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P55072

- TERA_HUMAN

UniProt

P55072 - TERA_HUMAN

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Protein
Transitional endoplasmic reticulum ATPase
Gene
VCP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei348 – 3481ATP
Binding sitei384 – 3841ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi247 – 2537ATP

GO - Molecular functioni

  1. ADP binding Source: Ensembl
  2. ATP binding Source: UniProtKB-KW
  3. ATPase activity Source: UniProtKB
  4. deubiquitinase activator activity Source: ParkinsonsUK-UCL
  5. lipid binding Source: UniProtKB-KW
  6. poly(A) RNA binding Source: UniProtKB
  7. polyubiquitin binding Source: BHF-UCL
  8. protein binding Source: UniProtKB
  9. protein domain specific binding Source: UniProtKB
  10. protein phosphatase binding Source: BHF-UCL
  11. ubiquitin-specific protease binding Source: ParkinsonsUK-UCL
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: UniProtKB
  2. ER to Golgi vesicle-mediated transport Source: Ensembl
  3. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  5. aggresome assembly Source: Ensembl
  6. cellular response to DNA damage stimulus Source: UniProtKB
  7. double-strand break repair Source: UniProtKB
  8. endoplasmic reticulum unfolded protein response Source: UniProtKB
  9. establishment of protein localization Source: UniProtKB
  10. positive regulation of Lys63-specific deubiquitinase activity Source: ParkinsonsUK-UCL
  11. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  12. positive regulation of protein K63-linked deubiquitination Source: ParkinsonsUK-UCL
  13. positive regulation of protein catabolic process Source: BHF-UCL
  14. positive regulation of protein complex assembly Source: BHF-UCL
  15. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  16. protein N-linked glycosylation via asparagine Source: UniProtKB
  17. protein homooligomerization Source: Ensembl
  18. protein ubiquitination Source: UniProtKB
  19. regulation of apoptotic process Source: UniProtKB
  20. retrograde protein transport, ER to cytosol Source: UniProtKB
  21. translesion synthesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Transport, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_200744. HSF1 activation.
SignaLinkiP55072.

Protein family/group databases

TCDBi3.A.16.1.1. the endoplasmic reticular retrotranslocon (er-rt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transitional endoplasmic reticulum ATPase (EC:3.6.4.6)
Short name:
TER ATPase
Alternative name(s):
15S Mg(2+)-ATPase p97 subunit
Valosin-containing protein
Short name:
VCP
Gene namesi
Name:VCP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:12666. VCP.

Subcellular locationi

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.5 Publications

GO - Cellular componenti

  1. Hrd1p ubiquitin ligase complex Source: UniProt
  2. cytoplasm Source: HPA
  3. cytosol Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. endoplasmic reticulum membrane Source: UniProt
  6. extracellular vesicular exosome Source: UniProt
  7. intracellular membrane-bounded organelle Source: UniProtKB
  8. lipid particle Source: MGI
  9. nucleus Source: UniProtKB
  10. perinuclear region of cytoplasm Source: ParkinsonsUK-UCL
  11. proteasome complex Source: BHF-UCL
  12. site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.6 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951R → 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. 3 Publications
VAR_033016
Natural varianti155 – 1551R → C in IBMPFD1; also in one patient without evidence of Paget disease of the bone. 2 Publications
VAR_033017
Natural varianti155 – 1551R → 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. 5 Publications
VAR_033018
Natural varianti155 – 1551R → P in IBMPFD1. 1 Publication
VAR_033019
Natural varianti159 – 1591R → H in IBMPFD1; without frontotemporal dementia; abolishes enhancement of K-315 methylation by ASPSCR1. 1 Publication
VAR_033020
Natural varianti191 – 1911R → Q in ALS14 and IBMPFD1; abolishes enhancement of K-315 methylation by ASPSCR1. 3 Publications
VAR_033021
Natural varianti232 – 2321A → E in IBMPFD1. 1 Publication
VAR_033022
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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551R → 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. 5 Publications
VAR_033018
Natural varianti159 – 1591R → G in ALS14. 2 Publications
VAR_065910
Natural varianti191 – 1911R → Q in ALS14 and IBMPFD1; abolishes enhancement of K-315 methylation by ASPSCR1. 3 Publications
VAR_033021
Natural varianti592 – 5921D → N in ALS14; ALS14 patients do not show frontotemporal dementia. 1 Publication
VAR_065911

