TERA_RAT - dbPTM
TERA_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TERA_RAT
UniProt AC P46462
Protein Name Transitional endoplasmic reticulum ATPase
Gene Name Vcp
Organism Rattus norvegicus (Rat).
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). [PubMed: 10930451]
Protein Sequence MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGNVYTEDNDDDLYG
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 Orthologous
Protein Cluster
2Acetylation------MASGADSKG
------CCCCCCCCC
19.37-
3Phosphorylation-----MASGADSKGD
-----CCCCCCCCCC
32.9627097102
7Phosphorylation-MASGADSKGDDLST
-CCCCCCCCCCCHHH
37.6927097102
8AcetylationMASGADSKGDDLSTA
CCCCCCCCCCCHHHH
67.8925786129
8UbiquitinationMASGADSKGDDLSTA
CCCCCCCCCCCHHHH
67.89-
13PhosphorylationDSKGDDLSTAILKQK
CCCCCCHHHHHHHCC
23.8428432305
14PhosphorylationSKGDDLSTAILKQKN
CCCCCHHHHHHHCCC
25.6428432305
18AcetylationDLSTAILKQKNRPNR
CHHHHHHHCCCCCCC
53.7822902405
37PhosphorylationEAINEDNSVVSLSQP
ECCCCCCCEEECCCC
35.90-
60AcetylationRGDTVLLKGKKRREA
CCCEEEECCCCCCEE
65.6022902405
73PhosphorylationEAVCIVLSDDTCSDE
EEEEEEEECCCCCHH
23.6525575281
76PhosphorylationCIVLSDDTCSDEKIR
EEEEECCCCCHHHHC
20.9225575281
78PhosphorylationVLSDDTCSDEKIRMN
EEECCCCCHHHHCHH
51.3925575281
148SuccinylationEAYRPIRKGDIFLVR
HHHCCCCCCCEEEEE
62.7526843850
197PhosphorylationKREDEEESLNEVGYD
CCCCCHHHHHHCCCC
39.5129779826
231UbiquitinationLRHPALFKAIGVKPP
CCCHHHHHHCCCCCC
39.69-
236UbiquitinationLFKAIGVKPPRGILL
HHHHCCCCCCCEEEE
44.05-
282PhosphorylationMSKLAGESESNLRKA
HHHHCCCCHHHHHHH
45.4627097102
284PhosphorylationKLAGESESNLRKAFE
HHCCCCHHHHHHHHH
50.9027097102
288AcetylationESESNLRKAFEEAEK
CCHHHHHHHHHHHHH
61.6722902405
288SuccinylationESESNLRKAFEEAEK
CCHHHHHHHHHHHHH
61.6726843850
315MethylationAIAPKREKTHGEVER
HHCCCCCCCCHHHHH
50.26-
315"N6,N6,N6-trimethyllysine"AIAPKREKTHGEVER
HHCCCCCCCCHHHHH
50.26-
336AcetylationLTLMDGLKQRAHVIV
HHHHHHHHHCCEEEE
43.1822902405
336UbiquitinationLTLMDGLKQRAHVIV
HHHHHHHHHCCEEEE
43.18-
436PhosphorylationLIDLEDETIDAEVMN
CCCCCCCCCCHHHHH
36.16-
457PhosphorylationDDFRWALSQSNPSAL
HHHHHHHHCCCHHHH
24.6627097102
459PhosphorylationFRWALSQSNPSALRE
HHHHHHCCCHHHHHH
47.5427097102
462PhosphorylationALSQSNPSALRETVV
HHHCCCHHHHHHHEE
44.1627097102
502UbiquitinationYPVEHPDKFLKFGMT
CCCCCCCCCCCCCCC
57.98-
502AcetylationYPVEHPDKFLKFGMT
CCCCCCCCCCCCCCC
57.98-
505AcetylationEHPDKFLKFGMTPSK
CCCCCCCCCCCCCCC
42.90-
509PhosphorylationKFLKFGMTPSKGVLF
CCCCCCCCCCCCEEE
25.4528432305
565AcetylationNVREIFDKARQAAPC
HHHHHHHHHHHHCCE
34.4222902405
614UbiquitinationEMDGMSTKKNVFIIG
HCCCCCCCCCEEEEE
34.74-
651AcetylationYIPLPDEKSRVAILK
EEECCCHHHHEEHHH
51.4422902405
651UbiquitinationYIPLPDEKSRVAILK
EEECCCHHHHEEHHH
51.44-
658UbiquitinationKSRVAILKANLRKSP
HHHEEHHHHHCCCCC
29.17-
668UbiquitinationLRKSPVAKDVDLEFL
CCCCCCCCCCCHHHH
59.52-
668SuccinylationLRKSPVAKDVDLEFL
CCCCCCCCCCCHHHH
59.52-
668SuccinylationLRKSPVAKDVDLEFL
CCCCCCCCCCCHHHH
59.52-
668AcetylationLRKSPVAKDVDLEFL
CCCCCCCCCCCHHHH
59.5222902405
702PhosphorylationCKLAIRESIESEIRR
HHHHHHHHHHHHHHH
23.0822108457
705PhosphorylationAIRESIESEIRRERE
HHHHHHHHHHHHHHH
36.3323984901
748PhosphorylationRFARRSVSDNDIRKY
HHHHHCCCHHHHHHH
31.7622673903
754AcetylationVSDNDIRKYEMFAQT
CCHHHHHHHHHHHHH
45.9922902405
770PhosphorylationQQSRGFGSFRFPSGN
HHHCCCCCEECCCCC
15.8125532521
775PhosphorylationFGSFRFPSGNQGGAG
CCCEECCCCCCCCCC
47.8928689409
784PhosphorylationNQGGAGPSQGSGGGT
CCCCCCCCCCCCCCC
46.3828689409
787PhosphorylationGAGPSQGSGGGTGGN
CCCCCCCCCCCCCCC
26.9928689409
797PhosphorylationGTGGNVYTEDNDDDL
CCCCCCCCCCCCCCC
32.3628689409
805PhosphorylationEDNDDDLYG------
CCCCCCCCC------
27.9922276854

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
352SPhosphorylationKinaseAKT-FAMILY-GPS
746SPhosphorylationKinaseAKT-FAMILY-GPS
748SPhosphorylationKinaseAKT-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
315KMethylation

-
315KMethylation

-

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBX2B_RATUbxn2bphysical
17141156
TERA_RATVcpphysical
12351637
UFD1_RATUfd1lphysical
12847084
NSF1C_RATNsfl1cphysical
12847084
CALX_RATCanxphysical
12847084
B2MG_RATB2mphysical
12847084
UBC_RATUbcphysical
12847084
NF1_RATNf1physical
22105171
NSF1C_RATNsfl1cphysical
10811609
UFD1_RATUfd1lphysical
10811609
UBE4A_RATUbe4aphysical
10811609
NPL4_RATNploc4physical
10811609

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TERA_RAT

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Related Literatures of Post-Translational Modification

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