Full text data of NVL
NVL
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear valosin-containing protein-like; NVLp; Nuclear VCP-like protein
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nuclear valosin-containing protein-like; NVLp; Nuclear VCP-like protein
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O15381
ID NVL_HUMAN Reviewed; 856 AA.
AC O15381; B4DMC4; B4DP98; Q96EM7;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Nuclear valosin-containing protein-like;
DE Short=NVLp;
DE Short=Nuclear VCP-like protein;
GN Name=NVL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT GLY-359,
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9286697; DOI=10.1006/geno.1997.4856;
RA Germain-Lee E.L., Obie C., Valle D.;
RT "NVL: a new member of the AAA family of ATPases localized to the
RT nucleus.";
RL Genomics 44:22-34(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND THR-138, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; THR-138; SER-211
RP AND SER-215, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INTERACTION WITH NCL/NUCLEOLIN.
RX PubMed=21474449; DOI=10.1074/jbc.M110.174680;
RA Fujiwara Y., Fujiwara K., Goda N., Iwaya N., Tenno T., Shirakawa M.,
RA Hiroaki H.;
RT "Structure and function of the N-terminal nucleolin binding domain of
RT nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar
RT localization signal.";
RL J. Biol. Chem. 286:21732-21741(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 574-845 IN COMPLEX WITH
RP PHOSPHATE.
RG Structural genomics consortium (SGC);
RT "Human nuclear valosin containing protein like (NVL), C-terminal AAA-
RT ATPase domain.";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- SUBUNIT: Interacts with NCL/nucleolin.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=NVLp.2;
CC IsoId=O15381-1; Sequence=Displayed;
CC Name=2; Synonyms=NVLp.1;
CC IsoId=O15381-2; Sequence=VSP_007771;
CC Name=3;
CC IsoId=O15381-3; Sequence=VSP_007771, VSP_007772;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=O15381-4; Sequence=VSP_045334, VSP_045335;
CC Name=5;
CC IsoId=O15381-5; Sequence=VSP_007772;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level of expression
CC in heart, placenta, skeletal muscle, pancreas and retina.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR EMBL; U68140; AAB70457.1; -; mRNA.
DR EMBL; U78772; AAB70460.1; -; mRNA.
DR EMBL; AK297396; BAG59836.1; -; mRNA.
DR EMBL; AK298244; BAG60510.1; -; mRNA.
DR EMBL; AC092809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012105; AAH12105.1; -; mRNA.
DR RefSeq; NP_001230075.1; NM_001243146.1.
DR RefSeq; NP_001230076.1; NM_001243147.1.
DR RefSeq; NP_002524.2; NM_002533.3.
DR RefSeq; NP_996671.1; NM_206840.2.
DR UniGene; Hs.497867; -.
DR PDB; 2X8A; X-ray; 2.60 A; A=574-845.
DR PDBsum; 2X8A; -.
DR ProteinModelPortal; O15381; -.
DR SMR; O15381; 1-74, 256-854.
DR IntAct; O15381; 4.
DR MINT; MINT-1423251; -.
DR STRING; 9606.ENSP00000281701; -.
DR PhosphoSite; O15381; -.
DR SWISS-2DPAGE; O15381; -.
DR PaxDb; O15381; -.
DR PRIDE; O15381; -.
DR DNASU; 4931; -.
DR Ensembl; ENST00000281701; ENSP00000281701; ENSG00000143748.
DR Ensembl; ENST00000340871; ENSP00000341362; ENSG00000143748.
DR Ensembl; ENST00000391875; ENSP00000375747; ENSG00000143748.
DR Ensembl; ENST00000469075; ENSP00000417826; ENSG00000143748.
DR GeneID; 4931; -.
DR KEGG; hsa:4931; -.
DR UCSC; uc010pve.2; human.
DR CTD; 4931; -.
DR GeneCards; GC01M224416; -.
DR HGNC; HGNC:8070; NVL.
DR HPA; HPA028207; -.
DR MIM; 602426; gene.
DR neXtProt; NX_O15381; -.
DR PharmGKB; PA31857; -.
DR eggNOG; COG0464; -.
DR HOGENOM; HOG000223225; -.
DR HOVERGEN; HBG001226; -.
DR InParanoid; O15381; -.
DR KO; K14571; -.
DR OMA; ICKMLIH; -.
DR PhylomeDB; O15381; -.
DR ChiTaRS; NVL; human.
DR EvolutionaryTrace; O15381; -.
DR GeneWiki; NVL_(gene); -.
DR GenomeRNAi; 4931; -.
