TGRM1_HUMAN - dbPTM
TGRM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGRM1_HUMAN
UniProt AC Q9Y4F4
Protein Name TOG array regulator of axonemal microtubules protein 1 {ECO:0000312|HGNC:HGNC:19959}
Gene Name TOGARAM1 {ECO:0000312|HGNC:HGNC:19959}
Organism Homo sapiens (Human).
Sequence Length 1720
Subcellular Localization Cell projection, cilium . Cytoplasm, cytoskeleton . Detected along the length of primary cilia and at the basal body. Colocalization with the cytoplasmic microtubule cytoskeleton upon heterologous expression is most likely an artifact.
Protein Description Required for normal structure and function of primary cilia. Plays a role in the organization of axoneme microtubule bundles in primary cilia (By similarity). Interacts with microtubules and promotes microtubule polymerization via its HEAT repeat domains, especially those in TOG region 2 and 4 (By similarity)..
Protein Sequence MAAAPSALLLLPPFPVLSTYRLQSRSRPSAPETDDSRVGGIMRGEKNYYFRGAAGDHGSCPTTTSPLASALLMPSEAVSSSWSESGGGLSGGDEEDTRLLQLLRTARDPSEAFQALQAALPRRGGRLGFPRRKEALYRALGRVLVEGGSDEKRLCLQLLSDVLRGQGEAGQLEEAFSLALLPQLVVSLREENPALRKDALQILHICLKRSPGEVLRTLIQQGLESTDARLRASTALLLPILLTTEDLLLGLDLTEVIISLARKLGDQETEEESETAFSALQQIGERLGQDRFQSYISRLPSALRRHYNRRLESQFGSQVPYYLELEASGFPEDPLPCAVTLSNSNLKFGIIPQELHSRLLDQEDYKNRTQAVEELKQVLGKFNPSSTPHSSLVGFISLLYNLLDDSNFKVVHGTLEVLHLLVIRLGEQVQQFLGPVIAASVKVLADNKLVIKQEYMKIFLKLMKEVGPQQVLCLLLEHLKHKHSRVREEVVNICICSLLTYPSEDFDLPKLSFDLAPALVDSKRRVRQAALEAFAVLASSMGSGKTSILFKAVDTVELQDNGDGVMNAVQARLARKTLPRLTEQGFVEYAVLMPSSAGGRSNHLAHGADTDWLLAGNRTQSAHCHCGDHVRDSMHIYGSYSPTICTRRVLSAGKGKNKLPWENEQPGIMGENQTSTSKDIEQFSTYDFIPSAKLKLSQGMPVNDDLCFSRKRVSRNLFQNSRDFNPDCLPLCAAGTTGTHQTNLSGKCAQLGFSQICGKTGSVGSDLQFLGTTSSHQEKVYASLNFGSKTQQTFGSQTECTSSNGQNPSPGAYILPSYPVSSPRTSPKHTSPLIISPKKSQDNSVNFSNSWPLKSFEGLSKPSPQKKLVSQKSSDPTGRNHGENSQEKPPVQLTPALVRSPSSRRGLNGTKPVPPIPRGISLLPDKADLSTVGHKKKEPDDIWKCEKDSLPIDLSELNFKDKDLDQEEMHSSLRSLRNSAAKKRAKLSGSTSDLESPDSAMKLDLTMDSPSLSSSPNINSYSESGVYSQESLTSSLSTTPQGKRIMSDIFPTFGSKPCPTRLSSAKKKISHIAEQSPSAGSSSNPQQISSFDFTTTKALSEDSVVVVGKGVFGSLSSAPATCSQSVISSVENGDTFSIKQSIEPPSGIYGRSVQQNISSYLDVENEKDAKVSISKSTYNKMRQKRKEEKELFHNKDCEKKEKNSWERMRHTGTEKMASESETPTGAISQYKERMPSVTHSPEIMDLSELRPFSKPEIALTEALRLLADEDWEKKIEGLNFIRCLAAFHSEILNTKLHETNFAVVQEVKNLRSGVSRAAVVCLSDLFTYLKKSMDQELDTTVKVLLHKAGESNTFIREDVDKALRAMVNNVTPARAVVSLINGGQRYYGRKMLFFMMCHPNFEKMLEKYVPSKDLPYIKDSVRNLQQKGLGEIPLDTPSAKGRRSHTGSVGNTRSSSVSRDAFNSAERAVTEVREVTRKSVPRNSLESAEYLKLITGLLNAKDFRDRINGIKQLLSDTENNQDLVVGNIVKIFDAFKSRLHDSNSKVNLVALETMHKMIPLLRDHLSPIINMLIPAIVDNNLNSKNPGIYAAATNVVQALSQHVDNYLLLQPFCTKAQFLNGKAKQDMTEKLADIVTELYQRKPHATEQKVLVVLWHLLGNMTNSGSLPGAGGNIRTATAKLSKALFAQMGQNLLNQAASQPPHIKKSLEELLDMTILNEL
