FUT11_HUMAN - dbPTM
FUT11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FUT11_HUMAN
UniProt AC Q495W5
Protein Name Alpha-(1,3)-fucosyltransferase 11
Gene Name FUT11
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Golgi apparatus, Golgi stack membrane
Single-pass type II membrane protein.
Protein Description Probable fucosyltransferase..
Protein Sequence MAAGPIRVVLVLLGVLSVCAASGHGSVAEREAGGEAEWAEPWDGAVFRPPSALGAVGVTRSSGTPRPGREEAGDLPVLLWWSPGLFPHFPGDSERIECARGACVASRNRRALRDSRTRALLFYGTDFRASAAPLPRLAHQSWALLHEESPLNNFLLSHGPGIRLFNLTSTFSRHSDYPLSLQWLPGTAYLRRPVPPPMERAEWRRRGYAPLLYLQSHCDVPADRDRYVRELMRHIPVDSYGKCLQNRELPTARLQDTATATTEDPELLAFLSRYKFHLALENAICNDYMTEKLWRPMHLGAVPVYRGSPSVRDWMPNNHSVILIDDFESPQKLAEFIDFLDKNDEEYMKYLAYKQPGGITNQFLLDSLKHREWGVNDPLLPNYLNGFECFVCDYELARLDAEKAHAASPGDSPVFEPHIAQPSHMDCPVPTPGFGNVEEIPENDSWKEMWLQDYWQGLDQGEALTAMIHNNETEQTKFWDYLHEIFMKRQHL
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
17PhosphorylationLVLLGVLSVCAASGH
HHHHHHHHHHHHHCC
16.85-
26PhosphorylationCAASGHGSVAEREAG
HHHHCCCCHHHHHCC
16.69-
59O-linked_GlycosylationALGAVGVTRSSGTPR
HHCCCCEECCCCCCC
20.9355834533
61PhosphorylationGAVGVTRSSGTPRPG
CCCCEECCCCCCCCC
24.6122210691
64O-linked_GlycosylationGVTRSSGTPRPGREE
CEECCCCCCCCCCHH
20.3355834537
130PhosphorylationYGTDFRASAAPLPRL
HCCCCCCCCCCCHHH
22.2522985185
166N-linked_GlycosylationGPGIRLFNLTSTFSR
CCCEEEEECEECCCC
47.18UniProtKB CARBOHYD
208PhosphorylationAEWRRRGYAPLLYLQ
HHHHHCCCCCHHHHH
11.8429759185
213PhosphorylationRGYAPLLYLQSHCDV
CCCCCHHHHHHCCCC
15.4629759185
216PhosphorylationAPLLYLQSHCDVPAD
CCHHHHHHCCCCCCC
24.4029759185
242UbiquitinationIPVDSYGKCLQNREL
CCCCCCHHHHCCCCC
24.4421963094
349UbiquitinationKNDEEYMKYLAYKQP
CCCHHHHHHHHHCCC
35.8929967540
350PhosphorylationNDEEYMKYLAYKQPG
CCHHHHHHHHHCCCC
4.69-
353PhosphorylationEYMKYLAYKQPGGIT
HHHHHHHHCCCCCCC
13.94-
354UbiquitinationYMKYLAYKQPGGITN
HHHHHHHCCCCCCCC
44.3929967540
443N-linked_GlycosylationNVEEIPENDSWKEMW
CCCCCCCCCCHHHHH
43.1719159218

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 FUT11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FUT11_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 FUT11_HUMAN !!

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

Oops, there are no PPI records of FUT11_HUMAN !!

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 FUT11_HUMAN

loading...

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-443, AND MASSSPECTROMETRY.

TOP