Full text data of NPLOC4
NPLOC4
(KIAA1499, NPL4)
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear protein localization protein 4 homolog; Protein NPL4
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nuclear protein localization protein 4 homolog; Protein NPL4
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8TAT6
ID NPL4_HUMAN Reviewed; 608 AA.
AC Q8TAT6; Q8N3J1; Q9H8V2; Q9H964; Q9NWR5; Q9P229;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Nuclear protein localization protein 4 homolog;
DE Short=Protein NPL4;
GN Name=NPLOC4; Synonyms=KIAA1499, NPL4;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 MRNA].
RC TISSUE=Pancreas;
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 [4]
RP PROTEIN SEQUENCE OF 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-608.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP INTERACTION WITH UFD1L, AND TISSUE SPECIFICITY.
RX PubMed=11574150; DOI=10.1016/S0378-1119(01)00649-7;
RA Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B.,
RA Novelli G.;
RT "Cloning and characterization of the gene encoding human NPL4, a
RT protein interacting with the ubiquitin fusion-degradation protein
RT (UFD1L).";
RL Gene 275:39-46(2001).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The ternary complex containing UFD1L, VCP and NPLOC4
CC binds ubiquitinated proteins and is necessary for the export of
CC misfolded proteins from the ER to the cytoplasm, where they are
CC degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates
CC spindle disassembly at the end of mitosis and is necessary for the
CC formation of a closed nuclear envelope (By similarity).
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent
CC pathway.
CC -!- SUBUNIT: Heterodimer with UFD1L. The heterodimer binds
CC ubiquitinated proteins. The heterodimer binds to VCP and inhibits
CC Golgi membrane fusion.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC Endoplasmic reticulum (By similarity). Nucleus (By similarity).
CC Note=Associated with the endoplasmic reticulum and nuclear (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TAT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAT6-2; Sequence=VSP_009789;
CC Note=May be due to an intron retention. No experimental
CC confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in brain, heart,
CC skeletal muscle, kidney and fetal liver.
CC -!- DOMAIN: Binds ubiquitinated proteins via its RanBP2-type zinc
CC finger.
CC -!- SIMILARITY: Belongs to the NPL4 family.
CC -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91314.1; Type=Erroneous initiation;
CC Sequence=BAA96023.1; Type=Erroneous initiation;
CC Sequence=BAB14372.1; Type=Erroneous initiation;
CC Sequence=BAB14499.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB040932; BAA96023.1; ALT_INIT; mRNA.
DR EMBL; AK000664; BAA91314.1; ALT_INIT; mRNA.
DR EMBL; AK023046; BAB14372.1; ALT_INIT; mRNA.
DR EMBL; AK023272; BAB14499.1; ALT_INIT; mRNA.
DR EMBL; BC025930; AAH25930.1; -; mRNA.
DR EMBL; AL834300; CAD38971.1; -; mRNA.
DR RefSeq; NP_060391.2; NM_017921.2.
DR UniGene; Hs.464333; -.
DR ProteinModelPortal; Q8TAT6; -.
DR SMR; Q8TAT6; 2-77, 579-608.
DR DIP; DIP-44059N; -.
DR IntAct; Q8TAT6; 16.
DR MINT; MINT-3043958; -.
DR STRING; 9606.ENSP00000331487; -.
DR TCDB; 3.A.16.1.1; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PhosphoSite; Q8TAT6; -.
DR DMDM; 50428974; -.
DR PaxDb; Q8TAT6; -.
DR PRIDE; Q8TAT6; -.
DR DNASU; 55666; -.
DR Ensembl; ENST00000331134; ENSP00000331487; ENSG00000182446.
DR Ensembl; ENST00000374747; ENSP00000363879; ENSG00000182446.
DR GeneID; 55666; -.
DR KEGG; hsa:55666; -.
DR UCSC; uc002kat.4; human.
DR CTD; 55666; -.
DR GeneCards; GC17M079523; -.
DR HGNC; HGNC:18261; NPLOC4.
DR HPA; HPA021560; -.
DR HPA; HPA023295; -.
DR MIM; 606590; gene.
DR neXtProt; NX_Q8TAT6; -.
DR PharmGKB; PA143485558; -.
DR eggNOG; COG5100; -.
DR HOGENOM; HOG000008139; -.
DR HOVERGEN; HBG052659; -.
DR KO; K14015; -.
