IF172_HUMAN - dbPTM
IF172_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF172_HUMAN
UniProt AC Q9UG01
Protein Name Intraflagellar transport protein 172 homolog
Gene Name IFT172
Organism Homo sapiens (Human).
Sequence Length 1749
Subcellular Localization Cell projection, cilium . Localized to the axoneme and around the base of the cilium.
Protein Description Required for the maintenance and formation of cilia. Plays an indirect role in hedgehog (Hh) signaling, cilia being required for all activity of the hedgehog pathway (By similarity)..
Protein Sequence MHLKHLRTLLSPQDGAAKVTCMAWSQNNAKFAVCTVDRVVLLYDEHGERRDKFSTKPADMKYGRKSYMVKGMAFSPDSTKIAIGQTDNIIYVYKIGEDWGDKKVICNKFIQTSAVTCLQWPAEYIIVFGLAEGKVRLANTKTNKSSTIYGTESYVVSLTTNCSGKGILSGHADGTIVRYFFDDEGSGESQGKLVNHPCPPYALAWATNSIVAAGCDRKIVAYGKEGHMLQTFDYSRDPQEREFTTAVSSPGGQSVVLGSYDRLRVFNWIPRRSIWEEAKPKEITNLYTITALAWKRDGSRLCVGTLCGGVEQFDCCLRRSIYKNKFELTYVGPSQVIVKNLSSGTRVVLKSHYGYEVEEVKILGKERYLVAHTSETLLLGDLNTNRLSEIAWQGSGGNEKYFFENENVCMIFNAGELTLVEYGNNDTLGSVRTEFMNPHLISVRINERCQRGTEDNKKLAYLIDIKTIAIVDLIGGYNIGTVSHESRVDWLELNETGHKLLFRDRKLRLHLYDIESCSKTMILNFCSYMQWVPGSDVLVAQNRNSLCVWYNIEAPERVTMFTIRGDVIGLERGGGKTEVMVMEGVTTVAYTLDEGLIEFGTAIDDGNYIRATAFLETLEMTPETEAMWKTLSKLALEARQLHIAERCFSALGQVAKARFLHETNEIADQVSREYGGEGTDFYQVRARLAMLEKNYKLAEMIFLEQNAVEEAMGMYQELHRWDECIAVAEAKGHPALEKLRRSYYQWLMDTQQEERAGELQESQGDGLAAISLYLKAGLPAKAARLVLTREELLANTELVEHITAALIKGELYERAGDLFEKIHNPQKALECYRKGNAFMKAVELARLAFPVEVVKLEEAWGDHLVQQKQLDAAINHYIEARCSIKAIEAALGARQWKKAIYILDLQDRNTASKYYPLVAQHYASLQEYEIAEELYTKGDRTKDAIDMYTQAGRWEQAHKLAMKCMRPEDVSVLYITQAQEMEKQGKYREAERLYVTVQEPDLAITMYKKHKLYDDMIRLVGKHHPDLLSDTHLHLGKELEAEGRLQEAEYHYLEAQEWKATVNMYRASGLWEEAYRVARTQGGANAHKHVAYLWAKSLGGEAAVRLLNKLGLLEAAVDHAADNCSFEFAFELSRLALKHKTPEVHLKYAMFLEDEGKFEEAEAEFIRAGKPKEAVLMFVHNQDWEAAQRVAEAHDPDSVAEVLVGQARGALEEKDFQKAEGLLLRAQRPGLALNYYKEAGLWSDALRICKDYVPSQLEALQEEYEREATKKGARGVEGFVEQARHWEQAGEYSRAVDCYLKVRDSGNSGLAEKCWMKAAELSIKFLPPQRNMEVVLAVGPQLIGIGKHSAAAELYLNLDLVKEAIDAFIEGEEWNKAKRVAKELDPRYEDYVDQHYKEFLKNQGKVDSLVGVDVIAALDLYVEQGQWDKCIETATKQNYKILHKYVALYATHLIREGSSAQALALYVQHGAPANPQNFNIYKRIFTDMVSSPGTNCAEAYHSWADLRDVLFNLCENLVKSSEANSPAHEEFKTMLLIAHYYATRSAAQSVKQLETVAARLSVSLLRHTQLLPVDKAFYEAGIAAKAVGWDNMAFIFLNRFLDLTDAIEEGTLDGLDHSDFQDTDIPFEVPLPAKQHVPEAEREEVRDWVLTVSMDQRLEQVLPRDERGAYEASLVAASTGVRALPCLITGYPILRNKIEFKRPGKAANKDNWNKFLMAIKTSHSPVCQDVLKFISQWCGGLPSTSFSFQ
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
1Acetylation-------MHLKHLRT
-------CCHHHHHH		37.9020388717
4Sumoylation----MHLKHLRTLLS
----CCHHHHHHHCC		42.38-
4Sumoylation----MHLKHLRTLLS
----CCHHHHHHHCC		42.38-
61AcetylationSTKPADMKYGRKSYM
CCCCCCCCCCCEEEE		45.137296989
66PhosphorylationDMKYGRKSYMVKGMA
CCCCCCEEEEEECEE		19.6622210691
67PhosphorylationMKYGRKSYMVKGMAF
