INP2_YEAST - dbPTM
INP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INP2_YEAST
UniProt AC Q03824
Protein Name Inheritance of peroxisomes protein 2
Gene Name INP2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 705
Subcellular Localization Peroxisome membrane
Single-pass membrane protein .
Protein Description Required for peroxisome inheritance. Acts as the peroxisome-specific receptor for the myosin V motor MYO2..
Protein Sequence MTTNSRPSALQAPGLQIFSMLKSSEEDGFMSSSLTLDSDNIIGVTENNRQEFYSTWRKPSLLSSRSVLHEYSPTIVGSNDCTFSPITVGKTTKFFNWDDIISRIFMQQPFGVTHQFFEEFRYSIITSHFLNDMNHYRLSLHLDQSIMNFHKSSTLLKNVPPKSVPFMATKYGKLAVAEDKKLYFRQNFNYLSMIITSYRVLTQLKKYCRKKNSPGLKRVVILILVAVYLSIQQEYFRRHLICYKTLLKVRKVLESLQQVDVMIHKYHLRFKEIKNHSFISRVSLISIADEHSSVIKELLVFSSDALFYKLKSIIPDIVIFSDTSELSKYCELYGIDVPNLYYNNTTTVKDLDGKLYRLKLLKKFMLCCLLSLDMTGNENLSNVNMRNALNKIFPDYMARVQLKKKYNPIGTFQNIVSLLRGLHSLLSTVLVSLNDHKQILYAFPEETSTNTGCERANVCSFSKNDKLFQALNYLKMIENNLLAIDIRNGITENDRNIIEDKLEELITFWKTSKICGNISRIQKVSPTNTINHGFHLDILKGRKSPRSSSVQGLSLERKVDFIDVAESVNDSFENDTELEEYEDYDCQEECSAGSRQNHRVDFIGKDSCRKPDFKQLSDNELRRKLDERILKLAQENREGRERLRTAKSFELLRKAQASMSVKFGFQKPLRDDAFLESRPLSKCKVSSEETIPFLYELKGLLGNDS
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
60PhosphorylationYSTWRKPSLLSSRSV
HHCCCCHHHHCCCCH		45.0023749301
71PhosphorylationSRSVLHEYSPTIVGS
CCCHHHHCCCCEECC		14.8123749301
74PhosphorylationVLHEYSPTIVGSNDC
HHHHCCCCEECCCCC		23.5023749301
82PhosphorylationIVGSNDCTFSPITVG
EECCCCCEECCCCCC		29.9723749301
84PhosphorylationGSNDCTFSPITVGKT
CCCCCEECCCCCCCC		9.3923749301
87PhosphorylationDCTFSPITVGKTTKF
CCEECCCCCCCCCCC		26.9623749301
275N-linked_GlycosylationLRFKEIKNHSFISRV
HHHHHHCCCCCEEEE		41.52-
312PhosphorylationALFYKLKSIIPDIVI
HHHHHHHHHCCCEEE		35.8723749301
321PhosphorylationIPDIVIFSDTSELSK
CCCEEEECCHHHHHH		28.9323749301
323PhosphorylationDIVIFSDTSELSKYC
CEEEECCHHHHHHHH		23.9323749301
343N-linked_GlycosylationDVPNLYYNNTTTVKD
CCCCCEECCCCCEEC		26.30-
344N-linked_GlycosylationVPNLYYNNTTTVKDL
CCCCEECCCCCEECC		23.76-
379N-linked_GlycosylationLDMTGNENLSNVNMR
CCCCCCCCCCCCHHH		53.41-
451PhosphorylationPEETSTNTGCERANV
CCCCCCCCCCCCCCC		43.2121551504
460PhosphorylationCERANVCSFSKNDKL
CCCCCCCCCCCCHHH		28.4223749301
517N-linked_GlycosylationKTSKICGNISRIQKV
HHCCCCCCHHHEEEE		25.34-
523UbiquitinationGNISRIQKVSPTNTI
CCHHHEEEECCCCCC		42.1617644757
525PhosphorylationISRIQKVSPTNTINH
HHHEEEECCCCCCCC		32.8021440633
527PhosphorylationRIQKVSPTNTINHGF
HEEEECCCCCCCCCE		37.1721440633
544PhosphorylationDILKGRKSPRSSSVQ