DR OMA; ECITAGM; -.
DR OrthoDB; EOG71RXJG; -.
DR UniPathway; UPA00144; -.
DR ChiTaRS; NPLOC4; human.
DR GeneWiki; NPLOC4; -.
DR GenomeRNAi; 55666; -.
DR NextBio; 60422; -.
DR PRO; PR:Q8TAT6; -.
DR ArrayExpress; Q8TAT6; -.
DR Bgee; Q8TAT6; -.
DR CleanEx; HS_NPLOC4; -.
DR Genevestigator; Q8TAT6; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; ISS:HGNC.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; ISS:HGNC.
DR GO; GO:0007030; P:Golgi organization; ISS:HGNC.
DR GO; GO:0061025; P:membrane fusion; ISS:HGNC.
DR InterPro; IPR007717; NPL4.
DR InterPro; IPR024682; Npl4_Ub-like_dom.
DR InterPro; IPR007716; NPL4_Zn-bd_put.
DR InterPro; IPR016563; PolyUb_recognition_cplx_Npl4.
DR InterPro; IPR001876; Znf_RanBP2.
DR Pfam; PF05021; NPL4; 1.
DR Pfam; PF11543; UN_NPL4; 1.
DR Pfam; PF05020; zf-NPL4; 1.
DR PIRSF; PIRSF010052; Polyub_prc_Npl4; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW Metal-binding; Nucleus; Reference proteome; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 608 Nuclear protein localization protein 4
FT homolog.
FT /FTId=PRO_0000057941.
FT ZN_FING 580 608 RanBP2-type.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 558 608 TVGGQLPGLHEYGAVGGSTHTATAAMWACQHCTFMNQPGTG
FT HCEMCSLPRT -> EYPHPLPRHPVAGAGEQPTLHSSPLPV
FT VPWIPHPAASWQVPSAMQRVETRPPCQARGRLR (in
FT isoform 2).
FT /FTId=VSP_009789.
FT CONFLICT 246 246 N -> S (in Ref. 2; BAB14499).
FT CONFLICT 248 248 H -> Q (in Ref. 2; BAA91314).
FT CONFLICT 573 573 G -> E (in Ref. 2; BAA91314).
FT CONFLICT 592 592 M -> V (in Ref. 2; BAB14499).
SQ SEQUENCE 608 AA; 68120 MW; 6ED6A0145F15C01D CRC64;
MAESIIIRVQ SPDGVKRITA TKRETAATFL KKVAKEFGFQ NNGFSVYINR NKTGEITASS
NKSLNLLKIK HGDLLFLFPS SLAGPSSEME TSVPPGFKVF GAPNVVEDEI DQYLSKQDGK
IYRSRDPQLC RHGPLGKCVH CVPLEPFDED YLNHLEPPVK HMSFHAYIRK LTGGADKGKF
VALENISCKI KSGCEGHLPW PNGICTKCQP SAITLNRQKY RHVDNIMFEN HTVADRFLDF
WRKTGNQHFG YLYGRYTEHK DIPLGIRAEV AAIYEPPQIG TQNSLELLED PKAEVVDEIA
AKLGLRKVGW IFTDLVSEDT RKGTVRYSRN KDTYFLSSEE CITAGDFQNK HPNMCRLSPD
GHFGSKFVTA VATGGPDNQV HFEGYQVSNQ CMALVRDECL LPCKDAPELG YAKESSSEQY
VPDVFYKDVD KFGNEITQLA RPLPVEYLII DITTTFPKDP VYTFSISQNP FPIENRDVLG
ETQDFHSLAT YLSQNTSSVF LDTISDFHLL LFLVTNEVMP LQDSISLLLE AVRTRNEELA
QTWKRSEQWA TIEQLCSTVG GQLPGLHEYG AVGGSTHTAT AAMWACQHCT FMNQPGTGHC
EMCSLPRT
//
ID NPL4_HUMAN Reviewed; 608 AA.
AC Q8TAT6; Q8N3J1; Q9H8V2; Q9H964; Q9NWR5; Q9P229;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Nuclear protein localization protein 4 homolog;
DE Short=Protein NPL4;
GN Name=NPLOC4; Synonyms=KIAA1499, NPL4;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 MRNA].
RC TISSUE=Pancreas;
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 [4]
RP PROTEIN SEQUENCE OF 2-8.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-608.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP INTERACTION WITH UFD1L, AND TISSUE SPECIFICITY.