CCCCCEEEEEECEEE		14.6822210691
70UbiquitinationGRKSYMVKGMAFSPD
CCEEEEEECEEECCC		26.83-
70UbiquitinationGRKSYMVKGMAFSPD
CCEEEEEECEEECCC		26.83-
91PhosphorylationGQTDNIIYVYKIGED
CCCCCEEEEEEECCC		8.24-
93PhosphorylationTDNIIYVYKIGEDWG
CCCEEEEEEECCCCC		4.66-
102UbiquitinationIGEDWGDKKVICNKF
ECCCCCCCEEEECHH		45.03-
102UbiquitinationIGEDWGDKKVICNKF
ECCCCCCCEEEECHH		45.03-
103UbiquitinationGEDWGDKKVICNKFI
CCCCCCCEEEECHHH		41.39-
146PhosphorylationNTKTNKSSTIYGTES
ECCCCCCCCEECCEE		22.04-
149PhosphorylationTNKSSTIYGTESYVV
CCCCCCEECCEEEEE		20.34-
151PhosphorylationKSSTIYGTESYVVSL
CCCCEECCEEEEEEE		12.56-
222PhosphorylationCDRKIVAYGKEGHML
CCCEEEEECCCCCEE		20.17-
244PhosphorylationDPQEREFTTAVSSPG
CHHHCEEEEEECCCC		14.75-
254PhosphorylationVSSPGGQSVVLGSYD
ECCCCCCEEEEECCC		19.91-
259PhosphorylationGQSVVLGSYDRLRVF
CCEEEEECCCHHEEC		21.50-
260PhosphorylationQSVVLGSYDRLRVFN
CEEEEECCCHHEECC		11.86-
273PhosphorylationFNWIPRRSIWEEAKP
CCCCCCHHHHHHCCC		33.08-
322PhosphorylationCCLRRSIYKNKFELT
HHHHCHHHCCCEEEE		15.12-
361UbiquitinationGYEVEEVKILGKERY
CCEEEEEEEECEEEE		35.18-
384PhosphorylationLLLGDLNTNRLSEIA
EEECCCCCCCCHHEE		29.0723312004
430PhosphorylationGNNDTLGSVRTEFMN
CCCCCCCCCCHHHCC		16.1324719451
457AcetylationQRGTEDNKKLAYLID
HCCCCCCCCEEEEEE		62.5830589453
461PhosphorylationEDNKKLAYLIDIKTI
CCCCCEEEEEECCEE		18.02-
467PhosphorylationAYLIDIKTIAIVDLI
EEEEECCEEEEEECC		18.90-
499UbiquitinationELNETGHKLLFRDRK
ECCCCCCCHHHCCCC		48.5121890473
499 (in isoform 1)Ubiquitination-48.5121890473
499 (in isoform 2)Ubiquitination-48.5121890473
499UbiquitinationELNETGHKLLFRDRK
ECCCCCCCHHHCCCC		48.5121890473
562PhosphorylationPERVTMFTIRGDVIG
CCCEEEEEEECCEEE		10.0324719451
633UbiquitinationAMWKTLSKLALEARQ
HHHHHHHHHHHHHHH		40.67-
656UbiquitinationSALGQVAKARFLHET
HHHHHHHHHHHHHHH		41.04-
672MethylationEIADQVSREYGGEGT
HHHHHHHHHHCCCCC		42.15-
693UbiquitinationARLAMLEKNYKLAEM
HHHHHHHHHHHHHHH		62.71-
731UbiquitinationCIAVAEAKGHPALEK
HHHHHHHCCCHHHHH		49.62-
738UbiquitinationKGHPALEKLRRSYYQ
CCCHHHHHHHHHHHH		48.41-
775UbiquitinationAAISLYLKAGLPAKA
HHHHHHHHCCCCHHH		27.18-
781UbiquitinationLKAGLPAKAARLVLT
HHCCCCHHHHHHHHC		40.41-
808UbiquitinationHITAALIKGELYERA
HHHHHHHHHHHHHHH		47.37-
821UbiquitinationRAGDLFEKIHNPQKA
HHHHHHHHHCCHHHH		41.76-
827UbiquitinationEKIHNPQKALECYRK
HHHCCHHHHHHHHHH		57.08-
855UbiquitinationAFPVEVVKLEEAWGD
CCCEEEEEHHHHHCC		56.19-
868UbiquitinationGDHLVQQKQLDAAIN
CCHHHHHHHHHHHHH		35.42-
898UbiquitinationLGARQWKKAIYILDL
HCCCHHHEEEEEEEC		36.74-
937UbiquitinationIAEELYTKGDRTKDA
HHHHHHHCCCCHHHH		45.30-
942UbiquitinationYTKGDRTKDAIDMYT
HHCCCCHHHHHHHHH		46.16-
959UbiquitinationGRWEQAHKLAMKCMR
CCHHHHHHHHHHHCC		40.74-
1022UbiquitinationDMIRLVGKHHPDLLS
HHHHHHHHCCHHHHC		31.12-
1031PhosphorylationHPDLLSDTHLHLGKE
