DCXR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DCXR_HUMAN
• UniProt AC: Q7Z4W1
• Protein Name: L-xylulose reductase
• Gene Name: DCXR
• Organism: Homo sapiens (Human).
• Sequence Length: 244
• Subcellular Localization: Membrane; Peripheral membrane protein. Probably recruited to membranes via an interaction with phosphatidylinositol..
• Protein Description: Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules..
• Protein Sequence: MELFLAGRRVLVTGAGKGIGRGTVQALHATGARVVAVSRTQADLDSLVRECPGIEPVCVDLGDWEATERALGSVGPVDLLVNNAAVALLQPFLEVTKEAFDRSFEVNLRAVIQVSQIVARGLIARGVPGAIVNVSSQCSQRAVTNHSVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTSMGQATWSDPHKAKTMLNRIPLGKFAEVEHVVNAILFLLSDRSGMTTGSTLPVEGGFWAC

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
1	Acetylation	-------MELFLAGR -------CCEEECCC	10.22	22814378
17	Acetylation	VLVTGAGKGIGRGTV EEEECCCCCCCHHHH	46.98	26051181
17	Ubiquitination	VLVTGAGKGIGRGTV EEEECCCCCCCHHHH	46.98	21906983
17	Malonylation	VLVTGAGKGIGRGTV EEEECCCCCCCHHHH	46.98	26320211
21	Methylation	GAGKGIGRGTVQALH CCCCCCCHHHHHHHH	35.37	24129315
23	Phosphorylation	GKGIGRGTVQALHAT CCCCCHHHHHHHHHC	14.21	-
38	Phosphorylation	GARVVAVSRTQADLD CCEEEEEECCHHHHH	21.63	23312004
40	Phosphorylation	RVVAVSRTQADLDSL EEEEEECCHHHHHHH	22.17	24275569
46	Phosphorylation	RTQADLDSLVRECPG CCHHHHHHHHHHCCC	35.74	28857561
67	Phosphorylation	DLGDWEATERALGSV ECCCHHHHHHHHCCC	17.94	24275569
102	Methylation	VTKEAFDRSFEVNLR HHHHHHHCCCCCCHH	36.47	-
115	Phosphorylation	LRAVIQVSQIVARGL HHHHHHHHHHHHHHH	9.60	22210691
135	Phosphorylation	PGAIVNVSSQCSQRA CCEEEECCCHHHCCC	14.97	22210691
144	Phosphorylation	QCSQRAVTNHSVYCS HHHCCCCCCCCHHHC	26.65	28152594
147	Phosphorylation	QRAVTNHSVYCSTKG CCCCCCCCHHHCHHH	19.49	28152594
149	Phosphorylation	AVTNHSVYCSTKGAL CCCCCCHHHCHHHHH	5.45	27273156
151	Phosphorylation	TNHSVYCSTKGALDM CCCCHHHCHHHHHHH	18.57	28152594
152	Phosphorylation	NHSVYCSTKGALDML CCCHHHCHHHHHHHH	29.90	28152594
153	Ubiquitination	HSVYCSTKGALDMLT CCHHHCHHHHHHHHH	26.37	-
161	Ubiquitination	GALDMLTKVMALELG HHHHHHHHHHHHHHC	26.50	21890473
171	Malonylation	ALELGPHKIRVNAVN HHHHCCCEEEEECCC	35.03	32601280
171	Acetylation	ALELGPHKIRVNAVN HHHHCCCEEEEECCC	35.03	25953088
171	Ubiquitination	ALELGPHKIRVNAVN HHHHCCCEEEEECCC	35.03	21890473
180	Phosphorylation	RVNAVNPTVVMTSMG EEECCCCCEEEEECC	22.11	24275569
184	Phosphorylation	VNPTVVMTSMGQATW CCCCEEEEECCCCCC	12.17	28857561
185	Phosphorylation	NPTVVMTSMGQATWS CCCEEEEECCCCCCC	11.65	28857561
190	Phosphorylation	MTSMGQATWSDPHKA EEECCCCCCCCHHHH	20.02	28857561
192	Phosphorylation	SMGQATWSDPHKAKT ECCCCCCCCHHHHHH	36.59	28857561
196	Ubiquitination	ATWSDPHKAKTMLNR CCCCCHHHHHHHHHC	57.90	21890473
198	Ubiquitination	WSDPHKAKTMLNRIP CCCHHHHHHHHHCCC	38.99	-
199	Phosphorylation	SDPHKAKTMLNRIPL CCHHHHHHHHHCCCC	31.58	22798277
227	Phosphorylation	LFLLSDRSGMTTGST HHHHHCCCCCCCCCC	37.60	28787133
230	Phosphorylation	LSDRSGMTTGSTLPV HHCCCCCCCCCCEEC	31.37	28787133
231	Phosphorylation	SDRSGMTTGSTLPVE HCCCCCCCCCCEECC	21.90	28787133
233	Phosphorylation	RSGMTTGSTLPVEGG CCCCCCCCCEECCCC	25.36	28787133

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DCXR_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DCXR_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 DCXR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
DCXR_HUMAN	DCXR	physical	25416956
CK054_HUMAN	C11orf54	physical	26344197
CAB39_HUMAN	CAB39	physical	26344197
CB39L_HUMAN	CAB39L	physical	26344197
AATC_HUMAN	GOT1	physical	26344197

Drug and Disease Associations

• Kegg Disease
• H01065: Pentosuria
• OMIM Disease
• 260800: Pentosuria (PNTSU)
• 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

Acetylation

"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 1-8, AND ACETYLATION AT MET-1.
PubMed: 12665801

Phosphorylation

"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-149, AND MASSSPECTROMETRY.
PubMed: 18083107