UFO_MOUSE - dbPTM
UFO_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UFO_MOUSE
UniProt AC Q00993
Protein Name Tyrosine-protein kinase receptor UFO
Gene Name Axl
Organism Mus musculus (Mouse).
Sequence Length 888
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response..
Protein Sequence MGRVPLAWWLALCCWGCAAHKDTQTEAGSPFVGNPGNITGARGLTGTLRCELQVQGEPPEVVWLRDGQILELADNTQTQVPLGEDWQDEWKVVSQLRISALQLSDAGEYQCMVHLEGRTFVSQPGFVGLEGLPYFLEEPEDKAVPANTPFNLSCQAQGPPEPVTLLWLQDAVPLAPVTGHSSQHSLQTPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQRPHHLHVVSRQPTELEVAWTPGLSGIYPLTHCNLQAVLSDDGVGIWLGKSDPPEDPLTLQVSVPPHQLRLEKLLPHTPYHIRISCSSSQGPSPWTHWLPVETTEGVPLGPPENVSAMRNGSQVLVRWQEPRVPLQGTLLGYRLAYRGQDTPEVLMDIGLTREVTLELRGDRPVANLTVSVTAYTSAGDGPWSLPVPLEPWRPGQGQPLHHLVSEPPPRAFSWPWWYVLLGALVAAACVLILALFLVHRRKKETRYGEVFEPTVERGELVVRYRVRKSYSRRTTEATLNSLGISEELKEKLRDVMVDRHKVALGKTLGEGEFGAVMEGQLNQDDSILKVAVKTMKIAICTRSELEDFLSEAVCMKEFDHPNVMRLIGVCFQGSDREGFPEPVVILPFMKHGDLHSFLLYSRLGDQPVFLPTQMLVKFMADIASGMEYLSTKRFIHRDLAARNCMLNENMSVCVADFGLSKKIYNGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPVDCLDGLYALMSRCWELNPRDRPSFAELREDLENTLKALPPAQEPDEILYVNMDEGGSHLEPRGAAGGADPPTQPDPKDSCSCLTAADVHSAGRYVLCPSTAPGPTLSADRGCPAPPGQEDGA
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
23PhosphorylationGCAAHKDTQTEAGSP
HHHHCCCCCCCCCCC
42.0425777480
25PhosphorylationAAHKDTQTEAGSPFV
HHCCCCCCCCCCCCC
29.8725777480
29PhosphorylationDTQTEAGSPFVGNPG
CCCCCCCCCCCCCCC
23.3925777480
37N-linked_GlycosylationPFVGNPGNITGARGL
CCCCCCCCCCCCCCC
29.88-
39PhosphorylationVGNPGNITGARGLTG
CCCCCCCCCCCCCCE
28.8725777480
104PhosphorylationRISALQLSDAGEYQC
EEEEEECCCCCCEEE
16.68-
109PhosphorylationQLSDAGEYQCMVHLE
ECCCCCCEEEEEEEC
13.19-
151N-linked_GlycosylationVPANTPFNLSCQAQG
CCCCCCCCEEEECCC
32.04-
192N-linked_GlycosylationSLQTPGLNKTSSFSC
CCCCCCCCCCCCCCC
52.02-
250PhosphorylationLSGIYPLTHCNLQAV
CCCEEECCCCCEEEE
21.63-
259PhosphorylationCNLQAVLSDDGVGIW
CCEEEEECCCCCEEE
27.36-
333N-linked_GlycosylationVPLGPPENVSAMRNG
CCCCCCCCHHCCCCC
38.53-
339N-linked_GlycosylationENVSAMRNGSQVLVR
CCHHCCCCCCEEEEE
41.19-
395N-linked_GlycosylationRGDRPVANLTVSVTA
CCCCCEEEEEEEEEE
36.16-
475PhosphorylationRRKKETRYGEVFEPT
HHCCCCCCCEEECCE
25.6722817900
502PhosphorylationRKSYSRRTTEATLNS
ECCCCCCCCHHHHHH
28.07-
503PhosphorylationKSYSRRTTEATLNSL
CCCCCCCCHHHHHHC
23.0825521595
506PhosphorylationSRRTTEATLNSLGIS
CCCCCHHHHHHCCCC
21.9025338131
509PhosphorylationTTEATLNSLGISEEL
CCHHHHHHCCCCHHH
30.9626824392
517UbiquitinationLGISEELKEKLRDVM
CCCCHHHHHHHHHHH
56.9622790023
534UbiquitinationRHKVALGKTLGEGEF
HHHHHHCCCCCCCCC
41.2322790023
564UbiquitinationKVAVKTMKIAICTRS
HHHHHHCEEEEECHH
33.93-
629PhosphorylationLHSFLLYSRLGDQPV
HHHHHHHHHHCCCCE
22.46-
640PhosphorylationDQPVFLPTQMLVKFM
CCCEEEEHHHHHHHH
28.8524719451
688PhosphorylationCVADFGLSKKIYNGD
EEEEECCCCCCCCCC
32.0823984901
692PhosphorylationFGLSKKIYNGDYYRQ
ECCCCCCCCCCCCCC
23.2129514104
696PhosphorylationKKIYNGDYYRQGRIA
CCCCCCCCCCCCCCC
11.2718515860
697PhosphorylationKIYNGDYYRQGRIAK
CCCCCCCCCCCCCCC
10.9520116462
753PhosphorylationGVENSEIYDYLRQGN
CCCCHHHHHHHHCCC
8.4225338131
755PhosphorylationENSEIYDYLRQGNRL
CCHHHHHHHHCCCCC
6.1922817900
763UbiquitinationLRQGNRLKQPVDCLD
HHCCCCCCCCHHHHH
49.6822790023
773PhosphorylationVDCLDGLYALMSRCW
HHHHHHHHHHHHHHH
11.83-
815PhosphorylationQEPDEILYVNMDEGG
CCCCCEEEEECCCCC
8.7428507225
860PhosphorylationDVHSAGRYVLCPSTA
HHHCCCCEEECCCCC
9.2425619855

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 UFO_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UFO_MOUSE !!

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 UFO_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TYRO3_MOUSETyro3physical
18787040
GRB2_MOUSEGrb2physical
18346204
P85A_MOUSEPik3r1physical
18346204

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UFO_MOUSE

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Related Literatures of Post-Translational Modification

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