Vcp

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) (PubMed:10930451, PubMed:12411482). Vesicle budding from the tER is an ATP-dependent process (PubMed:10930451, PubMed:12411482). The ternary complex containing UFD1, 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 (PubMed:10930451, PubMed:12411482). The NPLOC4-UFD1-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. 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. Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. Plays a role in the regulation of stress granules (SGs) clearance process upon arsenite-induced response (By similarity). 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. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy. Acts as a negative regulator of type I interferon production by interacting with DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I (By similarity). May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation (By similarity). May more particularly play a role in caveolins sorting in cells (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (By similarity).By similarity2 Publications

Catalytic activityⁱ

ATP + H₂O = ADP + phosphate.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	348	ATP 1By similarity		1
Binding siteⁱ	384	ATP 1By similarity		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	247 – 253	ATP 1By similarity		7
Nucleotide bindingⁱ	521 – 526	ATP 2By similarity		6

GO - Molecular functionⁱ

ADP binding
Source: RGD
Inferred from mutant phenotypeⁱ
- 18332143
ATPase activity
Source: RGD
Inferred from direct assayⁱ
- 7806566
ATP binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 7806566
BAT3 complex binding Source: Ensembl
deubiquitinase activator activity Source: Ensembl
identical protein binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 7806566
K48-linked polyubiquitin modification-dependent protein binding Source: Ensembl
lipid binding Source: UniProtKB-KW
MHC class I protein binding Source: Ensembl
polyubiquitin modification-dependent protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein-containing complex binding
Source: RGD
Inferred from physical interactionⁱ
- 10811609
protein domain specific binding Source: Ensembl
protein phosphatase binding Source: Ensembl
signaling receptor binding
Source: RGD
Inferred from direct assayⁱ
- 16103111
ubiquitin protein ligase binding Source: Ensembl
ubiquitin-specific protease binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
aggresome assembly Source: Ensembl
ATP metabolic process Source: Ensembl
autophagosome maturation Source: UniProtKB
autophagy Source: UniProtKB
cellular response to arsenite ion Source: UniProtKB
cellular response to DNA damage stimulus Source: UniProtKB
cellular response to heat Source: UniProtKB
double-strand break repair Source: UniProtKB
endoplasmic reticulum stress-induced pre-emptive quality control Source: UniProtKB
endosome to lysosome transport via multivesicular body sorting pathway Source: UniProtKB
ERAD pathway Source: UniProtKB
ER-associated misfolded protein catabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
ER to Golgi vesicle-mediated transport
Source: RGD
Inferred from mutant phenotypeⁱ
- 7806566
flavin adenine dinucleotide catabolic process Source: Ensembl
macroautophagy Source: UniProtKB
mitotic spindle disassembly
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
NADH metabolic process Source: Ensembl
positive regulation of ATP biosynthetic process Source: Ensembl
positive regulation of canonical Wnt signaling pathway Source: Ensembl
positive regulation of Lys63-specific deubiquitinase activity Source: Ensembl
positive regulation of mitochondrial membrane potential Source: Ensembl
positive regulation of oxidative phosphorylation Source: Ensembl
positive regulation of proteasomal ubiquitin-dependent protein catabolic process
Source: RGD
Inferred from mutant phenotypeⁱ
- 16103111
positive regulation of protein complex assembly Source: Ensembl
proteasomal protein catabolic process Source: UniProtKB
proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
protein hexamerization
Source: RGD
Inferred from direct assayⁱ
- 18332143
protein homooligomerization
Source: RGD
Inferred from direct assayⁱ
- 7806566
protein N-linked glycosylation via asparagine Source: UniProtKB
protein ubiquitination Source: UniProtKB
regulation of aerobic respiration Source: Ensembl
regulation of synapse organization
Source: SynGO
Inferred from direct assayⁱ
- 22105171
retrograde protein transport, ER to cytosol
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
stress granule disassembly Source: UniProtKB
translesion synthesis Source: UniProtKB
ubiquitin-dependent ERAD pathway Source: UniProtKB
viral genome replication Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Autophagy, DNA damage, DNA repair, Transport
Ligand	ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	3.6.4.6 5301
Reactomeⁱ	R-RNO-110320 Translesion Synthesis by POLH R-RNO-3371511 HSF1 activation R-RNO-382556 ABC-family proteins mediated transport R-RNO-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle R-RNO-5358346 Hedgehog ligand biogenesis R-RNO-5689896 Ovarian tumor domain proteases R-RNO-6798695 Neutrophil degranulation

