dbPTM

TERA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TERA_MOUSE
UniProt AC	Q01853
Protein Name	Transitional endoplasmic reticulum ATPase
Gene Name	Vcp
Organism	Mus musculus (Mouse).
Sequence Length	806
Subcellular Localization	Cytoplasm, cytosol . Endoplasmic reticulum . Nucleus . Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMFR/gp78. Following DNA double-strand breaks, recruited to the sites of damage. Recruited to stalled replic
Protein Description	Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy. Acts as a negative regulator of type I interferon production by interacting with DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I. May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation. May more particularly play a role in caveolins sorting in cells. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway..
Protein Sequence	MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDNDDDLYG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGADSKG ------CCCCCCCCC	19.37	-
3	Phosphorylation	-----MASGADSKGD -----CCCCCCCCCC	32.96	23527152
7	Phosphorylation	-MASGADSKGDDLST -CCCCCCCCCCCHHH	37.69	26824392
8	Acetylation	MASGADSKGDDLSTA CCCCCCCCCCCHHHH	67.89	6597409
13	Phosphorylation	DSKGDDLSTAILKQK CCCCCCHHHHHHHCC	23.84	25619855
14	Phosphorylation	SKGDDLSTAILKQKN CCCCCHHHHHHHCCC	25.64	25619855
18	Ubiquitination	DLSTAILKQKNRPNR CHHHHHHHCCCCCCC	53.78	22790023
37	Phosphorylation	EAINEDNSVVSLSQP ECCCCCCCEEECCCC	35.90	25338131
42	Phosphorylation	DNSVVSLSQPKMDEL CCCEEECCCCCCCCC	36.61	-
45	Ubiquitination	VVSLSQPKMDELQLF EEECCCCCCCCCHHH	51.88	22790023
60	Acetylation	RGDTVLLKGKKRREA CCCEEEECCCCCCEE	65.60	23806337
60	Succinylation	RGDTVLLKGKKRREA CCCEEEECCCCCCEE	65.60	23806337
60	Ubiquitination	RGDTVLLKGKKRREA CCCEEEECCCCCCEE	65.60	27667366
101	Phosphorylation	VRLGDVISIQPCPDV EECCCEEEEEECCCC	18.28	-
105	S-nitrosocysteine	DVISIQPCPDVKYGK CEEEEEECCCCCCCC	2.29	-
105	Glutathionylation	DVISIQPCPDVKYGK CEEEEEECCCCCCCC	2.29	24333276
105	S-nitrosylation	DVISIQPCPDVKYGK CEEEEEECCCCCCCC	2.29	20925432
105	S-palmitoylation	DVISIQPCPDVKYGK CEEEEEECCCCCCCC	2.29	28526873
109	Acetylation	IQPCPDVKYGKRIHV EEECCCCCCCCEEEE	56.52	23236377
109	Ubiquitination	IQPCPDVKYGKRIHV EEECCCCCCCCEEEE	56.52	22790023
112	Ubiquitination	CPDVKYGKRIHVLPI CCCCCCCCEEEEEEC	45.12	-
122	Phosphorylation	HVLPIDDTVEGITGN EEEECCCCCCCCCCC	19.40	29514104
127	Phosphorylation	DDTVEGITGNLFEVY CCCCCCCCCCEEEEE	30.76	29514104
148	Acetylation	EAYRPIRKGDIFLVR HHHCCCCCCCEEEEE	62.75	23806337
148	Malonylation	EAYRPIRKGDIFLVR HHHCCCCCCCEEEEE	62.75	26320211
148	Succinylation	EAYRPIRKGDIFLVR HHHCCCCCCCEEEEE	62.75	-
148	Ubiquitination	EAYRPIRKGDIFLVR HHHCCCCCCCEEEEE	62.75	-
173	Phosphorylation	VETDPSPYCIVAPDT EECCCCCCEEECCCE	10.11	22817900
174	S-nitrosocysteine	ETDPSPYCIVAPDTV ECCCCCCEEECCCEE	1.98	-
174	Glutathionylation	ETDPSPYCIVAPDTV ECCCCCCEEECCCEE	1.98	24333276
174	S-nitrosylation	ETDPSPYCIVAPDTV ECCCCCCEEECCCEE	1.98	20925432
197	Phosphorylation	KREDEEESLNEVGYD CCCCCHHHHHHCCCC	39.51	25521595
209	S-nitrosocysteine	GYDDIGGCRKQLAQI CCCCCCHHHHHHHHH	4.07	-
209	S-nitrosylation	GYDDIGGCRKQLAQI CCCCCCHHHHHHHHH	4.07	20925432
209	S-palmitoylation	GYDDIGGCRKQLAQI CCCCCCHHHHHHHHH	4.07	28526873
211	Ubiquitination	DDIGGCRKQLAQIKE CCCCHHHHHHHHHHH	54.46	22790023
217	Acetylation	RKQLAQIKEMVELPL HHHHHHHHHHHHCCC	27.90	22826441
217	Ubiquitination	RKQLAQIKEMVELPL HHHHHHHHHHHHCCC	27.90	22790023
231	Acetylation	LRHPALFKAIGVKPP CCCHHHHHHCCCCCC	39.69	22826441
231	Ubiquitination	LRHPALFKAIGVKPP CCCHHHHHHCCCCCC	39.69	22790023
236	Malonylation	LFKAIGVKPPRGILL HHHHCCCCCCCEEEE	44.05	26320211
236	Ubiquitination	LFKAIGVKPPRGILL HHHHCCCCCCCEEEE	44.05	27667366
244	Phosphorylation	PPRGILLYGPPGTGK CCCEEEEECCCCCCH	24.92	22817900
251	Acetylation	YGPPGTGKTLIARAV ECCCCCCHHHHHHHH	39.74	22826441
251	Ubiquitination	YGPPGTGKTLIARAV ECCCCCCHHHHHHHH	39.74	22790023
277	Ubiquitination	NGPEIMSKLAGESES ECHHHHHHHCCCCHH	25.61	-
282	Phosphorylation	MSKLAGESESNLRKA HHHHCCCCHHHHHHH	45.46	18779572
284	Phosphorylation	KLAGESESNLRKAFE HHCCCCHHHHHHHHH	50.90	18779572
288	Ubiquitination	ESESNLRKAFEEAEK CCHHHHHHHHHHHHH	61.67	22790023
295	Ubiquitination	KAFEEAEKNAPAIIF HHHHHHHHCCCEEEE	66.51	22790023
312	Ubiquitination	ELDAIAPKREKTHGE CHHHHCCCCCCCCHH	65.25	22790023
315	"N6,N6,N6-trimethyllysine"	AIAPKREKTHGEVER HHCCCCCCCCHHHHH	50.26	-
315	Methylation	AIAPKREKTHGEVER HHCCCCCCCCHHHHH	50.26	22948820
336	Acetylation	LTLMDGLKQRAHVIV HHHHHHHHHCCEEEE	43.18	22826441
336	Ubiquitination	LTLMDGLKQRAHVIV HHHHHHHHHCCEEEE	43.18	22790023
347	Phosphorylation	HVIVMAATNRPNSID EEEEEEECCCCCCCC	23.40	25293948
352	Phosphorylation	AATNRPNSIDPALRR EECCCCCCCCHHHHH	30.93	25168779
375	Phosphorylation	DIGIPDATGRLEILQ CCCCCCCCCCEEEEE	30.16	28059163
386	Ubiquitination	EILQIHTKNMKLADD EEEEEECCCCEECCC	40.66	22790023
389	Ubiquitination	QIHTKNMKLADDVDL EEECCCCEECCCCCH	50.33	-
415	Glutathionylation	GADLAALCSEAALQA HHHHHHHHHHHHHHH	2.72	24333276
415	S-palmitoylation	GADLAALCSEAALQA HHHHHHHHHHHHHHH	2.72	28526873
416	Phosphorylation	ADLAALCSEAALQAI HHHHHHHHHHHHHHH	30.99	29109428
436	Phosphorylation	LIDLEDETIDAEVMN CCCCCCCCCCHHHHH	36.16	-
462	Phosphorylation	ALSQSNPSALRETVV HHHCCCHHHHHHHEE	44.16	-
486	Ubiquitination	IGGLEDVKRELQELV CCCHHHHHHHHHHHH	53.10	22790023
502	Acetylation	YPVEHPDKFLKFGMT CCCCCCCCCCCCCCC	57.98	23806337
502	Ubiquitination	YPVEHPDKFLKFGMT CCCCCCCCCCCCCCC	57.98	22790023
505	Acetylation	EHPDKFLKFGMTPSK CCCCCCCCCCCCCCC	42.90	23806337
505	Ubiquitination	EHPDKFLKFGMTPSK CCCCCCCCCCCCCCC	42.90	22790023
509	Phosphorylation	KFLKFGMTPSKGVLF CCCCCCCCCCCCEEE	25.45	22817900
511	Phosphorylation	LKFGMTPSKGVLFYG CCCCCCCCCCEEEEC	32.64	24759943
512	Acetylation	KFGMTPSKGVLFYGP CCCCCCCCCEEEECC	55.00	22826441
512	Ubiquitination	KFGMTPSKGVLFYGP CCCCCCCCCEEEECC	55.00	22790023
522	Glutathionylation	LFYGPPGCGKTLLAK EEECCCCCCHHHHHH	6.61	24333276
522	S-palmitoylation	LFYGPPGCGKTLLAK EEECCCCCCHHHHHH	6.61	28526873
524	Ubiquitination	YGPPGCGKTLLAKAI ECCCCCCHHHHHHHH	39.82	22790023
529	Acetylation	CGKTLLAKAIANECQ CCHHHHHHHHHHHHH	40.05	22826441
529	Ubiquitination	CGKTLLAKAIANECQ CCHHHHHHHHHHHHH	40.05	22790023
535	S-nitrosocysteine	AKAIANECQANFISI HHHHHHHHHCCEEEE	4.67	-
535	Glutathionylation	AKAIANECQANFISI HHHHHHHHHCCEEEE	4.67	24333276
535	S-nitrosylation	AKAIANECQANFISI HHHHHHHHHCCEEEE	4.67	22588120
535	S-palmitoylation	AKAIANECQANFISI HHHHHHHHHCCEEEE	4.67	28526873
565	Acetylation	NVREIFDKARQAAPC HHHHHHHHHHHHCCE	34.42	22826441
565	Ubiquitination	NVREIFDKARQAAPC HHHHHHHHHHHHCCE	34.42	27667366
572	S-nitrosocysteine	KARQAAPCVLFFDEL HHHHHCCEEEEECCH	3.40	-
572	Glutathionylation	KARQAAPCVLFFDEL HHHHHCCEEEEECCH	3.40	24333276
572	S-nitrosylation	KARQAAPCVLFFDEL HHHHHCCEEEEECCH	3.40	20925432
572	S-palmitoylation	KARQAAPCVLFFDEL HHHHHCCEEEEECCH	3.40	28526873
584	Ubiquitination	DELDSIAKARGGNIG CCHHHHHHHCCCCCC	36.63	22790023
614	Ubiquitination	EMDGMSTKKNVFIIG HCCCCCCCCCEEEEE	34.74	22790023
615	Ubiquitination	MDGMSTKKNVFIIGA CCCCCCCCCEEEEEC	59.43	22790023
644	Phosphorylation	GRLDQLIYIPLPDEK CCCCEEEEEECCCHH	12.70	22817900
651	Acetylation	YIPLPDEKSRVAILK EEECCCHHHHEEHHH	51.44	23236377
651	Succinylation	YIPLPDEKSRVAILK EEECCCHHHHEEHHH	51.44	23954790
651	Ubiquitination	YIPLPDEKSRVAILK EEECCCHHHHEEHHH	51.44	27667366
658	Acetylation	KSRVAILKANLRKSP HHHEEHHHHHCCCCC	29.17	22826441
658	Malonylation	KSRVAILKANLRKSP HHHEEHHHHHCCCCC	29.17	26320211
658	Ubiquitination	KSRVAILKANLRKSP HHHEEHHHHHCCCCC	29.17	27667366
663	Ubiquitination	ILKANLRKSPVAKDV HHHHHCCCCCCCCCC	63.38	-
664	Phosphorylation	LKANLRKSPVAKDVD HHHHCCCCCCCCCCC	20.41	25338131
668	Acetylation	LRKSPVAKDVDLEFL CCCCCCCCCCCHHHH	59.52	23806337
668	Succinylation	LRKSPVAKDVDLEFL CCCCCCCCCCCHHHH	59.52	-
668	Succinylation	LRKSPVAKDVDLEFL CCCCCCCCCCCHHHH	59.52	23806337
668	Ubiquitination	LRKSPVAKDVDLEFL CCCCCCCCCCCHHHH	59.52	27667366
691	S-nitrosocysteine	GADLTEICQRACKLA CCCHHHHHHHHHHHH	1.50	-
691	S-nitrosylation	GADLTEICQRACKLA CCCHHHHHHHHHHHH	1.50	20925432
691	S-palmitoylation	GADLTEICQRACKLA CCCHHHHHHHHHHHH	1.50	28526873
