dbPTM

LST2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LST2_HUMAN
UniProt AC	Q9HCC9
Protein Name	Lateral signaling target protein 2 homolog
Gene Name	ZFYVE28
Organism	Homo sapiens (Human).
Sequence Length	887
Subcellular Localization	Cytoplasm, cytosol . Early endosome membrane . Localizes to early endosome membrane in absence of Lys-87 monoubiquitination. Localizes to cytosol when monoubiquitinated.
Protein Description	Negative regulator of epidermal growth factor receptor (EGFR) signaling. Acts by promoting EGFR degradation in endosomes when not monoubiquitinated..
Protein Sequence	MMNRFRKWLYKPKRSDPQLLARFYYADEELNQVAAELDSLDGRKDPQRCTLLVSQFRSCQDNVLNIINQIMDECIPQDRAPRDFCVKFPEEIRHDNLAGQLWFGAECLAAGSIIMNRELESMAMRPLAKELTRSLEDVRGALRDQALRDLNTYTEKMREALRHFDVLFAEFELSYVSAMVPVKSPREYYVQQEVIVLFCETVERALDFGYLTQDMIDDYEPALMFSIPRLAIVCGLVVYADGPLNLDRKVEDMSELFRPFHTLLRKIRDLLQTLTEEELHTLERNLCISQDVEFPIRADVQGPAALAPALSAPLPPEGPLSAKAKDPDAELACSMQYDDQELEQLSRMVHRAGDEMSSLLSPPIACQSPAHRPGAEGSPGGEASPGRPRLRSGSDEEERVFFMDDVEGTAEALARPESPAGPFGWAGSTWADPQEKGQGGPGGAAGISLPASEKEEDLSNNNLEAEGTDGASLAGTSSCSCLDSRLHLDGWEVGADDAETAEMIAHRTGGMKLSATVIFNPKSPTSLDSAVATQEAASEPVAEGMDGGPHKLSTGATNCLLHSCVCCGSCGDSREDVVERLREKCSPGGVIGASYAAGLAKASDRAPERQEEAPPPSEDASNGREPKAPTSDKCLPHTSGSQVDTASGLQGEAGVAGQQEPEARELHAGSPSAHEAPQALSGSSSSTAGSCSSDKMGPEAAPAATHAAPQATREKIRSRFHGSHDLIHRLFVCISGVADQLQTNYASDLRSILKTLFEVMATKPETDDKEKLRKVTQTLRSAALEDCALCQETLSSSELAAKTRDGDFEDPPEWVPDEACGFCTACKAPFTVIRRKHHCRSCGKIFCSRCSSHSAPLPRYGQVKPVRVCTHCYMFHVTPFYSDKAGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17 (in isoform 4)	Ubiquitination	-	28.15	21890473
17 (in isoform 3)	Ubiquitination	-	28.15	21890473
17	Neddylation	YKPKRSDPQLLARFY CCCCCCCHHHHHHHH	28.15	32015554
17	Ubiquitination	YKPKRSDPQLLARFY CCCCCCCHHHHHHHH	28.15	23000965
40	Neddylation	VAAELDSLDGRKDPQ HHHHHHCCCCCCCHH	8.92	32015554
40	Ubiquitination	VAAELDSLDGRKDPQ HHHHHHCCCCCCCHH	8.92	23000965
86	Ubiquitination	RAPRDFCVKFPEEIR CCCCCHHCCCCHHHC	7.85	21890473
87	Ubiquitination	APRDFCVKFPEEIRH CCCCHHCCCCHHHCC	57.28	23000965
87 (in isoform 1)	Ubiquitination	-	57.28	21890473
87 (in isoform 2)	Ubiquitination	-	57.28	21890473
87	Neddylation	APRDFCVKFPEEIRH CCCCHHCCCCHHHCC	57.28	32015554
239	Phosphorylation	IVCGLVVYADGPLNL HHCCCEEECCCCCCC	7.47	-
259 (in isoform 6)	Phosphorylation	-	20.31	22210691
260 (in isoform 6)	Phosphorylation	-	6.31	25022875
261 (in isoform 6)	Phosphorylation	-	20.49	25022875
262	Phosphorylation	ELFRPFHTLLRKIRD HHHHHHHHHHHHHHH	28.06	24260401
265 (in isoform 6)	Phosphorylation	-	35.15	22210691
270 (in isoform 6)	Phosphorylation	-	2.47	22210691
276 (in isoform 6)	Phosphorylation	-	53.22	25022875
321	Phosphorylation	LPPEGPLSAKAKDPD CCCCCCCCCCCCCCC	30.75	28787133
334	Phosphorylation	PDAELACSMQYDDQE CCCHHHHHCCCCHHH	11.87	22617229
337	Phosphorylation	ELACSMQYDDQELEQ HHHHHCCCCHHHHHH	16.91	23403867
346	Phosphorylation	DQELEQLSRMVHRAG HHHHHHHHHHHHHHH	20.30	27251275
368	Phosphorylation	SPPIACQSPAHRPGA CCCCCCCCCCCCCCC	24.76	27080861
378	Phosphorylation	HRPGAEGSPGGEASP CCCCCCCCCCCCCCC	16.33	27080861
384	Phosphorylation	GSPGGEASPGRPRLR CCCCCCCCCCCCCCC	24.47	27080861
392	Phosphorylation	PGRPRLRSGSDEEER CCCCCCCCCCCHHHE	47.44	28985074
394	Phosphorylation	RPRLRSGSDEEERVF CCCCCCCCCHHHEEE	42.99	28985074
514	Phosphorylation	RTGGMKLSATVIFNP HHCCCEEEEEEEECC	19.17	23186163
516	Phosphorylation	GGMKLSATVIFNPKS CCCEEEEEEEECCCC	15.68	28857561
523	Phosphorylation	TVIFNPKSPTSLDSA EEEECCCCCCCHHHH	34.37	22199227
525	Phosphorylation	IFNPKSPTSLDSAVA EECCCCCCCHHHHHH	49.35	22199227
526	Phosphorylation	FNPKSPTSLDSAVAT ECCCCCCCHHHHHHC	33.30	22199227
529	Phosphorylation	KSPTSLDSAVATQEA CCCCCHHHHHHCHHH	29.90	23312004
533	Phosphorylation	SLDSAVATQEAASEP CHHHHHHCHHHHHCC	21.97	23312004
538	Phosphorylation	VATQEAASEPVAEGM HHCHHHHHCCCCCCC	49.86	23312004
563	Phosphorylation	ATNCLLHSCVCCGSC CCCHHEECCCCCCCC	14.28	30624053
569	Phosphorylation	HSCVCCGSCGDSRED ECCCCCCCCCCCHHH	10.87	28985074
586	Phosphorylation	ERLREKCSPGGVIGA HHHHHHCCCCCCHHH	37.33	22777824
670	Phosphorylation	ARELHAGSPSAHEAP HHHHCCCCCCHHHCC	19.23	27080861
672	Phosphorylation	ELHAGSPSAHEAPQA HHCCCCCCHHHCCHH	43.91	27080861
718	Phosphorylation	ATREKIRSRFHGSHD HHHHHHHHHHCCCHH	42.65	24719451
751	Phosphorylation	NYASDLRSILKTLFE CCHHHHHHHHHHHHH	39.30	24719451
762	Phosphorylation	TLFEVMATKPETDDK HHHHHHCCCCCCCCH	29.09	29116813
766	Phosphorylation	VMATKPETDDKEKLR HHCCCCCCCCHHHHH	59.01	29116813
870	Phosphorylation	VKPVRVCTHCYMFHV CCCEEEECCEEEEEC	16.48	10997877

