NBAS_HUMAN
ID NBAS_HUMAN Reviewed; 2371 AA.
AC A2RRP1; O95790; Q2VPJ7; Q53TK6; Q86V39; Q8NFY8; Q9Y3W5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=NBAS subunit of NRZ tethering complex {ECO:0000312|HGNC:HGNC:15625};
DE AltName: Full=Neuroblastoma-amplified gene protein {ECO:0000303|PubMed:19369418};
DE AltName: Full=Neuroblastoma-amplified sequence {ECO:0000303|PubMed:12706883};
GN Name=NBAS {ECO:0000312|HGNC:HGNC:15625};
GN Synonyms=NAG {ECO:0000303|PubMed:19369418};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-655, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Neuroblastoma;
RX PubMed=12706883; DOI=10.1016/s0378-1119(03)00459-1;
RA Scott D.K., Board J.R., Lu X., Pearson A.D.J., Kenyon R.M., Lunec J.;
RT "The neuroblastoma amplified gene, NAG: genomic structure and
RT characterisation of the 7.3 kb transcript predominantly expressed in
RT neuroblastoma.";
RL Gene 307:1-11(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS VAL-243 AND
RP ARG-655.
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 834-2371 (ISOFORM 2), AND VARIANT THR-2074.
RC TISSUE=Eye, and PNS;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 993-2371 (ISOFORMS 1/2), AND TISSUE
RP SPECIFICITY.
RX PubMed=9926938; DOI=10.1038/sj.onc.1202287;
RA Wimmer K., Zhu X.X., Lamb B.J., Kuick R., Ambros P.F., Kovar H.,
RA Thoraval D., Motyka S., Alberts J.R., Hanash S.M.;
RT "Co-amplification of a novel gene, NAG, with the N-myc gene in
RT neuroblastoma.";
RL Oncogene 18:233-238(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1068-2371 (ISOFORMS 1/2).
RC TISSUE=Uterus;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 TISSUE SPECIFICITY.
RX PubMed=10882752; DOI=10.1136/jmg.37.7.501;
RA Fruehwald M.C., O'Dorisio M.S., Rush L.J., Reiter J.L., Smiraglia D.J.,
RA Wenger G., Costello J.F., White P.S., Krahe R., Brodeur G.M., Plass C.;
RT "Gene amplification in PNETs/medulloblastomas: mapping of a novel amplified
RT gene within the MYCN amplicon.";
RL J. Med. Genet. 37:501-509(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION, SUBUNIT, INTERACTION WITH USE1, AND SUBCELLULAR LOCATION.
RX PubMed=19369418; DOI=10.1091/mbc.e08-11-1104;
RA Aoki T., Ichimura S., Itoh A., Kuramoto M., Shinkawa T., Isobe T.,
RA Tagaya M.;
RT "Identification of the neuroblastoma-amplified gene product as a component
RT of the syntaxin 18 complex implicated in Golgi-to-endoplasmic reticulum
RT retrograde transport.";
RL Mol. Biol. Cell 20:2639-2649(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1057, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT SOPH HIS-1914, AND
RP VARIANTS GLU-44; LEU-949 AND SER-1009.
RX PubMed=20577004; DOI=10.1136/jmg.2009.074815;
RA Maksimova N., Hara K., Nikolaeva I., Chun-Feng T., Usui T., Takagi M.,
RA Nishihira Y., Miyashita A., Fujiwara H., Oyama T., Nogovicina A.,
RA Sukhomyasova A., Potapova S., Kuwano R., Takahashi H., Nishizawa M.,
RA Onodera O.;
RT "Neuroblastoma amplified sequence gene is associated with a novel short
RT stature syndrome characterised by optic nerve atrophy and Pelger-Huet
RT anomaly.";
RL J. Med. Genet. 47:538-548(2010).
RN [14]
RP INTERACTION WITH ZW10, AND IDENTIFICATION IN THE NRZ COMPLEX.
RX PubMed=20462495; DOI=10.1016/j.str.2010.02.014;
RA Civril F., Wehenkel A., Giorgi F.M., Santaguida S., Di Fonzo A.,
RA Grigorean G., Ciccarelli F.D., Musacchio A.;
RT "Structural analysis of the RZZ complex reveals common ancestry with
RT multisubunit vesicle tethering machinery.";
RL Structure 18:616-626(2010).
RN [15]
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., Buerckstuemmer T.,
RA 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP INVOLVEMENT IN ILFS2, AND VARIANTS ILFS2 ILE-187 DEL; LEU-202 DEL; SER-348;
RP HIS-777; PHE-842; ARG-903; SER-984 AND PRO-1055.
