IF122_HUMAN - dbPTM
IF122_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF122_HUMAN
UniProt AC Q9HBG6
Protein Name Intraflagellar transport protein 122 homolog
Gene Name IFT122
Organism Homo sapiens (Human).
Sequence Length 1241
Subcellular Localization Cytoplasm. Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body. Localizes to photoreceptor connecting cilia..
Protein Description Required for cilia formation during neuronal patterning. Acts as a negative regulator of Shh signaling. Required to recruit TULP3 to primary cilia (By similarity)..
Protein Sequence MRAVLTWRDKAEHCINDIAFKPDGTQLILAAGSRLLVYDTSDGTLLQPLKGHKDTVYCVAYAKDGKRFASGSADKSVIIWTSKLEGILKYTHNDAIQCVSYNPITHQLASCSSSDFGLWSPEQKSVSKHKSSSKIICCSWTNDGQYLALGMFNGIISIRNKNGEEKVKIERPGGSLSPIWSICWNPSSRWESFWMNRENEDAEDVIVNRYIQEIPSTLKSAVYSSQGSEAEEEEPEEEDDSPRDDNLEERNDILAVADWGQKVSFYQLSGKQIGKDRALNFDPCCISYFTKGEYILLGGSDKQVSLFTKDGVRLGTVGEQNSWVWTCQAKPDSNYVVVGCQDGTISFYQLIFSTVHGLYKDRYAYRDSMTDVIVQHLITEQKVRIKCKELVKKIAIYRNRLAIQLPEKILIYELYSEDLSDMHYRVKEKIIKKFECNLLVVCANHIILCQEKRLQCLSFSGVKEREWQMESLIRYIKVIGGPPGREGLLVGLKNGQILKIFVDNLFAIVLLKQATAVRCLDMSASRKKLAVVDENDTCLVYDIDTKELLFQEPNANSVAWNTQCEDMLCFSGGGYLNIKASTFPVHRQKLQGFVVGYNGSKIFCLHVFSISAVEVPQSAPMYQYLDRKLFKEAYQIACLGVTDTDWRELAMEALEGLDFETAKKAFIRVQDLRYLELISSIEERKKRGETNNDLFLADVFSYQGKFHEAAKLYKRSGHENLALEMYTDLCMFEYAKDFLGSGDPKETKMLITKQADWARNIKEPKAAVEMYISAGEHVKAIEICGDHGWVDMLIDIARKLDKAEREPLLLCATYLKKLDSPGYAAETYLKMGDLKSLVQLHVETQRWDEAFALGEKHPEFKDDIYMPYAQWLAENDRFEEAQKAFHKAGRQREAVQVLEQLTNNAVAESRFNDAAYYYWMLSMQCLDIAQDPAQKDTMLGKFYHFQRLAELYHGYHAIHRHTEDPFSVHRPETLFNISRFLLHSLPKDTPSGISKVKILFTLAKQSKALGAYRLARHAYDKLRGLYIPARFQKSIELGTLTIRAKPFHDSEELVPLCYRCSTNNPLLNNLGNVCINCRQPFIFSASSYDVLHLVEFYLEEGITDEEAISLIDLEVLRPKRDDRQLEIANNSSQILRLVETKDSIGDEDPFTAKLSFEQGGSEFVPVVVSRLVLRSMSRRDVLIKRWPPPLRWQYFRSLLPDASITMCPSCFQMFHSEDYELLVLQHGCCPYCRRCKDDPGP
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
10UbiquitinationAVLTWRDKAEHCIND
CEEEEHHHHHHHHCE
47.29-
10UbiquitinationAVLTWRDKAEHCIND
CEEEEHHHHHHHHCE
47.29-
10 (in isoform 4)Ubiquitination-47.29-
21UbiquitinationCINDIAFKPDGTQLI
HHCEEEECCCCCEEE
32.93-
21UbiquitinationCINDIAFKPDGTQLI
HHCEEEECCCCCEEE
32.93-
21 (in isoform 4)Ubiquitination-32.93-
50UbiquitinationGTLLQPLKGHKDTVY
CCEEECCCCCCCEEE
66.70-
50UbiquitinationGTLLQPLKGHKDTVY
CCEEECCCCCCCEEE
66.7021906983
50 (in isoform 1)Ubiquitination-66.7021890473
50 (in isoform 4)Ubiquitination-66.70-
53UbiquitinationLQPLKGHKDTVYCVA
EECCCCCCCEEEEEE
64.86-
53UbiquitinationLQPLKGHKDTVYCVA
EECCCCCCCEEEEEE
64.86-
53 (in isoform 4)Ubiquitination-64.86-
63UbiquitinationVYCVAYAKDGKRFAS