RX PubMed=11574150; DOI=10.1016/S0378-1119(01)00649-7;
RA Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B.,
RA Novelli G.;
RT "Cloning and characterization of the gene encoding human NPL4, a
RT protein interacting with the ubiquitin fusion-degradation protein
RT (UFD1L).";
RL Gene 275:39-46(2001).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The ternary complex containing UFD1L, VCP and NPLOC4
CC binds ubiquitinated proteins and is necessary for the export of
CC misfolded proteins from the ER to the cytoplasm, where they are
CC degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates
CC spindle disassembly at the end of mitosis and is necessary for the
CC formation of a closed nuclear envelope (By similarity).
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent
CC pathway.
CC -!- SUBUNIT: Heterodimer with UFD1L. The heterodimer binds
CC ubiquitinated proteins. The heterodimer binds to VCP and inhibits
CC Golgi membrane fusion.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC Endoplasmic reticulum (By similarity). Nucleus (By similarity).
CC Note=Associated with the endoplasmic reticulum and nuclear (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TAT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TAT6-2; Sequence=VSP_009789;
CC Note=May be due to an intron retention. No experimental
CC confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in brain, heart,
CC skeletal muscle, kidney and fetal liver.
CC -!- DOMAIN: Binds ubiquitinated proteins via its RanBP2-type zinc
CC finger.
CC -!- SIMILARITY: Belongs to the NPL4 family.
CC -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91314.1; Type=Erroneous initiation;
CC Sequence=BAA96023.1; Type=Erroneous initiation;
CC Sequence=BAB14372.1; Type=Erroneous initiation;
CC Sequence=BAB14499.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB040932; BAA96023.1; ALT_INIT; mRNA.
DR EMBL; AK000664; BAA91314.1; ALT_INIT; mRNA.
DR EMBL; AK023046; BAB14372.1; ALT_INIT; mRNA.
DR EMBL; AK023272; BAB14499.1; ALT_INIT; mRNA.
DR EMBL; BC025930; AAH25930.1; -; mRNA.
DR EMBL; AL834300; CAD38971.1; -; mRNA.
DR RefSeq; NP_060391.2; NM_017921.2.
DR UniGene; Hs.464333; -.
DR ProteinModelPortal; Q8TAT6; -.
DR SMR; Q8TAT6; 2-77, 579-608.
DR DIP; DIP-44059N; -.
DR IntAct; Q8TAT6; 16.
DR MINT; MINT-3043958; -.
DR STRING; 9606.ENSP00000331487; -.
DR TCDB; 3.A.16.1.1; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PhosphoSite; Q8TAT6; -.
DR DMDM; 50428974; -.
DR PaxDb; Q8TAT6; -.
DR PRIDE; Q8TAT6; -.
DR DNASU; 55666; -.
DR Ensembl; ENST00000331134; ENSP00000331487; ENSG00000182446.
DR Ensembl; ENST00000374747; ENSP00000363879; ENSG00000182446.
DR GeneID; 55666; -.
DR KEGG; hsa:55666; -.
DR UCSC; uc002kat.4; human.
DR CTD; 55666; -.
DR GeneCards; GC17M079523; -.
DR HGNC; HGNC:18261; NPLOC4.
DR HPA; HPA021560; -.
DR HPA; HPA023295; -.
DR MIM; 606590; gene.
DR neXtProt; NX_Q8TAT6; -.
DR PharmGKB; PA143485558; -.
DR eggNOG; COG5100; -.
DR HOGENOM; HOG000008139; -.
DR HOVERGEN; HBG052659; -.
DR KO; K14015; -.
DR OMA; ECITAGM; -.
DR OrthoDB; EOG71RXJG; -.
DR UniPathway; UPA00144; -.
DR ChiTaRS; NPLOC4; human.
DR GeneWiki; NPLOC4; -.
DR GenomeRNAi; 55666; -.
DR NextBio; 60422; -.
DR PRO; PR:Q8TAT6; -.
DR ArrayExpress; Q8TAT6; -.
DR Bgee; Q8TAT6; -.
DR CleanEx; HS_NPLOC4; -.
DR Genevestigator; Q8TAT6; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; ISS:HGNC.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; ISS:HGNC.
DR GO; GO:0007030; P:Golgi organization; ISS:HGNC.
DR GO; GO:0061025; P:membrane fusion; ISS:HGNC.
