TTC7B_HUMAN - dbPTM
TTC7B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTC7B_HUMAN
UniProt AC Q86TV6
Protein Name Tetratricopeptide repeat protein 7B
Gene Name TTC7B
Organism Homo sapiens (Human).
Sequence Length 843
Subcellular Localization Cytoplasm, cytosol . Cell membrane . Localizes to the cytosol and is recruited to the plasma membrane following interaction with EFR3 (EFR3A or EFR3B) (PubMed:23229899).
Protein Description Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and FAM126A, via direct interactions. [PubMed: 26571211]
Protein Sequence MATKKAGSRLETEIERCRSECQWERIPELVKQLSAKLIANDDMAELLLGESKLEQYLKEHPLRQGASPRGPKPQLTEVRKHLTAALDRGNLKSEFLQESNLIMAKLNYVEGDYKEALNIYARVGLDDLPLTAVPPYRLRVIAEAYATKGLCLEKLPISSSTSNLHVDREQDVITCYEKAGDIALLYLQEIERVILSNIQNRSPKPGPAPHDQELGFFLETGLQRAHVLYFKNGNLTRGVGRFRELLRAVETRTTQNLRMTIARQLAEILLRGMCEQSYWNPLEDPPCQSPLDDPLRKGANTKTYTLTRRARVYSGENIFCPQENTEEALLLLLISESMANRDAVLSRIPEHKSDRLISLQSASVVYDLLTIALGRRGQYEMLSECLERAMKFAFEEFHLWYQFALSLMAAGKSARAVKVLKECIRLKPDDATIPLLAAKLCMGSLHWLEEAEKFAKTVVDVGEKTSEFKAKGYLALGLTYSLQATDASLRGMQEVLQRKALLAFQRAHSLSPTDHQAAFYLALQLAISRQIPEALGYVRQALQLQGDDANSLHLLALLLSAQKHYHDALNIIDMALSEYPENFILLFSKVKLQSLCRGPDEALLTCKHMLQIWKSCYNLTNPSDSGRGSSLLDRTIADRRQLNTITLPDFSDPETGSVHATSVAASRVEQALSEVASSLQSSAPKQGPLHPWMTLAQIWLHAAEVYIGIGKPAEATACTQEAANLFPMSHNVLYMRGQIAELRGSMDEARRWYEEALAISPTHVKSMQRLALILHQLGRYSLAEKILRDAVQVNSTAHEVWNGLGEVLQAQGNDAAATECFLTALELEASSPAVPFTIIPRVL
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
34PhosphorylationPELVKQLSAKLIAND
HHHHHHHHHHHHHCC		22.36-
51PhosphorylationAELLLGESKLEQYLK
HHHHHCHHHHHHHHH		40.52-
58PhosphorylationSKLEQYLKEHPLRQG
HHHHHHHHHCCCCCC		49.3918220336
67PhosphorylationHPLRQGASPRGPKPQ
CCCCCCCCCCCCCCC		23.1928102081
72MalonylationGASPRGPKPQLTEVR
CCCCCCCCCCHHHHH		48.5026320211
93PhosphorylationLDRGNLKSEFLQESN
HHHCCCCHHHHHHHC		36.4323401153
158PhosphorylationCLEKLPISSSTSNLH
EEEECCCCCCCCCCC		19.1223401153
159PhosphorylationLEKLPISSSTSNLHV
EEECCCCCCCCCCCC		38.0530266825
160PhosphorylationEKLPISSSTSNLHVD
EECCCCCCCCCCCCC		29.1223401153
161PhosphorylationKLPISSSTSNLHVDR
ECCCCCCCCCCCCCC		24.4730266825
162PhosphorylationLPISSSTSNLHVDRE
CCCCCCCCCCCCCCH		39.0623927012
174PhosphorylationDREQDVITCYEKAGD
CCHHCEEEHHHHHCC		14.6423403867
176PhosphorylationEQDVITCYEKAGDIA
HHCEEEHHHHHCCCH		16.2923403867
196PhosphorylationEIERVILSNIQNRSP
HHHHHHHHCCCCCCC		22.2926074081
202PhosphorylationLSNIQNRSPKPGPAP
HHCCCCCCCCCCCCC		44.8429255136
220PhosphorylationELGFFLETGLQRAHV
HHHHHHHHCCCCEEE		45.3928102081
236PhosphorylationYFKNGNLTRGVGRFR
EEECCCCCCCCHHHH		29.40-
301PhosphorylationPLRKGANTKTYTLTR
CCCCCCCCCEEEEEE		24.9924719451
302MethylationLRKGANTKTYTLTRR
CCCCCCCCEEEEEEE		39.06-
303PhosphorylationRKGANTKTYTLTRRA
CCCCCCCEEEEEEEE		21.50-
304PhosphorylationKGANTKTYTLTRRAR
CCCCCCEEEEEEEEE		10.99-
307PhosphorylationNTKTYTLTRRARVYS
CCCEEEEEEEEEECC		15.4324719451
480PhosphorylationYLALGLTYSLQATDA
EEEEECEEEHHHCCH		16.6623403867
481PhosphorylationLALGLTYSLQATDAS
EEEECEEEHHHCCHH		14.5823403867