EEEEEEEECCCEECC
55.10-
63 (in isoform 3)Ubiquitination-55.10-
63 (in isoform 4)Ubiquitination-55.10-
66UbiquitinationVAYAKDGKRFASGSA
EEEEECCCEECCCCC
55.25-
72 (in isoform 4)Ubiquitination-30.69-
75UbiquitinationFASGSADKSVIIWTS
ECCCCCCCEEEEEEC
46.46-
75UbiquitinationFASGSADKSVIIWTS
ECCCCCCCEEEEEEC
46.46-
75 (in isoform 3)Ubiquitination-46.46-
82UbiquitinationKSVIIWTSKLEGILK
CEEEEEECCCCCHHH
21.90-
83UbiquitinationSVIIWTSKLEGILKY
EEEEEECCCCCHHHC
43.09-
83UbiquitinationSVIIWTSKLEGILKY
EEEEEECCCCCHHHC
43.09-
83 (in isoform 3)Ubiquitination-43.09-
116 (in isoform 4)Ubiquitination-10.53-
121UbiquitinationSDFGLWSPEQKSVSK
CCCCCCCHHHHCCCC
36.13-
124UbiquitinationGLWSPEQKSVSKHKS
CCCCHHHHCCCCCCC
51.68-
124 (in isoform 3)Ubiquitination-51.68-
125PhosphorylationLWSPEQKSVSKHKSS
CCCHHHHCCCCCCCC
31.1724275569
131PhosphorylationKSVSKHKSSSKIICC
HCCCCCCCCCCEEEE
39.2924275569
151 (in isoform 4)Ubiquitination-2.16-
156UbiquitinationLGMFNGIISIRNKNG
EEEECCEEEEECCCC
2.72-
160 (in isoform 4)Ubiquitination-40.24-
161AcetylationGIISIRNKNGEEKVK
CEEEEECCCCCCCEE
57.3826210075
165UbiquitinationIRNKNGEEKVKIERP
EECCCCCCCEEEECC
65.63-
180 (in isoform 4)Ubiquitination-5.75-
185UbiquitinationPIWSICWNPSSRWES
CCEEEECCCCHHHHH
23.36-
187PhosphorylationWSICWNPSSRWESFW
EEEECCCCHHHHHHE
29.35-
191 (in isoform 4)Ubiquitination-34.64-
192PhosphorylationNPSSRWESFWMNREN
CCCHHHHHHEECCCC
19.76-
196UbiquitinationRWESFWMNRENEDAE
HHHHHEECCCCCCHH
38.42-
198 (in isoform 4)Ubiquitination-61.03-
203UbiquitinationNRENEDAEDVIVNRY
CCCCCCHHHHHHHHH
66.20-
262UbiquitinationAVADWGQKVSFYQLS
EEECCCCCEEEEECC
35.59-
271UbiquitinationSFYQLSGKQIGKDRA
EEEECCCCCCCCCCC
35.05-
271 (in isoform 4)Ubiquitination-35.05-
276UbiquitinationSGKQIGKDRALNFDP
CCCCCCCCCCCCCCC
35.55-
291UbiquitinationCCISYFTKGEYILLG
CEEEEEECCCEEEEC
39.59-
294PhosphorylationSYFTKGEYILLGGSD
EEEECCCEEEECCCC
12.92-
302UbiquitinationILLGGSDKQVSLFTK
EEECCCCCEEEEEEC
55.05-
309UbiquitinationKQVSLFTKDGVRLGT
CEEEEEECCCEEECC
45.19-
352 (in isoform 4)Ubiquitination-7.33-
357UbiquitinationLIFSTVHGLYKDRYA
HHHHHHHHHHCCCCC
26.77-
366 (in isoform 4)Ubiquitination-22.74-
371UbiquitinationAYRDSMTDVIVQHLI
CHHHHCHHHHHHHHH
21.36-
382UbiquitinationQHLITEQKVRIKCKE
HHHHCCCCHHHHHHH
27.52-
412PhosphorylationLPEKILIYELYSEDL
CCHHEEEEECCCCCC
9.09-
415PhosphorylationKILIYELYSEDLSDM
HEEEEECCCCCCCCC
9.70-
417 (in isoform 4)Ubiquitination-49.79-
421UbiquitinationLYSEDLSDMHYRVKE
CCCCCCCCCHHHHHH
34.86-
422UbiquitinationYSEDLSDMHYRVKEK
CCCCCCCCHHHHHHH
2.41-
424PhosphorylationEDLSDMHYRVKEKII
CCCCCCHHHHHHHHH
15.51-
463UbiquitinationCLSFSGVKEREWQME