DR InterPro; IPR007717; NPL4.
DR InterPro; IPR024682; Npl4_Ub-like_dom.
DR InterPro; IPR007716; NPL4_Zn-bd_put.
DR InterPro; IPR016563; PolyUb_recognition_cplx_Npl4.
DR InterPro; IPR001876; Znf_RanBP2.
DR Pfam; PF05021; NPL4; 1.
DR Pfam; PF11543; UN_NPL4; 1.
DR Pfam; PF05020; zf-NPL4; 1.
DR PIRSF; PIRSF010052; Polyub_prc_Npl4; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW Metal-binding; Nucleus; Reference proteome; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 608 Nuclear protein localization protein 4
FT homolog.
FT /FTId=PRO_0000057941.
FT ZN_FING 580 608 RanBP2-type.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 558 608 TVGGQLPGLHEYGAVGGSTHTATAAMWACQHCTFMNQPGTG
FT HCEMCSLPRT -> EYPHPLPRHPVAGAGEQPTLHSSPLPV
FT VPWIPHPAASWQVPSAMQRVETRPPCQARGRLR (in
FT isoform 2).
FT /FTId=VSP_009789.
FT CONFLICT 246 246 N -> S (in Ref. 2; BAB14499).
FT CONFLICT 248 248 H -> Q (in Ref. 2; BAA91314).
FT CONFLICT 573 573 G -> E (in Ref. 2; BAA91314).
FT CONFLICT 592 592 M -> V (in Ref. 2; BAB14499).
SQ SEQUENCE 608 AA; 68120 MW; 6ED6A0145F15C01D CRC64;
MAESIIIRVQ SPDGVKRITA TKRETAATFL KKVAKEFGFQ NNGFSVYINR NKTGEITASS
NKSLNLLKIK HGDLLFLFPS SLAGPSSEME TSVPPGFKVF GAPNVVEDEI DQYLSKQDGK
IYRSRDPQLC RHGPLGKCVH CVPLEPFDED YLNHLEPPVK HMSFHAYIRK LTGGADKGKF
VALENISCKI KSGCEGHLPW PNGICTKCQP SAITLNRQKY RHVDNIMFEN HTVADRFLDF
WRKTGNQHFG YLYGRYTEHK DIPLGIRAEV AAIYEPPQIG TQNSLELLED PKAEVVDEIA
AKLGLRKVGW IFTDLVSEDT RKGTVRYSRN KDTYFLSSEE CITAGDFQNK HPNMCRLSPD
GHFGSKFVTA VATGGPDNQV HFEGYQVSNQ CMALVRDECL LPCKDAPELG YAKESSSEQY
VPDVFYKDVD KFGNEITQLA RPLPVEYLII DITTTFPKDP VYTFSISQNP FPIENRDVLG
ETQDFHSLAT YLSQNTSSVF LDTISDFHLL LFLVTNEVMP LQDSISLLLE AVRTRNEELA
QTWKRSEQWA TIEQLCSTVG GQLPGLHEYG AVGGSTHTAT AAMWACQHCT FMNQPGTGHC
EMCSLPRT
//
MIM
606590
*RECORD*
*FIELD* NO
606590
*FIELD* TI
*606590 NUCLEAR PROTEIN LOCALIZATION 4, S. CEREVISIAE, HOMOLOG OF; NPLOC4
;;NPL4, S. CEREVISIAE, HOMOLOG OF;;
read moreKIAA1499
*FIELD* TX
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (2000) identified a cDNA encoding the
human homolog of yeast Npl4, which they designated KIAA1499. The deduced
660-amino acid human protein was predicted to be 34% identical to the
yeast protein. RT-PCR analysis detected ubiquitous expression that was
highest in brain, followed by spleen. Within brain, expression was
strongest in amygdala and substantia nigra, followed by caudate nucleus.
UFD1L (601754), which maps to chromosome 22q11.2, a region deleted in
patients with DiGeorge syndrome (DGS; 188400) or velocardiofacial
syndrome (VCFS; 192420), is similar to a yeast protein essential for the
ubiquitin-mediated protein degradation pathway. Rat Ufd1l binds to Npl4,
a component of the nuclear pore complex. By RT-PCR with degenerate
primers based on rat Npl4, followed by database searching, Botta et al.