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
24PhosphorylationLSTYRLQSRSRPSAP
EEHHCCCCCCCCCCC
30576142
27DimethylationYRLQSRSRPSAPETD
HCCCCCCCCCCCCCC
-
37DimethylationAPETDDSRVGGIMRG
CCCCCCCCCCCCCCC
-
51DimethylationGEKNYYFRGAAGDHG
CCCCEEECCCCCCCC
-
366UbiquitinationLLDQEDYKNRTQAVE
HCCHHHHHHHHHHHH
-
448UbiquitinationVKVLADNKLVIKQEY
HHHHHCCCEEECHHH
-
637PhosphorylationVRDSMHIYGSYSPTI
CCCCCEEECCCCCCC
28348404
639PhosphorylationDSMHIYGSYSPTICT
CCCEEECCCCCCCCC
28348404
640PhosphorylationSMHIYGSYSPTICTR
CCEEECCCCCCCCCH
28348404
641PhosphorylationMHIYGSYSPTICTRR
CEEECCCCCCCCCHH
28348404
691PhosphorylationSTYDFIPSAKLKLSQ
HHCCCCCCCCEEHHC
24719451
693UbiquitinationYDFIPSAKLKLSQGM
CCCCCCCCEEHHCCC
-
709PhosphorylationVNDDLCFSRKRVSRN
CCCHHHHCCHHHHHH
24719451
760PhosphorylationFSQICGKTGSVGSDL
CHHHCCCCCCCCCCC
28857561
762PhosphorylationQICGKTGSVGSDLQF
HHCCCCCCCCCCCEE
25849741
765PhosphorylationGKTGSVGSDLQFLGT
CCCCCCCCCCEECCC
28857561
772PhosphorylationSDLQFLGTTSSHQEK
CCCEECCCCCCCCCE
23186163
773PhosphorylationDLQFLGTTSSHQEKV
CCEECCCCCCCCCEE
23186163
774PhosphorylationLQFLGTTSSHQEKVY
CEECCCCCCCCCEEE
23186163
775PhosphorylationQFLGTTSSHQEKVYA
EECCCCCCCCCEEEE
23186163
836PhosphorylationHTSPLIISPKKSQDN
CCCCEEECCCCCCCC
29255136
840PhosphorylationLIISPKKSQDNSVNF
EEECCCCCCCCCCCC
25954137
844PhosphorylationPKKSQDNSVNFSNSW
CCCCCCCCCCCCCCC
25954137
848PhosphorylationQDNSVNFSNSWPLKS
CCCCCCCCCCCCCCC
28348404
850PhosphorylationNSVNFSNSWPLKSFE
CCCCCCCCCCCCCCC
25954137
873PhosphorylationKKLVSQKSSDPTGRN
HHHCCCCCCCCCCCC
24719451
971PhosphorylationLDQEEMHSSLRSLRN
CCHHHHHHHHHHHHH
27251275
972PhosphorylationDQEEMHSSLRSLRNS
CHHHHHHHHHHHHHH
27251275
988PhosphorylationAKKRAKLSGSTSDLE
HHHHHHHCCCCCCCC
28348404
990PhosphorylationKRAKLSGSTSDLESP
HHHHHCCCCCCCCCC
28348404
991PhosphorylationRAKLSGSTSDLESPD
HHHHCCCCCCCCCCC
21815630
996PhosphorylationGSTSDLESPDSAMKL
CCCCCCCCCCCCCCC
-
1055PhosphorylationDIFPTFGSKPCPTRL
HCCCCCCCCCCCCCC
18187866
1064PhosphorylationPCPTRLSSAKKKISH
CCCCCCHHHHHHHHH
-
1100PhosphorylationFTTTKALSEDSVVVV
CCCCCCCCCCEEEEE
24719451
1103PhosphorylationTKALSEDSVVVVGKG
