GMDS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GMDS_HUMAN
• UniProt AC: O60547
• Protein Name: GDP-mannose 4,6 dehydratase
• Gene Name: GMDS
• Organism: Homo sapiens (Human).
• Sequence Length: 372
• Protein Description: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose..
• Protein Sequence: MAHAPARCPSARGSGDGEMGKPRNVALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTGRIEHLYKNPQAHIEGNMKLHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDLAEYTADVDGVGTLRLLDAVKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVVNFREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATGEVHSVREFVEKSFLHIGKTIVWEGKNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCTKAKQKLNWKPRVAFDELVREMVHADVELMRTNPNA

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
2	Acetylation	------MAHAPARCP ------CCCCCCCCC	13.93	19413330
10	Phosphorylation	HAPARCPSARGSGDG CCCCCCCCCCCCCCC	33.94	25159151
14	Phosphorylation	RCPSARGSGDGEMGK CCCCCCCCCCCCCCC	28.32	29255136
19	Sulfoxidation	RGSGDGEMGKPRNVA CCCCCCCCCCCCEEE	11.62	30846556
21	Ubiquitination	SGDGEMGKPRNVALI CCCCCCCCCCEEEEE	39.22	-
29	Phosphorylation	PRNVALITGITGQDG CCEEEEEECCCCCCC	24.31	22210691
37	Phosphorylation	GITGQDGSYLAEFLL CCCCCCCCHHHHHHH	25.84	22210691
38	Phosphorylation	ITGQDGSYLAEFLLE CCCCCCCHHHHHHHH	18.56	22210691
40	Ubiquitination	GQDGSYLAEFLLEKG CCCCCHHHHHHHHCC	9.39	21963094
57	Phosphorylation	VHGIVRRSSSFNTGR EEEEEECCCCCCCCC	21.55	24043423
58	Phosphorylation	HGIVRRSSSFNTGRI EEEEECCCCCCCCCH	36.82	24043423
59	Phosphorylation	GIVRRSSSFNTGRIE EEEECCCCCCCCCHH	24.62	24043423
62	Phosphorylation	RRSSSFNTGRIEHLY ECCCCCCCCCHHHEE	26.31	24043423
65	Ubiquitination	SSFNTGRIEHLYKNP CCCCCCCHHHEECCC	4.07	29967540
69	Phosphorylation	TGRIEHLYKNPQAHI CCCHHHEECCCCCEE	15.61	22817900
70	Ubiquitination	GRIEHLYKNPQAHIE CCHHHEECCCCCEEC	69.39	21906983
70	Acetylation	GRIEHLYKNPQAHIE CCHHHEECCCCCEEC	69.39	23954790
71	Ubiquitination	RIEHLYKNPQAHIEG CHHHEECCCCCEECC	21.99	22817900
81	Acetylation	AHIEGNMKLHYGDLT CEECCCCEEECCCCC	35.79	25953088
81	Ubiquitination	AHIEGNMKLHYGDLT CEECCCCEEECCCCC	35.79	21963094
84	Phosphorylation	EGNMKLHYGDLTDST CCCCEEECCCCCCCE	23.83	21253578
92	Glutathionylation	GDLTDSTCLVKIINE CCCCCCEEEEEEHHC	4.81	22555962
95	Ubiquitination	TDSTCLVKIINEVKP CCCEEEEEEHHCCCC	25.56	29967540
95	Acetylation	TDSTCLVKIINEVKP CCCEEEEEEHHCCCC	25.56	26051181
101	Ubiquitination	VKIINEVKPTEIYNL EEEHHCCCCCEEEEC	39.79	21906983
110	Ubiquitination	TEIYNLGAQSHVKIS CEEEECCCCCCEEEE	15.74	29967540
131	Ubiquitination	TADVDGVGTLRLLDA CCCCCCCCHHHHHHH	25.26	29967540
138	Ubiquitination	GTLRLLDAVKTCGLI CHHHHHHHHHHCCCC	12.50	21963094
140	Acetylation	LRLLDAVKTCGLINS HHHHHHHHHCCCCCC	39.56	26051181
140	Ubiquitination	LRLLDAVKTCGLINS HHHHHHHHHCCCCCC	39.56	29967540
141	Phosphorylation	RLLDAVKTCGLINSV HHHHHHHHCCCCCCE	12.76	21406692
147	Phosphorylation	KTCGLINSVKFYQAS HHCCCCCCEEEEEEE	21.49	24719451
149	Ubiquitination	CGLINSVKFYQASTS CCCCCCEEEEEEEHH	37.87	-
161	Ubiquitination	STSELYGKVQEIPQK EHHHHHCCCEECCCC	27.47	29967540
168	Ubiquitination	KVQEIPQKETTPFYP CCEECCCCCCCCCCC	52.23	21963094
171	Phosphorylation	EIPQKETTPFYPRSP ECCCCCCCCCCCCCC	16.70	23532336
174	Phosphorylation	QKETTPFYPRSPYGA CCCCCCCCCCCCCHH	10.03	23532336
177	Phosphorylation	TTPFYPRSPYGAAKL CCCCCCCCCCHHHHH	20.26	28555341
214	Ubiquitination	FNHESPRRGANFVTR CCCCCCCCCCCHHHH	52.54	22817900
231	Phosphorylation	SRSVAKIYLGQLECF HHHHHHHHCCCEEEE	12.22	-
246	Ubiquitination	SLGNLDAKRDWGHAK ECCCCCCCCCCCHHH	51.02	-
271	Ubiquitination	QNDEPEDFVIATGEV HCCCCCCEEEEECCC	4.00	22817900
301	Ubiquitination	KTIVWEGKNENEVGR CEEEECCCCCCCCCC	49.96	21906983
308	Ubiquitination	KNENEVGRCKETGKV CCCCCCCCCCCCCCE	33.25	29967540
322	Acetylation	VHVTVDLKYYRPTEV EEEEEEEEEECCCCC	35.45	23749302
323	Phosphorylation	HVTVDLKYYRPTEVD EEEEEEEEECCCCCE	16.41	22115753
324	Phosphorylation	VTVDLKYYRPTEVDF EEEEEEEECCCCCEE	14.45	22115753
327	Phosphorylation	DLKYYRPTEVDFLQG EEEEECCCCCEECCC	39.37	26657352
338	Acetylation	FLQGDCTKAKQKLNW ECCCCCHHHHHHCCC	60.98	26051181
338	Ubiquitination	FLQGDCTKAKQKLNW ECCCCCHHHHHHCCC	60.98	29967540
340	Ubiquitination	QGDCTKAKQKLNWKP CCCCHHHHHHCCCCC	49.90	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GMDS_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 GMDS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GMDS_HUMAN	GMDS	physical	16189514
TNKS1_HUMAN	TNKS	physical	22645305
PUR9_HUMAN	ATIC	physical	22863883
CAN2_HUMAN	CAPN2	physical	22863883
CGL_HUMAN	CTH	physical	22863883
NSF1C_HUMAN	NSFL1C	physical	22863883
PTMA_HUMAN	PTMA	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
TATD1_HUMAN	TATDN1	physical	22863883
GMDS_HUMAN	GMDS	physical	25416956
NTAQ1_HUMAN	WDYHV1	physical	25416956
NDUA9_HUMAN	NDUFA9	physical	26344197
PSMG4_HUMAN	PSMG4	physical	26344197
TNKS2_HUMAN	TNKS2	physical	28514442
TNKS1_HUMAN	TNKS	physical	28514442

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330