(2001) obtained a cDNA encoding human NPL4. Sequence analysis predicted
that the 608-amino acid transmembrane protein, which is 96% homologous
to the rat protein, contains 5 potential N-glycosylation sites, 8
potential N-myristoylation sites, several phosphorylation sites, and a
C-terminal zinc finger motif. Northern blot analysis detected a major
transcript of 4.5 kb and minor transcripts of 9.5 and 2.5 kb. Expression
was most abundant in brain, heart, skeletal muscle, kidney, and fetal
liver. Yeast 2-hybrid analysis confirmed the interaction of UFD1L and
NPL4 in human. Sequence analysis identified no pathologic variants in
the NPL4 gene in 7 DGS/VCFS patients with no 22q11 deletions or
mutations in the UFD1L gene.
GENE STRUCTURE
By Southern blot analysis, Botta et al. (2001) determined that the NPL4
gene spans 40 kb.
MAPPING
By analysis of a human-rodent hybrid panel, Nagase et al. (2000) mapped
the NPLOC4 gene, which they identified as KIAA1499, to chromosome 17.
Using FISH, Botta et al. (2001) refined the localization to 17qter.
*FIELD* RF
1. Botta, A.; Tandoi, C.; Fini, G.; Calabrese, G.; Dallapiccola, B.;
Novelli, G.: Cloning and characterization of the gene encoding human
NPL4, a protein interacting with the ubiquitin fusion-degradation
protein (UFD1L). Gene 275: 39-46, 2001.
2. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 143-150, 2000.
*FIELD* CD
Paul J. Converse: 1/3/2002
*FIELD* ED
alopez: 02/14/2012
mgross: 1/3/2002
*RECORD*
*FIELD* NO
606590
*FIELD* TI
*606590 NUCLEAR PROTEIN LOCALIZATION 4, S. CEREVISIAE, HOMOLOG OF; NPLOC4
;;NPL4, S. CEREVISIAE, HOMOLOG OF;;
read moreKIAA1499
*FIELD* TX
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (2000) identified a cDNA encoding the
human homolog of yeast Npl4, which they designated KIAA1499. The deduced
660-amino acid human protein was predicted to be 34% identical to the
yeast protein. RT-PCR analysis detected ubiquitous expression that was
highest in brain, followed by spleen. Within brain, expression was
strongest in amygdala and substantia nigra, followed by caudate nucleus.
UFD1L (601754), which maps to chromosome 22q11.2, a region deleted in
patients with DiGeorge syndrome (DGS; 188400) or velocardiofacial
syndrome (VCFS; 192420), is similar to a yeast protein essential for the
ubiquitin-mediated protein degradation pathway. Rat Ufd1l binds to Npl4,
a component of the nuclear pore complex. By RT-PCR with degenerate
primers based on rat Npl4, followed by database searching, Botta et al.
(2001) obtained a cDNA encoding human NPL4. Sequence analysis predicted
that the 608-amino acid transmembrane protein, which is 96% homologous
to the rat protein, contains 5 potential N-glycosylation sites, 8
potential N-myristoylation sites, several phosphorylation sites, and a
C-terminal zinc finger motif. Northern blot analysis detected a major
transcript of 4.5 kb and minor transcripts of 9.5 and 2.5 kb. Expression
was most abundant in brain, heart, skeletal muscle, kidney, and fetal
liver. Yeast 2-hybrid analysis confirmed the interaction of UFD1L and
NPL4 in human. Sequence analysis identified no pathologic variants in
the NPL4 gene in 7 DGS/VCFS patients with no 22q11 deletions or
mutations in the UFD1L gene.
GENE STRUCTURE
By Southern blot analysis, Botta et al. (2001) determined that the NPL4
gene spans 40 kb.
MAPPING
By analysis of a human-rodent hybrid panel, Nagase et al. (2000) mapped
the NPLOC4 gene, which they identified as KIAA1499, to chromosome 17.
Using FISH, Botta et al. (2001) refined the localization to 17qter.
*FIELD* RF
1. Botta, A.; Tandoi, C.; Fini, G.; Calabrese, G.; Dallapiccola, B.;
Novelli, G.: Cloning and characterization of the gene encoding human
NPL4, a protein interacting with the ubiquitin fusion-degradation
protein (UFD1L). Gene 275: 39-46, 2001.
2. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 143-150, 2000.
*FIELD* CD
Paul J. Converse: 1/3/2002
*FIELD* ED
alopez: 02/14/2012
mgross: 1/3/2002