696	Ubiquitination	EICQRACKLAIRESI HHHHHHHHHHHHHHH	39.71	22790023
702	Phosphorylation	CKLAIRESIESEIRR HHHHHHHHHHHHHHH	23.08	26824392
705	Phosphorylation	AIRESIESEIRRERE HHHHHHHHHHHHHHH	36.33	21082442
718	Phosphorylation	RERQTNPSAMEVEED HHHCCCCCCCCCCCC	42.17	26525534
746	Phosphorylation	AMRFARRSVSDNDIR HHHHHHHCCCHHHHH	22.03	26824392
748	Phosphorylation	RFARRSVSDNDIRKY HHHHHCCCHHHHHHH	31.76	29895711
754	Acetylation	VSDNDIRKYEMFAQT CCHHHHHHHHHHHHH	45.99	23806337
754	Ubiquitination	VSDNDIRKYEMFAQT CCHHHHHHHHHHHHH	45.99	22790023
755	Phosphorylation	SDNDIRKYEMFAQTL CHHHHHHHHHHHHHH	11.63	15879432
765	Phosphorylation	FAQTLQQSRGFGSFR HHHHHHHHCCCCCEE	22.78	24899341
770	Phosphorylation	QQSRGFGSFRFPSGN HHHCCCCCEECCCCC	15.81	27149854
775	Phosphorylation	FGSFRFPSGNQGGAG CCCEECCCCCCCCCC	47.89	25521595
784	Phosphorylation	NQGGAGPSQGSGGGT CCCCCCCCCCCCCCC	46.38	27087446
787	Phosphorylation	GAGPSQGSGGGTGGS CCCCCCCCCCCCCCC	26.99	26643407
791	Phosphorylation	SQGSGGGTGGSVYTE CCCCCCCCCCCCCCC	41.46	27087446
794	Phosphorylation	SGGGTGGSVYTEDND CCCCCCCCCCCCCCC	17.19	26643407
796	Phosphorylation	GGTGGSVYTEDNDDD CCCCCCCCCCCCCCC	13.20	8157674
797	Phosphorylation	GTGGSVYTEDNDDDL CCCCCCCCCCCCCCC	34.41	27087446
805	Phosphorylation	EDNDDDLYG------ CCCCCCCCC------	27.99	27087446

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 TERA_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
315	K	Methylation	22948820
Lys-315 methylation may decrease ATPase activity (By similarity).
315	K	Methylation	22948820
Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1.

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 TERA_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSN5_MOUSE	Cops5	physical	19826004
HERP1_MOUSE	Herpud1	physical	21600962
NICA_MOUSE	Ncstn	physical	21600962
RNF37_MOUSE	Ubox5	physical	15189447
UBE4B_MOUSE	Ube4b	physical	15189447
PP2AB_MOUSE	Ppp2cb	physical	20100830
VCIP1_MOUSE	Vcpip1	physical	14988733
NSF1C_MOUSE	Nsfl1c	physical	10811609
UFD1_MOUSE	Ufd1l	physical	10811609
UBE4B_MOUSE	Ube4b	physical	10811609
NPL4_MOUSE	Nploc4	physical	10811609
SVIP_MOUSE	Svip	physical	12529442
NSF1C_MOUSE	Nsfl1c	physical	12529442
UFD1_MOUSE	Ufd1l	physical	12529442
TAU_MOUSE	Mapt	physical	23719816
PRKDC_MOUSE	Prkdc	physical	23722536
UFD1_HUMAN	UFD1L	physical	24089527
PGH2_HUMAN	PTGS2	physical	24089527
DERL1_HUMAN	DERL1	physical	24089527
CAV1_HUMAN	CAV1	physical	24089527
HYOU1_MOUSE	Hyou1	physical	24218449
ATX1_MOUSE	Atxn1	physical	23652004

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TERA_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.	17242355 [Abstract]

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