dbPTM

PCKGC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCKGC_HUMAN
UniProt AC	P35558
Protein Name	Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Gene Name	PCK1 {ECO:0000312\|HGNC:HGNC:8724}
Organism	Homo sapiens (Human).
Sequence Length	622
Subcellular Localization	Cytoplasm.
Protein Description	Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle..
Protein Sequence	MPPQLQNGLNLSAKVVQGSLDSLPQAVREFLENNAELCQPDHIHICDGSEEENGRLLGQMEEEGILRRLKKYDNCWLALTDPRDVARIESKTVIVTQEQRDTVPIPKTGLSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGTPVLEAVGDGEFVKCLHSVGCPLPLQKPLVNNWPCNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGITNPEGEKKYLAAAFPSACGKTNLAMMNPSLPGWKVECVGDDIAWMKFDAQGHLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLASGVTITSWKNKEWSSEDGEPCAHPNSRFCTPASQCPIIDAAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPFAMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKEGKFLWPGFGENSRVLEWMFNRIDGKASTKLTPIGYIPKEDALNLKGLGHINMMELFSISKEFWEKEVEDIEKYLEDQVNADLPCEIEREILALKQRISQM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Phosphorylation	SAKVVQGSLDSLPQA CCEEHHCCHHHHHHH	16.35	29116813
22	Phosphorylation	VVQGSLDSLPQAVRE EHHCCHHHHHHHHHH	47.44	28857561
70	Acetylation	EGILRRLKKYDNCWL HHHHHHHHHCCCEEE	47.69	20167786
71	Acetylation	GILRRLKKYDNCWLA HHHHHHHHCCCEEEE	63.53	20167786
72	Phosphorylation	ILRRLKKYDNCWLAL HHHHHHHCCCEEEEE	15.71	28509920
90	Phosphorylation	RDVARIESKTVIVTQ HHHHHCCCCEEEEEC	31.12	32322062
91	Acetylation	DVARIESKTVIVTQE HHHHCCCCEEEEECC	33.74	30193097
102	O-linked_Glycosylation	VTQEQRDTVPIPKTG EECCCCCCCCCCCCC	30.30	31492838
111	Phosphorylation	PIPKTGLSQLGRWMS CCCCCCHHHHCCCCC	25.38	28857561
111	Ubiquitination	PIPKTGLSQLGRWMS CCCCCCHHHHCCCCC	25.38	22817900
112	Ubiquitination	IPKTGLSQLGRWMSE CCCCCHHHHCCCCCH	53.64	22817900
118	Phosphorylation	SQLGRWMSEEDFEKA HHHCCCCCHHHHHHH	30.76	28857561
124	Ubiquitination	MSEEDFEKAFNARFP CCHHHHHHHHHCCCC	59.27	32015554
140	Phosphorylation	CMKGRTMYVIPFSMG CCCCCEEEEEECCCC	8.46	29116813
