GAS6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GAS6_HUMAN
• UniProt AC: Q14393
• Protein Name: Growth arrest-specific protein 6
• Gene Name: GAS6
• Organism: Homo sapiens (Human).
• Sequence Length: 721
• Subcellular Localization: Secreted .
• Protein Description: Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. 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.; (Microbial infection) Can bridges virus envelope phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate viral entry by apoptotic mimicry. [PubMed: 21501828 Plays a role in Dengue cell entry by apoptotic mimicry]
• Protein Sequence: MAPSLSPGPAALRRAPQLLLLLLAAECALAALLPAREATQFLRPRQRRAFQVFEEAKQGHLERECVEELCSREEAREVFENDPETDYFYPRYLDCINKYGSPYTKNSGFATCVQNLPDQCTPNPCDRKGTQACQDLMGNFFCLCKAGWGGRLCDKDVNECSQENGGCLQICHNKPGSFHCSCHSGFELSSDGRTCQDIDECADSEACGEARCKNLPGSYSCLCDEGFAYSSQEKACRDVDECLQGRCEQVCVNSPGSYTCHCDGRGGLKLSQDMDTCELEAGWPCPRHRRDGSPAARPGRGAQGSRSEGHIPDRRGPRPWQDILPCVPFSVAKSVKSLYLGRMFSGTPVIRLRFKRLQPTRLVAEFDFRTFDPEGILLFAGGHQDSTWIVLALRAGRLELQLRYNGVGRVTSSGPVINHGMWQTISVEELARNLVIKVNRDAVMKIAVAGDLFQPERGLYHLNLTVGGIPFHEKDLVQPINPRLDGCMRSWNWLNGEDTTIQETVKVNTRMQCFSVTERGSFYPGSGFAFYSLDYMRTPLDVGTESTWEVEVVAHIRPAADTGVLFALWAPDLRAVPLSVALVDYHSTKKLKKQLVVLAVEHTALALMEIKVCDGQEHVVTVSLRDGEATLEVDGTRGQSEVSAAQLQERLAVLERHLRSPVLTFAGGLPDVPVTSAPVTAFYRGCMTLEVNRRLLDLDEAAYKHSDITAHSCPPVEPAAA

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
14 (in isoform 4)	Phosphorylation	-	52.01	29507054
71	Phosphorylation	ECVEELCSREEAREV HHHHHHHCHHHHHHH	56.18	26699800
85	Phosphorylation	VFENDPETDYFYPRY HHHCCCCCCCCCHHH	41.19	26074081
87	Phosphorylation	ENDPETDYFYPRYLD HCCCCCCCCCHHHHH	16.66	26074081
89	Phosphorylation	DPETDYFYPRYLDCI CCCCCCCCHHHHHHH	4.79	26074081
92	Phosphorylation	TDYFYPRYLDCINKY CCCCCHHHHHHHHHH	11.46	26074081
420	N-linked_Glycosylation	SGPVINHGMWQTISV CCCCCCCCCEEEEEH	17.97	16362042
463	N-linked_Glycosylation	ERGLYHLNLTVGGIP CCCEEEEEEEECCEE	21.98	16362042
617	Phosphorylation	IKVCDGQEHVVTVSL EEECCCCCEEEEEEE	44.15	18510355
621	Phosphorylation	DGQEHVVTVSLRDGE CCCCEEEEEEECCCE	11.86	24850871
633	Phosphorylation	DGEATLEVDGTRGQS CCEEEEEECCCCCCC	10.40	18510355
637	Phosphorylation	TLEVDGTRGQSEVSA EEEECCCCCCCHHCH	46.84	18510355
640	Phosphorylation	VDGTRGQSEVSAAQL ECCCCCCCHHCHHHH	42.67	-
660	Phosphorylation	VLERHLRSPVLTFAG HHHHHHCCCEEEECC	26.22	18510355
664	Phosphorylation	HLRSPVLTFAGGLPD HHCCCEEEECCCCCC	16.21	-
676	Phosphorylation	LPDVPVTSAPVTAFY CCCCCCCCCCCHHHH	30.70	18510355
680	Phosphorylation	PVTSAPVTAFYRGCM CCCCCCCHHHHCCCC	15.25	18510355
683	Phosphorylation	SAPVTAFYRGCMTLE CCCCHHHHCCCCCHH	12.02	-

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
71	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GAS6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of GAS6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TYRO3_HUMAN	TYRO3	physical	8939948
MERTK_HUMAN	MERTK	physical	8939948
UFO_HUMAN	AXL	physical	8939948

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structural basis for Gas6-Axl signalling.";
Sasaki T., Knyazev P.G., Clout N.J., Cheburkin Y., Goehring W.,Ullrich A., Timpl R., Hohenester E.;
EMBO J. 25:80-87(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 322-721 IN COMPLEX WITH AXL,SUBUNIT, GLYCOSYLATION AT ASN-463, AND MUTAGENESIS OF ARG-353 ANDLYS-355.
PubMed: 16362042