HHHCCCCCCCHHHHH
55.36-
468 (in isoform 4)Ubiquitination-22.47-
477UbiquitinationESLIRYIKVIGGPPG
HHHHHHHHHHCCCCC
20.90-
513UbiquitinationFAIVLLKQATAVRCL
HHHHHHHHHHHHHHC
43.8721890473
513UbiquitinationFAIVLLKQATAVRCL
HHHHHHHHHHHHHHC
43.8721906983
520 (in isoform 4)Ubiquitination-4.31-
523PhosphorylationAVRCLDMSASRKKLA
HHHHCCCCCCCCCEE
23.82-
525UbiquitinationRCLDMSASRKKLAVV
HHCCCCCCCCCEEEE
37.01-
525PhosphorylationRCLDMSASRKKLAVV
HHCCCCCCCCCEEEE
37.01-
528UbiquitinationDMSASRKKLAVVDEN
CCCCCCCCEEEECCC
40.34-
544UbiquitinationTCLVYDIDTKELLFQ
CEEEEECCCCCEEEC
49.1521906983
552 (in isoform 4)Ubiquitination-32.94-
553 (in isoform 4)Ubiquitination-34.16-
557UbiquitinationFQEPNANSVAWNTQC
ECCCCCCCCCEECCC
15.7121890473
558UbiquitinationQEPNANSVAWNTQCE
CCCCCCCCCEECCCC
7.79-
581UbiquitinationGYLNIKASTFPVHRQ
CEEEEEEECCCCCHH
26.11-
587UbiquitinationASTFPVHRQKLQGFV
EECCCCCHHHCCEEE
35.25-
594 (in isoform 4)Ubiquitination-4.11-
600 (in isoform 4)Ubiquitination-20.95-
603UbiquitinationGYNGSKIFCLHVFSI
EECCCEEEEEEEEEE
4.1021890473
603UbiquitinationGYNGSKIFCLHVFSI
EECCCEEEEEEEEEE
4.1021906983
621UbiquitinationEVPQSAPMYQYLDRK
ECCCCCCHHHHHCHH
3.05-
621UbiquitinationEVPQSAPMYQYLDRK
ECCCCCCHHHHHCHH
3.0521906983
624UbiquitinationQSAPMYQYLDRKLFK
CCCCHHHHHCHHHHH
7.96-
624PhosphorylationQSAPMYQYLDRKLFK
CCCCHHHHHCHHHHH
7.96-
629UbiquitinationYQYLDRKLFKEAYQI
HHHHCHHHHHHHHHH
8.4721890473
631UbiquitinationYLDRKLFKEAYQIAC
HHCHHHHHHHHHHHH
52.45-
634 (in isoform 4)Ubiquitination-11.09-
637 (in isoform 4)Ubiquitination-2.72-
641UbiquitinationYQIACLGVTDTDWRE
HHHHHHCCCCCCHHH
2.56-
642 (in isoform 4)Ubiquitination-31.23-
655UbiquitinationELAMEALEGLDFETA
HHHHHHHCCCCHHHH
65.83-
663UbiquitinationGLDFETAKKAFIRVQ
CCCHHHHHHHEEEHH
52.6421906983
663 (in isoform 1)Ubiquitination-52.6421890473
674PhosphorylationIRVQDLRYLELISSI
EEHHHHHHHHHHHHH
16.3021712546
679PhosphorylationLRYLELISSIEERKK
HHHHHHHHHHHHHHH
37.5821712546
680UbiquitinationRYLELISSIEERKKR
HHHHHHHHHHHHHHH
27.3321890473
680UbiquitinationRYLELISSIEERKKR
HHHHHHHHHHHHHHH
27.3321906983
686UbiquitinationSSIEERKKRGETNND
HHHHHHHHHCCCCCC
72.38-
693UbiquitinationKRGETNNDLFLADVF
HHCCCCCCCCHHHHH
40.65-
705UbiquitinationDVFSYQGKFHEAAKL
HHHHHCCCHHHHHHH
28.20-
706UbiquitinationVFSYQGKFHEAAKLY
HHHHCCCHHHHHHHH
8.8921890473
706 (in isoform 4)Ubiquitination-8.89-
711UbiquitinationGKFHEAAKLYKRSGH
CCHHHHHHHHHHCCC
60.44-
711UbiquitinationGKFHEAAKLYKRSGH
CCHHHHHHHHHHCCC
60.44-
719 (in isoform 4)Ubiquitination-58.42-
745UbiquitinationFLGSGDPKETKMLIT
HHCCCCHHHHEEEEH
80.77-
748UbiquitinationSGDPKETKMLITKQA
