Q01853 (TERA_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity.
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. 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 By similarity. Interacts with SELS/VIMP 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). Ref.6 Ref.8 Ref.10 Ref.12
Subcellular location	Cytoplasm › cytosol. Nucleus. Endoplasmic reticulum By similarity. Note: 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 By similarity.
Domain	The N-terminal domain shows evolutionary conservation with that of PEX1, and is able to bind phospholipids with a preference for phosphatidylinositol mono- and bisphosphates.
Post-translational modification	Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. ISGylated. Ref.7
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transport Ubl conjugation pathway
Cellular component	Cytoplasm Endoplasmic reticulum Nucleus
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 sequence or structural similarity. Source: UniProtKB activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay PubMed 14561754. Source: MGI aggresome assembly Inferred from genetic interaction PubMed 16810319. Source: MGI double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara positive regulation of protein complex assembly Inferred from electronic annotation. Source: Compara protein N-linked glycosylation via asparagine Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from electronic annotation. Source: Compara protein ubiquitination Inferred from sequence or structural similarity. Source: UniProtKB retrograde protein transport, ER to cytosol Inferred from sequence or structural similarity. Source: UniProtKB translesion synthesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome complex Inferred from electronic annotation. Source: Compara protein complex Inferred from physical interaction PubMed 17785525. Source: MGI site of double-strand break Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: Compara 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	Q9R049	4	EBI-80597,EBI-3648125
Ngly1	Q9JI78	3	EBI-80597,EBI-3648128
VIMP	Q9BQE4	4	EBI-80597,EBI-398970	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 806

805

Transitional endoplasmic reticulum ATPase

PRO_0000084573

Regions

Nucleotide binding

247 – 253

7

ATP

Region

797 – 806

10

Interaction with UBXN6 By similarity

Sites

Binding site

348

1

ATP

Binding site

384

1

ATP

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

3

1

Phosphoserine By similarity

Modified residue

7

1

Phosphoserine Ref.13

Modified residue

37

1

Phosphoserine By similarity

Modified residue

315

1

N6,N6,N6-trimethyllysine; by METTL21D Ref.14

Modified residue

436

1

Phosphothreonine By similarity

Modified residue

770

1

Phosphoserine By similarity

Modified residue

775

1

Phosphoserine By similarity

Modified residue

787

1

Phosphoserine By similarity

Experimental info

Mutagenesis

144

1

R → A: Loss of phospholipid-binding. Ref.11

Sequence conflict

73

1

S → Y in BAC27119. Ref.2

Sequence conflict

199

1

N → Y in BAE39824. Ref.2

Sequence conflict

206

1

I → V in CAA78412. Ref.1

Sequence conflict

359

1

R → Q in BAC27119. Ref.2

Sequence conflict

439

1

A → T in BAE40919. Ref.2

Sequence conflict

624

1

N → S in BAE34876. Ref.2

Sequence conflict

684

1

G → V in BAC25849. Ref.2

Secondary structure

1

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806

Helix Strand Turn

Details...

