P55072 (TERA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	806 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.13 Ref.17 Ref.36 Ref.37 Ref.39 Ref.41 Ref.42
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 METTL21D. Interacts with SPRTN; leading to recruitment to stalled replication forks. Ref.9 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.28 Ref.29 Ref.35 Ref.37 Ref.38 Ref.40 Ref.41 Ref.42 Ref.43
Subcellular location	Cytoplasm › cytosol. Endoplasmic reticulum. Nucleus. Note: Present in the neuronal hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy bodies specifically found in neurons from 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.13 Ref.17 Ref.37 Ref.42
Post-translational modification	Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation By similarity. ISGylated. Ref.15
Involvement in disease	Inclusion body myopathy with early-onset Paget disease and frontotemporal dementia (IBMPFD) [MIM:167320]: A disease with features of adult-onset proximal and distal muscle weakness (clinically resembling limb girdle muscular dystrophy), early-onset Paget disease of bone in most cases and premature frontotemporal dementia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.43 Ref.45 Ref.46 Ref.47 Ref.48 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.49
Sequence similarities	Belongs to the AAA ATPase family.
Caution	It is unclear how it participates to 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.37). According to a second report, it acts by removing 'Lys-48'-linked ubiquitination from sites of DNA damage (Ref.36).

Ontologies

Keywords
Biological process	DNA damage DNA repair Transport Ubl conjugation pathway
Cellular component	Cytoplasm Endoplasmic reticulum Nucleus
Disease	Amyotrophic lateral sclerosis Disease mutation Neurodegeneration
Ligand	ATP-binding Lipid-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ER to Golgi vesicle-mediated transport Inferred from electronic annotation. Source: Compara ER-associated protein catabolic process Inferred from mutant phenotype Ref.39. 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: Compara double-strand break repair Inferred from direct assay PubMed 10855792Ref.37. Source: UniProtKB endoplasmic reticulum unfolded protein response Traceable author statement Ref.14. Source: UniProtKB positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay PubMed 9452483. Source: BHF-UCL positive regulation of protein complex assembly Inferred from direct assay PubMed 18775313. Source: BHF-UCL protein N-linked glycosylation via asparagine Inferred from mutant phenotype Ref.39. Source: UniProtKB protein homooligomerization Inferred from electronic annotation. Source: Compara protein ubiquitination Inferred from direct assay Ref.37. Source: UniProtKB retrograde protein transport, ER to cytosol Inferred from direct assay Ref.14. Source: UniProtKB translesion synthesis Inferred from mutant phenotype Ref.42. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 10855792Ref.14. Source: UniProtKB endoplasmic reticulum Inferred from direct assay Ref.14. Source: UniProtKB nucleus Inferred from direct assay PubMed 10855792. Source: UniProtKB proteasome complex Inferred from direct assay PubMed 9452483. Source: BHF-UCL site of double-strand break Inferred from direct assay Ref.37. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Traceable author statement Ref.14. Source: UniProtKB lipid binding Inferred from electronic annotation. Source: UniProtKB-KW polyubiquitin binding Inferred from direct assay PubMed 11483959. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AMFR	Q9UKV5	6	EBI-355164,EBI-1046367
ASPSCR1	Q9BZE9	2	EBI-355164,EBI-1993677
ATXN3	P54252	5	EBI-355164,EBI-946046
ATXN3	P54252-1	10	EBI-355164,EBI-946068
CHEK2	O96017	2	EBI-355164,EBI-1180783
FCHSD2	O94868	2	EBI-355164,EBI-1215612
UBXN4	Q92575	2	EBI-355164,EBI-723441
UBXN6	Q9BZV1	7	EBI-355164,EBI-1993899

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

Chain

2 – 806

805

Transitional endoplasmic reticulum ATPase

PRO_0000084572

Regions

Nucleotide binding

247 – 253

7

ATP

Region

797 – 806

10

Interaction with UBXN6

Sites

Binding site

348

1

ATP

Binding site

384

1

ATP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8 Ref.30 Ref.34

Modified residue

3

1

Phosphoserine Ref.27 Ref.30 Ref.34

Modified residue

7

1

Phosphoserine By similarity

Modified residue

37

1

Phosphoserine Ref.30

Modified residue

315

1

N6,N6,N6-trimethyllysine; by METTL21D Ref.40

Modified residue

436

1

Phosphothreonine Ref.27

Modified residue

770

1

Phosphoserine Ref.31 Ref.34

Modified residue

775

1

Phosphoserine Ref.31

Modified residue

787

1

Phosphoserine Ref.27

Natural variations

Natural variant

95

1

R → G in IBMPFD; 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.43 Ref.45 Ref.48