DR NextBio; 19001; -.
DR PRO; PR:O15381; -.
DR ArrayExpress; O15381; -.
DR Bgee; O15381; -.
DR CleanEx; HS_NVL; -.
DR Genevestigator; O15381; -.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 856 Nuclear valosin-containing protein-like.
FT /FTId=PRO_0000084588.
FT NP_BIND 305 312 ATP (Potential).
FT NP_BIND 622 629 ATP (Probable).
FT MOTIF 49 52 Nucleolar localization signal (By
FT similarity).
FT MOD_RES 134 134 Phosphoserine.
FT MOD_RES 138 138 Phosphothreonine.
FT MOD_RES 191 191 Phosphoserine (By similarity).
FT MOD_RES 211 211 Phosphoserine.
FT MOD_RES 215 215 Phosphoserine.
FT VAR_SEQ 1 216 Missing (in isoform 4).
FT /FTId=VSP_045334.
FT VAR_SEQ 1 106 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_007771.
FT VAR_SEQ 115 205 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_007772.
FT VAR_SEQ 320 320 G -> GAECSGMITAHCSFDFSGSNDPPASASQ (in
FT isoform 4).
FT /FTId=VSP_045335.
FT VARIANT 295 295 V -> I (in dbSNP:rs12084919).
FT /FTId=VAR_048109.
FT VARIANT 359 359 C -> G.
FT /FTId=VAR_015890.
FT VARIANT 404 404 V -> I (in dbSNP:rs34631151).
FT /FTId=VAR_048110.
FT HELIX 585 597
FT HELIX 599 602
FT HELIX 604 609
FT STRAND 616 623
FT HELIX 628 638
FT STRAND 642 647
FT TURN 648 651
FT HELIX 657 672
FT STRAND 675 681
FT TURN 684 686
FT HELIX 701 710
FT STRAND 718 725
FT HELIX 727 729
FT HELIX 732 735
FT STRAND 742 745
FT HELIX 751 761
FT TURN 762 769
FT HELIX 776 780
FT HELIX 784 786
FT HELIX 790 808
FT HELIX 825 832
SQ SEQUENCE 856 AA; 95051 MW; 7A8B373FCAFB99B7 CRC64;
MKPRPAGFVD NKLKQRVIQY LTSNKCGKYV DIGVLASDLQ RVYSIDYGRR KRNAFRIQVE
KVFSIISSEK ELKNLTELED EHLAKRARQG EEDNEYTESY SDDDSSMEDY PDPQSANHMN
SSLLSLYRKG NPDSVSNTPE MEQRETTSST PRISSKTGSI PLKTPAKDSE GGWFIDKTPS
VKKDSFFLDL SCEKSNPKKP ITEIQDSKDS SLLESDMKRK GKLKNKGSKR KKEDLQEVDG
EIEAVLQKKA KARGLEFQIS NVKFEDVGGN DMTLKEVCKM LIHMRHPEVY HHLGVVPPRG
VLLHGPPGCG KTLLAHAIAG ELDLPILKVA APEIVSGVSG ESEQKLRELF EQAVSNAPCI
IFIDEIDAIT PKREVASKDM ERRIVAQLLT CMDDLNNVAA TARVLVIGAT NRPDSLDPAL
RRAGRFDREI CLGIPDEASR ERILQTLCRK LRLPQAFDFC HLAHLTPGFV GADLMALCRE
AAMCAVNRVL MKLQEQQKKN PEMEDLPSKG VQEERLGTEP TSETQDELQR LLGLLRDQDP
LSEEQMQGLC IELNDFIVAL SSVQPSAKRE GFVTVPNVTW ADIGALEDIR EELTMAILAP
VRNPDQFKAL GLVTPAGVLL AGPPGCGKTL LAKAVANESG LNFISVKGPE LLNMYVGESE
RAVRQVFQRA KNSAPCVIFF DEVDALCPRR SDRETGASVR VVNQLLTEMD GLEARQQVFI
MAATNRPDII DPAILRPGRL DKTLFVGLPP PADRLAILKT ITKNGTKPPL DADVNLEAIA
GDLRCDCYTG ADLSALVREA SICALRQEMA RQKSGNEKGE LKVSHKHFEE AFKKVRSSIS
KKDQIMYERL QESLSR
//
ID NVL_HUMAN Reviewed; 856 AA.
AC O15381; B4DMC4; B4DP98; Q96EM7;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Nuclear valosin-containing protein-like;
DE Short=NVLp;
DE Short=Nuclear VCP-like protein;
GN Name=NVL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT GLY-359,
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9286697; DOI=10.1006/geno.1997.4856;
RA Germain-Lee E.L., Obie C., Valle D.;
RT "NVL: a new member of the AAA family of ATPases localized to the
RT nucleus.";
RL Genomics 44:22-34(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND THR-138, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; THR-138; SER-211
RP AND SER-215, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INTERACTION WITH NCL/NUCLEOLIN.
RX PubMed=21474449; DOI=10.1074/jbc.M110.174680;
RA Fujiwara Y., Fujiwara K., Goda N., Iwaya N., Tenno T., Shirakawa M.,
RA Hiroaki H.;
RT "Structure and function of the N-terminal nucleolin binding domain of
RT nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar
RT localization signal.";
RL J. Biol. Chem. 286:21732-21741(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 574-845 IN COMPLEX WITH
RP PHOSPHATE.
RG Structural genomics consortium (SGC);
RT "Human nuclear valosin containing protein like (NVL), C-terminal AAA-
RT ATPase domain.";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- SUBUNIT: Interacts with NCL/nucleolin.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=NVLp.2;
CC IsoId=O15381-1; Sequence=Displayed;
CC Name=2; Synonyms=NVLp.1;
CC IsoId=O15381-2; Sequence=VSP_007771;
CC Name=3;
CC IsoId=O15381-3; Sequence=VSP_007771, VSP_007772;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=O15381-4; Sequence=VSP_045334, VSP_045335;
CC Name=5;
CC IsoId=O15381-5; Sequence=VSP_007772;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level of expression
CC in heart, placenta, skeletal muscle, pancreas and retina.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR EMBL; U68140; AAB70457.1; -; mRNA.
DR EMBL; U78772; AAB70460.1; -; mRNA.
DR EMBL; AK297396; BAG59836.1; -; mRNA.
DR EMBL; AK298244; BAG60510.1; -; mRNA.
DR EMBL; AC092809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012105; AAH12105.1; -; mRNA.
DR RefSeq; NP_001230075.1; NM_001243146.1.
DR RefSeq; NP_001230076.1; NM_001243147.1.
DR RefSeq; NP_002524.2; NM_002533.3.
DR RefSeq; NP_996671.1; NM_206840.2.
DR UniGene; Hs.497867; -.
DR PDB; 2X8A; X-ray; 2.60 A; A=574-845.
DR PDBsum; 2X8A; -.
DR ProteinModelPortal; O15381; -.
DR SMR; O15381; 1-74, 256-854.
DR IntAct; O15381; 4.
DR MINT; MINT-1423251; -.
DR STRING; 9606.ENSP00000281701; -.
DR PhosphoSite; O15381; -.
DR SWISS-2DPAGE; O15381; -.
DR PaxDb; O15381; -.
DR PRIDE; O15381; -.
DR DNASU; 4931; -.
DR Ensembl; ENST00000281701; ENSP00000281701; ENSG00000143748.
DR Ensembl; ENST00000340871; ENSP00000341362; ENSG00000143748.
DR Ensembl; ENST00000391875; ENSP00000375747; ENSG00000143748.
DR Ensembl; ENST00000469075; ENSP00000417826; ENSG00000143748.
DR GeneID; 4931; -.
DR KEGG; hsa:4931; -.
DR UCSC; uc010pve.2; human.
DR CTD; 4931; -.
DR GeneCards; GC01M224416; -.
DR HGNC; HGNC:8070; NVL.
DR HPA; HPA028207; -.
DR MIM; 602426; gene.
DR neXtProt; NX_O15381; -.
DR PharmGKB; PA31857; -.
DR eggNOG; COG0464; -.
DR HOGENOM; HOG000223225; -.
DR HOVERGEN; HBG001226; -.
DR InParanoid; O15381; -.
DR KO; K14571; -.
DR OMA; ICKMLIH; -.
DR PhylomeDB; O15381; -.
DR ChiTaRS; NVL; human.
DR EvolutionaryTrace; O15381; -.
DR GeneWiki; NVL_(gene); -.
DR GenomeRNAi; 4931; -.
DR NextBio; 19001; -.
DR PRO; PR:O15381; -.
DR ArrayExpress; O15381; -.
DR Bgee; O15381; -.
DR CleanEx; HS_NVL; -.
DR Genevestigator; O15381; -.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repeat.
FT CHAIN 1 856 Nuclear valosin-containing protein-like.
FT /FTId=PRO_0000084588.
FT NP_BIND 305 312 ATP (Potential).