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531R → A: Minor effect on affinity for ATP and ADP. 1 Publication
Mutagenesisi86 – 861R → A: Strongly increased affinity for ATP. Strongly reduced affinity for ADP. 1 Publication
Mutagenesisi251 – 2511K → Q: Impairs ERAD degradation of HMGCR and does not inhibit interaction with RHBDD1; when associated with Q-524. 2 Publications
Mutagenesisi312 – 3121K → A: Does not affect methylation by VCPKMT. 1 Publication
Mutagenesisi313 – 3131R → A: Does not affect methylation by VCPKMT. 1 Publication
Mutagenesisi314 – 3141E → A: Does not affect methylation by VCPKMT. 1 Publication
Mutagenesisi314 – 3141Missing: Strongly impairs methylation by VCPKMT. 1 Publication
Mutagenesisi315 – 3151K → L, Q or R: Abolishes methylation by VCPKMT. 2 Publications
Mutagenesisi316 – 3161T → A: Does not affect methylation by VCPKMT. 1 Publication
Mutagenesisi317 – 3171H → A: Does not affect methylation by VCPKMT. 1 Publication
Mutagenesisi318 – 3181G → A: Does not affect methylation by VCPKMT. 1 Publication
Mutagenesisi524 – 5241K → A: Impairs catalytic activity of RNF19A toward SOD1 mutant. Does not inhibit interaction with RHBDD1; when associated with A-251. 3 Publications
Mutagenesisi524 – 5241K → Q: Impairs ERAD degradation of HMGCR; when associated with Q-251. 3 Publications
Mutagenesisi578 – 5781E → Q: Does not inhibit interaction with RHBDD1. 1 Publication

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

MIMi167320. phenotype.
613954. phenotype.
Orphaneti329478. 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.
PharmGKBiPA37289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 806805Transitional endoplasmic reticulum ATPase
PRO_0000084572Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei3 – 31Phosphoserine3 Publications
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei315 – 3151N6,N6,N6-trimethyllysine; by VCPKMT2 Publications
Modified residuei436 – 4361Phosphothreonine1 Publication
Modified residuei502 – 5021N6-acetyllysine By similarity
Modified residuei505 – 5051N6-acetyllysine By similarity
Modified residuei668 – 6681N6-acetyllysine; alternate By similarity
Modified residuei668 – 6681N6-succinyllysine; alternate By similarity
Modified residuei754 – 7541N6-acetyllysine By similarity
Modified residuei770 – 7701Phosphoserine1 Publication
Modified residuei775 – 7751Phosphoserine1 Publication
Modified residuei787 – 7871Phosphoserine1 Publication
Modified residuei805 – 8051Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation By similarity.
ISGylated.1 Publication
Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity.2 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP55072.
PaxDbiP55072.
PRIDEiP55072.

2D gel databases

DOSAC-COBS-2DPAGEP55072.
OGPiP55072.
REPRODUCTION-2DPAGEIPI00022774.
P55072.

PTM databases

PhosphoSiteiP55072.

Expressioni

Gene expression databases

ArrayExpressiP55072.
BgeeiP55072.
CleanExiHS_VCP.
GenevestigatoriP55072.

Organism-specific databases

HPAiCAB005593.
HPA012728.
HPA012814.

Interactioni

Subunit structurei

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-terminal 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. Interacts with KIAA0196.24 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMFRQ9UKV56EBI-355164,EBI-1046367
ASPSCR1Q9BZE93EBI-355164,EBI-1993677
ATXN3P542528EBI-355164,EBI-946046
ATXN3P54252-110EBI-355164,EBI-946068
CHEK2O960172EBI-355164,EBI-1180783
FCHSD2O948682EBI-355164,EBI-1215612
NSFL1CQ9UNZ24EBI-355164,EBI-721577
PTPN3P260452EBI-355164,EBI-1047946
UBE4BB1AQ614EBI-355164,EBI-7931266
UBXN4Q925752EBI-355164,EBI-723441
UBXN6Q9BZV17EBI-355164,EBI-1993899
YWHAZP631042EBI-355164,EBI-347088

Protein-protein interaction databases

BioGridi113258. 458 interactions.
DIPiDIP-33543N.
IntActiP55072. 57 interactions.
MINTiMINT-272884.
STRINGi9606.ENSP00000351777.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni15 – 173
Beta strandi25 – 306
Beta strandi38 – 414
Helixi43 – 497
Beta strandi56 – 605
Helixi62 – 643
Beta strandi66 – 738
Beta strandi75 – 773
Beta strandi81 – 844
Helixi86 – 916
Beta strandi99 – 1046
Beta strandi112 – 1187
Helixi120 – 1234
Helixi130 – 1334
Helixi135 – 1395
Turni140 – 1423
Beta strandi145 – 1473
Beta strandi151 – 1555
Beta strandi157 – 17519
Beta strandi181 – 1833
Helixi191 – 1933
Helixi203 – 2053
Helixi210 – 21910
Helixi221 – 2255
Helixi227 – 2337
Beta strandi240 – 2445
Beta strandi246 – 2505
Helixi251 – 26111
Beta strandi263 – 2708
Helixi271 – 2755
Helixi281 – 29515
Beta strandi298 – 3058
Helixi306 – 3083
Helixi313 – 3153
Helixi319 – 33315
Helixi337 – 3393
Beta strandi341 – 3488
Helixi350 – 3523
Helixi355 – 3584
Beta strandi365 – 3684
Helixi374 – 38512
Helixi396 – 4016
Helixi408 – 42417
Turni425 – 4295
Beta strandi432 – 4365
Helixi439 – 4446
Helixi449 – 4579
Beta strandi458 – 4614
Turni462 – 4687