CHHHHCCCCCCCCCH		23.98-
1037UbiquitinationDTHLHLGKELEAEGR
CCCCCCCCHHHHHCC		66.54-
1088UbiquitinationQGGANAHKHVAYLWA
CCCCCHHHHHHHHHH		37.05-
1214UbiquitinationARGALEEKDFQKAEG
HCHHCHHHHHHHHHH		55.24-
1218 (in isoform 1)Ubiquitination-48.6921890473
1218 (in isoform 2)Ubiquitination-48.6921890473
1218UbiquitinationLEEKDFQKAEGLLLR
CHHHHHHHHHHHHHH		48.692190698
1250UbiquitinationSDALRICKDYVPSQL
HHHHHHHHHHCHHHH		50.12-
1301UbiquitinationRAVDCYLKVRDSGNS
EEEEEEEEECCCCCC		14.56-
1313UbiquitinationGNSGLAEKCWMKAAE
CCCCHHHHHHHHHHH		27.82-
1322PhosphorylationWMKAAELSIKFLPPQ
HHHHHHHHCEECCCC		18.4222673903
1376UbiquitinationIEGEEWNKAKRVAKE
HCCCHHHHHHHHHHH		57.25-
1397UbiquitinationDYVDQHYKEFLKNQG
HHHHHHHHHHHHHCC		39.61-
1401UbiquitinationQHYKEFLKNQGKVDS
HHHHHHHHHCCCCCH		53.17-
1436UbiquitinationKCIETATKQNYKILH
HHHHHHHHHHHHHHH		33.80-
1445PhosphorylationNYKILHKYVALYATH
HHHHHHHHHHHHHHH		4.7217053785
1449PhosphorylationLHKYVALYATHLIRE
HHHHHHHHHHHHHHC		10.3426503514
1482UbiquitinationPQNFNIYKRIFTDMV
CCCCCCHHHHHHHHC		34.91-
1533PhosphorylationPAHEEFKTMLLIAHY
HHHHHHHHHHHHHHH		20.55-
1549PhosphorylationATRSAAQSVKQLETV
HHHHHHHHHHHHHHH		26.93-
1670PhosphorylationPRDERGAYEASLVAA
CCCCCCHHHHHHHHH		18.1725852190
1673PhosphorylationERGAYEASLVAASTG
CCCHHHHHHHHHHCC		16.0725852190
1678PhosphorylationEASLVAASTGVRALP
HHHHHHHHCCCCHHC		18.8930631047
1679PhosphorylationASLVAASTGVRALPC
HHHHHHHCCCCHHCH		34.6625852190
1689PhosphorylationRALPCLITGYPILRN
CHHCHHHHCCHHHCC		20.08-
1691PhosphorylationLPCLITGYPILRNKI
HCHHHHCCHHHCCCE		4.3919413330
1709UbiquitinationRPGKAANKDNWNKFL
CCCCCCCCCCHHHHH		47.95-
1720UbiquitinationNKFLMAIKTSHSPVC
HHHHHHHHCCCCHHH		34.14-
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 IF172_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF172_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 IF172_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LHX3_HUMANLHX3physical
10788441
LHX4_HUMANLHX4physical
10788441
IFT74_HUMANIFT74physical
27173435
IFT46_HUMANIFT46physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615630Short-rib thoracic dysplasia 10 with or without polydactyly (SRTD10)
616394Retinitis pigmentosa 71 (RP71)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF172_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"In vivo identification of sumoylation sites by a signature tag andcysteine-targeted affinity purification.";
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,Eriksson J.E., Sistonen L.;
J. Biol. Chem. 285:19324-19329(2010).
Cited for: SUMOYLATION AT LYS-4, AND ACETYLATION AT MET-1.
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1445, AND MASSSPECTROMETRY.

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