dbPTM

DRG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DRG1_HUMAN
UniProt AC	Q9Y295
Protein Name	Developmentally-regulated GTP-binding protein 1
Gene Name	DRG1
Organism	Homo sapiens (Human).
Sequence Length	367
Subcellular Localization	Cytoplasm . The DRG1-DFRP2/ZC3H15 complex associates with polysomes.
Protein Description	Critical regulator of cell growth under specific conditions. Implicated in differentiation and cell cycle arrest..
Protein Sequence	MSSTLAKIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEGFDVAKTGDARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYLKLVRIYTKPKGQLPDYTSPVVLPYSRTTVEDFCMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSTLAKIA ------CCHHHHHHH	31.84	22814378
3	Phosphorylation	-----MSSTLAKIAE -----CCHHHHHHHH	26.58	24719451
7	Ubiquitination	-MSSTLAKIAEIEAE -CCHHHHHHHHHHHH	45.63	24816145
15	Sulfoxidation	IAEIEAEMARTQKNK HHHHHHHHHHHHHCH	3.84	21406390
18	Phosphorylation	IEAEMARTQKNKATA HHHHHHHHHHCHHHH	34.06	24719451
22	Ubiquitination	MARTQKNKATAHHLG HHHHHHCHHHHHHHH	54.90	29967540
22	Hydroxylation	MARTQKNKATAHHLG HHHHHHCHHHHHHHH	54.90	29915238
24	Phosphorylation	RTQKNKATAHHLGLL HHHHCHHHHHHHHHH	28.29	27422710
32	Ubiquitination	AHHLGLLKARLAKLR HHHHHHHHHHHHHHH	36.18	21963094
37	Ubiquitination	LLKARLAKLRRELIT HHHHHHHHHHHHHCC	47.31	22817900
46	Ubiquitination	RRELITPKGGGGGGP HHHHCCCCCCCCCCC	62.63	23000965
46	Malonylation	RRELITPKGGGGGGP HHHHCCCCCCCCCCC	62.63	26320211
61	Ubiquitination	GEGFDVAKTGDARIG CCCCCCCCCCCCEEE	53.54	23000965
61	2-Hydroxyisobutyrylation	GEGFDVAKTGDARIG CCCCCCCCCCCCEEE	53.54	-
94	Phosphorylation	VYSEVAAYEFTTLTT HHHHHHCEECCCCCC	11.22	-
100	Phosphorylation	AYEFTTLTTVPGVIR CEECCCCCCCCCEEE	24.53	18184589
101	Phosphorylation	YEFTTLTTVPGVIRY EECCCCCCCCCEEEE	28.02	18184589
109	Ubiquitination	VPGVIRYKGAKIQLL CCCEEEECCCEEEEE	42.41	22817900
112	Ubiquitination	VIRYKGAKIQLLDLP EEEECCCEEEEEECC	39.39	21906983
126	Ubiquitination	PGIIEGAKDGKGRGR CCHHCCCCCCCCCCH	77.27	21906983
129	Ubiquitination	IEGAKDGKGRGRQVI HCCCCCCCCCCHHHH	56.41	21906983
158	Ubiquitination	VLKPLGHKKIIENEL HHHHHCCHHHHHCHH	43.82	22817900
159	Ubiquitination	LKPLGHKKIIENELE HHHHCCHHHHHCHHC	43.15	21906983
175	Ubiquitination	FGIRLNSKPPNIGFK CCEECCCCCCCCCCC	64.52	21906983
182	Malonylation	KPPNIGFKKKDKGGI CCCCCCCCCCCCCCE	54.42	26320211
182	Acetylation	KPPNIGFKKKDKGGI CCCCCCCCCCCCCCE	54.42	25953088
182	Ubiquitination	KPPNIGFKKKDKGGI CCCCCCCCCCCCCCE	54.42	21906983
183	Ubiquitination	PPNIGFKKKDKGGIN CCCCCCCCCCCCCEE	65.03	22817900
184	Ubiquitination	PNIGFKKKDKGGINL CCCCCCCCCCCCEEC	66.32	22817900
186	Acetylation	IGFKKKDKGGINLTA CCCCCCCCCCEECEE	68.84	26051181
186	Ubiquitination	IGFKKKDKGGINLTA CCCCCCCCCCEECEE	68.84	21963094
206	Ubiquitination	ELDAETVKSILAEYK HCCHHHHHHHHHHHC	38.92	21963094
213	2-Hydroxyisobutyrylation	KSILAEYKIHNADVT HHHHHHHCCCCCCEE	29.06	-
213	Ubiquitination	KSILAEYKIHNADVT HHHHHHHCCCCCCEE	29.06	23000965
213	Acetylation	KSILAEYKIHNADVT HHHHHHHCCCCCCEE	29.06	25953088
213	Malonylation	KSILAEYKIHNADVT HHHHHHHCCCCCCEE	29.06	26320211
220	Phosphorylation	KIHNADVTLRSDATA CCCCCCEEECCCCCH	19.59	24719451
240	Phosphorylation	VVEGNRVYIPCIYVL HHCCCEEEEEEEEEE	8.91	29496907
245	Phosphorylation	RVYIPCIYVLNKIDQ EEEEEEEEEECCCCC	12.95	29496907
262	Phosphorylation	IEELDIIYKVPHCVP HHHCCEEEECCCCEE	13.28	25147952
263	Ubiquitination	EELDIIYKVPHCVPI HHCCEEEECCCCEEC	38.59	21963094
284	Ubiquitination	NFDDLLEKIWDYLKL CHHHHHHHHHHHHHH	49.41	23000965
290	Ubiquitination	EKIWDYLKLVRIYTK HHHHHHHHHHHHCCC	38.41	23000965
295	Phosphorylation	YLKLVRIYTKPKGQL HHHHHHHCCCCCCCC	9.72	27461979
296	Phosphorylation	LKLVRIYTKPKGQLP HHHHHHCCCCCCCCC	38.20	27461979
297	Ubiquitination	KLVRIYTKPKGQLPD HHHHHCCCCCCCCCC	27.97	21963094
299	Ubiquitination	VRIYTKPKGQLPDYT HHHCCCCCCCCCCCC	61.93	22817900
305	Phosphorylation	PKGQLPDYTSPVVLP CCCCCCCCCCCEEEC	13.74	28152594
306	Phosphorylation	KGQLPDYTSPVVLPY CCCCCCCCCCEEECC	33.65	28152594
307	Phosphorylation	GQLPDYTSPVVLPYS CCCCCCCCCEEECCC	14.96	28152594
313	Phosphorylation	TSPVVLPYSRTTVED CCCEEECCCCCCHHH	13.46	25884760
314	Phosphorylation	SPVVLPYSRTTVEDF CCEEECCCCCCHHHH	22.63	29496907
323	Sulfoxidation	TTVEDFCMKIHKNLI CCHHHHHHHHHHHHH	4.63	21406390
324	Ubiquitination	TVEDFCMKIHKNLIK CHHHHHHHHHHHHHH	42.72	29967540
327	Ubiquitination	DFCMKIHKNLIKEFK HHHHHHHHHHHHHHH	57.85	22817900
331	Acetylation	KIHKNLIKEFKYALV HHHHHHHHHHHHHHH	61.33	26051181
331	Ubiquitination	KIHKNLIKEFKYALV HHHHHHHHHHHHHHH	61.33	22817900
334	Ubiquitination	KNLIKEFKYALVWGL HHHHHHHHHHHHHCC	30.61	22817900
349	Ubiquitination	SVKHNPQKVGKDHTL CCCCCHHHCCCCCCC	54.96	22817900
352	Ubiquitination	HNPQKVGKDHTLEDE CCHHHCCCCCCCCCH	49.69	21906983
366	Ubiquitination	EDVIQIVKK------ HHHEHHHCC------	55.16	29967540
367	Acetylation	DVIQIVKK------- HHEHHHCC-------	55.46	18529277