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4KDIX-ray1.86A/B21-196[»]
4KDLX-ray1.81A21-196[»]
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[»]
4P0AX-ray2.30B/D797-806[»]
ProteinModelPortaliP55072.
SMRiP55072. Positions 14-763.

Miscellaneous databases

EvolutionaryTraceiP55072.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni797 – 80610Interaction with UBXN6

Sequence similaritiesi

Belongs to the AAA ATPase family.

Phylogenomic databases

eggNOGiCOG0464.
HOGENOMiHOG000223224.
HOVERGENiHBG001226.
InParanoidiP55072.
KOiK13525.
OMAiHKKVNLT.
OrthoDBiEOG7H4DSW.
PhylomeDBiP55072.
TreeFamiTF300542.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR005938. AAA_ATPase_CDC48.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
TIGRFAMsiTIGR01243. CDC48. 1 hit.
PROSITEiPS00674. AAA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55072-1 [UniParc]FASTAAdd to Basket

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MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ    50
LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI 100
SIQPCPDVKY GKRIHVLPID DTVEGITGNL FEVYLKPYFL EAYRPIRKGD 150
IFLVRGGMRA VEFKVVETDP SPYCIVAPDT VIHCEGEPIK REDEEESLNE 200
VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG ILLYGPPGTG 250
KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI 300
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP 350
NSIDPALRRF GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA 400
NETHGHVGAD LAALCSEAAL QAIRKKMDLI DLEDETIDAE VMNSLAVTMD 450
DFRWALSQSN PSALRETVVE VPQVTWEDIG GLEDVKRELQ ELVQYPVEHP 500
DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI SIKGPELLTM 550
WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 600
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE 650
KSRVAILKAN LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR 700
ESIESEIRRE RERQTNPSAM EVEEDDPVPE IRRDHFEEAM RFARRSVSDN 750
DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG AGPSQGSGGG TGGSVYTEDN 800
DDDLYG 806
Length:806
Mass (Da):89,322
Last modified:January 23, 2007 - v4
Checksum:i501B721D3A77BA8A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951R → 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. 3 Publications
VAR_033016
Natural varianti155 – 1551R → C in IBMPFD1; also in one patient without evidence of Paget disease of the bone. 2 Publications
VAR_033017
Natural varianti155 – 1551R → 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. 5 Publications
VAR_033018
Natural varianti155 – 1551R → P in IBMPFD1. 1 Publication
VAR_033019
Natural varianti159 – 1591R → G in ALS14. 2 Publications
VAR_065910
Natural varianti159 – 1591R → H in IBMPFD1; without frontotemporal dementia; abolishes enhancement of K-315 methylation by ASPSCR1. 1 Publication
VAR_033020
Natural varianti191 – 1911R → Q in ALS14 and IBMPFD1; abolishes enhancement of K-315 methylation by ASPSCR1. 3 Publications
VAR_033021
Natural varianti232 – 2321A → E in IBMPFD1. 1 Publication
VAR_033022
Natural varianti592 – 5921D → N in ALS14; ALS14 patients do not show frontotemporal dementia. 1 Publication
VAR_065911

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691D → H in AAI21795. 1 Publication
Sequence conflicti312 – 3121K → I in BAG35235. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6573.1.
PIRiT02243.
RefSeqiNP_009057.1. NM_007126.3.
UniGeneiHs.529782.

Genome annotation databases

EnsembliENST00000358901; ENSP00000351777; ENSG00000165280.
GeneIDi7415.
KEGGihsa:7415.
UCSCiuc003zvy.2. human.