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Transitional endoplasmic reticulum ATPase (EC:3.6.4.6By similarity) Short name: TER ATPase Alternative name(s): 15S Mg(2+)-ATPase p97 subunit Valosin-containing protein Short name: VCP
Gene namesⁱ	Name:Vcp
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 5

Organism-specific databases

Rat genome database More...RGDⁱ	621595 Vcp

RGDⁱ

621595 Vcp

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedBy similarity
ChainⁱPRO_0000084575	2 – 806	Transitional endoplasmic reticulum ATPaseAdd BLAST		805

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineBy similarity	1
Modified residueⁱ	3	PhosphoserineCombined sources	1
Modified residueⁱ	7	PhosphoserineCombined sources	1
Cross-linkⁱ	8	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	13	PhosphoserineBy similarity	1
Cross-linkⁱ	18	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	37	PhosphoserineBy similarity	1
Modified residueⁱ	315	N6,N6,N6-trimethyllysine; by VCPKMTBy similarity	1
Modified residueⁱ	436	PhosphothreonineBy similarity	1
Modified residueⁱ	462	PhosphoserineBy similarity	1
Modified residueⁱ	502	N6-acetyllysineBy similarity	1
Modified residueⁱ	505	N6-acetyllysineBy similarity	1
Modified residueⁱ	668	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	668	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	702	PhosphoserineBy similarity	1
Modified residueⁱ	754	N6-acetyllysineBy similarity	1
Modified residueⁱ	770	PhosphoserineBy similarity	1
Modified residueⁱ	775	PhosphoserineBy similarity	1
Modified residueⁱ	787	PhosphoserineBy similarity	1
Modified residueⁱ	805	PhosphotyrosineBy similarity	1

Post-translational modificationⁱ

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. Phosphorylated in mitotic cells.1 Publication

ISGylated.By similarity

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

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	P46462
PRIDEⁱ	P46462

2D gel databases

The World-2DPAGE database More...World-2DPAGEⁱ	0004:P46462

World-2DPAGEⁱ

0004:P46462

PTM databases

iPTMnetⁱ	P46462
PhosphoSitePlusⁱ	P46462
SwissPalmⁱ	P46462

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSRNOG00000034242 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
Genevisibleⁱ	P46462 RN

Interactionⁱ

Subunit structureⁱ

Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis. Interacts with RHBDD1 (via C-terminal domain). Interacts with SELENOS 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 UBXN4 and RNF19A. Interacts with CASR. Interacts with 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 SPRTN; leading to recruitment to stalled replication forks. 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 UFD1, 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, UFD1 and VCP. Interacts with WASHC5. Interacts with UBOX5. Interacts (via N-terminus) with UBXN7, UBXN8, and probably several other UBX domain-containing proteins (via UBX domains); the interactions are mutually exclusive with VIM-dependent interactions such as those with AMFR and SELENOS. Forms a complex with UBQLN1 and UBXN4 (By similarity). Interacts (via the PIM motif) with RNF31 (via the PUB domain) (By similarity). Interacts with DDX58/RIG-I and RNF125; interaction takes place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I (By similarity). Interacts with BAG6 (By similarity). Interacts with UBXN10 (By similarity). Interacts with UBXN6; the interaction with UBXN6 is direct and competitive with UFD1 (By similarity). Forms a ternary complex with CAV1 and UBXN6. Interacts with PLAA, UBXN6 and YOD1; may form a complex involved in macroautophagy (By similarity). Interacts with ANKZF1 (By similarity). Interacts with ubiquitin-binding protein FAF1 (By similarity). Interacts with ZFAND2B (via VIM motif); the interaction is direct (By similarity). Interacts with ZFAND1 (via its ubiquitin-like region); this interaction occurs in an arsenite-dependent manner (By similarity).By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Nsfl1c	O35987	12	EBI-399011,EBI-1993760

With

Entry

#Exp.

IntAct

Notes

Nsfl1c

O35987

12

EBI-399011,EBI-1993760

GO - Molecular functionⁱ

identical protein binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 7806566
K48-linked polyubiquitin modification-dependent protein binding Source: Ensembl
MHC class I protein binding Source: Ensembl
polyubiquitin modification-dependent protein binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein domain specific binding Source: Ensembl
protein phosphatase binding Source: Ensembl
signaling receptor binding
Source: RGD
Inferred from direct assayⁱ
- 16103111
ubiquitin protein ligase binding Source: Ensembl
ubiquitin-specific protease binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	250528, 25 interactors
ComplexPortalⁱ	CPX-138 Vcp-Npl4-Ufd1 AAA ATPase complex CPX-263 Nsfl1c-Vcp complex
CORUMⁱ	P46462
IntActⁱ	P46462, 9 interactors
Molecular INTeraction database More...MINTⁱ	P46462
STRINGⁱ	10116.ENSRNOP00000040121

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P46462
SMRⁱ	P46462
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	797 – 806	Interaction with UBXN6By similarity		10

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	802 – 806	PIM motifBy similarity		5

Domainⁱ

The PIM (PUB-interaction motif) motif mediates interaction with the PUB domain of RNF31.By similarity

Sequence similaritiesⁱ

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0730 Eukaryota COG0464 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00900000141071
HOGENOMⁱ	HOG000223224
HOVERGENⁱ	HBG001226
InParanoidⁱ	P46462
KEGG Orthology (KO) More...KOⁱ	K13525
OMAⁱ	PIDDTTE
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G024K
PhylomeDBⁱ	P46462
TreeFamⁱ	TF300542

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR005938 AAA_ATPase_CDC48 IPR009010 Asp_de-COase-like_dom_sf IPR003959 ATPase_AAA_core IPR003960 ATPase_AAA_CS IPR004201 Cdc48_dom2 IPR029067 CDC48_domain_2-like_sf IPR003338 CDC4_N-term_subdom IPR027417 P-loop_NTPase IPR015415 Vps4_C
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00004 AAA, 2 hits PF02933 CDC48_2, 1 hit PF02359 CDC48_N, 1 hit PF09336 Vps4_C, 1 hit
SMARTⁱ	View protein in SMART SM00382 AAA, 2 hits SM01072 CDC48_2, 1 hit SM01073 CDC48_N, 1 hit
SUPFAMⁱ	SSF50692 SSF50692, 1 hit SSF52540 SSF52540, 2 hits SSF54585 SSF54585, 1 hit
TIGRFAMsⁱ	TIGR01243 CDC48, 1 hit
PROSITEⁱ	View protein in PROSITE PS00674 AAA, 2 hits

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P46462-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ 
        60         70         80         90        100
LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI 
       110        120        130        140        150
SIQPCPDVKY GKRIHVLPID DTVEGITGNL FEVYLKPYFL EAYRPIRKGD 
       160        170        180        190        200
IFLVRGGMRA VEFKVVETDP SPYCIVAPDT VIHCEGEPIK REDEEESLNE 
       210        220        230        240        250
VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG ILLYGPPGTG 
       260        270        280        290        300
KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI 
       310        320        330        340        350
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP 
       360        370        380        390        400
NSIDPALRRF GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA 
       410        420        430        440        450
NETHGHVGAD LAALCSEAAL QAIRKKMDLI DLEDETIDAE VMNSLAVTMD 
       460        470        480        490        500
DFRWALSQSN PSALRETVVE VPQVTWEDIG GLEDVKRELQ ELVQYPVEHP 
       510        520        530        540        550
DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI SIKGPELLTM 
       560        570        580        590        600
WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 
       610        620        630        640        650
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE 
       660        670        680        690        700
KSRVAILKAN LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR 
       710        720        730        740        750
ESIESEIRRE RERQTNPSAM EVEEDDPVPE IRRDHFEEAM RFARRSVSDN 
       760        770        780        790        800
DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG AGPSQGSGGG TGGNVYTEDN 

DDDLYG

Length:806

Mass (Da):89,349

Last modified:January 23, 2007 - v3

Checksum:ⁱ501B721D205EBA8A

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U11760 mRNA Translation: AAC52154.1 BC060518 mRNA Translation: AAH60518.1
PIRⁱ	A55190
NCBI Reference Sequences More...RefSeqⁱ	NP_446316.1, NM_053864.2
UniGeneⁱ	Rn.98891

Genome annotation databases

Ensemblⁱ	ENSRNOT00000046102; ENSRNOP00000040121; ENSRNOG00000034242
GeneIDⁱ	116643
KEGGⁱ	rno:116643
UCSC genome browser More...UCSCⁱ	RGD:621595 rat