145	Phosphorylation	TMYVIPFSMGPLGSP EEEEEECCCCCCCCC	19.92	29116813
151	Phosphorylation	FSMGPLGSPLSKIGI CCCCCCCCCHHHHCE	30.28	29116813
154	Phosphorylation	GPLGSPLSKIGIELT CCCCCCHHHHCEEEC	26.13	29116813
163	Phosphorylation	IGIELTDSPYVVASM HCEEECCCCCEEEEH	16.94	29116813
165	Phosphorylation	IELTDSPYVVASMRI EEECCCCCEEEEHHH	16.11	29116813
169	Phosphorylation	DSPYVVASMRIMTRM CCCCEEEEHHHHHCC	9.29	29116813
178	Phosphorylation	RIMTRMGTPVLEAVG HHHHCCCCCEEEEEC	10.81	-
230	Phosphorylation	PDRREIISFGSGYGG CCCCEEEEECCCCCC	29.26	26074081
233	Phosphorylation	REIISFGSGYGGNSL CEEEEECCCCCCCHH	27.16	28152594
235	Phosphorylation	IISFGSGYGGNSLLG EEEECCCCCCCHHHH	24.45	28152594
239	Phosphorylation	GSGYGGNSLLGKKCF CCCCCCCHHHHHHHH	28.39	27080861
243	Ubiquitination	GGNSLLGKKCFALRM CCCHHHHHHHHHHHH	46.46	22817900
243	Malonylation	GGNSLLGKKCFALRM CCCHHHHHHHHHHHH	46.46	26320211
244	Ubiquitination	GNSLLGKKCFALRMA CCHHHHHHHHHHHHH	32.55	22817900
252	Phosphorylation	CFALRMASRLAKEEG HHHHHHHHHHHHHHC	20.63	26074081
286	Phosphorylation	YLAAAFPSACGKTNL HHHHHCHHCCCCCCC	29.72	28857561
291	Phosphorylation	FPSACGKTNLAMMNP CHHCCCCCCCCCCCC	22.28	20068231
299	Phosphorylation	NLAMMNPSLPGWKVE CCCCCCCCCCCCEEE	42.04	20068231
340	Phosphorylation	FGVAPGTSVKTNPNA EEECCCCCCCCCCCH	27.77	28857561
471	Ubiquitination	ATAAAEHKGKIIMHD HHHHHHHCCEEEEEC	54.10	-
473	Succinylation	AAAEHKGKIIMHDPF HHHHHCCEEEEECCC	33.59	27452117
473	Malonylation	AAAEHKGKIIMHDPF HHHHHCCEEEEECCC	33.59	26320211
473	Acetylation	AAAEHKGKIIMHDPF HHHHHCCEEEEECCC	33.59	25825284
521	Acetylation	VNWFRKDKEGKFLWP ECEECCCCCCCCCCC	71.98	-
524	Acetylation	FRKDKEGKFLWPGFG ECCCCCCCCCCCCCC	38.07	-
549	Phosphorylation	NRIDGKASTKLTPIG HHCCCCCCCCEEECE	29.57	28509920
550	Phosphorylation	RIDGKASTKLTPIGY HCCCCCCCCEEECEE	34.63	28509920
553	Phosphorylation	GKASTKLTPIGYIPK CCCCCCEEECEEECH	17.89	28509920
557	Phosphorylation	TKLTPIGYIPKEDAL CCEEECEEECHHHHC	18.12	20068231
594	Acetylation	KEVEDIEKYLEDQVN HHHHHHHHHHHHHHC	56.31	20167786
595	Phosphorylation	EVEDIEKYLEDQVNA HHHHHHHHHHHHHCC	11.52	18452278

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
90	S	Phosphorylation	Kinase	AKT1	P31749	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	UBR5	O95071	PMID:21726808

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
90	S	Phosphorylation	32322062
Phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes the protein kinase activity: phosphorylated PCK1 translocates to the endoplasmic reticulum, where it phosphorylates INSIG1 and INSIG2.
91	K	Acetylation	30193097
Deacetylation of Lys-91 is carried out by SIRT1 and depends on PCK1 phosphorylation levels.
91	K	Phosphorylation	30193097
Deacetylation of Lys-91 is carried out by SIRT1 and depends on PCK1 phosphorylation levels.

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 PCKGC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRS6B_HUMAN	PSMC4	physical	21726808
1C07_HUMAN	HLA-C	physical	21726808
1433T_HUMAN	YWHAQ	physical	21726808
ABCB7_HUMAN	ABCB7	physical	21726808
ACTB_HUMAN	ACTB	physical	21726808
AT2A1_HUMAN	ATP2A1	physical	21726808
BASI_HUMAN	BSG	physical	21726808
BAG6_HUMAN	BAG6	physical	21726808
CH60_HUMAN	HSPD1	physical	21726808
CPT1A_HUMAN	CPT1A	physical	21726808
DNJA1_HUMAN	DNAJA1	physical	21726808
GNAI1_HUMAN	GNAI1	physical	21726808
HS71L_HUMAN	HSPA1L	physical	21726808
LDHA_HUMAN	LDHA	physical	21726808
MAGD2_HUMAN	MAGED2	physical	21726808
PRS4_HUMAN	PSMC1	physical	21726808
PRS7_HUMAN	PSMC2	physical	21726808
PRS8_HUMAN	PSMC5	physical	21726808
PSA2_HUMAN	PSMA2	physical	21726808
PSA5_HUMAN	PSMA5	physical	21726808
PSB1_HUMAN	PSMB1	physical	21726808
PSB4_HUMAN	PSMB4	physical	21726808
PSD12_HUMAN	PSMD12	physical	21726808
RL4_HUMAN	RPL4	physical	21726808
RL10L_HUMAN	RPL10L	physical	21726808
RL14_HUMAN	RPL14	physical	21726808
RL23_HUMAN	RPL23	physical	21726808
RLA0_HUMAN	RPLP0	physical	21726808
RS3A_HUMAN	RPS3A	physical	21726808
RS6_HUMAN	RPS6	physical	21726808
RS15A_HUMAN	RPS15A	physical	21726808
SKP1_HUMAN	SKP1	physical	21726808
TCPA_HUMAN	TCP1	physical	21726808
TCPB_HUMAN	CCT2	physical	21726808
TCPD_HUMAN	CCT4	physical	21726808
TCPE_HUMAN	CCT5	physical	21726808
C1QBP_HUMAN	C1QBP	physical	21726808
T22D3_HUMAN	TSC22D3	physical	21726808
UBP11_HUMAN	USP11	physical	21726808
ELOC_HUMAN	TCEB1	physical	21726808
1B07_HUMAN	HLA-B	physical	21726808
1B18_HUMAN	HLA-B	physical	21726808
GNA12_HUMAN	GNA12	physical	21726808
GNAS3_HUMAN	GNAS	physical	21726808
GNAS2_HUMAN	GNAS	physical	21726808
ALEX_HUMAN	GNAS	physical	21726808
GNAS1_HUMAN	GNAS	physical	21726808
GEPH_HUMAN	GPHN	physical	21726808
DDX21_HUMAN	DDX21	physical	21726808
MAGD1_HUMAN	MAGED1	physical	21726808
DDX3X_HUMAN	DDX3X	physical	21726808
MYLK2_HUMAN	MYLK2	physical	21726808
NUP62_HUMAN	NUP62	physical	21726808
PSB7_HUMAN	PSMB7	physical	21726808
GGYF2_HUMAN	GIGYF2	physical	21726808
SQSTM_HUMAN	SQSTM1	physical	21726808
FAS_HUMAN	FASN	physical	21726808
PSMD2_HUMAN	PSMD2	physical	21726808
IRS4_HUMAN	IRS4	physical	21726808
SRPRB_HUMAN	SRPRB	physical	21726808
PCAT1_HUMAN	LPCAT1	physical	21726808
FAF2_HUMAN	FAF2	physical	21726808
PSMD6_HUMAN	PSMD6	physical	21726808
RS3_HUMAN	RPS3	physical	21726808
UBC_HUMAN	UBC	physical	21726808
PSDE_HUMAN	PSMD14	physical	21726808
UBR5_HUMAN	UBR5	physical	21726808
SIR2_HUMAN	SIRT2	physical	21726808
A4_HUMAN	APP	physical	21832049

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
261680	Cytosolic phosphoenolpyruvate carboxykinase deficiency (C-PEPCKD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PCKGC_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Acetylation regulates gluconeogenesis by promoting PEPCK1 degradationvia recruiting the UBR5 ubiquitin ligase."; Jiang W., Wang S., Xiao M., Lin Y., Zhou L., Lei Q., Xiong Y.,Guan K.L., Zhao S.; Mol. Cell 43:33-44(2011). Cited for: ACETYLATION AT LYS-70; LYS-71 AND LYS-594, DEACETYLATION BY SIRT2, ANDUBIQUITINATION BY UBR5.	21726808 [Abstract]
"Regulation of cellular metabolism by protein lysine acetylation."; Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L.,Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L.,Chin J., Yang P., Chen X., Lei Q., Xiong Y., Guan K.L.; Science 327:1000-1004(2010). Cited for: ACETYLATION AT LYS-70; LYS-71 AND LYS-594, ENZYME REGULATION, MASSSPECTROMETRY, AND MUTAGENESIS OF LYS-70; LYS-71 AND LYS-594.	20167786 [Abstract]

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