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P55072 (TERA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transitional endoplasmic reticulum ATPase

Short name=TER ATPase
EC=3.6.4.6
Alternative name(s):
15S Mg(2+)-ATPase p97 subunit
Valosin-containing protein
Short name=VCP
Gene names
Name:VCP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.14 Ref.18 Ref.39 Ref.40 Ref.42 Ref.45 Ref.46

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Part of a ternary complex containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer. The complex binds to membranes enriched in phosphatidylethanolamine-containing lipids and promotes Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1L, binding to this heterodimer inhibits Golgi-membrane fusion. Interaction with VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP. Part of a ternary complex containing NPLOC4, UFD1L and VCP. Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis By similarity. Interacts with VIMP/SELS and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Interacts with SVIP. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXD2 and RNF19A. Interacts with CASR. Interacts with UBXN6, UBE4B and YOD1. Interacts with clathrin. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with RHBDD1 (via C-terminus domain). Interacts with SPRTN; leading to recruitment to stalled replication forks. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP. Ref.9 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.31 Ref.36 Ref.38 Ref.40 Ref.41 Ref.45 Ref.46 Ref.47

Subcellular location

Cytoplasmcytosol. 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 Parkinson disease patients. 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 replication forks via interaction with SPRTN. Ref.11 Ref.14 Ref.18 Ref.40 Ref.46

Post-translational modification

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation By similarity.

ISGylated. Ref.16

Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity. Ref.11 Ref.44

Involvement in disease

Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 1 (IBMPFD1) [MIM:167320]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.47 Ref.49 Ref.50 Ref.51 Ref.52

Amyotrophic lateral sclerosis 14, with or without frontotemporal dementia (ALS14) [MIM:613954]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS14 may develop frontotemporal dementia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.53

Sequence similarities

Belongs to the AAA ATPase family.

Caution

It is unclear how it participates in the recruitment of TP53BP1 at DNA damage sites. According to a first report, participates in the recruitment of TP53BP1 by promoting ubiquitination and removal of L3MBTL1 from DNA damage sites (Ref.40). According to a second report, it acts by removing 'Lys-48'-linked ubiquitination from sites of DNA damage (Ref.39).

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
Endoplasmic reticulum
Nucleus
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Non-traceable author statement PubMed 16140914. Source: UniProtKB

ER to Golgi vesicle-mediated transport

Inferred from electronic annotation. Source: Ensembl

ER-associated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.42. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

aggresome assembly

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 16140914Ref.40Ref.46. Source: UniProtKB

double-strand break repair

Inferred from direct assay PubMed 10855792Ref.40. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Traceable author statement Ref.15. Source: UniProtKB

establishment of protein localization

Traceable author statement Ref.15. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 9452483. Source: BHF-UCL

positive regulation of protein catabolic process

Inferred from direct assay PubMed 11483959PubMed 18775313. Source: BHF-UCL

positive regulation of protein complex assembly

Inferred from direct assay PubMed 18775313. Source: BHF-UCL

proteasome-mediated ubiquitin-dependent protein catabolic process

Non-traceable author statement PubMed 15743842. Source: UniProtKB

protein N-linked glycosylation via asparagine

Inferred from mutant phenotype Ref.42. Source: UniProtKB

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from direct assay Ref.40. Source: UniProtKB

regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

retrograde protein transport, ER to cytosol

Inferred from direct assay Ref.15. Source: UniProtKB

translesion synthesis

Inferred from mutant phenotype Ref.46. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay PubMed 10855792Ref.15. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay Ref.15. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

intracellular membrane-bounded organelle

Inferred from sequence or structural similarity. Source: UniProtKB

lipid particle

Inferred from direct assay PubMed 23297223. Source: MGI

nucleus

Inferred from direct assay PubMed 10855792. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16275660. Source: ParkinsonsUK-UCL

proteasome complex

Inferred from direct assay PubMed 9452483. Source: BHF-UCL

site of double-strand break

Inferred from direct assay Ref.40. Source: UniProtKB

   Molecular_functionADP binding

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Traceable author statement Ref.15. Source: UniProtKB

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

polyubiquitin binding

Inferred from direct assay PubMed 11483959. Source: BHF-UCL

protein domain specific binding

Inferred from physical interaction Ref.13. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction PubMed 10364224. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8
Chain2 – 806805Transitional endoplasmic reticulum ATPase
PRO_0000084572

