ANO6_HUMAN - dbPTM
ANO6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANO6_HUMAN
UniProt AC Q4KMQ2
Protein Name Anoctamin-6
Gene Name ANO6
Organism Homo sapiens (Human).
Sequence Length 910
Subcellular Localization Cell membrane
Multi-pass membrane protein . Shows an intracellular localization according to PubMed:22075693.
Protein Description Small-conductance calcium-activated nonselective cation (SCAN) channel which acts as a regulator of phospholipid scrambling in platelets and osteoblasts. Phospholipid scrambling results in surface exposure of phosphatidylserine which in platelets is essential to trigger the clotting system whereas in osteoblasts is essential for the deposition of hydroxyapatite during bone mineralization. Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Can generate outwardly rectifying chloride channel currents in airway epithelial cells and Jurkat T lymphocytes..
Protein Sequence MKKMSRNVLLQMEEEEDDDDGDIVLENLGQTIVPDLGSLESQHDFRTPEFEEFNGKPDSLFFNDGQRRIDFVLVYEDESRKETNKKGTNEKQRRKRQAYESNLICHGLQLEATRSVLDDKLVFVKVHAPWEVLCTYAEIMHIKLPLKPNDLKNRSSAFGTLNWFTKVLSVDESIIKPEQEFFTAPFEKNRMNDFYIVDRDAFFNPATRSRIVYFILSRVKYQVINNVSKFGINRLVNSGIYKAAFPLHDCKFRRQSEDPSCPNERYLLYREWAHPRSIYKKQPLDLIRKYYGEKIGIYFAWLGYYTQMLLLAAVVGVACFLYGYLNQDNCTWSKEVCHPDIGGKIIMCPQCDRLCPFWKLNITCESSKKLCIFDSFGTLVFAVFMGVWVTLFLEFWKRRQAELEYEWDTVELQQEEQARPEYEARCTHVVINEITQEEERIPFTAWGKCIRITLCASAVFFWILLIIASVIGIIVYRLSVFIVFSAKLPKNINGTDPIQKYLTPQTATSITASIISFIIIMILNTIYEKVAIMITNFELPRTQTDYENSLTMKMFLFQFVNYYSSCFYIAFFKGKFVGYPGDPVYWLGKYRNEECDPGGCLLELTTQLTIIMGGKAIWNNIQEVLLPWIMNLIGRFHRVSGSEKITPRWEQDYHLQPMGKLGLFYEYLEMIIQFGFVTLFVASFPLAPLLALVNNILEIRVDAWKLTTQFRRLVPEKAQDIGAWQPIMQGIAILAVVTNAMIIAFTSDMIPRLVYYWSFSVPPYGDHTSYTMEGYINNTLSIFKVADFKNKSKGNPYSDLGNHTTCRYRDFRYPPGHPQEYKHNIYYWHVIAAKLAFIIVMEHVIYSVKFFISYAIPDVSKRTKSKIQREKYLTQKLLHENHLKDMTKNMGVIAERMIEAVDNNLRPKSE
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
13 (in isoform 3)Phosphorylation-49.6626503514
20 (in isoform 3)Phosphorylation-64.7526503514
23 (in isoform 3)Phosphorylation-4.6926503514
38PhosphorylationTIVPDLGSLESQHDF
EECCCHHCCCCCCCC		35.9469008461
41PhosphorylationPDLGSLESQHDFRTP
CCHHCCCCCCCCCCC		37.8024275569
56UbiquitinationEFEEFNGKPDSLFFN
CHHHHCCCCCCEEEE		46.9121890473
77 (in isoform 2)Ubiquitination-41.29-
120UbiquitinationTRSVLDDKLVFVKVH
HHHHHCCCEEEEEEE		46.33-
147UbiquitinationMHIKLPLKPNDLKNR
HCEECCCCCCCCCCC		39.57-
155PhosphorylationPNDLKNRSSAFGTLN
CCCCCCCHHHCHHHH		35.106146023
156PhosphorylationNDLKNRSSAFGTLNW
CCCCCCHHHCHHHHH		25.1222617229
160PhosphorylationNRSSAFGTLNWFTKV
CCHHHCHHHHHHHHH		15.5130831765
169PhosphorylationNWFTKVLSVDESIIK
HHHHHHEECCHHHCC		30.4328857561
173PhosphorylationKVLSVDESIIKPEQE
HHEECCHHHCCCHHH		25.7518491316
176UbiquitinationSVDESIIKPEQEFFT
ECCHHHCCCHHHCCC		40.6121890473
181PhosphorylationIIKPEQEFFTAPFEK
HCCCHHHCCCCCCCC		7.0527251275
188UbiquitinationFFTAPFEKNRMNDFY
CCCCCCCCCCCCCEE		50.6721890473
220AcetylationYFILSRVKYQVINNV
HHHHHCCHHHHHCCC		28.9327452117
229UbiquitinationQVINNVSKFGINRLV
HHHCCCHHHCHHHHH		43.24-
238PhosphorylationGINRLVNSGIYKAAF
CHHHHHHCCCCCCEE		21.0628060719
241PhosphorylationRLVNSGIYKAAFPLH
HHHHCCCCCCEEEHH		9.7128060719
256PhosphorylationDCKFRRQSEDPSCPN
