TTC17_HUMAN - dbPTM
TTC17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTC17_HUMAN
UniProt AC Q96AE7
Protein Name Tetratricopeptide repeat protein 17
Gene Name TTC17
Organism Homo sapiens (Human).
Sequence Length 1141
Subcellular Localization Cytoplasm . Cell membrane . Cytoplasm, cytoskeleton . Colocalized with CATIP at F-actin rich zones and at dynamic plasma membrane protrusions.
Protein Description Plays a role in primary ciliogenesis by modulating actin polymerization..
Protein Sequence MAAAVGVRGRYELPPCSGPGWLLSLSALLSVAARGAFATTHWVVTEDGKIQQQVDSPMNLKHPHDLVILMRQEATVNYLKELEKQLVAQKIHIEENEDRDTGLEQRHNKEDPDCIKAKVPLGDLDLYDGTYITLESKDISPEDYIDTESPVPPDPEQPDCTKILELPYSIHAFQHLRGVQERVNLSAPLLPKEDPIFTYLSKRLGRSIDDIGHLIHEGLQKNTSSWVLYNMASFYWRIKNEPYQVVECAMRALHFSSRHNKDIALVNLANVLHRAHFSADAAVVVHAALDDSDFFTSYYTLGNIYAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKLIQEEQILRNIIHETQMAKEAQLGNHQICRLVNQQHSLHCQWDQPVRYHRGDIFENVDYVQFGEDSSTSSMMSVNFDVQSNQSDINDSVKSSPVAHSILWIWGRDSDAYRDKQHILWPKRADCTESYPRVPVGGELPTYFLPPENKGLRIHELSSDDYSTEEEAQTPDCSITDFRKSHTLSYLVKELEVRMDLKAKMPDDHARKILLSRINNYTIPEEEIGSFLFHAINKPNAPIWLILNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQDVPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSLKLIRCMQFYPFLYNITSSVCSGTVVEESNGSDEMENSDETKMSEEILALVDEFQQAWPLEGFGGALEMKGRRLDLQGIRVLKKGPQDGVARSSCYGDCRSEDDEATEWITFQVKRVKKPKGDHKKTPGKKVETGQIENGHRYQANLEITGPKVASPGPQGKKRDYQRLGWPSPDECLKLRWVELTAIVSTWLAVSSKNIDITEHIDFATPIQQPAMEPLCNGNLPTSMHTLDHLHGVSNRASLHYTGESQLTEVLQNLGKDQYPQQSLEQIGTRIAKVLEKNQTSWVLSSMAALYWRVKGQGKKAIDCLRQALHYAPHQMKDVPLISLANILHNAKLWNDAVIVATMAVEIAPHFAVNHFTLGNVYVAMEEFEKALVWYESTLKLQPEFVPAKNRIQTIQCHLMLKKGRRSP
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
56PhosphorylationKIQQQVDSPMNLKHP
CEEEECCCCCCCCCH		27.4825159151
75PhosphorylationILMRQEATVNYLKEL
EEECCHHHHHHHHHH		14.4528842319
80UbiquitinationEATVNYLKELEKQLV
HHHHHHHHHHHHHHH		50.31-
80UbiquitinationEATVNYLKELEKQLV
HHHHHHHHHHHHHHH		50.31-
84UbiquitinationNYLKELEKQLVAQKI
HHHHHHHHHHHHHCC		62.65-
90UbiquitinationEKQLVAQKIHIEENE
HHHHHHHCCCCCCCC		26.89-
118UbiquitinationDPDCIKAKVPLGDLD
CCCHHEECCCCCCCC		39.11-
162UbiquitinationPEQPDCTKILELPYS
CCCCCCCEEECCCCH		52.18-
202UbiquitinationPIFTYLSKRLGRSID
HHHHHHHHHHCCCHH		49.39-
207PhosphorylationLSKRLGRSIDDIGHL
HHHHHCCCHHHHHHH		28.68-
239UbiquitinationASFYWRIKNEPYQVV
HHHHHHCCCCCHHHH		46.84-
239UbiquitinationASFYWRIKNEPYQVV
HHHHHHCCCCCHHHH		46.84-
335UbiquitinationFEQAIKRKHAVLCQQ
HHHHHHHHHHHHHHH		30.80-
343UbiquitinationHAVLCQQKLEQKLEA
HHHHHHHHHHHHHHH		28.28-
347UbiquitinationCQQKLEQKLEAQHRS
HHHHHHHHHHHHHHH		38.63-
347UbiquitinationCQQKLEQKLEAQHRS
HHHHHHHHHHHHHHH		38.63-
363UbiquitinationQRTLNELKEYQKQHD