VAR_033016

Natural variant

155

1

R → C in IBMPFD; also in one patient without evidence of Paget disease of the bone. Ref.45 Ref.46

VAR_033017

Natural variant

155

1

R → H in ALS14 and IBMPFD; 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.43 Ref.45 Ref.48 Ref.49

VAR_033018

Natural variant

155

1

R → P in IBMPFD. Ref.45

VAR_033019

Natural variant

159

1

R → G in ALS14. Ref.49

VAR_065910

Natural variant

159

1

R → H in IBMPFD; without frontotemporal dementia. Ref.47

VAR_033020

Natural variant

191

1

R → Q in ALS14 and IBMPFD. Ref.45 Ref.49

VAR_033021

Natural variant

232

1

A → E in IBMPFD. Ref.45

VAR_033022

Natural variant

592

1

D → N in ALS14; ALS14 patients do not show frontotemporal dementia. Ref.49

VAR_065911

Experimental info

Mutagenesis

53

1

R → A: Minor effect on affinity for ATP and ADP. Ref.43

Mutagenesis

86

1

R → A: Strongly increased affinity for ATP. Strongly reduced affinity for ADP. Ref.43

Mutagenesis

251

1

K → Q: Impairs ERAD degradation of HMGCR and does not inhibit interaction with RHBDD1; when associated with Q-524. Ref.17 Ref.35

Mutagenesis

312

1

K → A: Does not affect methylation by METTL21D. Ref.40

Mutagenesis

313

1

R → A: Does not affect methylation by METTL21D. Ref.40

Mutagenesis

314

1

E → A: Does not affect methylation by METTL21D. Ref.40

Mutagenesis

314

1

Missing: Strongly impairs methylation by METTL21D. Ref.40

Mutagenesis

315

1

K → L, Q or R: Abolishes methylation by METTL21D. Ref.40

Mutagenesis

316

1

T → A: Does not affect methylation by METTL21D. Ref.40

Mutagenesis

317

1

H → A: Does not affect methylation by METTL21D. Ref.40

Mutagenesis

318

1

G → A: Does not affect methylation by METTL21D. Ref.40

Mutagenesis

524

1

K → A: Impairs catalytic activity of RNF19A toward SOD1 mutant. Does not inhibit interaction with RHBDD1; when associated with A-251. Ref.13 Ref.17 Ref.35

Mutagenesis

524

1

K → Q: Impairs ERAD degradation of HMGCR; when associated with Q-251. Ref.13 Ref.17 Ref.35

Mutagenesis

578

1

E → Q: Does not inhibit interaction with RHBDD1. Ref.35

Sequence conflict

169

1

D → H in AAI21795. Ref.6

Sequence conflict

312

1

K → I in BAG35235. Ref.3

Secondary structure

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806

Helix Strand Turn

Details...