HCCCCCCCCCCCCCC		42.0029255136
260PhosphorylationRRQSEDPSCPNERYL
CCCCCCCCCCCCHHH		55.3023403867
277PhosphorylationREWAHPRSIYKKQPL
HCCCCCHHHHHCCCH		34.4227251275
279PhosphorylationWAHPRSIYKKQPLDL
CCCCHHHHHCCCHHH		17.2422817900
281UbiquitinationHPRSIYKKQPLDLIR
CCHHHHHCCCHHHHH		39.93-
302 (in isoform 2)Ubiquitination-2.57-
329N-linked_GlycosylationYGYLNQDNCTWSKEV
HHHHCCCCCCCCCCC		18.49UniProtKB CARBOHYD
361N-linked_GlycosylationLCPFWKLNITCESSK
CCCCEEEEEEECCCC		24.6417660510
493N-linked_GlycosylationAKLPKNINGTDPIQK
CCCCCCCCCCCCHHH		57.6217660510
589UbiquitinationDPVYWLGKYRNEECD
CCEEEEEEECCCCCC		38.5821890473
640PhosphorylationIGRFHRVSGSEKITP
HHCHHCCCCCCCCCC		36.2423403867
642PhosphorylationRFHRVSGSEKITPRW
CHHCCCCCCCCCCCC		28.3623403867
644UbiquitinationHRVSGSEKITPRWEQ
HCCCCCCCCCCCCCC		54.2821890473
646PhosphorylationVSGSEKITPRWEQDY
CCCCCCCCCCCCCCC		20.1923403867
663PhosphorylationQPMGKLGLFYEYLEM
CCCCHHHHHHHHHHH		6.3127251275
665 (in isoform 2)Ubiquitination-14.54-
775PhosphorylationTSYTMEGYINNTLSI
CCEEEEEEECCEEEE		6.2829759185
777N-linked_GlycosylationYTMEGYINNTLSIFK
EEEEEEECCEEEEEE		27.27UniProtKB CARBOHYD
779PhosphorylationMEGYINNTLSIFKVA
EEEEECCEEEEEEEE		19.8629759185
781PhosphorylationGYINNTLSIFKVADF
EEECCEEEEEEEECC		24.7624719451
790N-linked_GlycosylationFKVADFKNKSKGNPY
EEEECCCCCCCCCCC		54.55UniProtKB CARBOHYD
793UbiquitinationADFKNKSKGNPYSDL
ECCCCCCCCCCCHHC		65.40-
802N-linked_GlycosylationNPYSDLGNHTTCRYR
CCCHHCCCCCEECCC		36.31UniProtKB CARBOHYD
808PhosphorylationGNHTTCRYRDFRYPP
CCCCEECCCCCCCCC		19.3846306945
814 (in isoform 2)Ubiquitination-24.92-
871UbiquitinationKSKIQREKYLTQKLL
HHHHHHHHHHHHHHH		47.99-
876UbiquitinationREKYLTQKLLHENHL
HHHHHHHHHHHHHHH		48.0221890473
884UbiquitinationLLHENHLKDMTKNMG
HHHHHHHHHHHHHHH		37.59-
888UbiquitinationNHLKDMTKNMGVIAE
HHHHHHHHHHHHHHH		38.0021890473
897 (in isoform 2)Ubiquitination-2.15-
897UbiquitinationMGVIAERMIEAVDNN
HHHHHHHHHHHHHHC		2.1521890473
908UbiquitinationVDNNLRPKSE-----
HHHCCCCCCC-----		61.8621890473
909 (in isoform 2)Ubiquitination-51.74-
909PhosphorylationDNNLRPKSE------
HHCCCCCCC------		51.7430266825
909UbiquitinationDNNLRPKSE------
HHCCCCCCC------		51.7421890473
929 (in isoform 2)Ubiquitination--
930Phosphorylation---------------------------
---------------------------		24719451
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 ANO6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANO6_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 ANO6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTGE5_HUMANCTAGE5physical
28514442
CDC16_HUMANCDC16physical
28514442
CDC27_HUMANCDC27physical
28514442
APC4_HUMANANAPC4physical
28514442
CDC23_HUMANCDC23physical
28514442
LMA2L_HUMANLMAN2Lphysical
28514442
TGO1_HUMANMIA3physical
28514442
APC1_HUMANANAPC1physical
28514442
APC5_HUMANANAPC5physical
28514442
LEMD2_HUMANLEMD2physical
28514442
CDC26_HUMANCDC26physical
28514442
PREB_HUMANPREBphysical
28514442
Drug and Disease Associations
Kegg Disease
H01162 Scott syndrome
OMIM Disease
262890Scott syndrome (SCTS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANO6_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-493, AND MASSSPECTROMETRY.

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