HHHHHHHHHHHHHHH		48.47-
367UbiquitinationNELKEYQKQHDHYLR
HHHHHHHHHHHHHHH		49.01-
367UbiquitinationNELKEYQKQHDHYLR
HHHHHHHHHHHHHHH		49.01-
381UbiquitinationRQQEILEKHKLIQEE
HHHHHHHHHCCHHHH		42.46-
383UbiquitinationQEILEKHKLIQEEQI
HHHHHHHCCHHHHHH		59.35-
383UbiquitinationQEILEKHKLIQEEQI
HHHHHHHCCHHHHHH		59.35-
502UbiquitinationKQHILWPKRADCTES
CCCCCCCCCCCCCCC		48.95-
529UbiquitinationYFLPPENKGLRIHEL
EECCCCCCCCCEEEC		58.63-
529UbiquitinationYFLPPENKGLRIHEL
EECCCCCCCCCEEEC		58.6321906983
549PhosphorylationSTEEEAQTPDCSITD
CCHHHHCCCCCCHHH		28.30-
559UbiquitinationCSITDFRKSHTLSYL
CCHHHHHHHHCHHHH		46.73-
560PhosphorylationSITDFRKSHTLSYLV
CHHHHHHHHCHHHHH		19.90-
568UbiquitinationHTLSYLVKELEVRMD
HCHHHHHHHHHHHCC		54.72-
694PhosphorylationSEPLTFLSLGNAYLA
CCCCEEHHCCHHHHH		30.00-
730UbiquitinationPECENSLKLIRCMQF
CCHHHHHHHHHHHHH		41.51-
793 (in isoform 2)Phosphorylation-25.4026091039
801 (in isoform 2)Phosphorylation-41.0222210691
808 (in isoform 2)Phosphorylation-34.2422210691
814 (in isoform 2)Phosphorylation-37.6628985074
823 (in isoform 2)Phosphorylation-4.6722210691
835PhosphorylationRSEDDEATEWITFQV
CCCCCHHCEEEEEEE		29.7927174698
839PhosphorylationDEATEWITFQVKRVK
CHHCEEEEEEEEECC		14.7527174698
859UbiquitinationHKKTPGKKVETGQIE
CCCCCCCCCEECCCC		51.74-
884PhosphorylationITGPKVASPGPQGKK
EECCCCCCCCCCCCC		33.1229396449
941 (in isoform 2)Phosphorylation-44.3925159151
971PhosphorylationHGVSNRASLHYTGES
CCCCCCCEEEECCHH		16.6727080861
974PhosphorylationSNRASLHYTGESQLT
CCCCEEEECCHHHHH		23.0227080861
975PhosphorylationNRASLHYTGESQLTE
CCCEEEECCHHHHHH		24.5927080861
978PhosphorylationSLHYTGESQLTEVLQ
EEEECCHHHHHHHHH		31.6627080861
989UbiquitinationEVLQNLGKDQYPQQS
HHHHHCCCCCCCHHH		44.84-
1006UbiquitinationQIGTRIAKVLEKNQT
HHHHHHHHHHHHCCC		45.01-
1010AcetylationRIAKVLEKNQTSWVL
HHHHHHHHCCCHHHH		50.637934619
1013PhosphorylationKVLEKNQTSWVLSSM
HHHHHCCCHHHHHHH		33.6729759185
1014PhosphorylationVLEKNQTSWVLSSMA
HHHHCCCHHHHHHHH		12.8629759185
1019PhosphorylationQTSWVLSSMAALYWR
CCHHHHHHHHHHHHH		14.3129759185
1024PhosphorylationLSSMAALYWRVKGQG
HHHHHHHHHHHCCCC		6.09-
1032AcetylationWRVKGQGKKAIDCLR
HHHCCCCHHHHHHHH		31.017934629
1108PhosphorylationFEKALVWYESTLKLQ
HHHHHHHHHHCCCCC		7.79-
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 TTC17_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTC17_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 TTC17_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TTC17_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 TTC17_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1014, AND MASSSPECTROMETRY.

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