RX PubMed=26073778; DOI=10.1016/j.ajhg.2015.05.009;
RA Haack T.B., Staufner C., Koepke M.G., Straub B.K., Koelker S., Thiel C.,
RA Freisinger P., Baric I., McKiernan P.J., Dikow N., Harting I., Beisse F.,
RA Burgard P., Kotzaeridou U., Kuehr J., Himbert U., Taylor R.W.,
RA Distelmaier F., Vockley J., Ghaloul-Gonzalez L., Zschocke J., Kremer L.S.,
RA Graf E., Schwarzmayr T., Bader D.M., Gagneur J., Wieland T., Terrile C.,
RA Strom T.M., Meitinger T., Hoffmann G.F., Prokisch H.;
RT "Biallelic mutations in NBAS cause recurrent acute liver failure with onset
RT in infancy.";
RL Am. J. Hum. Genet. 97:163-169(2015).
RN [20]
RP INVOLVEMENT IN MULTISYSTEM DISEASE, AND VARIANTS VAL-95; TRP-137 AND
RP ARG-396.
RX PubMed=26286438; DOI=10.1002/ajmg.a.37338;
RA Garcia Segarra N., Ballhausen D., Crawford H., Perreau M.,
RA Campos-Xavier B., van Spaendonck-Zwarts K., Vermeer C., Russo M.,
RA Zambelli P.Y., Stevenson B., Royer-Bertrand B., Rivolta C., Candotti F.,
RA Unger S., Munier F.L., Superti-Furga A., Bonafe L.;
RT "NBAS mutations cause a multisystem disorder involving bone, connective
RT tissue, liver, immune system, and retina.";
RL Am. J. Med. Genet. A 167:2902-2912(2015).
RN [21]
RP VARIANTS ILFS2 196-GLN--VAL-2371 DEL; LYS-803 AND TYR-1199.
RX PubMed=28629372; DOI=10.1186/s12876-017-0636-3;
RA Li J.Q., Qiu Y.L., Gong J.Y., Dou L.M., Lu Y., Knisely A.S., Zhang M.H.,
RA Luan W.S., Wang J.S.;
RT "Novel NBAS mutations and fever-related recurrent acute liver failure in
RT Chinese children: a retrospective study.";
RL BMC Gastroenterol. 17:77-77(2017).
RN [22]
RP VARIANTS 678-GLU--VAL-2371; 1004-ARG--VAL-2371 DEL AND HIS-1914, AND
RP CHARACTERIZATION OF VARIANTS 678-GLU--VAL-2371; 1004-ARG--VAL-2371 AND
RP HIS-1914.
RX PubMed=27789416; DOI=10.1016/j.bone.2016.10.023;
RG DDD Study;
RA Balasubramanian M., Hurst J., Brown S., Bishop N.J., Arundel P., DeVile C.,
RA Pollitt R.C., Crooks L., Longman D., Caceres J.F., Shackley F.,
RA Connolly S., Payne J.H., Offiah A.C., Hughes D., Parker M.J., Hide W.,
RA Skerry T.M.;
RT "Compound heterozygous variants in NBAS as a cause of atypical osteogenesis
RT imperfecta.";
RL Bone 94:65-74(2017).
RN [23]
RP VARIANTS ILFS2 PRO-227 AND 583-TRP--VAL-2371 DEL.
RX PubMed=28576691; DOI=10.1016/j.ejmg.2017.05.005;
RA Regateiro F.S., Belkaya S., Neves N., Ferreira S., Silvestre P., Lemos S.,
RA Venancio M., Casanova J.L., Goncalves I., Jouanguy E., Diogo L.;
RT "Recurrent elevated liver transaminases and acute liver failure in two
RT siblings with novel bi-allelic mutations of NBAS.";
RL Eur. J. Med. Genet. 60:426-432(2017).
RN [24]
RP VARIANT 501-ARG--VAL-2371 DEL.
RX PubMed=30825388; DOI=10.1002/humu.23734;
RA Carli D., Giorgio E., Pantaleoni F., Bruselles A., Barresi S., Riberi E.,
RA Licciardi F., Gazzin A., Baldassarre G., Pizzi S., Niceta M., Radio F.C.,
RA Molinatto C., Montin D., Calvo P.L., Ciolfi A., Fleischer N., Ferrero G.B.,
RA Brusco A., Tartaglia M.;
RT "NBAS pathogenic variants: Defining the associated clinical and facial
RT phenotype and genotype-phenotype correlations.";
RL Hum. Mutat. 40:721-728(2019).
RN [25]
RP VARIANTS ILFS2 ARG-903 AND HIS-941.
RX PubMed=32146038; DOI=10.1016/j.arcped.2020.01.003;
RA Chavany J., Cano A., Roquelaure B., Bourgeois P., Boubnova J., Gaignard P.,
RA Hoebeke C., Reynaud R., Rhomer B., Slama A., Badens C., Chabrol B.,
RA Fabre A.;
RT "Mutations in NBAS and SCYL1, genetic causes of recurrent liver failure in
RT children: Three case reports and a literature review.";
RL Arch. Pediatr. 27:155-159(2020).
