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Protein

Nuclear valosin-containing protein-like

Gene

Nvl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi304 – 3118ATPSequence Analysis
Nucleotide bindingi621 – 6288ATPSequence Analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear valosin-containing protein-like
Short name:
NVLp
Short name:
Nuclear VCP-like protein
Gene namesi
Name:Nvl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1914709. Nvl.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 855855Nuclear valosin-containing protein-likePRO_0000084589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine1 Publication
Modified residuei133 – 1331PhosphoserineBy similarity
Modified residuei137 – 1371PhosphothreonineBy similarity
Modified residuei155 – 1551N6-acetyllysine1 Publication
Modified residuei190 – 1901Phosphoserine2 Publications
Modified residuei210 – 2101PhosphoserineBy similarity
Modified residuei214 – 2141PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9DBY8.
PaxDbiQ9DBY8.
PRIDEiQ9DBY8.

PTM databases

PhosphoSiteiQ9DBY8.

Expressioni

Gene expression databases

BgeeiQ9DBY8.
CleanExiMM_NVL.
ExpressionAtlasiQ9DBY8. baseline and differential.
GenevisibleiQ9DBY8. MM.

Interactioni

Subunit structurei

Interacts with NCL/nucleolin.1 Publication

Protein-protein interaction databases

BioGridi212203. 2 interactions.
IntActiQ9DBY8. 1 interaction.
MINTiMINT-4104517.
STRINGi10090.ENSMUSP00000027797.

Structurei

Secondary structure

1
855
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2313Combined sources
Beta strandi27 – 293Combined sources
Helixi32 – 4211Combined sources
Turni43 – 475Combined sources
Helixi52 – 6918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RRENMR-A1-74[»]
ProteinModelPortaliQ9DBY8.
SMRiQ9DBY8. Positions 1-74, 250-853.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DBY8.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi49 – 524Nucleolar localization signal

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00570000079239.
HOGENOMiHOG000223225.
HOVERGENiHBG001226.
InParanoidiQ9DBY8.
KOiK14571.
OMAiAANHMNS.
OrthoDBiEOG72VH5H.
PhylomeDBiQ9DBY8.
TreeFamiTF314681.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00674. AAA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPRPGVFVD RKLKQRVIQY LSSNRCGKYV DTGILASDLQ RLYSVDYGRR
60 70 80 90 100
KRNAFRIQVE KVFSIISSEK ELKNLKELED GHLAKRARQD EEDEYTESYS
110 120 130 140 150
DDDSNMEDYP DPQSANPMNS SLLSLYRRGN SESVSTTPKW GQREATTSTP
160 170 180 190 200
LLTSKTGSVP LKTPARESEG GWFIDKTPGG KKESLPLDLS DDQSNSKKQD
210 220 230 240 250
SEIQILKDSS LLESDKKRKG RAKGKGNKRK TENLQEVDGE IEALLQKKAK
260 270 280 290 300
ARSTELQISN VKFEDVGGND ATLKEVCKML IHMRHPEVYQ HLGVVPPRGV
310 320 330 340 350
LLHGPPGCGK TLLAHAIAGE LDLPILKVAA PEIVSGVSGE SEQKLRELFD
360 370 380 390 400
QAVSNAPCIV FIDEIDAITP KREVASKDME RRIVAQLLTC MDDLNNVAAT
410 420 430 440 450
ARVLVIGATN RPDSLDPALR RAGRFDREVC LGIPDEAARE RILQTLCRKL
460 470 480 490 500
RLPETFNFCH LAHLTPGFVG ADLMALCREA AMCAVNRVLM KQQAQQKKKP
510 520 530 540 550
EIEGLPSEGD QEERLGAEPT SETQDELQRL LGLLRDQDPL SEEQMQGLCI
560 570 580 590 600
ELNDFIVALA EVQPSAKREG FVTVPNVTWA DIGALEDIRD ELIMAILAPV
610 620 630 640 650
RNPDQFRTLG LGTPAGILLA GPPGCGKTLL AKAVANESGL NFISVKGPEL
660 670 680 690 700
LNMYVGESER AVRQVFQRAK NSAPCVIFFD EVDALCPRRS DRETGASVRV
710 720 730 740 750
VNQLLTEMDG LETRQQVFIL AATNRPDIID PAILRPGRLD KTLFVGLPPP
760 770 780 790 800
ADRVAILKTI TKNGTKPPLD EDVNLETIAN DLRCNCYTGA DLTALVREAS
810 820 830 840 850
LCALRQEITA QKNGVGAGEL KVSHKHFEDA FKKVKPSISI KDQVMYEALQ