CCCCCCCEEEEEECC
28348404
1172PhosphorylationNEKDAKVSISKSTYN
CCCCCEEEECHHHHH
29978859
1174PhosphorylationKDAKVSISKSTYNKM
CCCEEEECHHHHHHH
29978859
1176PhosphorylationAKVSISKSTYNKMRQ
CEEEECHHHHHHHHH
29978859
1177PhosphorylationKVSISKSTYNKMRQK
EEEECHHHHHHHHHH
29978859
1178PhosphorylationVSISKSTYNKMRQKR
EEECHHHHHHHHHHH
29978859
1204PhosphorylationCEKKEKNSWERMRHT
HHHHHHCHHHHHHHC
-
1230PhosphorylationPTGAISQYKERMPSV
CCCHHHHHHHHCCCC
22468782
1236PhosphorylationQYKERMPSVTHSPEI
HHHHHCCCCCCCCCC
22468782
1247PhosphorylationSPEIMDLSELRPFSK
CCCCCCHHHCCCCCC
22468782
1289PhosphorylationRCLAAFHSEILNTKL
HHHHHHHHHHHCCCC
-
1294PhosphorylationFHSEILNTKLHETNF
HHHHHHCCCCCCCCC
-
1312PhosphorylationQEVKNLRSGVSRAAV
HHHHHHCCCCCHHHH
-
1315PhosphorylationKNLRSGVSRAAVVCL
HHHCCCCCHHHHHHH
-
1332PhosphorylationLFTYLKKSMDQELDT
HHHHHHHHCCHHHHH
29523821
1339PhosphorylationSMDQELDTTVKVLLH
HCCHHHHHHHHHHHH
29523821
1340PhosphorylationMDQELDTTVKVLLHK
CCHHHHHHHHHHHHH
29523821
1351PhosphorylationLLHKAGESNTFIRED
HHHHCCCCCCEEHHH
28355574
1353PhosphorylationHKAGESNTFIREDVD
HHCCCCCCEEHHHHH
28355574
1403AcetylationMCHPNFEKMLEKYVP
HHCCCHHHHHHHHCC
30588677
1436PhosphorylationLGEIPLDTPSAKGRR
CCCCCCCCCCCCCCC
28348404
1438PhosphorylationEIPLDTPSAKGRRSH
CCCCCCCCCCCCCCC
29759185
1448PhosphorylationGRRSHTGSVGNTRSS
CCCCCCCCCCCCCCC
29449344
1452PhosphorylationHTGSVGNTRSSSVSR
CCCCCCCCCCCCCCH
29449344
1454PhosphorylationGSVGNTRSSSVSRDA
CCCCCCCCCCCCHHH
29449344
1455PhosphorylationSVGNTRSSSVSRDAF
CCCCCCCCCCCHHHH
29449344
1456PhosphorylationVGNTRSSSVSRDAFN
CCCCCCCCCCHHHHH
29449344
1458PhosphorylationNTRSSSVSRDAFNSA
CCCCCCCCHHHHHHH
29449344
1464PhosphorylationVSRDAFNSAERAVTE
CCHHHHHHHHHHHHH
-
1476PhosphorylationVTEVREVTRKSVPRN
HHHHHHHHHCCCCCC
-
1479PhosphorylationVREVTRKSVPRNSLE
HHHHHHCCCCCCCHH
24719451
1490PhosphorylationNSLESAEYLKLITGL
CCHHHHHHHHHHHHH
24719451
1639PhosphorylationADIVTELYQRKPHAT
HHHHHHHHHCCCCCC
29083192
1646PhosphorylationYQRKPHATEQKVLVV
HHCCCCCCHHHHHHH
29083192
1699PhosphorylationNLLNQAASQPPHIKK
HHHHHHHHCCCCHHH
-

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 TGRM1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGRM1_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 TGRM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TGRM1_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TGRM1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP