dbPTM

UFO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UFO_HUMAN
UniProt AC	P30530
Protein Name	Tyrosine-protein kinase receptor UFO
Gene Name	AXL
Organism	Homo sapiens (Human).
Sequence Length	894
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.; (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope.; (Microbial infection) Acts as a receptor for Ebolavirus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope..
Protein Sequence	MAWRCPRMGRVPLAWCLALCGWACMAPRGTQAEESPFVGNPGNITGARGLTGTLRCQLQVQGEPPEVHWLRDGQILELADSTQTQVPLGEDEQDDWIVVSQLRITSLQLSDTGQYQCLVFLGHQTFVSQPGYVGLEGLPYFLEEPEDRTVAANTPFNLSCQAQGPPEPVDLLWLQDAVPLATAPGHGPQRSLHVPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQQPRNLHLVSRQPTELEVAWTPGLSGIYPLTHCTLQAVLSDDGMGIQAGEPDPPEEPLTSQASVPPHQLRLGSLHPHTPYHIRVACTSSQGPSSWTHWLPVETPEGVPLGPPENISATRNGSQAFVHWQEPRAPLQGTLLGYRLAYQGQDTPEVLMDIGLRQEVTLELQGDGSVSNLTVCVAAYTAAGDGPWSLPVPLEAWRPGQAQPVHQLVKEPSTPAFSWPWWYVLLGAVVAAACVLILALFLVHRRKKETRYGEVFEPTVERGELVVRYRVRKSYSRRTTEATLNSLGISEELKEKLRDVMVDRHKVALGKTLGEGEFGAVMEGQLNQDDSILKVAVKTMKIAICTRSELEDFLSEAVCMKEFDHPNVMRLIGVCFQGSERESFPAPVVILPFMKHGDLHSFLLYSRLGDQPVYLPTQMLVKFMADIASGMEYLSTKRFIHRDLAARNCMLNENMSVCVADFGLSKKIYNGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPADCLDGLYALMSRCWELNPQDRPSFTELREDLENTLKALPPAQEPDEILYVNMDEGGGYPEPPGAAGGADPPTQPDPKDSCSCLTAAEVHPAGRYVLCPSTTPSPAQPADRGSPAAPGQEDGA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	N-linked_Glycosylation	PFVGNPGNITGARGL CCCCCCCCCCCCCCC	29.88	UniProtKB CARBOHYD
100	Phosphorylation	QDDWIVVSQLRITSL CCCEEEEEEEEEEEE	16.77	22817900
149	Phosphorylation	LEEPEDRTVAANTPF CCCCCCCEEECCCCC	27.15	26074081
154	Phosphorylation	DRTVAANTPFNLSCQ CCEEECCCCCCEEEE	25.24	26074081
157	N-linked_Glycosylation	VAANTPFNLSCQAQG EECCCCCCEEEECCC	32.04	UniProtKB CARBOHYD
159	Phosphorylation	ANTPFNLSCQAQGPP CCCCCCEEEECCCCC	12.80	24043423
182	Phosphorylation	QDAVPLATAPGHGPQ ECCCCCCCCCCCCCC	40.86	24043423
198	N-linked_Glycosylation	SLHVPGLNKTSSFSC CEECCCCCCCCCEEE	52.02	UniProtKB CARBOHYD
200	Phosphorylation	HVPGLNKTSSFSCEA ECCCCCCCCCEEEEE	28.64	-
201	Phosphorylation	VPGLNKTSSFSCEAH CCCCCCCCCEEEEEC	30.87	-
202	Phosphorylation	PGLNKTSSFSCEAHN CCCCCCCCEEEEECC	26.81	-
204	Phosphorylation	LNKTSSFSCEAHNAK CCCCCCEEEEECCCC	17.00	-
284	Phosphorylation	DPPEEPLTSQASVPP CCCCCCCCCCCCCCH	29.52	27732954
285	Phosphorylation	PPEEPLTSQASVPPH CCCCCCCCCCCCCHH	31.28	27732954
288	Phosphorylation	EPLTSQASVPPHQLR CCCCCCCCCCHHHEE	27.76	27732954
303	Phosphorylation	LGSLHPHTPYHIRVA CCCCCCCCCEEEEEE	29.96	-
339	N-linked_Glycosylation	VPLGPPENISATRNG CCCCCCCCCCCCCCC	39.01	UniProtKB CARBOHYD
345	N-linked_Glycosylation	ENISATRNGSQAFVH CCCCCCCCCCCCEEE	50.54	UniProtKB CARBOHYD
401	N-linked_Glycosylation	QGDGSVSNLTVCVAA CCCCCCCCEEEEEEE	37.26	UniProtKB CARBOHYD
