CEX1_YEAST - dbPTM
CEX1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CEX1_YEAST
UniProt AC Q12453
Protein Name Cytoplasmic export protein 1
Gene Name CEX1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 761
Subcellular Localization Cytoplasm .
Protein Description Component of the nuclear tRNA export machinery that my collect tRNA from the nuclear tRNA export receptors of the aminoacylation-dependent export and may deliver aminoacylated tRNAs to the translation machinery pathway at the nuclear pore complex..
Protein Sequence MNFSSIFKSISNFQFPYTIEETAITETALWQCFDGTRKADSLPVTVFKAKRSPENESLILNAVHKSKILKIPGLCTVLETFDSDPQSTFIVTERVVPFPWDNLGSLSQNKFGVELGISQLLATLGFLKNFVLGTLSKDSVFINIKGEWVLFGLELCSSKEGLSAFEFASRARSYYNIIGSQLPCEDPNTIDSMGLGLLIKSLMAPSCLPKDWIVNVNMISDGKITIENFRKRLENTETWRSNPLINFYQELRELHIKDPQGKLVVMSNLENLYLESREIFRNLTPGMIENFIIPELCEIIKLLMTQSISSAASPIGMNFNASHKLVPFLAIVLDLTSETNTFPVGFNDLITQSFKLPDRQVRFLLLIYLPKLIGPLSKSEISSRIYPHFIQGLTDSDATLRLQTLKTIPCIVSCLTERQLNNELLRFLAKTQVDSDVEIRTWTVIIISKISTILSTSVGNRSNILATAFTKSLKDPQVKPRLAALYGLEKSIELFDVNTIANKILTVIAPGLLDKSPIVRGRAKILFEEYLEKLEKEAQLIQTNDSTADSEDVKDIDFENYGCDEEDMNKEDNLLAAQFLNNLRLNSPSATTPSNITESEIDSAQDGSGWDDLSDTDGFITNGTTESFDETTNPVTTASTPKLFGKPIKINKSWNDELNDDGWIQDESGPSKVPQKHTRPQNSTLAKSIAPSSRLSIKKKKTTILAPRNIASNSTVTTKSSLSNKTARSKPISSIRGSVTKKGNVDGWDDDGDSDSWDTNW
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
5Phosphorylation---MNFSSIFKSISN
---CCHHHHHHHHHC		28.1030377154
173PhosphorylationEFASRARSYYNIIGS
HHHHHHHHHHHCCCC		30.8627017623
174PhosphorylationFASRARSYYNIIGSQ
HHHHHHHHHHCCCCC		8.5827017623
175PhosphorylationASRARSYYNIIGSQL
HHHHHHHHHCCCCCC		10.9227017623
201PhosphorylationGLGLLIKSLMAPSCL
HHHHHHHHHHCCCCC		19.1827017623
206PhosphorylationIKSLMAPSCLPKDWI
HHHHHCCCCCCCCEE		20.8127017623
377PhosphorylationPKLIGPLSKSEISSR
HHHHCCCCHHHHHHC		36.9519779198
379PhosphorylationLIGPLSKSEISSRIY
HHCCCCHHHHHHCHH		36.4719779198
383PhosphorylationLSKSEISSRIYPHFI
CCHHHHHHCHHHHHH		28.4919779198
503UbiquitinationDVNTIANKILTVIAP
EHHHHHHHHHHHHCC		30.0317644757
515AcetylationIAPGLLDKSPIVRGR
HCCCCCCCCCCCCCH		59.0924489116
515UbiquitinationIAPGLLDKSPIVRGR
HCCCCCCCCCCCCCH		59.0917644757
546PhosphorylationQLIQTNDSTADSEDV
HHHHCCCCCCCHHHH		27.8021551504
649AcetylationKLFGKPIKINKSWND
HHCCCCEEECCCCCC		49.0725381059
653PhosphorylationKPIKINKSWNDELND
CCEEECCCCCCCCCC		26.9930377154
688PhosphorylationQNSTLAKSIAPSSRL
CCCHHHHHCCCCCCC		20.5517563356
692PhosphorylationLAKSIAPSSRLSIKK
HHHHCCCCCCCCCCC		21.0421440633
693PhosphorylationAKSIAPSSRLSIKKK
HHHCCCCCCCCCCCC		35.8621440633
696PhosphorylationIAPSSRLSIKKKKTT