FT NP_BIND 622 629 ATP (Probable).
FT MOTIF 49 52 Nucleolar localization signal (By
FT similarity).
FT MOD_RES 134 134 Phosphoserine.
FT MOD_RES 138 138 Phosphothreonine.
FT MOD_RES 191 191 Phosphoserine (By similarity).
FT MOD_RES 211 211 Phosphoserine.
FT MOD_RES 215 215 Phosphoserine.
FT VAR_SEQ 1 216 Missing (in isoform 4).
FT /FTId=VSP_045334.
FT VAR_SEQ 1 106 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_007771.
FT VAR_SEQ 115 205 Missing (in isoform 3 and isoform 5).
FT /FTId=VSP_007772.
FT VAR_SEQ 320 320 G -> GAECSGMITAHCSFDFSGSNDPPASASQ (in
FT isoform 4).
FT /FTId=VSP_045335.
FT VARIANT 295 295 V -> I (in dbSNP:rs12084919).
FT /FTId=VAR_048109.
FT VARIANT 359 359 C -> G.
FT /FTId=VAR_015890.
FT VARIANT 404 404 V -> I (in dbSNP:rs34631151).
FT /FTId=VAR_048110.
FT HELIX 585 597
FT HELIX 599 602
FT HELIX 604 609
FT STRAND 616 623
FT HELIX 628 638
FT STRAND 642 647
FT TURN 648 651
FT HELIX 657 672
FT STRAND 675 681
FT TURN 684 686
FT HELIX 701 710
FT STRAND 718 725
FT HELIX 727 729
FT HELIX 732 735
FT STRAND 742 745
FT HELIX 751 761
FT TURN 762 769
FT HELIX 776 780
FT HELIX 784 786
FT HELIX 790 808
FT HELIX 825 832
SQ SEQUENCE 856 AA; 95051 MW; 7A8B373FCAFB99B7 CRC64;
MKPRPAGFVD NKLKQRVIQY LTSNKCGKYV DIGVLASDLQ RVYSIDYGRR KRNAFRIQVE
KVFSIISSEK ELKNLTELED EHLAKRARQG EEDNEYTESY SDDDSSMEDY PDPQSANHMN
SSLLSLYRKG NPDSVSNTPE MEQRETTSST PRISSKTGSI PLKTPAKDSE GGWFIDKTPS
VKKDSFFLDL SCEKSNPKKP ITEIQDSKDS SLLESDMKRK GKLKNKGSKR KKEDLQEVDG
EIEAVLQKKA KARGLEFQIS NVKFEDVGGN DMTLKEVCKM LIHMRHPEVY HHLGVVPPRG
VLLHGPPGCG KTLLAHAIAG ELDLPILKVA APEIVSGVSG ESEQKLRELF EQAVSNAPCI
IFIDEIDAIT PKREVASKDM ERRIVAQLLT CMDDLNNVAA TARVLVIGAT NRPDSLDPAL
RRAGRFDREI CLGIPDEASR ERILQTLCRK LRLPQAFDFC HLAHLTPGFV GADLMALCRE
AAMCAVNRVL MKLQEQQKKN PEMEDLPSKG VQEERLGTEP TSETQDELQR LLGLLRDQDP
LSEEQMQGLC IELNDFIVAL SSVQPSAKRE GFVTVPNVTW ADIGALEDIR EELTMAILAP
VRNPDQFKAL GLVTPAGVLL AGPPGCGKTL LAKAVANESG LNFISVKGPE LLNMYVGESE
RAVRQVFQRA KNSAPCVIFF DEVDALCPRR SDRETGASVR VVNQLLTEMD GLEARQQVFI
MAATNRPDII DPAILRPGRL DKTLFVGLPP PADRLAILKT ITKNGTKPPL DADVNLEAIA
GDLRCDCYTG ADLSALVREA SICALRQEMA RQKSGNEKGE LKVSHKHFEE AFKKVRSSIS
KKDQIMYERL QESLSR
//
MIM
602426
*RECORD*
*FIELD* NO
602426
*FIELD* TI
*602426 NUCLEAR VALOSIN-CONTAINING PROTEIN-LIKE; NVL
;;NUCLEAR VCP-LIKE
*FIELD* TX
read more
CLONING
Members of the AAA (ATPases associated with diverse cellular activities)
family have 1 or 2 copies of a highly conserved, approximately 230-amino
acid ATP-binding module that contains the Walker A and B motifs. By
degenerate PCR and screening of a human kidney cDNA library, Germain-Lee
et al. (1997) cloned cDNAs encoding nuclear VCP (601023)-like (NVL)
protein, a novel member of the AAA family. The authors identified 2
cDNAs, which they designated NVL.1 and NVL.2, that appeared to represent
alternatively spliced transcripts. NVL.2 contains a 74-bp insert near
the 5-prime end that produces a frameshift, enabling a more 5-prime ATG
to encode the initiating methionine. NVL.1 and NVL.2 encode 750- and
856-amino acid proteins, respectively, and the sequences of both are
identical over the 750 C-terminal amino acids. Both proteins are
hydrophilic without obvious membrane-spanning domains and contain 2
ATP-binding modules that are 51% identical. NVL shows greatest
similarity to the VCP subfamily of AAA proteins, including 35% amino
acid identity with porcine VCP. However, the authors noted that NVLp is
not the human ortholog of porcine VCP. NVL.2, but not NVL.1, contains a
SRC kinase phosphorylation consensus sequence. In vitro expression of
NVL.2 produced 95- and 110-kD proteins; the 110-kD form is likely
phosphorylated. NVL.1 is approximately 83 kD and is not phosphorylated.
