dbPTM

LRC59_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LRC59_HUMAN
UniProt AC	Q96AG4
Protein Name	Leucine-rich repeat-containing protein 59
Gene Name	LRRC59
Organism	Homo sapiens (Human).
Sequence Length	307
Subcellular Localization	Microsome membrane Single-pass type II membrane protein. Endoplasmic reticulum membrane Single-pass type II membrane protein. Nucleus envelope. Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1.
Protein Description	Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores..
Protein Sequence	MTKAGSKGGNLRDKLDGNELDLSLSDLNEVPVKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLQQLPADFGRLVNLQHLDLLNNKLVTLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQAPKSKSGSRPRKPPPRKHTRSWAVLKLLLLLLLFGVAGGLVACRVTELQQQPLCTSVNTIYDNAVQGLRRHEILQWVLQTDSQQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTKAGSKG -------CCCCCCCC	8.60	25944712
2	Acetylation	------MTKAGSKGG ------CCCCCCCCC	29.60	25489052
6	Phosphorylation	--MTKAGSKGGNLRD --CCCCCCCCCCHHH	32.74	21955146
7	Ubiquitination	-MTKAGSKGGNLRDK -CCCCCCCCCCHHHC	70.67	24816145
14	Ubiquitination	KGGNLRDKLDGNELD CCCCHHHCCCCCEEC	41.88	21906983
14	Acetylation	KGGNLRDKLDGNELD CCCCHHHCCCCCEEC	41.88	23236377
23	Phosphorylation	DGNELDLSLSDLNEV CCCEECCCHHHHCCC	26.03	30266825
25	Phosphorylation	NELDLSLSDLNEVPV CEECCCHHHHCCCCH	36.35	30266825
33	Ubiquitination	DLNEVPVKELAALPK HHCCCCHHHHHHCCC	40.72	21906983
33	2-Hydroxyisobutyrylation	DLNEVPVKELAALPK HHCCCCHHHHHHCCC	40.72	-
33	Acetylation	DLNEVPVKELAALPK HHCCCCHHHHHHCCC	40.72	26051181
40	Acetylation	KELAALPKATILDLS HHHHHCCCCEEEECC	60.04	26051181
40	Ubiquitination	KELAALPKATILDLS HHHHHCCCCEEEECC	60.04	23000965
40	Ubiquitination	KELAALPKATILDLS HHHHHCCCCEEEECC	60.04	21890473
40	2-Hydroxyisobutyrylation	KELAALPKATILDLS HHHHHCCCCEEEECC	60.04	-
47	Phosphorylation	KATILDLSCNKLTTL CCEEEECCCCCCCCC	18.47	21712546
48	S-nitrosocysteine	ATILDLSCNKLTTLP CEEEECCCCCCCCCC	7.28	-
48	Glutathionylation	ATILDLSCNKLTTLP CEEEECCCCCCCCCC	7.28	22555962
48	S-nitrosylation	ATILDLSCNKLTTLP CEEEECCCCCCCCCC	7.28	19483679
50	Acetylation	ILDLSCNKLTTLPSD EEECCCCCCCCCCCC	52.08	26051181
50	Ubiquitination	ILDLSCNKLTTLPSD EEECCCCCCCCCCCC	52.08	32015554
52	Phosphorylation	DLSCNKLTTLPSDFC ECCCCCCCCCCCCCC	28.09	28348404
53	Phosphorylation	LSCNKLTTLPSDFCG CCCCCCCCCCCCCCC	47.29	28348404
56	Phosphorylation	NKLTTLPSDFCGLTH CCCCCCCCCCCCCHH	46.56	28348404
59	S-nitrosylation	TTLPSDFCGLTHLVK CCCCCCCCCCHHHHH	5.39	19483679
59	Glutathionylation	TTLPSDFCGLTHLVK CCCCCCCCCCHHHHH	5.39	22555962
59	S-nitrosocysteine	TTLPSDFCGLTHLVK CCCCCCCCCCHHHHH	5.39	-
66	2-Hydroxyisobutyrylation	CGLTHLVKLDLSKNK CCCHHHHHHCCCCCH	42.52	-
66	Ubiquitination	CGLTHLVKLDLSKNK CCCHHHHHHCCCCCH	42.52	21890473
66	Ubiquitination	CGLTHLVKLDLSKNK CCCHHHHHHCCCCCH	42.52	22817900
71	Acetylation	LVKLDLSKNKLQQLP HHHHCCCCCHHHCCC	66.45	23749302
71	2-Hydroxyisobutyrylation	LVKLDLSKNKLQQLP HHHHCCCCCHHHCCC	66.45	-
71	Ubiquitination	LVKLDLSKNKLQQLP HHHHCCCCCHHHCCC	66.45	23000965
73	Succinylation	KLDLSKNKLQQLPAD HHCCCCCHHHCCCCC	51.95	-
73	Malonylation	KLDLSKNKLQQLPAD HHCCCCCHHHCCCCC	51.95	26320211
73	Ubiquitination	KLDLSKNKLQQLPAD HHCCCCCHHHCCCCC	51.95	23000965
73	Ubiquitination	KLDLSKNKLQQLPAD HHCCCCCHHHCCCCC	51.95	21890473
73	Succinylation	KLDLSKNKLQQLPAD HHCCCCCHHHCCCCC	51.95	-
73	2-Hydroxyisobutyrylation	KLDLSKNKLQQLPAD HHCCCCCHHHCCCCC	51.95	-
