AHI1_HUMAN - dbPTM
AHI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AHI1_HUMAN
UniProt AC Q8N157
Protein Name Jouberin
Gene Name AHI1
Organism Homo sapiens (Human).
Sequence Length 1196
Subcellular Localization Cytoplasm, cytoskeleton, cilium basal body . Cell junction, adherens junction . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole .
Protein Description Involved in vesicle trafficking and required for ciliogenesis, formation of primary non-motile cilium, and recruitment of RAB8A to the basal body of primary cilium. Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in neuronal differentiation. As a positive modulator of classical Wnt signaling, may play a crucial role in ciliary signaling during cerebellum embryonic development. [PubMed: 21623382]
Protein Sequence MPTAESEAKVKTKVRFEELLKTHSDLMREKKKLKKKLVRSEENISPDTIRSNLHYMKETTSDDPDTIRSNLPHIKETTSDDVSAANTNNLKKSTRVTKNKLRNTQLATENPNGDASVEEDKQGKPNKKVIKTVPQLTTQDLKPETPENKVDSTHQKTHTKPQPGVDHQKSEKANEGREETDLEEDEELMQAYQCHVTEEMAKEIKRKIRKKLKEQLTYFPSDTLFHDDKLSSEKRKKKKEVPVFSKAETSTLTISGDTVEGEQKKESSVRSVSSDSHQDDEISSMEQSTEDSMQDDTKPKPKKTKKKTKAVADNNEDVDGDGVHEITSRDSPVYPKCLLDDDLVLGVYIHRTDRLKSDFMISHPMVKIHVVDEHTGQYVKKDDSGRPVSSYYEKENVDYILPIMTQPYDFKQLKSRLPEWEEQIVFNENFPYLLRGSDESPKVILFFEILDFLSVDEIKNNSEVQNQECGFRKIAWAFLKLLGANGNANINSKLRLQLYYPPTKPRSPLSVVEAFEWWSKCPRNHYPSTLYVTVRGLKVPDCIKPSYRSMMALQEEKGKPVHCERHHESSSVDTEPGLEESKEVIKWKRLPGQACRIPNKHLFSLNAGERGCFCLDFSHNGRILAAACASRDGYPIILYEIPSGRFMRELCGHLNIIYDLSWSKDDHYILTSSSDGTARIWKNEINNTNTFRVLPHPSFVYTAKFHPAVRELVVTGCYDSMIRIWKVEMREDSAILVRQFDVHKSFINSLCFDTEGHHMYSGDCTGVIVVWNTYVKINDLEHSVHHWTINKEIKETEFKGIPISYLEIHPNGKRLLIHTKDSTLRIMDLRILVARKFVGAANYREKIHSTLTPCGTFLFAGSEDGIVYVWNPETGEQVAMYSDLPFKSPIRDISYHPFENMVAFCAFGQNEPILLYIYDFHVAQQEAEMFKRYNGTFPLPGIHQSQDALCTCPKLPHQGSFQIDEFVHTESSSTKMQLVKQRLETVTEVIRSCAAKVNKNLSFTSPPAVSSQQSKLKQSNMLTAQEILHQFGFTQTGIISIERKPCNHQVDTAPTVVALYDYTANRSDELTIHRGDIIRVFFKDNEDWWYGSIGKGQEGYFPANHVASETLYQELPPEIKERSPPLSPEEKTKIEKSPAPQKQSINKNKSQDFRLGSESMTHSEMRKEQSHEDQGHIMDTRMRKNKQAGRKVTLIE
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
45PhosphorylationVRSEENISPDTIRSN
HHCCCCCCHHHHHHH		28.4521815630
48PhosphorylationEENISPDTIRSNLHY
CCCCCHHHHHHHHHH		22.9823186163
60PhosphorylationLHYMKETTSDDPDTI
HHHHHHCCCCCHHHH		31.1122210691
77PhosphorylationNLPHIKETTSDDVSA
CCCCCCCCCCCCCHH		26.9725404012
78PhosphorylationLPHIKETTSDDVSAA
CCCCCCCCCCCCHHH		31.1125404012
79PhosphorylationPHIKETTSDDVSAAN
CCCCCCCCCCCHHHC		38.9525404012
145PhosphorylationTQDLKPETPENKVDS
CCCCCCCCCCCCCCC		44.4228985074
152PhosphorylationTPENKVDSTHQKTHT
CCCCCCCCCCCCCCC		30.6727135362
153PhosphorylationPENKVDSTHQKTHTK
CCCCCCCCCCCCCCC		24.7027135362
180PhosphorylationANEGREETDLEEDEE
HHCCCCCCCHHHHHH		40.92115773
192PhosphorylationDEELMQAYQCHVTEE
HHHHHHHHHHHCHHH		8.5227642862
213UbiquitinationRKIRKKLKEQLTYFP
HHHHHHHHHHHHCCC		52.90-
229UbiquitinationDTLFHDDKLSSEKRK
