NVJ1_YEAST - dbPTM
NVJ1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NVJ1_YEAST
UniProt AC P38881
Protein Name Nucleus-vacuole junction protein 1
Gene Name NVJ1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 321
Subcellular Localization Nucleus outer membrane
Single-pass membrane protein .
Protein Description Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13..
Protein Sequence MTRPPLVRGIFSLGLSVAVLKGVEKTVRKHLERQGWIEPQKVDYELIFTIDRLKNLVDNKREALTAEQPDAGELSWRKVFNFISRQSSELDTRIYVLILLLSFLLPIAWTVLDGDRETTLEDKDNDCNVDLIENERRLKHYNDGERAVLQFGKNRSEPIILSYKDMNVLEGEHEFTSKEEHSNSHLTSKSENALNQVGSEDLLGCHLEKQLEEDKNEPNGEADGEDDNNREKDCSSSSEVESQSKCRKESTAEPDSLSRDTRTTSSLKSSTSFPISFKGSIDLKSLNQPSSLLHIQVSPTKSSNLDAQVNTEQAYSQPFRY
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
156PhosphorylationLQFGKNRSEPIILSY
HHCCCCCCCCEEEEE		58.0622369663
163PhosphorylationSEPIILSYKDMNVLE
CCCEEEEECCCCCCC		13.9427017623
177PhosphorylationEGEHEFTSKEEHSNS
CCCEECCCCCCCCCC		43.3121440633
182PhosphorylationFTSKEEHSNSHLTSK
CCCCCCCCCCCCCCH		43.2219779198
188PhosphorylationHSNSHLTSKSENALN
CCCCCCCCHHHHHHH		40.3119779198
190PhosphorylationNSHLTSKSENALNQV
CCCCCCHHHHHHHHC		35.5322369663
199PhosphorylationNALNQVGSEDLLGCH
HHHHHCCCHHHHHHH		29.1329136822
235PhosphorylationNNREKDCSSSSEVES
CCCCCCCCCHHHHHH		43.3128889911
236PhosphorylationNREKDCSSSSEVESQ
CCCCCCCCHHHHHHH		44.1923749301
237PhosphorylationREKDCSSSSEVESQS
CCCCCCCHHHHHHHH		17.7728889911
238PhosphorylationEKDCSSSSEVESQSK
CCCCCCHHHHHHHHH		47.8428889911
242PhosphorylationSSSSEVESQSKCRKE
CCHHHHHHHHHHCCC		44.9523749301
244PhosphorylationSSEVESQSKCRKEST
HHHHHHHHHHCCCCC		42.9023749301
250PhosphorylationQSKCRKESTAEPDSL
HHHHCCCCCCCCCCC		35.6322369663
251PhosphorylationSKCRKESTAEPDSLS
HHHCCCCCCCCCCCC		35.8122369663
256PhosphorylationESTAEPDSLSRDTRT
CCCCCCCCCCCCCCC		38.6719823750
258PhosphorylationTAEPDSLSRDTRTTS
CCCCCCCCCCCCCCC		31.8724961812
261PhosphorylationPDSLSRDTRTTSSLK
CCCCCCCCCCCCCCC		28.8919823750
263PhosphorylationSLSRDTRTTSSLKSS
CCCCCCCCCCCCCCC		32.8721440633
264PhosphorylationLSRDTRTTSSLKSST
CCCCCCCCCCCCCCC		17.0221551504
265PhosphorylationSRDTRTTSSLKSSTS
CCCCCCCCCCCCCCC		32.8221440633
266PhosphorylationRDTRTTSSLKSSTSF
CCCCCCCCCCCCCCC		37.4128152593
269PhosphorylationRTTSSLKSSTSFPIS
CCCCCCCCCCCCCEE		44.1129136822
270PhosphorylationTTSSLKSSTSFPISF
CCCCCCCCCCCCEEE		26.8729136822
271PhosphorylationTSSLKSSTSFPISFK
CCCCCCCCCCCEEEE		41.2929136822
272PhosphorylationSSLKSSTSFPISFKG
CCCCCCCCCCEEEEC		30.8521551504
276PhosphorylationSSTSFPISFKGSIDL
CCCCCCEEEECEEEH		22.5729136822
285PhosphorylationKGSIDLKSLNQPSSL
ECEEEHHHCCCCCCE		39.5922369663
290PhosphorylationLKSLNQPSSLLHIQV
HHHCCCCCCEEEEEE		24.6922369663
291PhosphorylationKSLNQPSSLLHIQVS
HHCCCCCCEEEEEEC		41.4522369663
298PhosphorylationSLLHIQVSPTKSSNL
CEEEEEECCCCCCCC		15.5222369663
300PhosphorylationLHIQVSPTKSSNLDA
EEEEECCCCCCCCCC		35.7320377248
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 NVJ1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NVJ1_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 NVJ1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAC8_YEASTVAC8physical
10888680
TECR_YEASTTSC13physical
15958487
TECR_YEASTTSC13physical
16912077
OSH1_YEASTSWH1physical
16912077
RLI1_YEASTRLI1physical
16093310
CYC7_YEASTCYC7physical
16093310
ATC7_YEASTNEO1physical
16093310
PRM10_YEASTPRM10physical
16093310
OAC1_YEASTOAC1physical
16093310
CY1_YEASTCYT1physical
16093310
RNQ1_YEASTRNQ1genetic
22529103
HSP71_YEASTSSA1physical
22940862
CKS1_YEASTCKS1genetic
27708008
SCC1_YEASTMCD1genetic
27708008
COG3_YEASTCOG3genetic
27708008
ACT_YEASTACT1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
NU192_YEASTNUP192genetic
27708008
NTR2_YEASTNTR2genetic
27708008
NEP1_YEASTEMG1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
SEN1_YEASTSEN1genetic
27708008
ORC1_YEASTORC1genetic
27708008
MCM1_YEASTMCM1genetic
27708008
MED11_YEASTMED11genetic
27708008
ROT1_YEASTROT1genetic
27708008
LST8_YEASTLST8genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NVJ1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-156; SER-190; SER-199;THR-251; SER-272; SER-285 AND SER-298, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-250 ANDTHR-251, AND MASS SPECTROMETRY.
"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-156, AND MASSSPECTROMETRY.

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