Regions

Nucleotide binding247 – 2537ATP
Region797 – 80610Interaction with UBXN6

Sites

Binding site3481ATP
Binding site3841ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.30 Ref.32 Ref.37 Ref.43
Modified residue31Phosphoserine Ref.28 Ref.32 Ref.37
Modified residue371Phosphoserine Ref.32
Modified residue3151N6,N6,N6-trimethyllysine; by VCPKMT Ref.11 Ref.44
Modified residue4361Phosphothreonine Ref.28
Modified residue5021N6-acetyllysine By similarity
Modified residue5051N6-acetyllysine By similarity
Modified residue6681N6-acetyllysine; alternate By similarity
Modified residue6681N6-succinyllysine; alternate By similarity
Modified residue7541N6-acetyllysine By similarity
Modified residue7701Phosphoserine Ref.33
Modified residue7751Phosphoserine Ref.33
Modified residue7871Phosphoserine Ref.28
Modified residue8051Phosphotyrosine By similarity

Natural variations

Natural variant951R → G in IBMPFD1; cultured cells expressing the mutant protein show a marked general increase in the level of ubiquitin-conjugated proteins and impaired protein degradation through the endoplasmic reticulum-associated degradation (ERAD) pathway; shows strongly reduced affinity for ADP and increased affinity for ATP; abolishes enhancement of K-315 methylation by ASPSCR1. Ref.47 Ref.49 Ref.52
VAR_033016
Natural variant1551R → C in IBMPFD1; also in one patient without evidence of Paget disease of the bone. Ref.49 Ref.50
VAR_033017
Natural variant1551R → H in ALS14 and IBMPFD1; ALS14 patients do not manifest frontotemporal dementia; properly assembles into a hexameric structure and shows normal ATPase activity; cultured cells expressing the mutant protein show a marked general increase in the level of ubiquitin-conjugated proteins and impaired protein degradation through the endoplasmic reticulum-associated degradation (ERAD) pathway; shows strongly reduced affinity for ADP and increased affinity for ATP. Ref.11 Ref.47 Ref.49 Ref.52 Ref.53
VAR_033018
Natural variant1551R → P in IBMPFD1. Ref.49
VAR_033019
Natural variant1591R → G in ALS14. Ref.11 Ref.53
VAR_065910
Natural variant1591R → H in IBMPFD1; without frontotemporal dementia; abolishes enhancement of K-315 methylation by ASPSCR1. Ref.51
VAR_033020
Natural variant1911R → Q in ALS14 and IBMPFD1; abolishes enhancement of K-315 methylation by ASPSCR1. Ref.11 Ref.49 Ref.53
VAR_033021
Natural variant2321A → E in IBMPFD1. Ref.49
VAR_033022
Natural variant5921D → N in ALS14; ALS14 patients do not show frontotemporal dementia. Ref.53
VAR_065911

Experimental info

Mutagenesis531R → A: Minor effect on affinity for ATP and ADP. Ref.47
Mutagenesis861R → A: Strongly increased affinity for ATP. Strongly reduced affinity for ADP. Ref.47
Mutagenesis2511K → Q: Impairs ERAD degradation of HMGCR and does not inhibit interaction with RHBDD1; when associated with Q-524. Ref.18 Ref.38
Mutagenesis3121K → A: Does not affect methylation by VCPKMT. Ref.44
Mutagenesis3131R → A: Does not affect methylation by VCPKMT. Ref.44
Mutagenesis3141E → A: Does not affect methylation by VCPKMT. Ref.44
Mutagenesis3141Missing: Strongly impairs methylation by VCPKMT. Ref.44
Mutagenesis3151K → L, Q or R: Abolishes methylation by VCPKMT. Ref.11 Ref.44
Mutagenesis3161T → A: Does not affect methylation by VCPKMT. Ref.44
Mutagenesis3171H → A: Does not affect methylation by VCPKMT. Ref.44
Mutagenesis3181G → A: Does not affect methylation by VCPKMT. Ref.44
Mutagenesis5241K → A: Impairs catalytic activity of RNF19A toward SOD1 mutant. Does not inhibit interaction with RHBDD1; when associated with A-251. Ref.14 Ref.18 Ref.38
Mutagenesis5241K → Q: Impairs ERAD degradation of HMGCR; when associated with Q-251. Ref.14 Ref.18 Ref.38
Mutagenesis5781E → Q: Does not inhibit interaction with RHBDD1. Ref.38
Sequence conflict1691D → H in AAI21795. Ref.6
Sequence conflict3121K → I in BAG35235. Ref.3

Secondary structure

............................................................................................. 806
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55072 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 501B721D3A77BA8A

FASTA80689,322
        10         20         30         40         50         60 
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK 

        70         80         90        100        110        120 
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID 

       130        140        150        160        170        180 
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT 

       190        200        210        220        230        240 
VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG 

       250        260        270        280        290        300 
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI 

       310        320        330        340        350        360 
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF 

       370        380        390        400        410        420 
GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL 

       430        440        450        460        470        480 
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG 

       490        500        510        520        530        540 
GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI 

       550        560        570        580        590        600 
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 

       610        620        630        640        650        660 
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRVAILKAN 

       670        680        690        700        710        720 
LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM 

       730        740        750        760        770        780 
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG 

       790        800 
AGPSQGSGGG TGGSVYTEDN DDDLYG 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of a human P1 clone containing the XRCC9 DNA repair gene."
Lamerdin J.E., McCready P.M., Skowronski E., Adamson A.W., Burkhart-Schultz K., Gordon L., Kyle A., Ramirez M., Stilwagen S., Phan H., Velasco N., Garnes J., Danganan L., Poundstone P., Christensen M., Georgescu A., Avila J., Liu S. expand/collapse author list , Attix C., Andreise T., Trankheim M., Amico-Keller G., Coefield J., Duarte S., Lucas S., Bruce R., Thomas P., Quan G., Kronmiller B., Arellano A., Montgomery M., Ow D., Nolan M., Trong S., Kobayashi A., Olsen A.O., Carrano A.V.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-25.
Tissue: Platelet.
[8]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-18; 148-155; 278-287; 296-312; 366-377; 466-487; 587-599; 639-651 AND 669-677, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[9]"Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein."
Pleasure I.T., Black M.M., Keen J.H.
Nature 365:459-462(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-41 AND 233-238, INTERACTION WITH CLATHRIN.
Tissue: Glial tumor.
[10]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 46-53; 66-81; 96-109; 148-155; 240-251; 323-336; 454-502; 530-560; 600-614; 639-651; 678-693; 714-732 AND 754-766, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[11]"A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 314-322, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, METHYLATION AT LYS-315, MUTAGENESIS OF LYS-315, CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155 AND GLN-191, CHARACTERIZATION OF VARIANT ALS14 GLY-159.
[12]"Characterization of different mRNA types expressed in human brain."
Dmitrenko V.V., Garifulin O.M., Kavsan V.M.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 388-483.
Tissue: Fetal brain.
[13]"A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs."
McNeill H., Knebel A., Arthur J.S., Cuenda A., Cohen P.
Biochem. J. 384:391-400(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGLY1.
[14]"Physical and functional interaction between dorfin and valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders."
Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S., Kakizuka A., Tanaka K., Sobue G.
J. Biol. Chem. 279:51376-51385(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RNF19A, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524.
[15]"A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol."
Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A.
Nature 429:841-847(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VIMP.
[16]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[17]"The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway."
Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., Koning F., Kloetzel P.-M., Seeger M.
J. Mol. Biol. 354:1021-1027(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYVN1 AND DERL1.
[18]"Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase."
Song B.L., Sever N., DeBose-Boyd R.A.
Mol. Cell 19:829-840(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AMFR, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-251 AND LYS-524.
[19]"Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane."
Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E., Rapoport T.A.
Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DERL1; AMFR; SYVN1 AND VIMP.
[20]"Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane."
Lilley B.N., Ploegh H.L.
Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DERL1 AND DERL2.
[21]"Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin."
Huang Y., Niwa J., Sobue G., Breitwieser G.E.
J. Biol. Chem. 281:11610-11617(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASR AND RNF19A.
[22]"Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation."
Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.
J. Cell Biol. 172:383-393(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DERL1; DERL2 AND DERL3.
[23]"Characterization of erasin (UBXD2): a new ER protein that promotes ER-associated protein degradation."
Liang J., Yin C., Doong H., Fang S., Peterhoff C., Nixon R.A., Monteiro M.J.
J. Cell Sci. 119:4011-4024(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBXD2.
[24]"The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD."
Lerner M., Corcoran M., Cepeda D., Nielsen M.L., Zubarev R., Ponten F., Uhlen M., Hober S., Grander D., Sangfelt O.
Mol. Biol. Cell 18:1670-1682(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM13.
[25]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[26]"Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated degradation pathway."
Maruyama Y., Yamada M., Takahashi K., Yamada M.
Biochem. Biophys. Res. Commun. 374:737-741(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF103.
[27]"Ubxd1 is a novel co-factor of the human p97 ATPase."
Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M., Hartmann-Petersen R.
Int. J. Biochem. Cell Biol. 40:2927-2942(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBXN6.
[28]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-436 AND SER-787, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"Ro52 functionally interacts with IgG1 and regulates its quality control via the ERAD system."
