TTC7A_HUMAN - dbPTM
TTC7A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTC7A_HUMAN
UniProt AC Q9ULT0
Protein Name Tetratricopeptide repeat protein 7A {ECO:0000305}
Gene Name TTC7A {ECO:0000312|HGNC:HGNC:19750}
Organism Homo sapiens (Human).
Sequence Length 858
Subcellular Localization Cytoplasm . Cell membrane . Localizes to the cytosol and is recruited to the plasma membrane following interaction with EFR3 (EFR3A or EFR3B).
Protein Description Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. [PubMed: 23229899]
Protein Sequence MAAKGAHGSYLKVESELERCRAEGHWDRMPELVRQLQTLSMPGGGGNRRGSPSAAFTFPDTDDFGKLLLAEALLEQCLKENHAKIKDSMPLLEKNEPKMSEAKNYLSSILNHGRLSPQYMCEAMLILGKLHYVEGSYRDAISMYARAGIDDMSMENKPLYQMRLLSEAFVIKGLSLERLPNSIASRFRLTEREEEVITCFERASWIAQVFLQELEKTTNNSTSRHLKGCHPLDYELTYFLEAALQSAYVKNLKKGNIVKGMRELREVLRTVETKATQNFKVMAAKHLAGVLLHSLSEECYWSPLSHPLPEFMGKEESSFATQALRKPHLYEGDNLYCPKDNIEEALLLLLISESMATRDVVLSRVPEQEEDRTVSLQNAAAIYDLLSITLGRRGQYVMLSECLERAMKFAFGEFHLWYQVALSMVACGKSAYAVSLLRECVKLRPSDPTVPLMAAKVCIGSLRWLEEAEHFAMMVISLGEEAGEFLPKGYLALGLTYSLQATDATLKSKQDELHRKALQTLERAQQLAPSDPQVILYVSLQLALVRQISSAMEQLQEALKVRKDDAHALHLLALLFSAQKHHQHALDVVNMAITEHPENFNLMFTKVKLEQVLKGPEEALVTCRQVLRLWQTLYSFSQLGGLEKDGSFGEGLTMKKQSGMHLTLPDAHDADSGSRRASSIAASRLEEAMSELTMPSSVLKQGPMQLWTTLEQIWLQAAELFMEQQHLKEAGFCIQEAAGLFPTSHSVLYMRGRLAEVKGNLEEAKQLYKEALTVNPDGVRIMHSLGLMLSRLGHKSLAQKVLRDAVERQSTCHEAWQGLGEVLQAQGQNEAAVDCFLTALELEASSPVLPFSIIPREL
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
4Ubiquitination----MAAKGAHGSYL
----CCCCCCCCCCC		47.28-
4Ubiquitination----MAAKGAHGSYL
----CCCCCCCCCCC		47.28-
9PhosphorylationAAKGAHGSYLKVESE
CCCCCCCCCCCHHHH		19.88-
12UbiquitinationGAHGSYLKVESELER
CCCCCCCCHHHHHHH		35.41-
51PhosphorylationGGGNRRGSPSAAFTF
CCCCCCCCCCCCEEC		17.5529255136
53PhosphorylationGNRRGSPSAAFTFPD
CCCCCCCCCCEECCC		33.6529255136
57PhosphorylationGSPSAAFTFPDTDDF
CCCCCCEECCCCCHH		29.5430266825
61PhosphorylationAAFTFPDTDDFGKLL
CCEECCCCCHHHHHH		37.3923403867
79UbiquitinationALLEQCLKENHAKIK
HHHHHHHHHCCCCHH		65.19-
79UbiquitinationALLEQCLKENHAKIK
HHHHHHHHHCCCCHH		65.19-
84UbiquitinationCLKENHAKIKDSMPL
HHHHCCCCHHCCCCH		42.62-
100PhosphorylationEKNEPKMSEAKNYLS
HCCCCCHHHHHHHHH		40.2924719451
103UbiquitinationEPKMSEAKNYLSSIL
CCCHHHHHHHHHHHH		41.91-
103UbiquitinationEPKMSEAKNYLSSIL
CCCHHHHHHHHHHHH		41.91-
105PhosphorylationKMSEAKNYLSSILNH
CHHHHHHHHHHHHHC		13.7824719451
108PhosphorylationEAKNYLSSILNHGRL
HHHHHHHHHHHCCCC		28.6224719451
116PhosphorylationILNHGRLSPQYMCEA
HHHCCCCCHHHHHHH		14.48-
157UbiquitinationDDMSMENKPLYQMRL
CCCCCCCCCHHHHHH		24.08-
157UbiquitinationDDMSMENKPLYQMRL
CCCCCCCCCHHHHHH		24.08-
160PhosphorylationSMENKPLYQMRLLSE
CCCCCCHHHHHHHHH		14.59-
172 (in isoform 1)Ubiquitination-48.8021890473
172UbiquitinationLSEAFVIKGLSLERL
HHHHHHHCCCCHHHC		48.8021890473
175PhosphorylationAFVIKGLSLERLPNS
HHHHCCCCHHHCCCC		36.5329978859
182PhosphorylationSLERLPNSIASRFRL
CHHHCCCCHHHCCCC		20.0023401153
185PhosphorylationRLPNSIASRFRLTER
HCCCCHHHCCCCCCC		30.2230266825
221PhosphorylationLEKTTNNSTSRHLKG
HHHHCCCCCCCCCCC		29.8124719451
259UbiquitinationLKKGNIVKGMRELRE
CCCCCHHHHHHHHHH		43.10-
259UbiquitinationLKKGNIVKGMRELRE
CCCCCHHHHHHHHHH		43.10-
274UbiquitinationVLRTVETKATQNFKV
HHHHHHCHHCCCHHH		35.61-
280UbiquitinationTKATQNFKVMAAKHL
CHHCCCHHHHHHHHH		38.35-
280UbiquitinationTKATQNFKVMAAKHL
CHHCCCHHHHHHHHH		38.35-
326UbiquitinationFATQALRKPHLYEGD