481	Phosphorylation	RRKKETRYGEVFEPT HHCCCCCCCEEECCE	25.67	28152594
503	Phosphorylation	VRYRVRKSYSRRTTE EEEEEECCCCCCCCH	20.13	-
508	Phosphorylation	RKSYSRRTTEATLNS ECCCCCCCCHHHHHH	28.07	28857561
509	Phosphorylation	KSYSRRTTEATLNSL CCCCCCCCHHHHHHC	23.08	28857561
512	Phosphorylation	SRRTTEATLNSLGIS CCCCCHHHHHHCCCC	21.90	28857561
514 (in isoform 2)	Ubiquitination	-	30.73	21906983
515	Phosphorylation	TTEATLNSLGISEEL CCHHHHHHCCCCHHH	30.96	28857561
519	Phosphorylation	TLNSLGISEELKEKL HHHHCCCCHHHHHHH	24.18	23312004
523 (in isoform 1)	Ubiquitination	-	56.96	21906983
523	Ubiquitination	LGISEELKEKLRDVM CCCCHHHHHHHHHHH	56.96	21906983
525	Ubiquitination	ISEELKEKLRDVMVD CCHHHHHHHHHHHCH	47.43	-
531 (in isoform 2)	Ubiquitination	-	6.17	21906983
535	Ubiquitination	DVMVDRHKVALGKTL HHHCHHHHHHHCCCC	30.05	-
540 (in isoform 1)	Ubiquitination	-	41.23	21906983
540	Ubiquitination	RHKVALGKTLGEGEF HHHHHHCCCCCCCCC	41.23	21906983
554 (in isoform 2)	Ubiquitination	-	24.76	21906983
560	Phosphorylation	GQLNQDDSILKVAVK ECCCCCCHHHHHHHH	37.80	24719451
563	Ubiquitination	NQDDSILKVAVKTMK CCCCHHHHHHHHHCE	26.86	21906983
563 (in isoform 1)	Ubiquitination	-	26.86	21906983
570	Ubiquitination	KVAVKTMKIAICTRS HHHHHHCEEEEECHH	33.93	-
608	Phosphorylation	IGVCFQGSERESFPA EEEEECCCCCCCCCC	23.77	23607784
612	Phosphorylation	FQGSERESFPAPVVI ECCCCCCCCCCCEEE	42.63	17494752
634	Phosphorylation	DLHSFLLYSRLGDQP CHHHHHHHHHHCCCC	8.22	27259358
635	Phosphorylation	LHSFLLYSRLGDQPV HHHHHHHHHHCCCCE	22.46	24719451
643	Phosphorylation	RLGDQPVYLPTQMLV HHCCCCEEEEHHHHH	17.41	27259358
657 (in isoform 2)	Ubiquitination	-	10.69	21906983
666 (in isoform 1)	Ubiquitination	-	41.77	21906983
666	Ubiquitination	GMEYLSTKRFIHRDL HCHHHHHHHHHHHHH	41.77	2190698
685	Phosphorylation	CMLNENMSVCVADFG CCCCCCCEEEEEEEC	24.77	28851738
694	Phosphorylation	CVADFGLSKKIYNGD EEEEECCCCCCCCCC	32.08	30108239
696	Ubiquitination	ADFGLSKKIYNGDYY EEECCCCCCCCCCCC	47.23	-
698	Phosphorylation	FGLSKKIYNGDYYRQ ECCCCCCCCCCCCCC	23.21	21945579
702	Phosphorylation	KKIYNGDYYRQGRIA CCCCCCCCCCCCCCC	11.27	21945579
703	Phosphorylation	KIYNGDYYRQGRIAK CCCCCCCCCCCCCCC	10.95	21945579
705 (in isoform 2)	Ubiquitination	-	29.42	21906983
710	Ubiquitination	YRQGRIAKMPVKWIA CCCCCCCCCCCEEEE	41.17	-
714	Ubiquitination	RIAKMPVKWIAIESL CCCCCCCEEEEHHHH	27.32	-
714 (in isoform 1)	Ubiquitination	-	27.32	21906983
724	Dimethylation	AIESLADRVYTSKSD EHHHHHHHHCCCHHH	20.10	-
726	Phosphorylation	ESLADRVYTSKSDVW HHHHHHHCCCHHHHH	13.24	22817900
756	Phosphorylation	PYPGVENSEIYDYLR CCCCCCHHHHHHHHH	16.33	27259358
759	Phosphorylation	GVENSEIYDYLRQGN CCCHHHHHHHHHCCC	8.42	27259358
760 (in isoform 2)	Ubiquitination	-	41.47	-
761	Phosphorylation	ENSEIYDYLRQGNRL CHHHHHHHHHCCCCC	6.19	27642862
769	Ubiquitination	LRQGNRLKQPADCLD HHCCCCCCCHHHHHH	51.50	-