RSLSQ
Length:855
Mass (Da):94,476
Last modified:June 1, 2001 - v1
Checksum:iF69A173AB40E0AE9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti513 – 5131E → K in AAH31847 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004676 mRNA. Translation: BAB23464.1.
AK054502 mRNA. Translation: BAC35806.1.
AK140509 mRNA. Translation: BAE24409.1.
BC031847 mRNA. Translation: AAH31847.1.
CCDSiCCDS15581.1.
RefSeqiNP_080447.1. NM_026171.1.
UniGeneiMm.263464.
Mm.413001.

Genome annotation databases

EnsembliENSMUST00000027797; ENSMUSP00000027797; ENSMUSG00000026516.
GeneIDi67459.
KEGGimmu:67459.
UCSCiuc007dxb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004676 mRNA. Translation: BAB23464.1.
AK054502 mRNA. Translation: BAC35806.1.
AK140509 mRNA. Translation: BAE24409.1.
BC031847 mRNA. Translation: AAH31847.1.
CCDSiCCDS15581.1.
RefSeqiNP_080447.1. NM_026171.1.
UniGeneiMm.263464.
Mm.413001.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RRENMR-A1-74[»]
ProteinModelPortaliQ9DBY8.
SMRiQ9DBY8. Positions 1-74, 250-853.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212203. 2 interactions.
IntActiQ9DBY8. 1 interaction.
MINTiMINT-4104517.
STRINGi10090.ENSMUSP00000027797.

PTM databases

PhosphoSiteiQ9DBY8.

Proteomic databases

MaxQBiQ9DBY8.
PaxDbiQ9DBY8.
PRIDEiQ9DBY8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027797; ENSMUSP00000027797; ENSMUSG00000026516.
GeneIDi67459.
KEGGimmu:67459.
UCSCiuc007dxb.1. mouse.

Organism-specific databases

CTDi4931.
MGIiMGI:1914709. Nvl.

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00570000079239.
HOGENOMiHOG000223225.
HOVERGENiHBG001226.
InParanoidiQ9DBY8.
KOiK14571.
OMAiAANHMNS.
OrthoDBiEOG72VH5H.
PhylomeDBiQ9DBY8.
TreeFamiTF314681.

Miscellaneous databases

EvolutionaryTraceiQ9DBY8.
NextBioi324638.
PROiQ9DBY8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBY8.
CleanExiMM_NVL.
ExpressionAtlasiQ9DBY8. baseline and differential.
GenevisibleiQ9DBY8. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00674. AAA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: C57BL/6J.
    Tissue: Cerebellum, Lung and Ovary.
  2. "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].
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. "Structure and function of the N-terminal nucleolin binding domain of nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar localization signal."
    Fujiwara Y., Fujiwara K., Goda N., Iwaya N., Tenno T., Shirakawa M., Hiroaki H.
    J. Biol. Chem. 286:21732-21741(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-74, SUBCELLULAR LOCATION, INTERACTION WITH NCL/NUCLEOLIN, NUCLEOLAR LOCALIZATION SIGNAL.

Entry informationi

Entry nameiNVL_MOUSE
AccessioniPrimary (citable) accession number: Q9DBY8
Secondary accession number(s): Q3USC4, Q8BW27, Q8K2B5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: June 1, 2001
Last modified: July 22, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.