HHHHHHCCCCCCCCC		37.32-
326UbiquitinationFATQALRKPHLYEGD
HHHHHHCCCCCCCCC		37.32-
389PhosphorylationIYDLLSITLGRRGQY
HHHHHHCCCCCCCCE		21.5624719451
396PhosphorylationTLGRRGQYVMLSECL
CCCCCCCEEEHHHHH		7.22-
400PhosphorylationRGQYVMLSECLERAM
CCCEEEHHHHHHHHH		14.25-
418PhosphorylationFGEFHLWYQVALSMV
HCCHHHHHHHHHHHH		10.2427461979
423PhosphorylationLWYQVALSMVACGKS
HHHHHHHHHHHCCHH		11.0627461979
449PhosphorylationKLRPSDPTVPLMAAK
HCCCCCCCCHHHHHH		39.4817322306
461PhosphorylationAAKVCIGSLRWLEEA
HHHHHHHHHHHHHHH		8.5424719451
505PhosphorylationSLQATDATLKSKQDE
EEHHHCHHHHHHHHH		37.2120068231
516UbiquitinationKQDELHRKALQTLER
HHHHHHHHHHHHHHH		42.58-
516UbiquitinationKQDELHRKALQTLER
HHHHHHHHHHHHHHH		42.58-
560 (in isoform 1)Ubiquitination-47.2221890473
560UbiquitinationEQLQEALKVRKDDAH
HHHHHHHHCCCCHHH		47.2221890473
560UbiquitinationEQLQEALKVRKDDAH
HHHHHHHHCCCCHHH		47.2221906983
647PhosphorylationGGLEKDGSFGEGLTM
CCCCCCCCCCCCCCC		39.9625159151
653PhosphorylationGSFGEGLTMKKQSGM
CCCCCCCCCCCCCCC		37.4923403867
655 (in isoform 1)Ubiquitination-42.2921890473
655UbiquitinationFGEGLTMKKQSGMHL
CCCCCCCCCCCCCEE		42.2921906983
656UbiquitinationGEGLTMKKQSGMHLT
CCCCCCCCCCCCEEE		38.58-
658PhosphorylationGLTMKKQSGMHLTLP
CCCCCCCCCCEEECC		47.1423312004
663PhosphorylationKQSGMHLTLPDAHDA
CCCCCEEECCCCCCC		22.9023312004
672PhosphorylationPDAHDADSGSRRASS
CCCCCCCCCCHHHHH		40.1525849741
674PhosphorylationAHDADSGSRRASSIA
CCCCCCCCHHHHHHH		23.6528857561
678PhosphorylationDSGSRRASSIAASRL
CCCCHHHHHHHHHHH		22.0728985074
679PhosphorylationSGSRRASSIAASRLE
CCCHHHHHHHHHHHH		18.4328985074
679UbiquitinationSGSRRASSIAASRLE
CCCHHHHHHHHHHHH		18.4321890473
680UbiquitinationGSRRASSIAASRLEE
CCHHHHHHHHHHHHH		3.25-
683PhosphorylationRASSIAASRLEEAMS
HHHHHHHHHHHHHHH		28.5123090842
690PhosphorylationSRLEEAMSELTMPSS
HHHHHHHHHCCCCHH		36.1829255136
693PhosphorylationEEAMSELTMPSSVLK
HHHHHHCCCCHHHHH		24.0024292712
696PhosphorylationMSELTMPSSVLKQGP
HHHCCCCHHHHHCCH		23.4329255136
697PhosphorylationSELTMPSSVLKQGPM
HHCCCCHHHHHCCHH		26.1230108239
758UbiquitinationRGRLAEVKGNLEEAK
CHHHHHHCCCHHHHH		33.32-
765UbiquitinationKGNLEEAKQLYKEAL
CCCHHHHHHHHHHHH		44.0821890473
765 (in isoform 1)Ubiquitination-44.0821890473
769UbiquitinationEEAKQLYKEALTVNP
HHHHHHHHHHHCCCC		45.14-
782UbiquitinationNPDGVRIMHSLGLML
CCCHHHHHHHHHHHH		0.92-
784PhosphorylationDGVRIMHSLGLMLSR
CHHHHHHHHHHHHHH		13.5220068231
793UbiquitinationGLMLSRLGHKSLAQK
HHHHHHCCCHHHHHH		25.68-
795UbiquitinationMLSRLGHKSLAQKVL
HHHHCCCHHHHHHHH		45.42-
800UbiquitinationGHKSLAQKVLRDAVE
CCHHHHHHHHHHHHH		37.312189047
800 (in isoform 1)Ubiquitination-37.3121890473
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 TTC7A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTC7A_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 TTC7A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAMKV_HUMANCAMKVphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
243150Gastrointestinal defects and immunodeficiency syndrome (GIDID)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTC7A_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-51, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-182, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-647, 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-51 AND SER-647, AND MASSSPECTROMETRY.

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