TTC8_HUMAN - dbPTM
TTC8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTC8_HUMAN
UniProt AC Q8TAM2
Protein Name Tetratricopeptide repeat protein 8
Gene Name TTC8
Organism Homo sapiens (Human).
Sequence Length 541
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cell projection, cilium membrane . Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite . Cell projection, cilium .
Protein Description The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization..
Protein Sequence MSSEMEPLLLAWSYFRRRKFQLCADLCTQMLEKSPYDQEPDPELPVHQAAWILKARALTEMVYIDEIDVDQEGIAEMMLDENAIAQVPRPGTSLKLPGTNQTGGPSQAVRPITQAGRPITGFLRPSTQSGRPGTMEQAIRTPRTAYTARPITSSSGRFVRLGTASMLTSPDGPFINLSRLNLTKYSQKPKLAKALFEYIFHHENDVKTIHLEDVVLHLGIYPFLLRNKNHIEKNALDLAALSTEHSQYKDWWWKVQIGKCYYRLGMYREAEKQFKSALKQQEMVDTFLYLAKVYVSLDQPVTALNLFKQGLDKFPGEVTLLCGIARIYEEMNNMSSAAEYYKEVLKQDNTHVEAIACIGSNHFYSDQPEIALRFYRRLLQMGIYNGQLFNNLGLCCFYAQQYDMTLTSFERALSLAENEEEAADVWYNLGHVAVGIGDTNLAHQCFRLALVNNNNHAEAYNNLAVLEMRKGHVEQARALLQTASSLAPHMYEPHFNFATISDKIGDLQRSYVAAQKSEAAFPDHVDTQHLIKQLRQHFAML
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
13PhosphorylationEPLLLAWSYFRRRKF
HHHHHHHHHHHHHHH		14.58-
14PhosphorylationPLLLAWSYFRRRKFQ
HHHHHHHHHHHHHHH		7.15-
44UbiquitinationDQEPDPELPVHQAAW
CCCCCCCCCHHHHHH		6.9821890473
44 (in isoform 1)Ubiquitination-6.9821890473
44 (in isoform 3)Ubiquitination-6.9821890473
44 (in isoform 4)Ubiquitination-6.9821890473
54UbiquitinationHQAAWILKARALTEM
HHHHHHHHHHHHCCE		27.05-
85UbiquitinationMLDENAIAQVPRPGT
HCCCCCEECCCCCCC		11.25-
126PhosphorylationITGFLRPSTQSGRPG
CCEEECCCCCCCCCC		32.4222468782
127PhosphorylationTGFLRPSTQSGRPGT
CEEECCCCCCCCCCC		29.4522468782
129PhosphorylationFLRPSTQSGRPGTME
EECCCCCCCCCCCHH		36.5422468782
134PhosphorylationTQSGRPGTMEQAIRT
CCCCCCCCHHHHCCC		21.88-
144PhosphorylationQAIRTPRTAYTARPI
HHCCCCCCEEECCCC		25.8130576142
146PhosphorylationIRTPRTAYTARPITS
CCCCCCEEECCCCCC		10.5829496907
147PhosphorylationRTPRTAYTARPITSS
CCCCCEEECCCCCCC		17.46-
153PhosphorylationYTARPITSSSGRFVR
EECCCCCCCCCCEEE		24.1930576142
154PhosphorylationTARPITSSSGRFVRL
ECCCCCCCCCCEEEE		28.3224719451
155PhosphorylationARPITSSSGRFVRLG
CCCCCCCCCCEEEEE		33.48-
163 (in isoform 4)Phosphorylation-21.8327251275
163PhosphorylationGRFVRLGTASMLTSP
CCEEEEECCHHHCCC		21.8328857561
165PhosphorylationFVRLGTASMLTSPDG
EEEEECCHHHCCCCC		17.7328348404
174UbiquitinationLTSPDGPFINLSRLN
HCCCCCCCEEHHHCC		7.66-
178 (in isoform 3)Phosphorylation-30.1829888752
184MalonylationLSRLNLTKYSQKPKL
HHHCCCCCCCCCHHH		46.1826320211
184AcetylationLSRLNLTKYSQKPKL
HHHCCCCCCCCCHHH		46.1825953088
184 (in isoform 4)Ubiquitination-46.18-
186 (in isoform 3)Phosphorylation-33.0329888752
187 (in isoform 3)Phosphorylation-64.0829888752
190 (in isoform 3)Phosphorylation-69.0229888752
192 (in isoform 3)Phosphorylation-10.9529888752
208 (in isoform 4)Phosphorylation-17.3029888752
212 (in isoform 2)Ubiquitination-34.3021890473
213 (in isoform 3)Ubiquitination-42.0321890473
216 (in isoform 4)Phosphorylation-2.5129888752
217 (in isoform 4)Phosphorylation-15.4829888752
220 (in isoform 4)Phosphorylation-5.0629888752
222 (in isoform 4)Phosphorylation-16.1029888752
223 (in isoform 3)Ubiquitination-5.87-
223 (in isoform 4)Ubiquitination-5.87-
225 (in isoform 2)Ubiquitination-6.0821890473
