HEH2_YEAST - dbPTM
HEH2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HEH2_YEAST
UniProt AC Q03281
Protein Name Inner nuclear membrane protein HEH2
Gene Name HEH2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 663
Subcellular Localization Nucleus inner membrane
Single-pass membrane protein . Targeting to the inner nuclear membrane requires the SRP1 and KAP95 karyopherins and the Ran cycle.
Protein Description
Protein Sequence MDHRNLDPKTLKVSQLRRVLVENDVAFPANARKPVLVKLFEEKVRQRLQSSPEASKVRTSIQKVVKSGAKNADRKKTLKSKKLESSSSESKTVKDENVETNKRKREQISTDNEAKMQIQEEKSPKKKRKKRSSKANKPPESPPQSKSDGKATSADLTSELETVEELHKKDSSDDKPRVKELPKPELPNLKVSNEFLAQLNKELASAATENYDHSIKSTDLSSIRIETEEPVGPSTGAETRNESEVMENINLEVQPEVKEAKEELTKISETFDNQDEEDTSRLSSKKNIRSPKGRTRHFIANKTKRGIDIMKPFIAHLFIWLWNGAIFLSIICPILFGLWYREQRIQVGYCGHEKPLKSLAISAFPQTERVDSVLQAYRPNCLECPEHGICSSFMNVECEPGYEPKSSILETYGIIPFPKYCAKDESKEKEVDELVWKVNEYLKKKNAQHECGEGENLFESGETETKLYDIFSHSRPSWESQREFNDHWKNVLEILKKKDDIIWLPLDFETNGKREKSKSNNTNYIYRSTSKKWVTLQCHLEGDIQEYITKYGGSLFITLGVLFLIKKIQSTLDNYVQGEQIIEKLVKEAIDKLKDVKKNKGEEPFLTTVQLRATLLSDIPNIKEQNNLWAQTKEKIMKEQSENIELYLLEENGEIMTCWEWKE
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
12AcetylationNLDPKTLKVSQLRRV
CCCHHHCCHHHHHHH		45.1025381059
50PhosphorylationKVRQRLQSSPEASKV
HHHHHHHHCHHHHHH		53.0729136822
51PhosphorylationVRQRLQSSPEASKVR
HHHHHHHCHHHHHHH		17.5025752575
55PhosphorylationLQSSPEASKVRTSIQ
HHHCHHHHHHHHHHH		29.9819823750
109PhosphorylationKRKREQISTDNEAKM
HHHHHHHCCCHHHHH		29.4227717283
110PhosphorylationRKREQISTDNEAKMQ
HHHHHHCCCHHHHHH		44.4623749301
123PhosphorylationMQIQEEKSPKKKRKK
HHHHHHCCHHHHHHH		45.2721082442
141PhosphorylationKANKPPESPPQSKSD
CCCCCCCCCCCCCCC		47.8825521595
145PhosphorylationPPESPPQSKSDGKAT
CCCCCCCCCCCCCCC		39.6419823750
152PhosphorylationSKSDGKATSADLTSE
CCCCCCCCHHHHHHH		28.1229734811
153PhosphorylationKSDGKATSADLTSEL
CCCCCCCHHHHHHHH		25.3325752575
157PhosphorylationKATSADLTSELETVE
CCCHHHHHHHHHHHH		22.2429136822
158PhosphorylationATSADLTSELETVEE
CCHHHHHHHHHHHHH		47.7029136822
162PhosphorylationDLTSELETVEELHKK
HHHHHHHHHHHHHHC		45.9329136822
192PhosphorylationELPNLKVSNEFLAQL
CCCCCCCCHHHHHHH		29.1121440633
205PhosphorylationQLNKELASAATENYD
HHHHHHHHHHHHCCC		30.9424961812
208PhosphorylationKELASAATENYDHSI
HHHHHHHHHCCCCCC		25.2024961812
221PhosphorylationSIKSTDLSSIRIETE
CCCCCCCCCCEEEEC		26.9119779198
227PhosphorylationLSSIRIETEEPVGPS
CCCCEEEECCCCCCC		43.1927017623
235PhosphorylationEEPVGPSTGAETRNE
CCCCCCCCCCCCCCH		43.4727214570
243PhosphorylationGAETRNESEVMENIN
CCCCCCHHHHHHHCC		38.7527017623
279PhosphorylationDNQDEEDTSRLSSKK
CCCCHHHHHHHHHCC		21.0121440633
280PhosphorylationNQDEEDTSRLSSKKN
CCCHHHHHHHHHCCC		43.4723749301
284PhosphorylationEDTSRLSSKKNIRSP
HHHHHHHHCCCCCCC		52.8427017623
633UbiquitinationNNLWAQTKEKIMKEQ
CCHHHHHHHHHHHHH		44.9523749301
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 HEH2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HEH2_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 HEH2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARC1_YEASTARC1genetic
19061648
NAM7_YEASTNAM7genetic
19061648
FHL1_YEASTFHL1genetic
19061648
PO152_YEASTPOM152physical
21346187
NU170_YEASTNUP170physical
21346187
NUP85_YEASTNUP85physical
21346187
NUP59_YEASTASM4genetic
21346187
NU170_YEASTNUP170genetic
21346187
NU188_YEASTNUP188genetic
21346187
NUP84_YEASTNUP84genetic
21346187
NU120_YEASTNUP120genetic
21346187
POM34_YEASTPOM34genetic
21346187
NU157_YEASTNUP157genetic
21346187
NUP53_YEASTNUP53genetic
21346187
APQ12_YEASTAPQ12genetic
21346187
SEC22_YEASTSEC22genetic
27708008
TFB1_YEASTTFB1genetic
27708008
ACT_YEASTACT1genetic
27708008
TAF4_YEASTTAF4genetic
27708008
APC5_YEASTAPC5genetic
27708008
PSA7_YEASTPRE10genetic
27708008
TF2B_YEASTSUA7genetic
27708008
YJE9_YEASTYJL049Wphysical
27733427
SNF7_YEASTSNF7physical
27733427
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HEH2_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-141, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory