INVS_HUMAN - dbPTM
INVS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INVS_HUMAN
UniProt AC Q9Y283
Protein Name Inversin
Gene Name INVS
Organism Homo sapiens (Human).
Sequence Length 1065
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Membrane
Peripheral membrane protein. Nucleus. Cell projection, cilium . Associates with several components of the cytoskeleton including ciliary, random and polarized microtubule
Protein Description Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin-proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling. Involved in the organization of apical junctions in kidney cells together with NPHP1, NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity)..
Protein Sequence MNKSENLLFAGSSLASQVHAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSQRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLTTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYNNPEHVKLLIKHDSNIGIPDVEGKIPLHWAANHKDPSAVHTVRCILDAAPTESLLNWQDYEGRTPLHFAVADGNVTVVDVLTSYESCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTIPSDSQGATPLHYAAQSNFAETVKVFLKHPSVKDDSDLEGRTSFMWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLENNAQVDATDVMKHTPLFRACEMGHKDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAFKIQAVYKGYKVRKAFRDRKNLLMKHEQLRKDAAAKKREEENKRKEAEQQKGRRSPDSCRPQALPCLPSTQDVPSRQSRAPSKQPPAGNVAQGPEPRDSRGSPGGSLGGALQKEQHVSSDLQGTNSRRPNETAREHSKGQSACVHFRPNEGSDGSRHPGVPSVEKSRGETAGDERCAKGKGFVKQPSCIRVAGPDEKGEDSRRAAASLPPHDSHWKPSRRHDTEPKAKCAPQKRRTQELRGGRCSPAGSSRPGSARGEAVHAGQNPPHHRTPRNKVTQAKLTGGLYSHLPQSTEELRSGARRLETSTLSEDFQVSKETDPAPGPLSGQSVNIDLLPVELRLQIIQRERRRKELFRKKNKAAAVIQRAWRSYQLRKHLSHLRHMKQLGAGDVDRWRQESTALLLQVWRKELELKFPQTTAVSKAPKSPSKGTSGTKSTKHSVLKQIYGCSHEGKIHHPTRSVKASSVLRLNSVSNLQCIHLLENSGRSKNFSYNLQSATQPKNKTKP
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
41UbiquitinationIVGNSALKDKEDQFG
HHCCHHHCCCCCCCC		67.48-
75HydroxylationLKAGADVNKTDHSQR
HHCCCCCCCCCHHHH		41.9023793029
91UbiquitinationALHLAAQKGNYRFMK
HHHHHHHHCCHHHHH		44.38-
110UbiquitinationRRANWMQKDLEEMTP
HHCHHHHHCHHHCCC		48.45-
126PhosphorylationHLTTRHRSPKCLALL
CCCCCCCCHHHHHHH		23.68-
170UbiquitinationEHVKLLIKHDSNIGI
HHHEEEEECCCCCCC		41.13-
196PhosphorylationAANHKDPSAVHTVRC
HHCCCCHHHHHHEEH		53.7224719451
200PhosphorylationKDPSAVHTVRCILDA
CCHHHHHHEEHHHHC		11.7524719451
310UbiquitinationETVKVFLKHPSVKDD
HHHHHHHHCCCCCCC		41.84-
313PhosphorylationKVFLKHPSVKDDSDL
HHHHHCCCCCCCCCC		41.3328122231
318PhosphorylationHPSVKDDSDLEGRTS
CCCCCCCCCCCCCCH		54.9828122231
332UbiquitinationSFMWAAGKGSDDVLR
HHHHHCCCCCHHHHH		50.98-
355UbiquitinationIDINMADKYGGTALH
CCCCCCHHCCHHHHH		35.94-
390UbiquitinationVDATDVMKHTPLFRA
CCCHHHHHCCHHHHH		44.1421890473
390 (in isoform 1)Ubiquitination-44.1421890473
390UbiquitinationVDATDVMKHTPLFRA
CCCHHHHHCCHHHHH		44.1421890473
390 (in isoform 2)Ubiquitination-44.1421890473
390UbiquitinationVDATDVMKHTPLFRA
CCCHHHHHCCHHHHH		44.1421890473
403UbiquitinationRACEMGHKDVIQTLI
HHHHCCCHHHHHHHH		48.22-
579UbiquitinationRKAFRDRKNLLMKHE
HHHHHHHHHHHHHHH		57.12-
584UbiquitinationDRKNLLMKHEQLRKD
HHHHHHHHHHHHHHH		43.91-
614PhosphorylationEQQKGRRSPDSCRPQ
HHHHCCCCCCCCCCC		31.5323401153
617PhosphorylationKGRRSPDSCRPQALP
HCCCCCCCCCCCCCC		18.5323927012
628PhosphorylationQALPCLPSTQDVPSR
CCCCCCCCCCCCCCC		26.2523927012
629PhosphorylationALPCLPSTQDVPSRQ
CCCCCCCCCCCCCCC		27.1823927012
634PhosphorylationPSTQDVPSRQSRAPS
