TTYH3_HUMAN - dbPTM
TTYH3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTYH3_HUMAN
UniProt AC Q9C0H2
Protein Name Protein tweety homolog 3
Gene Name TTYH3
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction..
Protein Sequence MAGVSYAAPWWVSLLHRLPHFDLSWEATSSQFRPEDTDYQQALLLLGAAALACLALDLLFLLFYSFWLCCRRRKSEEHLDADCCCTAWCVIIATLVCSAGIAVGFYGNGETSDGIHRATYSLRHANRTVAGVQDRVWDTAVGLNHTAEPSLQTLERQLAGRPEPLRAVQRLQGLLETLLGYTAAIPFWRNTAVSLEVLAEQVDLYDWYRWLGYLGLLLLDVIICLLVLVGLIRSSKGILVGVCLLGVLALVISWGALGLELAVSVGSSDFCVDPDAYVTKMVEEYSVLSGDILQYYLACSPRAANPFQQKLSGSHKALVEMQDVVAELLRTVPWEQPATKDPLLRVQEVLNGTEVNLQHLTALVDCRSLHLDYVQALTGFCYDGVEGLIYLALFSFVTALMFSSIVCSVPHTWQQKRGPDEDGEEEAAPGPRQAHDSLYRVHMPSLYSCGSSYGSETSIPAAAHTVSNAPVTEYMSQNANFQNPRCENTPLIGRESPPPSYTSSMRAKYLATSQPRPDSSGSH
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
121PhosphorylationGIHRATYSLRHANRT
CHHHHHEHHHHCCCC		17.9924719451
126N-linked_GlycosylationTYSLRHANRTVAGVQ
HEHHHHCCCCCCCCC		33.75UniProtKB CARBOHYD
144N-linked_GlycosylationWDTAVGLNHTAEPSL
HHHCCCCCCCCCCCH		25.2419159218
310UbiquitinationAANPFQQKLSGSHKA
CCCHHHHHCCCCHHH		33.56-
312PhosphorylationNPFQQKLSGSHKALV
CHHHHHCCCCHHHHH		45.3328634298
314PhosphorylationFQQKLSGSHKALVEM
HHHHCCCCHHHHHHH		20.5928634298
316UbiquitinationQKLSGSHKALVEMQD
HHCCCCHHHHHHHHH		45.15-
331PhosphorylationVVAELLRTVPWEQPA
HHHHHHHCCCCCCCC		30.7828634298
337 (in isoform 3)Ubiquitination-30.3121890473
339PhosphorylationVPWEQPATKDPLLRV
CCCCCCCCCCCCCHH		42.5428634298
340UbiquitinationPWEQPATKDPLLRVQ
CCCCCCCCCCCCHHH		60.50-
351PhosphorylationLRVQEVLNGTEVNLQ
CHHHHHHCCCEEEHH		61.5917081983
351N-linked_GlycosylationLRVQEVLNGTEVNLQ
CHHHHHHCCCEEEHH		61.5915010458
437PhosphorylationGPRQAHDSLYRVHMP
CCCCCCHHHEECCCC		19.8923401153
439PhosphorylationRQAHDSLYRVHMPSL
CCCCHHHEECCCCCH		17.9723403867
445PhosphorylationLYRVHMPSLYSCGSS
HEECCCCCHHCCCCC		32.1527080861
447PhosphorylationRVHMPSLYSCGSSYG
ECCCCCHHCCCCCCC		13.2727080861
448PhosphorylationVHMPSLYSCGSSYGS
CCCCCHHCCCCCCCC		19.8027080861
451PhosphorylationPSLYSCGSSYGSETS
CCHHCCCCCCCCCCC		25.3927080861
452PhosphorylationSLYSCGSSYGSETSI
CHHCCCCCCCCCCCC		20.8527080861
453PhosphorylationLYSCGSSYGSETSIP
HHCCCCCCCCCCCCC		26.7727080861
455PhosphorylationSCGSSYGSETSIPAA
CCCCCCCCCCCCCCC		29.4827080861
457PhosphorylationGSSYGSETSIPAAAH
CCCCCCCCCCCCCCC		33.3827080861
458PhosphorylationSSYGSETSIPAAAHT
CCCCCCCCCCCCCCC		23.6427080861
465PhosphorylationSIPAAAHTVSNAPVT
CCCCCCCCCCCCCHH		22.3927080861
467PhosphorylationPAAAHTVSNAPVTEY
CCCCCCCCCCCHHHH		28.5627080861
472PhosphorylationTVSNAPVTEYMSQNA
CCCCCCHHHHHCCCC		21.9725884760
474PhosphorylationSNAPVTEYMSQNANF
CCCCHHHHHCCCCCC		7.8425884760
476PhosphorylationAPVTEYMSQNANFQN
CCHHHHHCCCCCCCC		21.2725884760
476UbiquitinationAPVTEYMSQNANFQN
CCHHHHHCCCCCCCC		21.2721890473
476 (in isoform 2)Ubiquitination-21.2721890473
489PhosphorylationQNPRCENTPLIGRES
CCCCCCCCCCCCCCC		9.3630266825
489 (in isoform 4)Phosphorylation-9.3630266825
496PhosphorylationTPLIGRESPPPSYTS
CCCCCCCCCCCCCCH		41.1523401153
496 (in isoform 4)Phosphorylation-41.1530266825
500PhosphorylationGRESPPPSYTSSMRA
CCCCCCCCCCHHHHH		46.9823663014
500 (in isoform 4)Phosphorylation-46.9827732954
501PhosphorylationRESPPPSYTSSMRAK
CCCCCCCCCHHHHHH		19.2030266825
502PhosphorylationESPPPSYTSSMRAKY
CCCCCCCCHHHHHHH		20.7530266825
503PhosphorylationSPPPSYTSSMRAKYL
CCCCCCCHHHHHHHH		17.5730266825
504PhosphorylationPPPSYTSSMRAKYLA
CCCCCCHHHHHHHHH		12.4230266825
508UbiquitinationYTSSMRAKYLATSQP
CCHHHHHHHHHCCCC		30.3621890473
508 (in isoform 1)Ubiquitination-30.3621890473
509PhosphorylationTSSMRAKYLATSQPR
CHHHHHHHHHCCCCC		10.6923927012
512PhosphorylationMRAKYLATSQPRPDS
HHHHHHHCCCCCCCC		25.8722167270
513PhosphorylationRAKYLATSQPRPDSS
HHHHHHCCCCCCCCC		32.3629255136
517 (in isoform 4)Ubiquitination-53.14-
519PhosphorylationTSQPRPDSSGSH---
CCCCCCCCCCCC---		39.0030266825
520PhosphorylationSQPRPDSSGSH----
CCCCCCCCCCC----		52.2530266825
522PhosphorylationPRPDSSGSH------
CCCCCCCCC------		28.1529255136
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 TTYH3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTYH3_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 TTYH3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEDD4_HUMANNEDD4physical
18577513
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTYH3_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-144, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-522, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND MASSSPECTROMETRY.

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