CCCCCCCCCCHHHHH		57.22-
231PhosphorylationLFHDDKLSSEKRKKK
CCCCCCCCHHHHHCC		42.0425627689
232PhosphorylationFHDDKLSSEKRKKKK
CCCCCCCHHHHHCCC		58.5325627689
245PhosphorylationKKEVPVFSKAETSTL
CCCCCCEEECCCEEE		31.0624702127
250PhosphorylationVFSKAETSTLTISGD
CEEECCCEEEEEECC		16.9628555341
258PhosphorylationTLTISGDTVEGEQKK
EEEEECCCCCCCCCC		24.7968723363
271PhosphorylationKKESSVRSVSSDSHQ
CCCCCCCCCCCCCCC		24.9722210691
273PhosphorylationESSVRSVSSDSHQDD
CCCCCCCCCCCCCCH		29.6722210691
274PhosphorylationSSVRSVSSDSHQDDE
CCCCCCCCCCCCCHH		40.7629449344
276PhosphorylationVRSVSSDSHQDDEIS
CCCCCCCCCCCHHHH		25.6229449344
283PhosphorylationSHQDDEISSMEQSTE
CCCCHHHHCCHHHHH		22.9129449344
284PhosphorylationHQDDEISSMEQSTED
CCCHHHHCCHHHHHH		31.8129449344
309UbiquitinationKKTKKKTKAVADNNE
CCCCCCCCCCCCCCC		50.14-
327PhosphorylationGDGVHEITSRDSPVY
CCCCEECCCCCCCCC		18.0927966365
328PhosphorylationDGVHEITSRDSPVYP
CCCEECCCCCCCCCC		39.4925159151
331PhosphorylationHEITSRDSPVYPKCL
EECCCCCCCCCCHHC		18.3721815630
334PhosphorylationTSRDSPVYPKCLLDD
CCCCCCCCCHHCCCC		10.6023186163
380UbiquitinationEHTGQYVKKDDSGRP
CCCCCEEECCCCCCC		45.62-
381UbiquitinationHTGQYVKKDDSGRPV
CCCCEEECCCCCCCC		57.64-
394UbiquitinationPVSSYYEKENVDYIL
CCCCCEEECCCCEEE		38.17-
411UbiquitinationMTQPYDFKQLKSRLP
CCCCCCHHHHHHCCC		52.39-
503PhosphorylationLQLYYPPTKPRSPLS
EEEECCCCCCCCCCC		49.5346160661
507PhosphorylationYPPTKPRSPLSVVEA
CCCCCCCCCCCHHHH		38.4346160655
531PhosphorylationNHYPSTLYVTVRGLK
CCCCCEEEEEECCCC		8.317319647
538UbiquitinationYVTVRGLKVPDCIKP
EEEECCCCCCCCCCH		55.32-
544UbiquitinationLKVPDCIKPSYRSMM
CCCCCCCCHHHHHHH		33.95-
557UbiquitinationMMALQEEKGKPVHCE
HHHHHHHCCCCCCCH		72.05-
582UbiquitinationEPGLEESKEVIKWKR
CCCHHHHHHHHCHHC		60.32-
582AcetylationEPGLEESKEVIKWKR
CCCHHHHHHHHCHHC		60.327468615
588AcetylationSKEVIKWKRLPGQAC
HHHHHCHHCCCCCCC		38.777468625
643PhosphorylationIILYEIPSGRFMREL
EEEEECCCCHHHHHH		48.5426074081
658PhosphorylationCGHLNIIYDLSWSKD
HCCCEEEEEECCCCC		13.6626074081
661PhosphorylationLNIIYDLSWSKDDHY
CEEEEEECCCCCCCE		26.8026074081
663PhosphorylationIIYDLSWSKDDHYIL
EEEEECCCCCCCEEE		23.8826074081
682UbiquitinationDGTARIWKNEINNTN
CCCEEEEECCCCCCC		42.19-
733PhosphorylationKVEMREDSAILVRQF
EEEECCCCEEEEEEE		16.6850564091
791UbiquitinationVHHWTINKEIKETEF
EEEEEECHHHHCCEE		57.89-
799UbiquitinationEIKETEFKGIPISYL
HHHCCEECCCCCEEE		50.10-
804PhosphorylationEFKGIPISYLEIHPN
EECCCCCEEEEECCC		20.5068736233
805PhosphorylationFKGIPISYLEIHPNG
ECCCCCEEEEECCCC		14.7468736239
819PhosphorylationGKRLLIHTKDSTLRI
CCEEEEEECCCCCHH		29.5622617229
822PhosphorylationLLIHTKDSTLRIMDL
EEEEECCCCCHHHHH		30.7822617229
823PhosphorylationLIHTKDSTLRIMDLR
EEEECCCCCHHHHHH		30.1422617229
960PhosphorylationPKLPHQGSFQIDEFV
CCCCCCCCEECEEEE		13.8628348404
975UbiquitinationHTESSSTKMQLVKQR
ECCCCCHHHHHHHHH		26.96-
980UbiquitinationSTKMQLVKQRLETVT
CHHHHHHHHHHHHHH		37.99-
985PhosphorylationLVKQRLETVTEVIRS