CCCCCCCCCCCCCCC		42.6823927012
637PhosphorylationQDVPSRQSRAPSKQP
CCCCCCCCCCCCCCC		29.3322210691
642AcetylationRQSRAPSKQPPAGNV
CCCCCCCCCCCCCCC		66.8125953088
658PhosphorylationQGPEPRDSRGSPGGS
CCCCCCCCCCCCCCC		39.5625159151
661PhosphorylationEPRDSRGSPGGSLGG
CCCCCCCCCCCCHHH		21.1823401153
665PhosphorylationSRGSPGGSLGGALQK
CCCCCCCCHHHHHHH		29.7429978859
700PhosphorylationREHSKGQSACVHFRP
HHHHCCCCEEEECCC		32.10-
725PhosphorylationGVPSVEKSRGETAGD
CCCCCCCCCCCCCCH		31.8228787133
726DimethylationVPSVEKSRGETAGDE
CCCCCCCCCCCCCHH		59.02-
726MethylationVPSVEKSRGETAGDE
CCCCCCCCCCCCCHH		59.0224412505
734DimethylationGETAGDERCAKGKGF
CCCCCHHHCCCCCCC		30.36-
734MethylationGETAGDERCAKGKGF
CCCCCHHHCCCCCCC		30.3624412513
746PhosphorylationKGFVKQPSCIRVAGP
CCCCCCCCEEEEECC		21.49-
795PhosphorylationCAPQKRRTQELRGGR
CCCCCCCCCCCCCCC		30.35-
799MethylationKRRTQELRGGRCSPA
CCCCCCCCCCCCCCC		44.78115480379
841PhosphorylationKVTQAKLTGGLYSHL
HCCHHHHHCCHHHCC		28.6228796482
845PhosphorylationAKLTGGLYSHLPQST
HHHHCCHHHCCCCCH		9.4128796482
846PhosphorylationKLTGGLYSHLPQSTE
HHHCCHHHCCCCCHH		24.4828796482
851PhosphorylationLYSHLPQSTEELRSG
HHHCCCCCHHHHHHH		35.5329978859
852PhosphorylationYSHLPQSTEELRSGA
HHCCCCCHHHHHHHC		28.3829978859
864PhosphorylationSGARRLETSTLSEDF
HHCHHHHHCCCCCCC		31.44-
865PhosphorylationGARRLETSTLSEDFQ
HCHHHHHCCCCCCCC		20.27-
866PhosphorylationARRLETSTLSEDFQV
CHHHHHCCCCCCCCC		41.54-
980PhosphorylationFPQTTAVSKAPKSPS
CCCCCCCCCCCCCCC		22.19-
984AcetylationTAVSKAPKSPSKGTS
CCCCCCCCCCCCCCC		78.7512433953
985PhosphorylationAVSKAPKSPSKGTSG
CCCCCCCCCCCCCCC		33.0928176443
988AcetylationKAPKSPSKGTSGTKS
CCCCCCCCCCCCCCC		70.3712433963
1012UbiquitinationYGCSHEGKIHHPTRS
HCCCCCCCCCCCCCC		35.56-
1019PhosphorylationKIHHPTRSVKASSVL
CCCCCCCCCCHHHCE		30.37-
1023PhosphorylationPTRSVKASSVLRLNS
CCCCCCHHHCEECCC		18.4323090842
1024PhosphorylationTRSVKASSVLRLNSV
CCCCCHHHCEECCCC		29.9923090842
1030PhosphorylationSSVLRLNSVSNLQCI
HHCEECCCCCCCEEE		31.3627251275
1032PhosphorylationVLRLNSVSNLQCIHL
CEECCCCCCCEEEEH		31.48-
1050PhosphorylationSGRSKNFSYNLQSAT
CCCCCCCCCCCCCCC		23.6229759185
1051PhosphorylationGRSKNFSYNLQSATQ
CCCCCCCCCCCCCCC		18.7629759185
1055PhosphorylationNFSYNLQSATQPKNK
CCCCCCCCCCCCCCC		36.1329978859
1057PhosphorylationSYNLQSATQPKNKTK
CCCCCCCCCCCCCCC		51.1329978859
1062AcetylationSATQPKNKTKP----
CCCCCCCCCCC----		65.147826263
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
795TPhosphorylationKinasePKACAP17612
PSP
864TPhosphorylationKinaseAKT1P31749
PSP
865SPhosphorylationKinaseAKT1P31749
PSP
866TPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
75NHydroxylation

23793029
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 INVS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIF1N_HUMANHIF1ANphysical
16189514
NPHP1_HUMANNPHP1physical
12872123
CE164_HUMANCEP164physical
22863007
DDB1_HUMANDDB1physical
22863007
MIC25_HUMANCHCHD6physical
27173435
Drug and Disease Associations
Kegg Disease
H00537 Nephronophthisis-medullary cystic kidney disease, including; Nephronophthisis (NPH) ; Nephronophthis
OMIM Disease
602088Nephronophthisis 2 (NPHP2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INVS_HUMAN

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Related Literatures of Post-Translational Modification

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