CCCHHHHEEEEHHHH
32.57-
753UbiquitinationETKMLITKQADWARN
HHEEEEHHHHHHHHH
36.1721906983
753 (in isoform 1)Ubiquitination-36.1721890473
762UbiquitinationADWARNIKEPKAAVE
HHHHHHCCCCHHHHE
72.08-
765UbiquitinationARNIKEPKAAVEMYI
HHHCCCCHHHHEEHH
50.50-
776 (in isoform 4)Ubiquitination-45.27-
816UbiquitinationLLCATYLKKLDSPGY
HHHHHHHHHCCCCCC
40.66-
817UbiquitinationLCATYLKKLDSPGYA
HHHHHHHHCCCCCCC
55.73-
830UbiquitinationYAAETYLKMGDLKSL
CCHHHHHCCCCHHHH
30.3521906983
830 (in isoform 1)Ubiquitination-30.3521890473
835UbiquitinationYLKMGDLKSLVQLHV
HHCCCCHHHHHHHHH
46.62-
846UbiquitinationQLHVETQRWDEAFAL
HHHHHHCCHHHHHHH
50.67-
856UbiquitinationEAFALGEKHPEFKDD
HHHHHCCCCCCCCCC
63.76-
861UbiquitinationGEKHPEFKDDIYMPY
CCCCCCCCCCCCHHH
53.48-
864UbiquitinationHPEFKDDIYMPYAQW
CCCCCCCCCHHHHHH
4.56-
872UbiquitinationYMPYAQWLAENDRFE
CHHHHHHHHHCCCHH
2.59-
874UbiquitinationPYAQWLAENDRFEEA
HHHHHHHHCCCHHHH
58.45-
877 (in isoform 4)Ubiquitination-53.08-
881UbiquitinationENDRFEEAQKAFHKA
HCCCHHHHHHHHHHH
14.69-
883UbiquitinationDRFEEAQKAFHKAGR
CCHHHHHHHHHHHHH
61.13-
884UbiquitinationRFEEAQKAFHKAGRQ
CHHHHHHHHHHHHHH
10.33-
885 (in isoform 4)Ubiquitination-8.60-
887 (in isoform 4)Ubiquitination-46.19-
894 (in isoform 4)Ubiquitination-10.14-
897 (in isoform 4)Ubiquitination-5.23-
898UbiquitinationQREAVQVLEQLTNNA
HHHHHHHHHHHHCCH
1.62-
910UbiquitinationNNAVAESRFNDAAYY
CCHHHHHHHCHHHHH
26.37-
911AcetylationNAVAESRFNDAAYYY
CHHHHHHHCHHHHHH
15.7119608861
911 (in isoform 4)Ubiquitination-15.71-
922UbiquitinationAYYYWMLSMQCLDIA
HHHHHHHHHHHHHHH
7.24-
923UbiquitinationYYYWMLSMQCLDIAQ
HHHHHHHHHHHHHHC
2.6221890473
923UbiquitinationYYYWMLSMQCLDIAQ
HHHHHHHHHHHHHHC
2.6221890473
923 (in isoform 4)Ubiquitination-2.62-
935 (in isoform 4)Ubiquitination-58.22-
962AcetylationYHAIHRHTEDPFSVH
CCHHCCCCCCCCCCC
41.8819608861
974UbiquitinationSVHRPETLFNISRFL
CCCCHHHHHHHHHHH
2.7021890473
974 (in isoform 3)Ubiquitination-2.70-
974UbiquitinationSVHRPETLFNISRFL
CCCCHHHHHHHHHHH
2.7021890473
987UbiquitinationFLLHSLPKDTPSGIS
HHHHCCCCCCCCCCH
78.50-
991UbiquitinationSLPKDTPSGISKVKI
CCCCCCCCCCHHHHH
51.3421890473
995UbiquitinationDTPSGISKVKILFTL
CCCCCCHHHHHHHHH
45.70-
997UbiquitinationPSGISKVKILFTLAK
CCCCHHHHHHHHHHH
37.11-
1001PhosphorylationSKVKILFTLAKQSKA
HHHHHHHHHHHHHHH
23.51-
1003UbiquitinationVKILFTLAKQSKALG
HHHHHHHHHHHHHHH
12.5621890473
1004UbiquitinationKILFTLAKQSKALGA
HHHHHHHHHHHHHHH
59.21-
1006PhosphorylationLFTLAKQSKALGAYR
HHHHHHHHHHHHHHH
21.13-
1007UbiquitinationFTLAKQSKALGAYRL
HHHHHHHHHHHHHHH
45.17-
1014AcetylationKALGAYRLARHAYDK
HHHHHHHHHHHHHHH
2.9819608861
1018UbiquitinationAYRLARHAYDKLRGL
HHHHHHHHHHHHCCC
14.5221890473
1021AcetylationLARHAYDKLRGLYIP
HHHHHHHHHCCCCCC
27.6619608861
1021UbiquitinationLARHAYDKLRGLYIP
HHHHHHHHHCCCCCC
27.6619608861
1030UbiquitinationRGLYIPARFQKSIEL
CCCCCCHHHHCCEEE
29.2221890473
1031 (in isoform 4)Ubiquitination-13.41-
1033UbiquitinationYIPARFQKSIELGTL
CCCHHHHCCEEECEE
51.1721890473
1033 (in isoform 1)Ubiquitination-51.1721890473
1034UbiquitinationIPARFQKSIELGTLT
CCHHHHCCEEECEEE
15.5421890473
1045UbiquitinationGTLTIRAKPFHDSEE
CEEEEEEEECCCCHH
38.07-
1061UbiquitinationVPLCYRCSTNNPLLN
HHCHHHHCCCCCHHC
25.77-
1072AcetylationPLLNNLGNVCINCRQ
CHHCCCCCEECCCCC
28.7519608861
1074 (in isoform 4)Ubiquitination-1.83-
1084UbiquitinationCRQPFIFSASSYDVL
CCCCEEEECCHHHHH
23.5621890473
1131PhosphorylationQLEIANNSSQILRLV
CEEECCCHHHHHHHE
24.3528555341
1132PhosphorylationLEIANNSSQILRLVE
EEECCCHHHHHHHEE
24.3028555341
1141UbiquitinationILRLVETKDSIGDED
HHHHEECCCCCCCCC
35.6521906983
1141 (in isoform 1)Ubiquitination-35.6521890473
1142 (in isoform 2)Ubiquitination-53.56-
1143PhosphorylationRLVETKDSIGDEDPF
HHEECCCCCCCCCCC
29.9927251275
1153UbiquitinationDEDPFTAKLSFEQGG
CCCCCEEEEEECCCC
41.422190698
1153 (in isoform 1)Ubiquitination-41.4221890473
1154 (in isoform 2)Ubiquitination-7.04-
1155PhosphorylationDPFTAKLSFEQGGSE
CCCEEEEEECCCCCC
26.4828348404
1175PhosphorylationVSRLVLRSMSRRDVL
HHHHHHHHCCCCCCH
19.5624043423
1177PhosphorylationRLVLRSMSRRDVLIK
HHHHHHCCCCCCHHH
25.9624043423
1184UbiquitinationSRRDVLIKRWPPPLR
CCCCCHHHCCCCCCH
44.22-
1194PhosphorylationPPPLRWQYFRSLLPD
CCCCHHHHHHHHCCC
8.2627251275

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 IF122_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF122_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 IF122_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF140_HUMANIFT140physical
26186194
WDR35_HUMANWDR35physical
26186194
CAB45_HUMANSDF4physical
26186194
WDR19_HUMANWDR19physical
26186194
IFT43_HUMANIFT43physical
26186194
PIHD1_HUMANPIH1D1physical
26186194
WDR35_HUMANWDR35physical
28514442
WDR19_HUMANWDR19physical
28514442
IF140_HUMANIFT140physical
28514442
DNJC7_HUMANDNAJC7physical
28514442
IFT43_HUMANIFT43physical
27173435
WDR35_HUMANWDR35physical
27173435
TT21B_HUMANTTC21Bphysical
27173435
PFKAP_HUMANPFKPphysical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
218330Cranioectodermal dysplasia 1 (CED1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF122_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1021, AND MASS SPECTROMETRY.

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