HHCCCCCCCCCCCCC		24.9619823750
547PhosphorylationKGRKSPRSSSVQGLS
CCCCCCCCCCCCCCC		30.2821551504
548PhosphorylationGRKSPRSSSVQGLSL
CCCCCCCCCCCCCCC		35.4919823750
549PhosphorylationRKSPRSSSVQGLSLE
CCCCCCCCCCCCCCE		21.5021551504
554PhosphorylationSSSVQGLSLERKVDF
CCCCCCCCCEECCEE		34.7019823750
569N-linked_GlycosylationIDVAESVNDSFENDT
EEHHHHCCCCCCCCC		48.79-
574N-linked_GlycosylationSVNDSFENDTELEEY
HCCCCCCCCCCHHHH		60.54-
605AcetylationHRVDFIGKDSCRKPD
CCCCCCCCCCCCCCC		41.4725381059
617PhosphorylationKPDFKQLSDNELRRK
CCCHHHCCHHHHHHH		35.5821440633
648PhosphorylationERLRTAKSFELLRKA
HHHHHHHHHHHHHHH		22.8421440633
681PhosphorylationFLESRPLSKCKVSSE
CHHCCCCCCCCCCCC		38.4021551504
686PhosphorylationPLSKCKVSSEETIPF
CCCCCCCCCCHHHHH		19.9527017623
687PhosphorylationLSKCKVSSEETIPFL
CCCCCCCCCHHHHHH		42.3021440633
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 INP2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INP2_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 INP2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO2_YEASTMYO2physical
16678774
PEX19_YEASTPEX19physical
11283351
MYO2_YEASTMYO2physical
19687257
MYO2_YEASTMYO2physical
22753895
TIM22_YEASTTIM22genetic
27708008
SEC7_YEASTSEC7genetic
27708008
NUP57_YEASTNUP57genetic
27708008
BUD31_YEASTBUD31genetic
27708008
PRP6_YEASTPRP6genetic
27708008
TECR_YEASTTSC13genetic
27708008
PRP11_YEASTPRP11genetic
27708008
UAP1_YEASTQRI1genetic
27708008
CDC53_YEASTCDC53genetic
27708008
GLE1_YEASTGLE1genetic
27708008
CDC13_YEASTCDC13genetic
27708008
MAK21_YEASTMAK21genetic
27708008
GPI11_YEASTGPI11genetic
27708008
TFB1_YEASTTFB1genetic
27708008
RPB7_YEASTRPB7genetic
27708008
PANK_YEASTCAB1genetic
27708008
ACT_YEASTACT1genetic
27708008
RPN11_YEASTRPN11genetic
27708008
CDC20_YEASTCDC20genetic
27708008
MPPA_YEASTMAS2genetic
27708008
PRP21_YEASTPRP21genetic
27708008
SEC22_YEASTSEC22genetic
27708008
ORC1_YEASTORC1genetic
27708008
TIM23_YEASTTIM23genetic
27708008
HRP1_YEASTHRP1genetic
27708008
TYSY_YEASTCDC21genetic
27708008
MED4_YEASTMED4genetic
27708008
NSL1_YEASTNSL1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
PRP4_YEASTPRP4genetic
27708008
THRC_YEASTTHR4genetic
27708008
VPS41_YEASTVPS41genetic
27708008
STB5_YEASTSTB5genetic
27708008
YJ24_YEASTKCH1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
ORM2_YEASTORM2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INP2_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 THR-74, AND MASSSPECTROMETRY.

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