Polymorphism databases

DMDMi6094447.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6573.1.
PIRi T02243.
RefSeqi NP_009057.1. NM_007126.3.
UniGenei Hs.529782.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EBB X-ray 1.90 E/F/G/H 797-806 [» ]
3HU1 X-ray 2.81 A/B/C/D/E/F 1-481 [» ]
3HU2 X-ray 2.85 A/B/C/D/E/F 1-481 [» ]
3HU3 X-ray 2.20 A/B 1-481 [» ]
3QC8 X-ray 2.20 A 21-196 [» ]
3QQ7 X-ray 2.65 A 2-187 [» ]
3QQ8 X-ray 2.00 A 2-187 [» ]
3QWZ X-ray 2.00 A 1-208 [» ]
3TIW X-ray 1.80 A/B 1-187 [» ]
4KDI X-ray 1.86 A/B 21-196 [» ]
4KDL X-ray 1.81 A 21-196 [» ]
4KLN X-ray 2.62 A/B/C/D/E/F 1-481 [» ]
4KO8 X-ray 1.98 A/B 1-481 [» ]
4KOD X-ray 2.96 A/B/C/D/E/F/G/H/I/J/K/L 1-481 [» ]
4P0A X-ray 2.30 B/D 797-806 [» ]
ProteinModelPortali P55072.
SMRi P55072. Positions 14-763.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113258. 458 interactions.
DIPi DIP-33543N.
IntActi P55072. 57 interactions.
MINTi MINT-272884.
STRINGi 9606.ENSP00000351777.

Chemistry

BindingDBi P55072.
ChEMBLi CHEMBL1075145.

Protein family/group databases

TCDBi 3.A.16.1.1. the endoplasmic reticular retrotranslocon (er-rt) family.

PTM databases

PhosphoSitei P55072.

Polymorphism databases

DMDMi 6094447.

2D gel databases

DOSAC-COBS-2DPAGE P55072.
OGPi P55072.
REPRODUCTION-2DPAGE IPI00022774.
P55072.

Proteomic databases

MaxQBi P55072.
PaxDbi P55072.
PRIDEi P55072.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358901 ; ENSP00000351777 ; ENSG00000165280 .
GeneIDi 7415.
KEGGi hsa:7415.
UCSCi uc003zvy.2. human.

Organism-specific databases

CTDi 7415.
GeneCardsi GC09M035056.
GeneReviewsi VCP.
HGNCi HGNC:12666. VCP.
HPAi CAB005593.
HPA012728.
HPA012814.
MIMi 167320. phenotype.
601023. gene.
613954. phenotype.
neXtProti NX_P55072.
Orphaneti 329478. 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.
PharmGKBi PA37289.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0464.
HOGENOMi HOG000223224.
HOVERGENi HBG001226.
InParanoidi P55072.
KOi K13525.
OMAi HKKVNLT.
OrthoDBi EOG7H4DSW.
PhylomeDBi P55072.
TreeFami TF300542.

Enzyme and pathway databases

Reactomei REACT_200744. HSF1 activation.
SignaLinki P55072.

Miscellaneous databases

ChiTaRSi VCP. human.
EvolutionaryTracei P55072.
GeneWikii Valosin-containing_protein.
GenomeRNAii 7415.
NextBioi 29034.
PROi P55072.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55072.
Bgeei P55072.
CleanExi HS_VCP.
Genevestigatori P55072.

Family and domain databases

Gene3Di 3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR005938. AAA_ATPase_CDC48.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view ]
Pfami PF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
TIGRFAMsi TIGR01243. CDC48. 1 hit.
PROSITEi PS00674. AAA. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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.
    , 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.
    , 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. 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. 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. 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. 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. 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. "Strumpellin is a novel valosin-containing protein binding partner linking hereditary spastic paraplegia to protein aggregation diseases."
    Clemen C.S., Tangavelou K., Strucksberg K.H., Just S., Gaertner L., Regus-Leidig H., Stumpf M., Reimann J., Coras R., Morgan R.O., Fernandez M.P., Hofmann A., Muller S., Schoser B., Hanisch F.G., Rottbauer W., Blumcke I., von Horsten S., Eichinger L., Schroder R.
    Brain 133:2920-2941(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIAA0196.
  35. "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.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "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.
  38. "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].
  39. "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.
  40. "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.
  41. "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.
  42. "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.
  43. "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.
  44. "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].
  45. "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.
  46. "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.
  47. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPRTN.
  48. "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.
  49. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 797-806 IN COMPLEX WITH PLAA.
  50. "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.
  51. "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.
  52. "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.
  53. "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.
  54. Cited for: VARIANTS ALS14 HIS-155; GLY-159; GLN-191 AND ASN-592.

Entry informationi

Entry nameiTERA_HUMAN
AccessioniPrimary (citable) accession number: P55072
Secondary accession number(s): B2R5T8
, Q0V924, Q2TAI5, Q969G7, Q9UCD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 159 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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 (1 Publication). According to a second report, it acts by removing 'Lys-48'-linked ubiquitination from sites of DNA damage (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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