Takahata M., Bohgaki M., Tsukiyama T., Kondo T., Asaka M., Hatakeyama S.
Mol. Immunol. 45:2045-2054(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM21.
[30]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER."
Ernst R., Mueller B., Ploegh H.L., Schlieker C.
Mol. Cell 36:28-38(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YOD1.
[32]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770 AND SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[34]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CANX; DERL1; DERL2; DDOST; RPN1; RPN2; SELK; STT3A AND VIMP.
[37]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins."
Fleig L., Bergbold N., Sahasrabudhe P., Geiger B., Kaltak L., Lemberg M.K.
Mol. Cell 47:558-569(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHBDD1, MUTAGENESIS OF LYS-251; LYS-524 AND GLU-578, IDENTIFICATION BY MASS SPECTROMETRY.
[39]"The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks."
Meerang M., Ritz D., Paliwal S., Garajova Z., Bosshard M., Mailand N., Janscak P., Hubscher U., Meyer H., Ramadan K.
Nat. Cell Biol. 13:1376-1382(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[40]"The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks."
Acs K., Luijsterburg M.S., Ackermann L., Salomons F.A., Hoppe T., Dantuma N.P.
Nat. Struct. Mol. Biol. 18:1345-1350(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH L3MBTL1.
[41]"Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a regulator of translesion synthesis."
Ghosal G., Leung J.W., Nair B.C., Fong K.W., Chen J.
J. Biol. Chem. 287:34225-34233(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPRTN.
[42]"STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein."
Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T., Morino-Koga S., Wada I., Kai H.
Mol. Cell 47:99-110(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ERAD PATHWAY.
[43]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"Lysine methylation of VCP by a member of a novel human protein methyltransferase family."
Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S., Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.
Nat. Commun. 3:1038-1038(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-315, MUTAGENESIS OF LYS-312; ARG-313; GLU-314; LYS-315; THR-316; HIS-317 AND GLY-318.
[45]"DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA damage."
Davis E.J., Lachaud C., Appleton P., Macartney T.J., Nathke I., Rouse J.
Nat. Struct. Mol. Biol. 19:1093-1100(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SPRTN.
[46]"DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes ubiquitin-dependent responses to replication blocks."
Mosbech A., Gibbs-Seymour I., Kagias K., Thorslund T., Beli P., Povlsen L., Nielsen S.V., Smedegaard S., Sedgwick G., Lukas C., Hartmann-Petersen R., Lukas J., Choudhary C., Pocock R., Bekker-Jensen S., Mailand N.
Nat. Struct. Mol. Biol. 19:1084-1092(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPRTN.
[47]"A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants."
Tang W.K., Li D., Li C.C., Esser L., Dai R., Guo L., Xia D.
EMBO J. 29:2217-2229(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-481 IN COMPLEX WITH ATP ANALOG, CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95 AND HIS-155, MUTAGENESIS OF ARG-53 AND ARG-86, SUBUNIT.
[48]"Structure and function of the PLAA/Ufd3-p97/Cdc48 complex."
Qiu L., Pashkova N., Walker J.R., Winistorfer S., Allali-Hassani A., Akutsu M., Piper R., Dhe-Paganon S.
J. Biol. Chem. 285:365-372(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 797-806 IN COMPLEX WITH PLAA.
[49]"Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein."
Watts G.D.J., Wymer J., Kovach M.J., Mehta S.G., Mumm S., Darvish D., Pestronk A., Whyte M.P., Kimonis V.E.
Nat. Genet. 36:377-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBMPFD1 GLY-95; CYS-155; HIS-155; PRO-155; GLN-191 AND GLU-232.
[50]"Mutant valosin-containing protein causes a novel type of frontotemporal dementia."
Schroeder R., Watts G.D.J., Mehta S.G., Evert B.O., Broich P., Fliessbach K., Pauls K., Hans V.H., Kimonis V., Thal D.R.
Ann. Neurol. 57:457-461(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IBMPFD1 CYS-155.
[51]"Inclusion body myopathy and Paget disease is linked to a novel mutation in the VCP gene."
Haubenberger D., Bittner R.E., Rauch-Shorny S., Zimprich F., Mannhalter C., Wagner L., Mineva I., Vass K., Auff E., Zimprich A.
Neurology 65:1304-1305(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IBMPFD1 HIS-159.
[52]"Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation."
Weihl C.C., Dalal S., Pestronk A., Hanson P.I.
Hum. Mol. Genet. 15:189-199(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95 AND HIS-155.
[53]"Exome sequencing reveals VCP mutations as a cause of familial ALS."
Johnson J.O., Mandrioli J., Benatar M., Abramzon Y., Van Deerlin V.M., Trojanowski J.Q., Gibbs J.R., Brunetti M., Gronka S., Wuu J., Ding J., McCluskey L., Martinez-Lage M., Falcone D., Hernandez D.G., Arepalli S., Chong S., Schymick J.C. expand/collapse author list , Rothstein J., Landi F., Wang Y.D., Calvo A., Mora G., Sabatelli M., Monsurro M.R., Battistini S., Salvi F., Spataro R., Sola P., Borghero G., Galassi G., Scholz S.W., Taylor J.P., Restagno G., Chio A., Traynor B.J.
Neuron 68:857-864(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS14 HIS-155; GLY-159; GLN-191 AND ASN-592.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC004472 Genomic DNA. Translation: AAC07984.1.
AF100752 mRNA. Translation: AAD43016.1.
AK312310 mRNA. Translation: BAG35235.1.
AL353795 Genomic DNA. Translation: CAH70993.1.
CH471071 Genomic DNA. Translation: EAW58404.1.
BC110913 mRNA. Translation: AAI10914.1.
BC121794 mRNA. Translation: AAI21795.1.
Z70768 mRNA. Translation: CAA94809.1.
PIRT02243.
RefSeqNP_009057.1. NM_007126.3.
UniGeneHs.529782.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EBBX-ray1.90E/F/G/H797-806[»]
3HU1X-ray2.81A/B/C/D/E/F1-481[»]
3HU2X-ray2.85A/B/C/D/E/F1-481[»]
3HU3X-ray2.20A/B1-481[»]
3QC8X-ray2.20A21-196[»]
3QQ7X-ray2.65A2-187[»]
3QQ8X-ray2.00A2-187[»]
3QWZX-ray2.00A1-208[»]
3TIWX-ray1.80A/B1-187[»]
4KLNX-ray2.62A/B/C/D/E/F1-481[»]
4KO8X-ray1.98A/B1-481[»]
4KODX-ray2.96A/B/C/D/E/F/G/H/I/J/K/L1-481[»]
ProteinModelPortalP55072.
SMRP55072. Positions 10-763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113258. 448 interactions.
DIPDIP-33543N.
IntActP55072. 55 interactions.
MINTMINT-272884.
STRING9606.ENSP00000351777.

