GTR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GTR1_HUMAN
• UniProt AC: P11166
• Protein Name: Solute carrier family 2, facilitated glucose transporter member 1
• Gene Name: SLC2A1
• Organism: Homo sapiens (Human).
• Sequence Length: 492
• Subcellular Localization: Cell membrane; Multi-pass membrane protein. Melanosome. Localizes primarily at the cell surface. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
• Protein Description: Facilitative glucose transporter. This isoform may be responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses..
• Protein Sequence: MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV

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	-------MEPSSKKL -------CCCCHHHH	18.03	22814378
4	Phosphorylation	----MEPSSKKLTGR ----CCCCHHHHHHH	41.29	28509920
5	Phosphorylation	---MEPSSKKLTGRL ---CCCCHHHHHHHH	44.52	29083192
45	N-linked_Glycosylation	KVIEEFYNQTWVHRY HHHHHHHCCCCHHHC	37.82	3839598
45	N-linked_Glycosylation	KVIEEFYNQTWVHRY HHHHHHHCCCCHHHC	37.82	8662691
113	Phosphorylation	SAVLMGFSKLGKSFE HHHHHCHHHHCHHHH	22.65	20860994
118	Phosphorylation	GFSKLGKSFEMLILG CHHHHCHHHHHHHHH	25.33	20068231
226	Phosphorylation	NEENRAKSVLKKLRG CHHHHHHHHHHHHHC	31.53	20815410
234	Phosphorylation	VLKKLRGTADVTHDL HHHHHHCCCCCHHCH	17.16	25159151
238	Phosphorylation	LRGTADVTHDLQEMK HHCCCCCHHCHHHHH	15.37	21712546
244	Sulfoxidation	VTHDLQEMKEESRQM CHHCHHHHHHHHHHH	4.22	30846556
245	Ubiquitination	THDLQEMKEESRQMM HHCHHHHHHHHHHHH	58.54	21906983
245	Acetylation	THDLQEMKEESRQMM HHCHHHHHHHHHHHH	58.54	26051181
248	Phosphorylation	LQEMKEESRQMMREK HHHHHHHHHHHHHHH	28.98	23025827
258	Phosphorylation	MMREKKVTILELFRS HHHHHCCHHHHHHCC	28.82	-
459	Phosphorylation	VPETKGRTFDEIASG CCCCCCCCHHHHHHH	44.07	29514088
465	Phosphorylation	RTFDEIASGFRQGGA CCHHHHHHHHHCCCC	44.09	19664994
465	O-linked_Glycosylation	RTFDEIASGFRQGGA CCHHHHHHHHHCCCC	44.09	19664994
473	Phosphorylation	GFRQGGASQSDKTPE HHHCCCCCCCCCCHH	33.23	30266825
475	Phosphorylation	RQGGASQSDKTPEEL HCCCCCCCCCCHHHH	38.28	30266825
477	Acetylation	GGASQSDKTPEELFH CCCCCCCCCHHHHCC	71.83	26051181
477	Sumoylation	GGASQSDKTPEELFH CCCCCCCCCHHHHCC	71.83	-
477	Ubiquitination	GGASQSDKTPEELFH CCCCCCCCCHHHHCC	71.83	21906983
478	Phosphorylation	GASQSDKTPEELFHP CCCCCCCCHHHHCCC	40.71	30266825
490	Phosphorylation	FHPLGADSQV----- CCCCCCCCCC-----	32.10	19664994

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
226	S	Phosphorylation	Kinase	PRKCB	P05771	Uniprot
490	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
226	S	Phosphorylation	Phosphorylation at Ser-226 by PKC promotes glucose uptake by increasing cell membrane localization.	25982116

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GTR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSN6_HUMAN	COPS6	physical	16169070
FAK2_HUMAN	PTK2B	physical	11007796
CALX_HUMAN	CANX	physical	8662691
LMP1_EBVB9	LMP1	physical	28732079

Drug and Disease Associations

• Kegg Disease
• H00831: Primary dystonia
• H00836: GLUT1 deficiency syndrome (GLUT1DS); Glucose transport defect of the blood-brain barrier
• OMIM Disease
• 606777: GLUT1 deficiency syndrome 1 (GLUT1DS1)
• 612126: GLUT1 deficiency syndrome 2 (GLUT1DS2)
• 614847: Epilepsy, idiopathic generalized 12 (EIG12)
• 601042: Dystonia 9 (DYT9)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00292: Etomidate

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45, AND MASS SPECTROMETRY.
PubMed: 19349973

"Sequence and structure of a human glucose transporter.";
Mueckler M., Caruso C., Baldwin S.A., Panico M., Blench I.,Morris H.R., Allard W.J., Lienhard G.E., Lodish H.F.;
Science 229:941-945(1985).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION ATASN-45, LACK OF GLYCOSYLATION AT ASN-411, AND MASS SPECTROMETRY.
PubMed: 3839598

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, AND MASSSPECTROMETRY.
PubMed: 17525332