772	Phosphorylation	GNRLKQPADCLDGLY CCCCCCHHHHHHHHH	20.04	9178760
779	Phosphorylation	ADCLDGLYALMSRCW HHHHHHHHHHHHHHH	11.83	27259358
806	Phosphorylation	LREDLENTLKALPPA HHHHHHHHHHHCCCC	21.91	23403867
814	Phosphorylation	LKALPPAQEPDEILY HHHCCCCCCCCCEEE	69.40	9178760
821	Phosphorylation	QEPDEILYVNMDEGG CCCCCEEEEECCCCC	8.74	27259358
830	Phosphorylation	NMDEGGGYPEPPGAA ECCCCCCCCCCCCCC	14.01	27642862
853	Phosphorylation	PDPKDSCSCLTAAEV CCCCCCCCEEEEEEE	19.00	28555341
859	Phosphorylation	CSCLTAAEVHPAGRY CCEEEEEEEECCCCE	38.61	9178760
866	Phosphorylation	EVHPAGRYVLCPSTT EEECCCCEEECCCCC	9.24	22322096
871	Phosphorylation	GRYVLCPSTTPSPAQ CCEEECCCCCCCCCC	43.87	28152594
872	Phosphorylation	RYVLCPSTTPSPAQP CEEECCCCCCCCCCC	28.06	22199227
873	Phosphorylation	YVLCPSTTPSPAQPA EEECCCCCCCCCCCC	26.55	28152594
875	Phosphorylation	LCPSTTPSPAQPADR ECCCCCCCCCCCCCC	30.67	30175587
884	Phosphorylation	AQPADRGSPAAPGQE CCCCCCCCCCCCCCC	16.56	21712546

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
772	Y	Phosphorylation	Kinase	UFO	P30530	PhosphoELM
779	Y	Phosphorylation	Kinase	AXL	P30530	GPS
814	Y	Phosphorylation	Kinase	UFO	P30530	PhosphoELM
821	Y	Phosphorylation	Kinase	AXL	P30530	GPS
859	Y	Phosphorylation	Kinase	UFO	P30530	PhosphoELM
866	Y	Phosphorylation	Kinase	AXL	P30530	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UFO_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 UFO_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TNS2_HUMAN	TENC1	physical	12470648
GRB2_HUMAN	GRB2	physical	9178760
LCK_HUMAN	LCK	physical	9178760
SRC_HUMAN	SRC	physical	9178760
P85A_HUMAN	PIK3R1	physical	9178760
P85B_HUMAN	PIK3R2	physical	9178760
ACK1_HUMAN	TNK2	physical	19815557
HS90A_HUMAN	HSP90AA1	physical	23629654
RANB9_HUMAN	RANBP9	physical	15964779
TYRO3_HUMAN	TYRO3	physical	15964779
P85A_HUMAN	PIK3R1	physical	18346204
ABL2_HUMAN	ABL2	physical	18346204
GRB2_HUMAN	GRB2	physical	18346204

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of UFO_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-884, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.	18187866 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-702, AND MASSSPECTROMETRY.	19534553 [Abstract]
"In brain, Axl recruits Grb2 and the p85 regulatory subunit of PI3kinase; in vitro mutagenesis defines the requisite binding sites fordownstream Akt activation."; Weinger J.G., Gohari P., Yan Y., Backer J.M., Varnum B.,Shafit-Zagardo B.; J. Neurochem. 106:134-146(2008). Cited for: INTERACTION WITH GRB2; PIK3R1 AND PIK3R2, AND PHOSPHORYLATION ATTYR-779; TYR-821 AND TYR-866.	18346204 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-866, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-702 AND TYR-703, ANDMASS SPECTROMETRY.	18083107 [Abstract]