Chemistry

BindingDBP55072.
ChEMBLCHEMBL1075145.

Protein family/group databases

TCDB3.A.16.1.1. the endoplasmic reticular retrotranslocon (er-rt) family.

PTM databases

PhosphoSiteP55072.

Polymorphism databases

DMDM6094447.

2D gel databases

DOSAC-COBS-2DPAGEP55072.
OGPP55072.
REPRODUCTION-2DPAGEIPI00022774.
P55072.

Proteomic databases

PaxDbP55072.
PRIDEP55072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358901; ENSP00000351777; ENSG00000165280.
GeneID7415.
KEGGhsa:7415.
UCSCuc003zvy.2. human.

Organism-specific databases

CTD7415.
GeneCardsGC09M035056.
HGNCHGNC:12666. VCP.
HPACAB005593.
HPA012728.
HPA012814.
MIM167320. phenotype.
601023. gene.
613954. phenotype.
neXtProtNX_P55072.
Orphanet329478. Adult-onset distal myopathy due to VCP mutation.
803. Amyotrophic lateral sclerosis.
275864. Behavioral variant of frontotemporal dementia.
52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
100070. Progressive non-fluent aphasia.
100069. Semantic dementia.
329475. Spastic paraplegia - Paget disease of bone.
PharmGKBPA37289.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0464.
HOGENOMHOG000223224.
HOVERGENHBG001226.
InParanoidP55072.
KOK13525.
OMADKFLKYG.
OrthoDBEOG7H4DSW.
PhylomeDBP55072.
TreeFamTF300542.

Enzyme and pathway databases

SignaLinkP55072.

Gene expression databases

ArrayExpressP55072.
BgeeP55072.
CleanExHS_VCP.
GenevestigatorP55072.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR005938. AAA_ATPase_CDC48.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR01243. CDC48. 1 hit.
PROSITEPS00674. AAA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVCP. human.
EvolutionaryTraceP55072.
GeneWikiValosin-containing_protein.
GenomeRNAi7415.
NextBio29034.
PROP55072.
SOURCESearch...

Entry information

Entry nameTERA_HUMAN
AccessionPrimary (citable) accession number: P55072
Secondary accession number(s): B2R5T8 expand/collapse secondary AC list , Q0V924, Q2TAI5, Q969G7, Q9UCD5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM