dbPTM

PYC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PYC_HUMAN
UniProt AC	P11498
Protein Name	Pyruvate carboxylase, mitochondrial
Gene Name	PC
Organism	Homo sapiens (Human).
Sequence Length	1178
Subcellular Localization	Mitochondrion matrix.
Protein Description	Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate..
Protein Sequence	MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
19	Phosphorylation	RLLGIRRTSTAPAAS EEEEEEECCCCCCCC	22.15	29396449
20	Phosphorylation	LLGIRRTSTAPAASP EEEEEECCCCCCCCC	22.29	28258704
21	Phosphorylation	LGIRRTSTAPAASPN EEEEECCCCCCCCCC	35.73	29396449
26	Phosphorylation	TSTAPAASPNVRRLE CCCCCCCCCCCEECC	21.07	25159151
35	Acetylation	NVRRLEYKPIKKVMV CCEECCCCCCCEEEE	30.78	-
39	Acetylation	LEYKPIKKVMVANRG CCCCCCCEEEEECCC	35.96	-
67	Phosphorylation	GIRTVAIYSEQDTGQ CCCEEEEEEECCCCC	9.09	22817900
72	Phosphorylation	AIYSEQDTGQMHRQK EEEEECCCCCCCHHH	29.07	20860994
79	Succinylation	TGQMHRQKADEAYLI CCCCCHHHHHHHHHC	58.73	-
79	Acetylation	TGQMHRQKADEAYLI CCCCCHHHHHHHHHC	58.73	-
79	Succinylation	TGQMHRQKADEAYLI CCCCCHHHHHHHHHC	58.73	-
107	Ubiquitination	PDIIKVAKENNVDAV CHHHHHHHHCCCCEE	65.05	-
118	Phosphorylation	VDAVHPGYGFLSERA CCEECCCCCHHHHHH	14.78	21253578
142	Phosphorylation	GVRFIGPSPEVVRKM CCCEECCCHHHHHHH	28.60	28857561
148	Acetylation	PSPEVVRKMGDKVEA CCHHHHHHHCCHHHH	35.31	-
152	Acetylation	VVRKMGDKVEARAIA HHHHHCCHHHHHHHH	35.92	-
175	Phosphorylation	PGTDAPITSLHEAHE CCCCCCCCCHHHHHH	24.95	24275569
176	Phosphorylation	GTDAPITSLHEAHEF CCCCCCCCHHHHHHH	28.57	24275569
197	Phosphorylation	PIIFKAAYGGGGRGM CEEEEECCCCCCCCC	22.59	-
210	Phosphorylation	GMRVVHSYEELEENY CCEEECCHHHHHHHH	9.88	-
217	Phosphorylation	YEELEENYTRAYSEA HHHHHHHHHHHHHHH	10.82	-
218	Phosphorylation	EELEENYTRAYSEAL HHHHHHHHHHHHHHH	22.02	-
241	Acetylation	FVEKFIEKPRHIEVQ EEHHHHCCCCCEEEE	42.40	-
289	Phosphorylation	HLDPQLRTRLTSDSV HCCHHHHHHCCHHHH	38.33	20068231
292	Phosphorylation	PQLRTRLTSDSVKLA HHHHHHCCHHHHHHH	27.48	20068231
293	Phosphorylation	QLRTRLTSDSVKLAK HHHHHCCHHHHHHHH	32.26	20068231
295	Phosphorylation	RTRLTSDSVKLAKQV HHHCCHHHHHHHHHH	22.40	20068231
297	Ubiquitination	RLTSDSVKLAKQVGY HCCHHHHHHHHHHCC	46.83	-
297	Acetylation	RLTSDSVKLAKQVGY HCCHHHHHHHHHHCC	46.83	-
304	Phosphorylation	KLAKQVGYENAGTVE HHHHHHCCCCCCEEE	13.73	20068231
309	Phosphorylation	VGYENAGTVEFLVDR HCCCCCCEEEEEEEC	17.91	20068231
319	Acetylation	FLVDRHGKHYFIEVN EEEECCCCEEEEEEC	29.07	-
319	Succinylation	FLVDRHGKHYFIEVN EEEECCCCEEEEEEC	29.07	23954790
386	Phosphorylation	TTEDPARSFQPDTGR ECCCCCHHCCCCCCC	30.27	27499020
419	Phosphorylation	AFQGAVISPHYDSLL CCCCCEECCCCHHHH	10.06	-
434	Ubiquitination	VKVIAHGKDHPTAAT HHHHHCCCCCHHHHH	42.89	-
434	Acetylation	VKVIAHGKDHPTAAT HHHHHCCCCCHHHHH	42.89	-
434	2-Hydroxyisobutyrylation	VKVIAHGKDHPTAAT HHHHHCCCCCHHHHH	42.89	-
442	Succinylation	DHPTAATKMSRALAE CCHHHHHHHHHHHHH	30.10	-
442	Succinylation	DHPTAATKMSRALAE CCHHHHHHHHHHHHH	30.10	27452117
503	Phosphorylation	RAQKLLHYLGHVMVN HHHHHHHHHCCCEEC	17.85	24248375
513	Phosphorylation	HVMVNGPTTPIPVKA CCEECCCCCCCCCCC	46.75	24248375
514	Phosphorylation	VMVNGPTTPIPVKAS CEECCCCCCCCCCCC	23.50	24248375
521	Phosphorylation	TPIPVKASPSPTDPV CCCCCCCCCCCCCCC	21.86	28348404
523	Phosphorylation	IPVKASPSPTDPVVP CCCCCCCCCCCCCCC	37.63	28348404
525	Phosphorylation	VKASPSPTDPVVPAV CCCCCCCCCCCCCCC	58.22	28348404
568	Phosphorylation	PGLLLMDTTFRDAHQ CCEEEEECCCHHHHH	17.54	26074081
569	Phosphorylation	GLLLMDTTFRDAHQS CEEEEECCCHHHHHH	16.65	26074081
576	Phosphorylation	TFRDAHQSLLATRVR CCHHHHHHHHHHHHC	18.58	26074081
580	Phosphorylation	AHQSLLATRVRTHDL HHHHHHHHHHCCCCH	29.66	26074081
584	Phosphorylation	LLATRVRTHDLKKIA HHHHHHCCCCHHHHH	19.51	26074081
589	Ubiquitination	VRTHDLKKIAPYVAH HCCCCHHHHHHHHHH	51.93	-
589	Acetylation	VRTHDLKKIAPYVAH HCCCCHHHHHHHHHH	51.93	-
661	Acetylation	YPDNVVFKFCEVAKE CCCCEEEEHHHHHHH	37.18	-
667	Acetylation	FKFCEVAKENGMDVF EEHHHHHHHCCCCHH	57.81	26051181
717	Acetylation	VADPSRTKYSLQYYM CCCCCCCHHHHHHHH	31.56	-
741	N6-carboxylysine	GTHILCIKDMAGLLK CCEEEEEECCCCCCC	40.22	-
741	Carboxylation	GTHILCIKDMAGLLK CCEEEEEECCCCCCC	40.22	18297087
748	Acetylation	KDMAGLLKPTACTML ECCCCCCCHHHHHHH	45.42	-
757	Phosphorylation	TACTMLVSSLRDRFP HHHHHHHHHHHHHCC	21.50	24719451
758	Phosphorylation	ACTMLVSSLRDRFPD HHHHHHHHHHHHCCC	21.68	24719451
824	Phosphorylation	TRGTPLDTEVPMERV CCCCCCCCCCCHHHC	46.71	-
835	Phosphorylation	MERVFDYSEYWEGAR HHHCCCHHHHHCCCC	26.50	-
837	Phosphorylation	RVFDYSEYWEGARGL HCCCHHHHHCCCCHH	11.65	-
892	Acetylation	SKFKEVKKAYVEANQ HHHHHHHHHHHHHHH	50.56	-
892	Ubiquitination	SKFKEVKKAYVEANQ HHHHHHHHHHHHHHH	50.56	-
894	Phosphorylation	FKEVKKAYVEANQML HHHHHHHHHHHHHHH	14.01	17924679
927	Phosphorylation	FMVQNGLSRAEAEAQ HHHHCCCCHHHHHHH	30.73	21712546
939	Phosphorylation	EAQAEELSFPRSVVE HHHHHHCCCCHHHHH	36.16	24719451
969	Ubiquitination	PFRSKVLKDLPRVEG HHHHHHHHCCCCCCC	61.27	-
969	Acetylation	PFRSKVLKDLPRVEG HHHHHHHHCCCCCCC	61.27	-
992	Acetylation	LDLQALEKELVDRHG CCHHHHHHHHHHHCC	58.14	20167786
992	Ubiquitination	LDLQALEKELVDRHG CCHHHHHHHHHHHCC	58.14	-
1003	Phosphorylation	DRHGEEVTPEDVLSA HHCCCCCCHHHHHHH	25.00	27251275
1009	Phosphorylation	VTPEDVLSAAMYPDV CCHHHHHHHHHCHHH	17.52	-
1061	Acetylation	RGKTLHIKALAVSDL CCCEEEEEEEEHHHC	26.97	-
1090	2-Hydroxyisobutyrylation	QLRSILVKDTQAMKE EEEEEEECCHHHHHH	52.17	-
1090	Acetylation	QLRSILVKDTQAMKE EEEEEEECCHHHHHH	52.17	19608861
1090	Succinylation	QLRSILVKDTQAMKE EEEEEEECCHHHHHH	52.17	27452117
1124	Acetylation	PGKVIDIKVVAGAKV CCCEEEEEEEECCEE	27.23	26051181
1144	N6-biotinyllysine	LCVLSAMKMETVVTS EEEEEEECCEEEEEC	33.05	-
1144	Biotinylation	LCVLSAMKMETVVTS EEEEEEECCEEEEEC	33.05	6548474
1144	Lipoylation	LCVLSAMKMETVVTS EEEEEEECCEEEEEC	33.05	7918683
1147	Phosphorylation	LSAMKMETVVTSPME EEEECCEEEEECCCC	19.44	21406692
1150	Phosphorylation	MKMETVVTSPMEGTV ECCEEEEECCCCCCE	23.83	21406692
1151	Phosphorylation	KMETVVTSPMEGTVR CCEEEEECCCCCCEE	15.61	21406692
1156	Phosphorylation	VTSPMEGTVRKVHVT EECCCCCCEEEEEEC	12.11	21406692

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
748	K	Acetylation		-
Acetylation of Lys-748 might play a role in catalytic activity regulation.

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 PYC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDHM_HUMAN	MDH2	physical	8349677
AATC_HUMAN	GOT1	physical	8349677
RS3A_HUMAN	RPS3A	physical	22939629
PYR1_HUMAN	CAD	physical	26344197
TCPZ_HUMAN	CCT6A	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
CP27A_HUMAN	CYP27A1	physical	26344197
FAS_HUMAN	FASN	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
PUR4_HUMAN	PFAS	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
266150	Pyruvate carboxylase deficiency (PC deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00121	Biotin
DB00119	Pyruvic acid

Regulatory Network of PYC_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1090, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-894, AND MASSSPECTROMETRY.	17924679 [Abstract]

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