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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Transitional endoplasmic reticulum ATPase

UniprotKB/SwissProt ID: TERA_HUMAN (P55072)

Gene Name: VCP

Organism: Homo sapiens (Human).

Function: 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 UFD1L, 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-UFD1L-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 (By similarity). 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. 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.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus. Note=Present in the neuronal hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy bodies specifically found in neurons from Parki

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Protein disease:
Disease database Database Entry Disease information
HPRD03013Inclusion body myopathy with early-onset paget disease
HPRD03013Inclusion body myopathy with early-onset paget disease and frontotemporal dementia
Network with metabolic pathway:
Kegg map ID Pathway Link
map05134Legionellosis
map04141Protein processing in endoplasmic reticulum
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR003338
IPR003593
IPR003959
IPR003960
IPR005938
IPR009010

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
3EBB X-ray 1.90 A E/F/G/H797-806Link
3HU1 X-ray 2.81 A A/B/C/D/E/F1-481Link
3HU2 X-ray 2.85 A A/B/C/D/E/F1-481Link
3HU3 X-ray 2.20 A A/B1-481Link
3QC8 X-ray 2.20 A A21-196Link
3QQ7 X-ray 2.65 A A2-187Link
3QQ8 X-ray 2.00 A A2-187Link
3QWZ X-ray 2.00 A A1-208Link
3TIW X-ray 1.80 A A/B1-187Link
4KLN X-ray 2.62 A A/B/C/D/E/F1-481Link
4KO8 X-ray 1.98 A A/B1-481Link
4KOD X-ray 2.96 A A/B/C/D/E/F/G/H/I/J/K/L1-481Link

The S-nitrosylation sites of TERA_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1105RLGDVISIQP C PDVKYGKRIH CCCCCEEEEE C CCCCCCCEEE 2.29%HC1022178444-
2105RLGDVISIQP C PDVKYGKRIH CCCCCEEEEE C CCCCCCCEEE 2.29%HC1019483679in vivo
3105RLGDVISIQP C PDVKYGKRIH CCCCCEEEEE C CCCCCCCEEE 2.29%HC1020140087in vivo
4522KGVLFYGPPG C GKTLLAKAIA CCEEEECCCC C CHHHHHHHHH 6.61%HC0522178444-
5535TLLAKAIANE C QANFISIKGP HHHHHHHHHH C CCCEEEEEHH 4.67%HC1219483679in vivo
6572IFDKARQAAP C VLFFDELDSI HHHHHHHCCC C EEEEECHHHH 3.40%HC0119483679in vivo