TXD11_HUMAN - dbPTM
TXD11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TXD11_HUMAN
UniProt AC Q6PKC3
Protein Name Thioredoxin domain-containing protein 11
Gene Name TXNDC11
Organism Homo sapiens (Human).
Sequence Length 985
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein .
Protein Description May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation..
Protein Sequence MSECGGRGGGSSSSEDAEDEGGGGGGPAGSDCLSSSPTLATASSAGRLRRGLRGAFLMARQRPELLCGAVALGCALLLALKFTCSRAKDVIIPAKPPVSFFSLRSPVLDLFQGQLDYAEYVRRDSEVVLLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGKCRKQKHFFYFPVIYLYHRSFGPIEYKGPMSAVYIEKFVRRVMKPLLYIPSQSELLDFLSNYEPGVLGYFEFSGSPQPPGYLTFFTSALHSLKKALESTSSPRALVSFTGEWHLETKIYVLDYLGTVRFGVITNKHLAKLVSLVHSGSVYLHRHFNTSLVFPREVLNYTAENICKWALENQETLFRWLRPHGGKSLLLNNELKKGPALFLFIPFNPLAESHPLIDEITEVALEYNNCHGDQVVERLLQHLRRVDAPVLESLALEVPAQLPDPPTITASPCCNTVVLPQWHSFSRTHNVCELCVNQTSGGMKPSSVSVPQCSFFEMAAALDSFYLKEQTFYHVASDSIECSNFLTSYSPFSYYTACCRTISRGVSGFIDSEQGVFEAPTVAFSSLEKKCEVDAPSSVPHIEENRYLFPEVDMTSTNFTGLSCRTNKTLNIYLLDSNLFWLYAERLGAPSSTQVKEFAAIVDVKEESHYILDPKQALMKLTLESFIQNFSVLYSPLKRHLIGSGSAQFPSQHLITEVTTDTFWEVVLQKQDVLLLYYAPWCGFCPSLNHIFIQLARNLPMDTFTVARIDVSQNDLPWEFMVDRLPTVLFFPCNRKDLSVKYPEDVPITLPNLLRFILHHSDPASSPQNVANSPTKECLQSEAVLQRGHISHLEREIQKLRAEISSLQRAQVQVESQLSSARRDEHRLRQQQRALEEQHSLLHAHSEQLQALYEQKTRELQELARKLQELADASENLLTENTWLKILVATMERKLEGRDGAESLAAQREVHPKQPEPSATPQLPGSSPPPANVSATLVSERNKENRTD
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
99PhosphorylationIPAKPPVSFFSLRSP
EECCCCCEEEECCCH		26.7526270265
102PhosphorylationKPPVSFFSLRSPVLD
CCCCEEEECCCHHHH		22.3626270265
120PhosphorylationGQLDYAEYVRRDSEV
CCCCHHHHHCCCCCE		7.35-
133PhosphorylationEVVLLFFYAPWCGQS
CEEEEEEECCCCCHH		12.38-
207UbiquitinationMSAVYIEKFVRRVMK
CCHHHHHHHHHHHHH		39.33-
230PhosphorylationSELLDFLSNYEPGVL
HHHHHHHHCCCCCEE		37.04-
232PhosphorylationLLDFLSNYEPGVLGY
HHHHHHCCCCCEEEE		21.81-
289PhosphorylationWHLETKIYVLDYLGT
EEEEEEEEEEECCCC		9.1226699800
293PhosphorylationTKIYVLDYLGTVRFG
EEEEEEECCCCCEEE		11.6726699800
296PhosphorylationYVLDYLGTVRFGVIT
EEEECCCCCEEEEEC		13.1026699800
316PhosphorylationKLVSLVHSGSVYLHR
HHHHHHHCCCEEEEE		25.8628509920
318PhosphorylationVSLVHSGSVYLHRHF
HHHHHCCCEEEEECC		15.5928509920
320PhosphorylationLVHSGSVYLHRHFNT
HHHCCCEEEEECCCC		9.8628509920
539 (in isoform 2)Ubiquitination-1.0521906983
558O-linked_GlycosylationQGVFEAPTVAFSSLE
CCEEECCEEEEHHHH		31.36OGP
566UbiquitinationVAFSSLEKKCEVDAP
EEEHHHHHHCCCCCC		68.932190698
566 (in isoform 1)Ubiquitination-68.9321906983
659PhosphorylationKQALMKLTLESFIQN
HHHHHHHHHHHHHHH		23.9827273156
671PhosphorylationIQNFSVLYSPLKRHL
HHHHHHHHHHHHHHC		13.1927273156
672PhosphorylationQNFSVLYSPLKRHLI
HHHHHHHHHHHHHCC		21.4227273156
675UbiquitinationSVLYSPLKRHLIGSG
HHHHHHHHHHCCCCC		40.95-
776PhosphorylationPCNRKDLSVKYPEDV
ECCCCCCCCCCCCCC		27.05-
813UbiquitinationNVANSPTKECLQSEA
CCCCCCCHHHHHHHH		50.22-
828PhosphorylationVLQRGHISHLEREIQ
HHHHCCHHHHHHHHH		19.1514702039
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 TXD11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TXD11_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 TXD11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBP_HUMANCREBBPphysical
26186194
TXLNA_HUMANTXLNAphysical
26186194
RBL2_HUMANRBL2physical
26186194
ZN703_HUMANZNF703physical
26186194
USO1_HUMANUSO1physical
26186194
C102A_HUMANCCDC102Aphysical
26186194
RBL1_HUMANRBL1physical
26186194
PCNT_HUMANPCNTphysical
26186194
HAUS4_HUMANHAUS4physical
26186194
RBL1_HUMANRBL1physical
28514442
RBL2_HUMANRBL2physical
28514442
TXLNA_HUMANTXLNAphysical
28514442
USO1_HUMANUSO1physical
28514442
CBP_HUMANCREBBPphysical
28514442
PCNT_HUMANPCNTphysical
28514442
HAUS4_HUMANHAUS4physical
28514442
CCNA2_HUMANCCNA2physical
28514442
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 TXD11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, AND MASSSPECTROMETRY.

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