Northern blot analysis detected a 3.2-kb transcript in most human
tissues, with the highest levels in heart, placenta, skeletal muscle,
pancreas, and retina. Immunohistochemistry showed that NVL is localized
to the cell nucleus. Germain-Lee et al. (1997) speculated that NVL is
involved in an ATP-dependent nuclear process.
MAPPING
By somatic cell hybrid analysis and fluorescence in situ hybridization,
Germain-Lee et al. (1997) mapped the NVL gene to chromosome 1q41-q42.2.
*FIELD* RF
1. Germain-Lee, E. L.; Obie, C.; Valle, D.: NVL: a new member of
the AAA family of ATPases localized to the nucleus. Genomics 44:
22-34, 1997.
*FIELD* CD
Patti M. Sherman: 3/9/1998
*FIELD* ED
alopez: 09/17/2010
dholmes: 3/9/1998
*RECORD*
*FIELD* NO
602426
*FIELD* TI
*602426 NUCLEAR VALOSIN-CONTAINING PROTEIN-LIKE; NVL
;;NUCLEAR VCP-LIKE
*FIELD* TX
read more
CLONING
Members of the AAA (ATPases associated with diverse cellular activities)
family have 1 or 2 copies of a highly conserved, approximately 230-amino
acid ATP-binding module that contains the Walker A and B motifs. By
degenerate PCR and screening of a human kidney cDNA library, Germain-Lee
et al. (1997) cloned cDNAs encoding nuclear VCP (601023)-like (NVL)
protein, a novel member of the AAA family. The authors identified 2
cDNAs, which they designated NVL.1 and NVL.2, that appeared to represent
alternatively spliced transcripts. NVL.2 contains a 74-bp insert near
the 5-prime end that produces a frameshift, enabling a more 5-prime ATG
to encode the initiating methionine. NVL.1 and NVL.2 encode 750- and
856-amino acid proteins, respectively, and the sequences of both are
identical over the 750 C-terminal amino acids. Both proteins are
hydrophilic without obvious membrane-spanning domains and contain 2
ATP-binding modules that are 51% identical. NVL shows greatest
similarity to the VCP subfamily of AAA proteins, including 35% amino
acid identity with porcine VCP. However, the authors noted that NVLp is
not the human ortholog of porcine VCP. NVL.2, but not NVL.1, contains a
SRC kinase phosphorylation consensus sequence. In vitro expression of
NVL.2 produced 95- and 110-kD proteins; the 110-kD form is likely
phosphorylated. NVL.1 is approximately 83 kD and is not phosphorylated.
Northern blot analysis detected a 3.2-kb transcript in most human
tissues, with the highest levels in heart, placenta, skeletal muscle,
pancreas, and retina. Immunohistochemistry showed that NVL is localized
to the cell nucleus. Germain-Lee et al. (1997) speculated that NVL is
involved in an ATP-dependent nuclear process.
MAPPING
By somatic cell hybrid analysis and fluorescence in situ hybridization,
Germain-Lee et al. (1997) mapped the NVL gene to chromosome 1q41-q42.2.
*FIELD* RF
1. Germain-Lee, E. L.; Obie, C.; Valle, D.: NVL: a new member of
the AAA family of ATPases localized to the nucleus. Genomics 44:
22-34, 1997.
*FIELD* CD
Patti M. Sherman: 3/9/1998
*FIELD* ED
alopez: 09/17/2010
dholmes: 3/9/1998