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P46462	Transitional endoplasmic reticulum ATPase		BOVIN		806	UniRef90_P46462
Transitional endoplasmic reticulum ATPase		DANRE		806
Transitional endoplasmic reticulum ATPase		PIG		806
Transitional endoplasmic reticulum ATPase		XENTR		805
Transitional endoplasmic reticulum ATPase		XENLA		805
+194

Protein	Similar proteins		Species	Score	Length	Source
P46462	Cell division control protein 48		YEAST		835	UniRef50_P25694
Cell division control protein 48		EMENI		823
Transitional endoplasmic reticulum ATPase		PIG		806
Transitional endoplasmic reticulum ATPase		DANRE		806
Transitional endoplasmic reticulum ATPase		BOVIN		806
+1134

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U11760 mRNA Translation: AAC52154.1 BC060518 mRNA Translation: AAH60518.1
PIRⁱ	A55190
RefSeqⁱ	NP_446316.1, NM_053864.2
UniGeneⁱ	Rn.98891

3D structure databases

ProteinModelPortalⁱ	P46462
SMRⁱ	P46462
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	250528, 25 interactors
ComplexPortalⁱ	CPX-138 Vcp-Npl4-Ufd1 AAA ATPase complex CPX-263 Nsfl1c-Vcp complex
CORUMⁱ	P46462
IntActⁱ	P46462, 9 interactors
MINTⁱ	P46462
STRINGⁱ	10116.ENSRNOP00000040121

PTM databases

iPTMnetⁱ	P46462
PhosphoSitePlusⁱ	P46462
SwissPalmⁱ	P46462

2D gel databases

World-2DPAGEⁱ	0004:P46462

World-2DPAGEⁱ

0004:P46462

Proteomic databases

PaxDbⁱ	P46462
PRIDEⁱ	P46462

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000046102; ENSRNOP00000040121; ENSRNOG00000034242
GeneIDⁱ	116643
KEGGⁱ	rno:116643
UCSCⁱ	RGD:621595 rat

Organism-specific databases

CTDⁱ	7415
RGDⁱ	621595 Vcp

Phylogenomic databases

eggNOGⁱ	KOG0730 Eukaryota COG0464 LUCA
GeneTreeⁱ	ENSGT00900000141071
HOGENOMⁱ	HOG000223224
HOVERGENⁱ	HBG001226
InParanoidⁱ	P46462
KOⁱ	K13525
OMAⁱ	PIDDTTE
OrthoDBⁱ	EOG091G024K
PhylomeDBⁱ	P46462
TreeFamⁱ	TF300542

Enzyme and pathway databases

BRENDAⁱ	3.6.4.6 5301
Reactomeⁱ	R-RNO-110320 Translesion Synthesis by POLH R-RNO-3371511 HSF1 activation R-RNO-382556 ABC-family proteins mediated transport R-RNO-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle R-RNO-5358346 Hedgehog ligand biogenesis R-RNO-5689896 Ovarian tumor domain proteases R-RNO-6798695 Neutrophil degranulation

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P46462

PROⁱ

PR:P46462

Gene expression databases

Bgeeⁱ	ENSRNOG00000034242 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
Genevisibleⁱ	P46462 RN

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR005938 AAA_ATPase_CDC48 IPR009010 Asp_de-COase-like_dom_sf IPR003959 ATPase_AAA_core IPR003960 ATPase_AAA_CS IPR004201 Cdc48_dom2 IPR029067 CDC48_domain_2-like_sf IPR003338 CDC4_N-term_subdom IPR027417 P-loop_NTPase IPR015415 Vps4_C
Pfamⁱ	View protein in Pfam PF00004 AAA, 2 hits PF02933 CDC48_2, 1 hit PF02359 CDC48_N, 1 hit PF09336 Vps4_C, 1 hit
SMARTⁱ	View protein in SMART SM00382 AAA, 2 hits SM01072 CDC48_2, 1 hit SM01073 CDC48_N, 1 hit
SUPFAMⁱ	SSF50692 SSF50692, 1 hit SSF52540 SSF52540, 2 hits SSF54585 SSF54585, 1 hit
TIGRFAMsⁱ	TIGR01243 CDC48, 1 hit
PROSITEⁱ	View protein in PROSITE PS00674 AAA, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TERA_RAT
Accessionⁱ	P46462Primary (citable) accession number: P46462
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 178 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

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Supporting data

UniProtKB - P46462 (TERA_RAT)

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Transitional endoplasmic reticulum ATPase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Endoplasmic reticulum

Cytosol

Other locations

Cytosol

Endoplasmic reticulum

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