73	Acetylation	KLDLSKNKLQQLPAD HHCCCCCHHHCCCCC	51.95	23749302
96	Ubiquitination	HLDLLNNKLVTLPVS HHHHHCCCEEEEECC	43.17	21963094
96	Acetylation	HLDLLNNKLVTLPVS HHHHHCCCEEEEECC	43.17	26051181
99	Phosphorylation	LLNNKLVTLPVSFAQ HHCCCEEEEECCHHH	35.46	28102081
103	Phosphorylation	KLVTLPVSFAQLKNL CEEEEECCHHHHCCC	16.96	28102081
108	Ubiquitination	PVSFAQLKNLKWLDL ECCHHHHCCCCCCCC	48.42	21963094
108	Acetylation	PVSFAQLKNLKWLDL ECCHHHHCCCCCCCC	48.42	25953088
108	2-Hydroxyisobutyrylation	PVSFAQLKNLKWLDL ECCHHHHCCCCCCCC	48.42	-
111	Malonylation	FAQLKNLKWLDLKDN HHHHCCCCCCCCCCC	55.92	26320211
111	Ubiquitination	FAQLKNLKWLDLKDN HHHHCCCCCCCCCCC	55.92	21890473
111	Acetylation	FAQLKNLKWLDLKDN HHHHCCCCCCCCCCC	55.92	25825284
111	2-Hydroxyisobutyrylation	FAQLKNLKWLDLKDN HHHHCCCCCCCCCCC	55.92	-
111	Ubiquitination	FAQLKNLKWLDLKDN HHHHCCCCCCCCCCC	55.92	22817900
116	2-Hydroxyisobutyrylation	NLKWLDLKDNPLDPV CCCCCCCCCCCCCHH	55.94	-
116	Ubiquitination	NLKWLDLKDNPLDPV CCCCCCCCCCCCCHH	55.94	21906983
116	Acetylation	NLKWLDLKDNPLDPV CCCCCCCCCCCCCHH	55.94	26051181
126	2-Hydroxyisobutyrylation	PLDPVLAKVAGDCLD CCCHHHHHHHHHCCC	28.58	-
126	Ubiquitination	PLDPVLAKVAGDCLD CCCHHHHHHHHHCCC	28.58	21963094
126	Acetylation	PLDPVLAKVAGDCLD CCCHHHHHHHHHCCC	28.58	25953088
131	Glutathionylation	LAKVAGDCLDEKQCK HHHHHHHCCCHHHHH	5.16	22555962
131	S-nitrosylation	LAKVAGDCLDEKQCK HHHHHHHCCCHHHHH	5.16	19483679
131	S-nitrosocysteine	LAKVAGDCLDEKQCK HHHHHHHCCCHHHHH	5.16	-
135	2-Hydroxyisobutyrylation	AGDCLDEKQCKQCAN HHHCCCHHHHHHHHH	61.74	-
135	Malonylation	AGDCLDEKQCKQCAN HHHCCCHHHHHHHHH	61.74	26320211
135	Ubiquitination	AGDCLDEKQCKQCAN HHHCCCHHHHHHHHH	61.74	21963094
135	Succinylation	AGDCLDEKQCKQCAN HHHCCCHHHHHHHHH	61.74	27452117
135	Acetylation	AGDCLDEKQCKQCAN HHHCCCHHHHHHHHH	61.74	23749302
138	Ubiquitination	CLDEKQCKQCANKVL CCCHHHHHHHHHHHH	46.01	22817900
143	Malonylation	QCKQCANKVLQHMKA HHHHHHHHHHHHHHH	26.29	26320211
143	Acetylation	QCKQCANKVLQHMKA HHHHHHHHHHHHHHH	26.29	25953088
149	Ubiquitination	NKVLQHMKAVQADQE HHHHHHHHHHHHHHH	43.19	21963094
149	Acetylation	NKVLQHMKAVQADQE HHHHHHHHHHHHHHH	43.19	25953088
149	Malonylation	NKVLQHMKAVQADQE HHHHHHHHHHHHHHH	43.19	26320211
149	2-Hydroxyisobutyrylation	NKVLQHMKAVQADQE HHHHHHHHHHHHHHH	43.19	-
192	Ubiquitination	RELRKREKAEEKERR HHHHHHHHHHHHHHH	66.19	24816145
201	2-Hydroxyisobutyrylation	EEKERRRKEYDALKA HHHHHHHHHHHHHHH	59.83	-
201	Ubiquitination	EEKERRRKEYDALKA HHHHHHHHHHHHHHH	59.83	33845483
203	Phosphorylation	KERRRKEYDALKAAK HHHHHHHHHHHHHHH	15.00	28796482
207	Malonylation	RKEYDALKAAKREQE HHHHHHHHHHHHHHH	48.28	26320211
207	Ubiquitination	RKEYDALKAAKREQE HHHHHHHHHHHHHHH	48.28	33845483
207	Methylation	RKEYDALKAAKREQE HHHHHHHHHHHHHHH	48.28	115972615
207	Acetylation	RKEYDALKAAKREQE HHHHHHHHHHHHHHH	48.28	25953088
216	Ubiquitination	AKREQEKKPKKEANQ HHHHHHHCCHHHHHC	62.41	24816145
226	Ubiquitination	KEANQAPKSKSGSRP HHHHCCCCCCCCCCC	73.80	33845483
305	Phosphorylation	QWVLQTDSQQ----- HHHHHHCCCC-----	33.59	-

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 LRC59_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LRC59_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 LRC59_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
A4_HUMAN	APP	physical	21832049

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 LRC59_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-25, AND MASSSPECTROMETRY.	18669648 [Abstract]