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
100	T	Phosphorylation	Kinase	STK16	O75716	Uniprot
101	T	Phosphorylation	Kinase	STK16	O75716	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
22	K	Hydroxylation	29915238
Hydroxylated (with S stereochemistry) at C-3 of Lys-22 by JMJD7; this modification hinders trypsin-catalyzed proteolysis in vitro.
100	T	Phosphorylation	18184589
Phosphorylated at Thr-100 by STK16.

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 DRG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RWDD1_HUMAN	RWDD1	physical	16189514
CPNS1_HUMAN	CAPNS1	physical	16169070
ZC3HF_HUMAN	ZC3H15	physical	15676025
SKIL_HUMAN	SKIL	physical	25416956
COIL_HUMAN	COIL	physical	25416956
STK16_HUMAN	STK16	physical	25416956
RWDD1_HUMAN	RWDD1	physical	25416956
ZC3HF_HUMAN	ZC3H15	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
LRC41_HUMAN	LRRC41	physical	26186194
ZC3HF_HUMAN	ZC3H15	physical	26186194
NTM1A_HUMAN	NTMT1	physical	26186194
HAOX1_HUMAN	HAO1	physical	26186194
CAND1_HUMAN	CAND1	physical	26344197
CAND2_HUMAN	CAND2	physical	26344197
IFRD2_HUMAN	IFRD2	physical	26344197
KIF23_HUMAN	KIF23	physical	26344197
NAA15_HUMAN	NAA15	physical	26344197
ZC3HF_HUMAN	ZC3H15	physical	21516116
LRC41_HUMAN	LRRC41	physical	28514442
NTM1A_HUMAN	NTMT1	physical	28514442
ZC3HF_HUMAN	ZC3H15	physical	28514442
OSCP1_HUMAN	OSCP1	physical	28514442
SARNP_HUMAN	SARNP	physical	27173435
CHRD1_HUMAN	CHORDC1	physical	27173435
ZCCHV_HUMAN	ZC3HAV1	physical	27173435
SEPT7_HUMAN	SEPT7	physical	27173435
PRCC_HUMAN	PRCC	physical	27173435

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 DRG1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Structure of the human protein kinase MPSK1 reveals an atypicalactivation loop architecture."; Eswaran J., Bernad A., Ligos J.M., Guinea B., Debreczeni J.E.,Sobott F., Parker S.A., Najmanovich R., Turk B.E., Knapp S.; Structure 16:115-124(2008). Cited for: PHOSPHORYLATION AT THR-100, AND MASS SPECTROMETRY.	18184589 [Abstract]

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