233 (in isoform 4)Ubiquitination-47.09-
241 (in isoform 2)Ubiquitination-5.6021890473
242 (in isoform 3)Ubiquitination-27.3321890473
243 (in isoform 4)Ubiquitination-38.2721890473
249UbiquitinationSTEHSQYKDWWWKVQ
CCCCHHHCHHHHHHH		38.96-
252 (in isoform 3)Ubiquitination-8.64-
253 (in isoform 4)Ubiquitination-6.16-
261PhosphorylationKVQIGKCYYRLGMYR
HHHHHHHHHHHHCHH		8.63-
262PhosphorylationVQIGKCYYRLGMYRE
HHHHHHHHHHHCHHH		14.61-
267PhosphorylationCYYRLGMYREAEKQF
HHHHHHCHHHHHHHH		11.96-
269 (in isoform 1)Ubiquitination-43.6321890473
269UbiquitinationYRLGMYREAEKQFKS
HHHHCHHHHHHHHHH		43.63-
272 (in isoform 4)Ubiquitination-68.9921890473
276 (in isoform 3)Ubiquitination-39.8721890473
279UbiquitinationKQFKSALKQQEMVDT
HHHHHHHHHHHHHHH		50.0421906983
286 (in isoform 3)Ubiquitination-12.25-
298UbiquitinationAKVYVSLDQPVTALN
HHHHHCCCCHHHHHH		43.14-
298 (in isoform 1)Ubiquitination-43.1421890473
306 (in isoform 4)Ubiquitination-6.2021890473
308UbiquitinationVTALNLFKQGLDKFP
HHHHHHHHCCHHHCC		46.7721906983
332UbiquitinationARIYEEMNNMSSAAE
HHHHHHHCCCHHHHH		44.31-
332 (in isoform 1)Ubiquitination-44.3121890473
341PhosphorylationMSSAAEYYKEVLKQD
CHHHHHHHHHHHHCC		7.6822468782
342UbiquitinationSSAAEYYKEVLKQDN
HHHHHHHHHHHHCCC		40.2121906983
437 (in isoform 3)Ubiquitination-29.7521890473
450 (in isoform 3)Ubiquitination-5.1221890473
466 (in isoform 3)Ubiquitination-3.3921890473
467 (in isoform 4)Ubiquitination-30.2821890473
477 (in isoform 4)Ubiquitination-26.01-
480 (in isoform 4)Ubiquitination-4.0821890473
490 (in isoform 4)Ubiquitination-3.84-
491PhosphorylationSSLAPHMYEPHFNFA
HHHCHHHCCCCCCEE		24.2327642862
493 (in isoform 1)Ubiquitination-21.6321890473
493UbiquitinationLAPHMYEPHFNFATI
HCHHHCCCCCCEEEH		21.63-
496 (in isoform 4)Ubiquitination-23.7021890473
496UbiquitinationHMYEPHFNFATISDK
HHCCCCCCEEEHHHH		23.7021890473
503UbiquitinationNFATISDKIGDLQRS
CEEEHHHHHHHHHHH		41.6221906983
506 (in isoform 1)Ubiquitination-43.0021890473
506UbiquitinationTISDKIGDLQRSYVA
EHHHHHHHHHHHHHH		43.0021890473
506UbiquitinationTISDKIGDLQRSYVA
EHHHHHHHHHHHHHH		43.0021890473
506 (in isoform 4)Ubiquitination-43.00-
506UbiquitinationTISDKIGDLQRSYVA
EHHHHHHHHHHHHHH		43.00-
516UbiquitinationRSYVAAQKSEAAFPD
HHHHHHHHCHHCCCC		45.6021906983
522 (in isoform 1)Ubiquitination-26.5221890473
522UbiquitinationQKSEAAFPDHVDTQH
HHCHHCCCCCCCHHH		26.52-
532UbiquitinationVDTQHLIKQLRQHFA
CCHHHHHHHHHHHHH		50.032189047
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 TTC8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTC8_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 TTC8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BBS5_HUMANBBS5physical
27173435
PTHB1_HUMANBBS9physical
27173435
BBS4_HUMANBBS4physical
27173435
BBS1_HUMANBBS1physical
27173435
BBS7_HUMANBBS7physical
27173435
BBS2_HUMANBBS2physical
27173435
LZTL1_HUMANLZTFL1physical
27173435
Drug and Disease Associations
Kegg Disease
H00418 Bardet-Biedl syndrome (BBS)
OMIM Disease
613464Retinitis pigmentosa 51 (RP51)
615985Bardet-Biedl syndrome 8 (BBS8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTC8_HUMAN

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Related Literatures of Post-Translational Modification

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