485PhosphorylationLTYSLQATDASLRGM
CEEEHHHCCHHHHHH		21.0923403867
488PhosphorylationSLQATDASLRGMQEV
EHHHCCHHHHHHHHH		22.7823403867
528PhosphorylationLALQLAISRQIPEAL
HHHHHHHHCCHHHHH		16.7224719451
588PhosphorylationENFILLFSKVKLQSL
CCEEHHEEHHHHHHH		36.1924719451
594PhosphorylationFSKVKLQSLCRGPDE
EEHHHHHHHCCCCCH		39.6124719451
615PhosphorylationHMLQIWKSCYNLTNP
HHHHHHHHHHCCCCC		13.5629691806
617PhosphorylationLQIWKSCYNLTNPSD
HHHHHHHHCCCCCCC		21.9429691806
620PhosphorylationWKSCYNLTNPSDSGR
HHHHHCCCCCCCCCC		41.2529691806
623PhosphorylationCYNLTNPSDSGRGSS
HHCCCCCCCCCCCCH		46.6130631047
625PhosphorylationNLTNPSDSGRGSSLL
CCCCCCCCCCCCHHH		34.4322617229
629PhosphorylationPSDSGRGSSLLDRTI
CCCCCCCCHHHHHHH		19.2230266825
630PhosphorylationSDSGRGSSLLDRTIA
CCCCCCCHHHHHHHH		35.4623401153
635PhosphorylationGSSLLDRTIADRRQL
CCHHHHHHHHCCCCC		21.8628270605
644PhosphorylationADRRQLNTITLPDFS
HCCCCCCEEECCCCC		24.7527080861
646PhosphorylationRRQLNTITLPDFSDP
CCCCCEEECCCCCCC		30.1427080861
651PhosphorylationTITLPDFSDPETGSV
EEECCCCCCCCCCCE		60.6829507054
655PhosphorylationPDFSDPETGSVHATS
CCCCCCCCCCEEEHH		39.9027050516
657PhosphorylationFSDPETGSVHATSVA
CCCCCCCCEEEHHHH		20.3927050516
661PhosphorylationETGSVHATSVAASRV
CCCCEEEHHHHHHHH		14.6228060719
662PhosphorylationTGSVHATSVAASRVE
CCCEEEHHHHHHHHH		15.5628060719
666PhosphorylationHATSVAASRVEQALS
EEHHHHHHHHHHHHH		27.4128060719
673PhosphorylationSRVEQALSEVASSLQ
HHHHHHHHHHHHHHH		32.8029255136
677PhosphorylationQALSEVASSLQSSAP
HHHHHHHHHHHHCCC		36.4430266825
678PhosphorylationALSEVASSLQSSAPK
HHHHHHHHHHHCCCC		22.2329255136
681PhosphorylationEVASSLQSSAPKQGP
HHHHHHHHCCCCCCC		33.4930266825
682PhosphorylationVASSLQSSAPKQGPL
HHHHHHHCCCCCCCC		35.3130266825
719PhosphorylationPAEATACTQEAANLF
CCHHHHHCHHHHHHC		27.2923898821
729PhosphorylationAANLFPMSHNVLYMR
HHHHCCCCCHHHEEH		16.4923898821
745PhosphorylationQIAELRGSMDEARRW
HHHHHCCCHHHHHHH		19.3423898821
753PhosphorylationMDEARRWYEEALAIS
HHHHHHHHHHHHCCC		11.3329978859
760PhosphorylationYEEALAISPTHVKSM
HHHHHCCCHHHHHHH		20.3829978859
762PhosphorylationEALAISPTHVKSMQR
HHHCCCHHHHHHHHH		32.2929978859
766PhosphorylationISPTHVKSMQRLALI
CCHHHHHHHHHHHHH		21.0429978859
780PhosphorylationILHQLGRYSLAEKIL
HHHHHCCHHHHHHHH		13.26-
781PhosphorylationLHQLGRYSLAEKILR
HHHHCCHHHHHHHHH		21.53-
785UbiquitinationGRYSLAEKILRDAVQ
CCHHHHHHHHHHHHH		41.242189047
785 (in isoform 1)Ubiquitination-41.2421890473
802 (in isoform 2)Ubiquitination-40.7721890473
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 TTC7B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTC7B_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 TTC7B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TTC7B_HUMAN !!
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 TTC7B_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-673, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-678, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND MASSSPECTROMETRY.

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