CCCCCCCCCCCCCEE		31.1117330950
702PhosphorylationLSIKKKKTTILAPRN
CCCCCCCEEEECCCC		28.1321440633
703PhosphorylationSIKKKKTTILAPRNI
CCCCCCEEEECCCCC		23.9121440633
712PhosphorylationLAPRNIASNSTVTTK
ECCCCCCCCCCEECH		27.7630377154
715PhosphorylationRNIASNSTVTTKSSL
CCCCCCCCEECHHHH		26.5628889911
720PhosphorylationNSTVTTKSSLSNKTA
CCCEECHHHHCCCCC		34.1322890988
721PhosphorylationSTVTTKSSLSNKTAR
CCEECHHHHCCCCCC		37.0622890988
723PhosphorylationVTTKSSLSNKTARSK
EECHHHHCCCCCCCC		37.9222890988
726PhosphorylationKSSLSNKTARSKPIS
HHHHCCCCCCCCCCC		31.3922890988
729PhosphorylationLSNKTARSKPISSIR
HCCCCCCCCCCCCCC		40.0822890988
733PhosphorylationTARSKPISSIRGSVT
CCCCCCCCCCCCEEE		28.3922890988
734PhosphorylationARSKPISSIRGSVTK
CCCCCCCCCCCEEEC		19.6122890988
738PhosphorylationPISSIRGSVTKKGNV
CCCCCCCEEECCCCC		19.4327717283
740PhosphorylationSSIRGSVTKKGNVDG
CCCCCEEECCCCCCC		28.8327717283
754PhosphorylationGWDDDGDSDSWDTNW
CCCCCCCCCCCCCCC		38.7917330950
756PhosphorylationDDDGDSDSWDTNW--
CCCCCCCCCCCCC--		30.7021440633
759PhosphorylationGDSDSWDTNW-----
CCCCCCCCCC-----		32.4621440633
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 CEX1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CEX1_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 CEX1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NAP1_YEASTNAP1physical
14759368
CEX1_YEASTCEX1physical
14759368
NU116_YEASTNUP116physical
17203074
XPOT_YEASTLOS1physical
17203074
MSN5_YEASTMSN5physical
17203074
GSP1_YEASTGSP1physical
17203074
EF1A_YEASTTEF2genetic
17203074
SSB1_YEASTSSB1physical
19536198
RNA1_YEASTRNA1genetic
22008473
GSP1_YEASTGSP1physical
22008473
RNA1_YEASTRNA1physical
22008473
UME6_YEASTUME6genetic
27708008
ATC3_YEASTDRS2genetic
27708008
VAM6_YEASTVAM6genetic
27708008
ARO1_YEASTARO1genetic
27708008
DHAS_YEASTHOM2genetic
27708008
CEM1_YEASTCEM1genetic
27708008
PALF_YEASTRIM8genetic
27708008
CHO2_YEASTCHO2genetic
27708008
SYS1_YEASTSYS1genetic
27708008
LPLA_YEASTAIM22genetic
27708008
VPS35_YEASTVPS35genetic
27708008
HOC1_YEASTHOC1genetic
27708008
DHOM_YEASTHOM6genetic
27708008
RIC1_YEASTRIC1genetic
27708008
YPT6_YEASTYPT6genetic
27708008
COG8_YEASTCOG8genetic
27708008
PALI_YEASTRIM9genetic
27708008
COG6_YEASTCOG6genetic
27708008
ATG3_YEASTATG3genetic
27708008
ARL3_YEASTARL3genetic
27708008
WDR6_YEASTRTT10genetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CEX1_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-688, AND MASSSPECTROMETRY.
"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-754, AND MASSSPECTROMETRY.

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