Beta strand

25 – 29

5

Beta strand

38 – 41

4

Helix

43 – 48

6

Beta strand

56 – 60

5

Helix

62 – 64

3

Beta strand

66 – 73

8

Beta strand

75 – 77

3

Beta strand

79 – 83

5

Helix

86 – 91

6

Beta strand

99 – 104

6

Beta strand

106 – 110

5

Beta strand

114 – 119

6

Helix

120 – 122

3

Turn

123 – 125

3

Helix

130 – 133

4

Helix

135 – 139

5

Turn

140 – 142

3

Beta strand

144 – 147

4

Beta strand

151 – 156

6

Beta strand

159 – 176

18

Beta strand

181 – 183

3

Beta strand

193 – 195

3

Beta strand

198 – 200

3

Helix

203 – 205

3

Helix

211 – 225

15

Helix

227 – 232

6

Beta strand

240 – 244

5

Helix

251 – 261

11

Beta strand

265 – 269

5

Helix

271 – 274

4

Helix

281 – 295

15

Beta strand

298 – 305

8

Helix

306 – 308

3

Helix

312 – 315

4

Helix

321 – 333

13

Helix

337 – 339

3

Beta strand

341 – 348

8

Helix

350 – 352

3

Helix

355 – 357

3

Beta strand

365 – 368

4

Helix

374 – 383

10

Turn

384 – 387

4

Beta strand

388 – 390

3

Helix

396 – 402

7

Helix

408 – 430

23

Helix

439 – 444

6

Helix

449 – 456

8

Beta strand

457 – 460

4

Helix

476 – 478

3

Helix

483 – 498

16

Helix

500 – 506

7

Beta strand

512 – 517

6

Beta strand

519 – 523

5

Helix

524 – 534

11

Beta strand

538 – 542

5

Helix

544 – 552

9

Helix

558 – 568

11

Beta strand

571 – 576

6

Helix

581 – 585

5

Turn

586 – 590

5

Helix

599 – 609

11

Beta strand

615 – 624

10

Helix

626 – 628

3

Helix

631 – 634

4

Turn

636 – 638

3

Beta strand

641 – 644

4

Helix

650 – 661

12

Helix

672 – 677

6

Helix

684 – 706

23

Helix

733 – 740

8

Helix

749 – 762

14

Sequences

	Sequence		Length	Mass (Da)
	Q01853 [UniParc]. Last modified May 1, 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]	"VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation." Egerton M., Ashe O.R., Chen D., Druker B.J., Burgess W.H., Samelson L.E. EMBO J. 11:3533-3540(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-40; 295-309 AND 425-438. Strain: MRL/LPR.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c and C57BL/6J. Tissue: Bone marrow, Head and Kidney.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"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]. Strain: C57BL/6. Tissue: Brain.
[5]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 9-18; 26-53; 87-93; 96-109; 148-155; 192-210; 218-231; 240-251; 278-287; 296-312; 324-336; 363-386; 454-502; 513-524; 530-560; 600-614; 639-651; 669-677; 701-709; 714-732 AND 754-766, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[6]	"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: INTERACTION WITH RNF19A.
[7]	"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.
[8]	"Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome." Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J. Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NGLY1.
[9]	Erratum Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J. Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006)
[10]	"p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase and at the end of mitosis." Uchiyama K., Totsukawa G., Puhka M., Kaneko Y., Jokitalo E., Dreveny I., Beuron F., Zhang X., Freemont P., Kondo H. Dev. Cell 11:803-816(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NSFL1C-LIKE PROTEIN P37.
[11]	"The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97." Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N., Shimozawa N., Shirakawa M., Hiroaki H. FEBS J. 273:4959-4971(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHOLIPID BINDING, MUTAGENESIS OF ARG-144.
[12]	"The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor." Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J. Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AMFR; SAKS1; RAD23B AND NGLY1.
[13]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY. Tissue: Liver.
[14]	"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.
[15]	"Structure of the AAA ATPase p97." Zhang X., Shaw A., Bates P.A., Newman R.H., Gowen B., Orlova E., Gorman M.A., Kondo H., Dokurno P., Lally J., Leonard G., Meyer H., van Heel M., Freemont P.S. Mol. Cell 6:1473-1484(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-458.
[16]	"Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains." DeLaBarre B., Brunger A.T. Nat. Struct. Biol. 10:856-863(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.7 ANGSTROMS).
[17]	"The crystal structure of murine p97/VCP at 3.6A." Huyton T., Pye V.E., Briggs L.C., Flynn T.C., Beuron F., Kondo H., Ma J., Zhang X., Freemont P.S. J. Struct. Biol. 144:337-348(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
[18]	"Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47." Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S. EMBO J. 23:1030-1039(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-458.
[19]	"Nucleotide dependent motion and mechanism of action of p97/VCP." DeLaBarre B., Brunger A.T. J. Mol. Biol. 347:437-452(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z14044 mRNA. Translation: CAA78412.1.
AK028264 mRNA. Translation: BAC25849.1.
AK030751 mRNA. Translation: BAC27119.1.
AK149931 mRNA. Translation: BAE29175.1.
AK151109 mRNA. Translation: BAE30119.1.
AK151418 mRNA. Translation: BAE30383.1.
AK153249 mRNA. Translation: BAE31840.1.
AK159177 mRNA. Translation: BAE34876.1.
AK159509 mRNA. Translation: BAE35141.1.
AK167794 mRNA. Translation: BAE39824.1.
AK169140 mRNA. Translation: BAE40919.1.
AL672276 Genomic DNA. Translation: CAM14316.1.
BC043053 mRNA. Translation: AAH43053.1.
BC049114 mRNA. Translation: AAH49114.1.

IPI

IPI00622235.

PIR

S25197.

RefSeq

NP_033529.3. NM_009503.4.

UniGene

Mm.245976.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E32	X-ray	2.90	A	1-458	[»]
1R7R	X-ray	3.60	A	1-806	[»]
1S3S	X-ray	2.90	A/B/C/D/E/F	1-458	[»]
2PJH	NMR	-	B	21-213	[»]
3CF0	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N	463-763	[»]
3CF1	X-ray	4.40	A/B/C	1-806	[»]
3CF2	X-ray	3.50	A/B/C/D	1-806	[»]
3CF3	X-ray	4.25	A/B/C	1-806	[»]

DisProt

DP00435.

ProteinModelPortal

Q01853.

ModBase

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Protein-protein interaction databases

DIP

DIP-29796N.

IntAct

Q01853. 22 interactions.

MINT

MINT-220770.

PTM databases

PhosphoSite

Q01853.

2D gel databases

REPRODUCTION-2DPAGE

Q01853.

UCD-2DPAGE

Q01853.

Proteomic databases

PaxDb

Q01853.

PRIDE

Q01853.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452.

GeneID

269523.

KEGG

mmu:269523.

UCSC

uc008sor.2. mouse.

Organism-specific databases

CTD

7415.

MGI

MGI:99919. Vcp.

Phylogenomic databases

eggNOG

COG0464.

GeneTree

ENSGT00700000104534.

HOVERGEN

HBG001226.

InParanoid

Q01853.

KO

K13525.

OMA

AYRPIHK.

OrthoDB

EOG45TCMK.

Gene expression databases

ArrayExpress

Q01853.

Bgee

Q01853.

CleanEx

MM_VCP.

Genevestigator

Q01853.

GermOnline

ENSMUSG00000028452. Mus musculus.

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.
IPR027417. P-loop_NTPase.
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.
SSF52540. SSF52540. 2 hits.

TIGRFAMs

TIGR01243. CDC48. 1 hit.

PROSITE

PS00674. AAA. 2 hits.
[Graphical view]

ProtoNet

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Other

BindingDB

Q01853.

ChiTaRS

VCP. mouse.

EvolutionaryTrace

Q01853.

NextBio

392876.

SOURCE

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Entry information

Entry name

TERA_MOUSE

Accession

Primary (citable) accession number: Q01853
Secondary accession number(s): Q3TFH9 , Q3TIM2, Q3TXN9, Q6PI18, Q8BSR6, Q8CEG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	May 1, 2007
Last modified:	May 29, 2013
This is version 142 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program