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
586	S	Phosphorylation	Kinase	MAP2K-FAMILY	-	GPS
586	S	Phosphorylation	Kinase	MAP2K	-	Uniprot
870	T	Phosphorylation	Kinase	MAP2K-FAMILY	-	GPS
870	T	Phosphorylation	Kinase	MAP2K	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
87	K	ubiquitylation		19460345
Monoubiquitination at Lys-87 prevents binding to phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes.

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 LST2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EGF_HUMAN	EGF	physical	19460345
TRIM3_MOUSE	Trim3	physical	19460345
RAB5A_HUMAN	RAB5A	physical	19460345
RAB4A_HUMAN	RAB4A	physical	19460345
RAB7A_HUMAN	RAB7A	physical	19460345
EGFR_HUMAN	EGFR	physical	19460345

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 LST2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Monoubiquitinylation regulates endosomal localization of Lst2, anegative regulator of EGF receptor signaling."; Mosesson Y., Chetrit D., Schley L., Berghoff J., Ziv T., Carvalho S.,Milanezi F., Admon A., Schmitt F., Ehrlich M., Yarden Y.; Dev. Cell 16:687-698(2009). Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN FYVE-TYPE ZINC FINGER,INTERACTION WITH TRIM3, PHOSPHORYLATION AT SER-586 AND THR-870,UBIQUITINATION AT LYS-87, AND MUTAGENESIS OF LYS-87 AND CYS-823.	19460345 [Abstract]
Ubiquitylation
Reference	PubMed
"Monoubiquitinylation regulates endosomal localization of Lst2, anegative regulator of EGF receptor signaling."; Mosesson Y., Chetrit D., Schley L., Berghoff J., Ziv T., Carvalho S.,Milanezi F., Admon A., Schmitt F., Ehrlich M., Yarden Y.; Dev. Cell 16:687-698(2009). Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN FYVE-TYPE ZINC FINGER,INTERACTION WITH TRIM3, PHOSPHORYLATION AT SER-586 AND THR-870,UBIQUITINATION AT LYS-87, AND MUTAGENESIS OF LYS-87 AND CYS-823.	19460345 [Abstract]

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