstract]
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-824, AND MASSSPECTROMETRY.	17330950 [Abstract]