HHHHHHHHHHHHHHH		37.0029978859
987PhosphorylationKQRLETVTEVIRSCA
HHHHHHHHHHHHHHH		31.7729978859
992PhosphorylationTVTEVIRSCAAKVNK
HHHHHHHHHHHHCCC		9.2929978859
999UbiquitinationSCAAKVNKNLSFTSP
HHHHHCCCCCCCCCC		63.35-
1002PhosphorylationAKVNKNLSFTSPPAV
HHCCCCCCCCCCCCC		35.5525159151
1004PhosphorylationVNKNLSFTSPPAVSS
CCCCCCCCCCCCCCH		36.6328555341
1005PhosphorylationNKNLSFTSPPAVSSQ
CCCCCCCCCCCCCHH		27.2025159151
1010PhosphorylationFTSPPAVSSQQSKLK
CCCCCCCCHHHHHHH		25.2450564103
1015UbiquitinationAVSSQQSKLKQSNML
CCCHHHHHHHHCCCC		56.20-
1071PhosphorylationANRSDELTIHRGDII
CCCCCCEEEECCCEE		16.8227820677
1095UbiquitinationWWYGSIGKGQEGYFP
CEEEECCCCCCCEEC		56.61-
1112PhosphorylationHVASETLYQELPPEI
HCCCHHHHHHCCHHH		13.8330457727
1120UbiquitinationQELPPEIKERSPPLS
HHCCHHHHHCCCCCC		45.47-
1123PhosphorylationPPEIKERSPPLSPEE
CHHHHHCCCCCCHHH		31.7729255136
1127PhosphorylationKERSPPLSPEEKTKI
HHCCCCCCHHHHCCC		35.7225159151
1142UbiquitinationEKSPAPQKQSINKNK
CCCCCCCCCCCCCCC		44.98-
1144PhosphorylationSPAPQKQSINKNKSQ
CCCCCCCCCCCCCCC		34.8525002506
1150PhosphorylationQSINKNKSQDFRLGS
CCCCCCCCCCCCCCC		44.3681442363
1157PhosphorylationSQDFRLGSESMTHSE
CCCCCCCCCCCCHHH		30.9622260955
1159PhosphorylationDFRLGSESMTHSEMR
CCCCCCCCCCHHHHH		30.5829449344
1161PhosphorylationRLGSESMTHSEMRKE
CCCCCCCCHHHHHHH		31.3729449344
1163PhosphorylationGSESMTHSEMRKEQS
CCCCCCHHHHHHHHC		24.7522260961
1170PhosphorylationSEMRKEQSHEDQGHI
HHHHHHHCHHHHCCH		29.9023403867
1180PhosphorylationDQGHIMDTRMRKNKQ
HHCCHHHHHHHHHHC		14.6923403867
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 AHI1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AHI1_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 AHI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYN2_HUMANDNM2physical
22623184
OFD1_HUMANOFD1physical
26638075
PCM1_HUMANPCM1physical
26638075
DESP_HUMANDSPphysical
26638075
DVL1_HUMANDVL1physical
26638075
ECD_HUMANECDphysical
26638075
HAUS8_HUMANHAUS8physical
26638075
IQCB1_HUMANIQCB1physical
26638075
MK09_HUMANMAPK9physical
26638075
M21D2_HUMANMB21D2physical
26638075
NMT1_HUMANNMT1physical
26638075
PP2AA_HUMANPPP2CAphysical
26638075
2AAA_HUMANPPP2R1Aphysical
26638075
2ABA_HUMANPPP2R2Aphysical
26638075
SIR2_HUMANSIRT2physical
26638075
ADIP_HUMANSSX2IPphysical
26638075
UN45A_HUMANUNC45Aphysical
26638075
CP131_HUMANCEP131physical
26638075
PYR1_HUMANCADphysical
26638075
CC138_HUMANCCDC138physical
26638075
LRC49_HUMANLRRC49physical
26638075
MED4_HUMANMED4physical
26638075
2ABB_HUMANPPP2R2Bphysical
26638075
SRP72_HUMANSRP72physical
26638075
WRP73_HUMANWRAP73physical
26638075
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608629Joubert syndrome 3 (JBTS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AHI1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1123 AND SER-1127, ANDMASS SPECTROMETRY.

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