Helix

14 – 17

4

Beta strand

25 – 30

6

Beta strand

38 – 41

4

Helix

43 – 49

7

Beta strand

56 – 60

5

Helix

62 – 64

3

Beta strand

66 – 73

8

Beta strand

75 – 77

3

Beta strand

81 – 84

4

Helix

86 – 91

6

Beta strand

99 – 104

6

Beta strand

112 – 118

7

Helix

120 – 122

3

Helix

123 – 126

4

Helix

130 – 133

4

Helix

135 – 139

5

Turn

140 – 142

3

Beta strand

145 – 147

3

Beta strand

151 – 155

5

Beta strand

157 – 175

19

Beta strand

181 – 183

3

Helix

193 – 195

3

Helix

203 – 205

3

Helix

210 – 219

10

Helix

221 – 225

5

Helix

227 – 233

7

Beta strand

240 – 244

5

Helix

251 – 261

11

Beta strand

263 – 270

8

Helix

271 – 275

5

Helix

281 – 295

15

Beta strand

298 – 305

8

Helix

306 – 309

4

Beta strand

313 – 315

3

Helix

319 – 334

16

Helix

337 – 339

3

Beta strand

341 – 348

8

Helix

350 – 352

3

Helix

355 – 358

4

Beta strand

365 – 368

4

Helix

374 – 384

11

Turn

385 – 387

3

Helix

396 – 401

6

Helix

408 – 424

17

Turn

425 – 429

5

Beta strand

432 – 436

5

Helix

439 – 444

6

Helix

449 – 456

8

Helix

459 – 465

7

Helix

466 – 468

3

Sequences

	Sequence		Length	Mass (Da)
	P55072 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 501B721D3A77BA8A	FASTA	806	89,322
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	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. , 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, 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, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[11]	"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.
[12]	"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.
[13]	"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, MASS SPECTROMETRY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-524.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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.
[29]	"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.
[30]	"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, MASS SPECTROMETRY.
[31]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[32]	"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.
[33]	"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].
[34]	"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 AND SER-770, MASS SPECTROMETRY.
[35]	"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, MASS SPECTROMETRY.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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, SUBUNIT, INTERACTION WITH METTL21D, MUTAGENESIS OF LYS-312; ARG-313; GLU-314; LYS-315; THR-316; HIS-317 AND GLY-318.
[41]	"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.
[42]	"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.
[43]	"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 IBMPFD GLY-95 AND HIS-155, MUTAGENESIS OF ARG-53 AND ARG-86, SUBUNIT.
[44]	"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.
[45]	"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 IBMPFD GLY-95; CYS-155; HIS-155; PRO-155; GLN-191 AND GLU-232.
[46]	"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 IBMPFD CYS-155.
[47]	"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 IBMPFD HIS-159.
[48]	"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 IBMPFD GLY-95 AND HIS-155.
[49]	"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. , 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

GeneReviews

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.

IPI

IPI00022774.

PIR

T02243.

RefSeq

NP_009057.1. NM_007126.3.

UniGene

Hs.529782.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P55072.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33543N.

IntAct

P55072. 44 interactions.

MINT

MINT-272884.

STRING

9606.ENSP00000351777.

Protein family/group databases

TCDB

3.A.16.1.1. endoplasmic reticular retrotranslocon (ER-RT) family.

PTM databases

PhosphoSite

P55072.

Polymorphism databases

DMDM

6094447.

2D gel databases

DOSAC-COBS-2DPAGE

P55072.

OGP

P55072.

REPRODUCTION-2DPAGE

IPI00022774.
P55072.

Proteomic databases

PaxDb

P55072.

PRIDE

P55072.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358901; ENSP00000351777; ENSG00000165280.

GeneID

7415.

KEGG

hsa:7415.

UCSC

uc003zvy.2. human.

Organism-specific databases

CTD

7415.

GeneCards

GC09M035056.

HGNC

HGNC:12666. VCP.

HPA

CAB005593.
HPA012728.
HPA012814.

MIM

167320. phenotype.
601023. gene.
613954. phenotype.

neXtProt

NX_P55072.

Orphanet

803. Amyotrophic lateral sclerosis.
52430. Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.

PharmGKB

PA37289.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0464.

HOGENOM

HOG000223224.

HOVERGEN

HBG001226.

InParanoid

P55072.

KO

K13525.

OMA

AYRPIHK.

OrthoDB

EOG45TCMK.

Gene expression databases

ArrayExpress

P55072.

Bgee

P55072.

CleanEx

HS_VCP.

Genevestigator

P55072.

GermOnline

ENSG00000165280. Homo sapiens.

Family and domain databases

Gene3D

2.40.40.20. 1 hit.

InterPro

IPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR005938. ATPase_AAA_CDC48.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR003338. CDC4_N-term_subdom.
IPR015415. Vps4_C.
[Graphical view]

PANTHER

PTHR23077:SF18. PTHR23077:SF18. 1 hit.

Pfam

PF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]

SUPFAM

SSF50692. Asp_decarb_fold. 1 hit.

TIGRFAMs

TIGR01243. CDC48. 1 hit.

PROSITE

PS00674. AAA. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P55072.

ChEMBL

CHEMBL1075145.

ChiTaRS

VCP. human.

EvolutionaryTrace

P55072.

GenomeRNAi

7415.

NextBio

29034.

SOURCE

Search...

Entry information

Entry name

TERA_HUMAN

Accession

Primary (citable) accession number: P55072
Secondary accession number(s): B2R5T8 , Q0V924, Q2TAI5, Q969G7, Q9UCD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 144 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.