TX264_HUMAN - dbPTM
TX264_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TX264_HUMAN
UniProt AC Q9Y6I9
Protein Name Testis-expressed protein 264
Gene Name TEX264
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Secreted .
Protein Description
Protein Sequence MSDLLLLGLIGGLTLLLLLTLLAFAGYSGLLAGVEVSAGSPPIRNVTVAYKFHMGLYGETGRLFTESCSISPKLRSIAVYYDNPHMVPPDKCRCAVGSILSEGEESPSPELIDLYQKFGFKVFSFPAPSHVVTATFPYTTILSIWLATRRVHPALDTYIKERKLCAYPRLEIYQEDQIHFMCPLARQGDFYVPEMKETEWKWRGLVEAIDTQVDGTGADTMSDTSSVSLEVSPGSRETSAATLSPGASSRGWDDGDTRSEHSYSESGASGSSFEELDLEGEGPLGESRLDPGTEPLGTTKWLWEPTAPEKGKE
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
2Phosphorylation------MSDLLLLGL
------CCHHHHHHH		36.6424043423
14PhosphorylationLGLIGGLTLLLLLTL
HHHHHHHHHHHHHHH		20.7324043423
20PhosphorylationLTLLLLLTLLAFAGY
HHHHHHHHHHHHCCC		21.5024043423
27PhosphorylationTLLAFAGYSGLLAGV
HHHHHCCCHHHHCCC		8.9924043423
28PhosphorylationLLAFAGYSGLLAGVE
HHHHCCCHHHHCCCE		23.2624043423
37PhosphorylationLLAGVEVSAGSPPIR
HHCCCEECCCCCCCE		17.2624043423
40PhosphorylationGVEVSAGSPPIRNVT
CCEECCCCCCCEEEE		27.5024043423
45N-linked_GlycosylationAGSPPIRNVTVAYKF
CCCCCCEEEEEEEEE		34.23UniProtKB CARBOHYD
57PhosphorylationYKFHMGLYGETGRLF
EEECCEEECCCCCEE		13.7427642862
60PhosphorylationHMGLYGETGRLFTES
CCEEECCCCCEEEEC		24.2024719451
68S-nitrosylationGRLFTESCSISPKLR
CCEEEECCCCCHHHC		3.2219483679
68S-nitrosocysteineGRLFTESCSISPKLR
CCEEEECCCCCHHHC		3.22-
71PhosphorylationFTESCSISPKLRSIA
EEECCCCCHHHCEEE		10.3325159151
73UbiquitinationESCSISPKLRSIAVY
ECCCCCHHHCEEEEE		50.14-
91UbiquitinationPHMVPPDKCRCAVGS
CCCCCCHHCCCCHHH		29.38-
160UbiquitinationPALDTYIKERKLCAY
HHHHHHHHHHCCCCC		40.84-
163UbiquitinationDTYIKERKLCAYPRL
HHHHHHHCCCCCCCC		49.35-
196UbiquitinationDFYVPEMKETEWKWR
CEECCCCCCCCEEEE		60.88-
201UbiquitinationEMKETEWKWRGLVEA
CCCCCCEEEEHHHHH		22.30-
224O-linked_GlycosylationGADTMSDTSSVSLEV
CCCCCCCCCEEEEEE		18.65OGP
232PhosphorylationSSVSLEVSPGSRETS
CEEEEEECCCCCCCC		17.7330266825
235PhosphorylationSLEVSPGSRETSAAT
EEEECCCCCCCCEEE		30.2630266825
238PhosphorylationVSPGSRETSAATLSP
ECCCCCCCCEEEECC		23.6630266825
239PhosphorylationSPGSRETSAATLSPG
CCCCCCCCEEEECCC		15.9130266825
242PhosphorylationSRETSAATLSPGASS
CCCCCEEEECCCCCC		27.7330266825
244PhosphorylationETSAATLSPGASSRG
CCCEEEECCCCCCCC		19.5530266825
248PhosphorylationATLSPGASSRGWDDG
EEECCCCCCCCCCCC		26.8729255136
249PhosphorylationTLSPGASSRGWDDGD
EECCCCCCCCCCCCC		33.9929255136
259PhosphorylationWDDGDTRSEHSYSES
CCCCCCCCCCCCCCC		41.5826657352
262PhosphorylationGDTRSEHSYSESGAS
CCCCCCCCCCCCCCC		26.7130108239
263PhosphorylationDTRSEHSYSESGASG
CCCCCCCCCCCCCCC		20.5426657352
264PhosphorylationTRSEHSYSESGASGS
CCCCCCCCCCCCCCC		28.4430108239
266PhosphorylationSEHSYSESGASGSSF
CCCCCCCCCCCCCCC		33.4526657352
269PhosphorylationSYSESGASGSSFEEL
CCCCCCCCCCCCEEC		42.6130108239
271PhosphorylationSESGASGSSFEELDL
CCCCCCCCCCEECCC		29.3830108239
272PhosphorylationESGASGSSFEELDLE
CCCCCCCCCEECCCC		39.9626657352
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 TX264_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TX264_HUMAN !!
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 TX264_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TMM79_HUMANTMEM79physical
25416956
KC1A_HUMANCSNK1A1physical
26186194
POTEI_HUMANPOTEIphysical
26186194
CHK2_HUMANCHEK2physical
26186194
SNX14_HUMANSNX14physical
26186194
PLPL6_HUMANPNPLA6physical
26186194
PKHG4_HUMANPLEKHG4physical
26186194
TYW1B_HUMANTYW1Bphysical
26186194
STAT1_HUMANSTAT1physical
26186194
PLD1_HUMANPLD1physical
26186194
PLD2_HUMANPLD2physical
26186194
UPK3L_HUMANUPK3BLphysical
26186194
OSBL8_HUMANOSBPL8physical
26186194
MINK1_HUMANMINK1physical
26186194
M4K4_HUMANMAP4K4physical
26186194
ENTP7_HUMANENTPD7physical
26186194
PDE3B_HUMANPDE3Bphysical
26186194
FOXK1_HUMANFOXK1physical
26186194
CP131_HUMANCEP131physical
26186194
PDZD8_HUMANPDZD8physical
26186194
DIP2A_HUMANDIP2Aphysical
26186194
TERF2_HUMANTERF2physical
26186194
SUN1_HUMANSUN1physical
26186194
KC1E_HUMANCSNK1Ephysical
26186194
KC1D_HUMANCSNK1Dphysical
26186194
VANG2_HUMANVANGL2physical
26186194
PER1_HUMANPER1physical
26186194
MCM10_HUMANMCM10physical
26186194
MRP7_HUMANABCC10physical
26186194
EDA_HUMANEDAphysical
26186194
JPH1_HUMANJPH1physical
26186194
CA043_HUMANC1orf43physical
26186194
CNEP1_HUMANCTDNEP1physical
26186194
MINK1_HUMANMINK1physical
28514442
POTEI_HUMANPOTEIphysical
28514442
ENTP7_HUMANENTPD7physical
28514442
CHK2_HUMANCHEK2physical
28514442
PLD1_HUMANPLD1physical
28514442
CA043_HUMANC1orf43physical
28514442
CP131_HUMANCEP131physical
28514442
MCM10_HUMANMCM10physical
28514442
MRP7_HUMANABCC10physical
28514442
EDA_HUMANEDAphysical
28514442
SNX14_HUMANSNX14physical
28514442
KC1A_HUMANCSNK1A1physical
28514442
ACTBL_HUMANACTBL2physical
28514442
PER1_HUMANPER1physical
28514442
TERF2_HUMANTERF2physical
28514442
PDE3B_HUMANPDE3Bphysical
28514442
M4K4_HUMANMAP4K4physical
28514442
TYW1B_HUMANTYW1Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TX264_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASSSPECTROMETRY.

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