CC -!- FUNCTION: Involved in Golgi-to-endoplasmic reticulum (ER) retrograde
CC transport; the function is proposed to depend on its association in the
CC NRZ complex which is believed to play a role in SNARE assembly at the
CC ER (PubMed:19369418). Required for normal embryonic development (By
CC similarity). May play a role in the nonsense-mediated decay pathway of
CC mRNAs containing premature stop codons (By similarity).
CC {ECO:0000250|UniProtKB:Q5TYW4, ECO:0000269|PubMed:19369418}.
CC -!- SUBUNIT: Component of the NRZ complex composed of NBAS, ZW10 and
CC RINT1/TIP20L; NRZ associates with SNAREs STX18, USE1, BNIP1/SEC20L and
CC SEC22B (the assembly has been described as syntaxin 18 complex); links
CC NRZ to SNARE USE1 (PubMed:19369418). {ECO:0000269|PubMed:19369418,
CC ECO:0000269|PubMed:20462495}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20577004}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:19369418}. Endoplasmic
CC reticulum membrane; Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2RRP1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2RRP1-2; Sequence=VSP_026445;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in heart and
CC skeletal muscle, and lowest levels in liver, small intestine and
CC thymus. Well expressed in retinal ganglion cells, epidermal skin cells,
CC and leukocytes. Up-regulated together with N-myc in some neuroblastoma
CC cell lines. {ECO:0000269|PubMed:10882752, ECO:0000269|PubMed:12706883,
CC ECO:0000269|PubMed:20577004, ECO:0000269|PubMed:9926938}.
CC -!- DISEASE: Short stature, optic nerve atrophy, and Pelger-Huet anomaly
CC (SOPH) [MIM:614800]: An autosomal recessive syndrome characterized by
CC severe postnatal growth retardation, facial dysmorphism with senile
CC face, small hands and feet, normal intelligence, abnormal nuclear shape
CC in neutrophil granulocytes (Pelger-Huet anomaly), and optic atrophy
CC with loss of visual acuity and color vision.
CC {ECO:0000269|PubMed:20577004}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Infantile liver failure syndrome 2 (ILFS2) [MIM:616483]: A
CC form of infantile liver failure syndrome, a life-threatening disorder
CC of hepatic function that manifests with acute liver failure in the
CC first few months of life. Clinical features include anemia, renal
CC tubulopathy, developmental delay, seizures, failure to thrive, and
CC liver steatosis and fibrosis. {ECO:0000269|PubMed:26073778,
CC ECO:0000269|PubMed:28576691, ECO:0000269|PubMed:28629372,
CC ECO:0000269|PubMed:32146038}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=NBAS mutations have been found in a multisystem disease
CC affecting the liver, eye, immune system, connective tissue, and bone.
CC Clinical manifestations include a progeroid appearance, short stature,
CC slender bones, epiphyseal dysplasia with multiple phalangeal pseudo-
CC epiphyses, cervical instability, myelopathy, elevated transaminases,
CC hypogammaglobulinemia, reduced natural killer cells, Pelger-Huet
CC anomaly of granulocytes, and in some cases retinal dystrophy and optic
CC atrophy. {ECO:0000269|PubMed:26286438, ECO:0000269|PubMed:27789416,
CC ECO:0000269|PubMed:30825388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD18133.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD18133.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB43382.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF388385; AAM93544.1; -; mRNA.
DR EMBL; AC007738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008282; AAY24347.1; -; Genomic_DNA.
DR EMBL; BC051792; AAH51792.2; -; mRNA.
DR EMBL; BC108693; AAI08694.1; ALT_TERM; mRNA.
DR EMBL; BC131735; AAI31736.1; -; mRNA.
DR EMBL; AF056195; AAD18133.1; ALT_SEQ; mRNA.
DR EMBL; AL050281; CAB43382.1; ALT_INIT; mRNA.
DR CCDS; CCDS1685.1; -. [A2RRP1-1]
DR PIR; T13150; T13150.
DR RefSeq; NP_056993.2; NM_015909.3. [A2RRP1-1]
DR AlphaFoldDB; A2RRP1; -.
DR BioGRID; 119627; 101.
DR ComplexPortal; CPX-6201; NRZ tethering complex.
DR DIP; DIP-56726N; -.
DR IntAct; A2RRP1; 29.
DR STRING; 9606.ENSP00000281513; -.
DR iPTMnet; A2RRP1; -.
DR MetOSite; A2RRP1; -.
DR PhosphoSitePlus; A2RRP1; -.
DR BioMuta; NBAS; -.
DR EPD; A2RRP1; -.
DR jPOST; A2RRP1; -.
DR MassIVE; A2RRP1; -.
DR MaxQB; A2RRP1; -.
DR PaxDb; A2RRP1; -.
DR PeptideAtlas; A2RRP1; -.
DR PRIDE; A2RRP1; -.
DR ProteomicsDB; 478; -. [A2RRP1-1]
DR ProteomicsDB; 479; -. [A2RRP1-2]
DR Antibodypedia; 26924; 91 antibodies from 25 providers.
DR DNASU; 51594; -.
DR Ensembl; ENST00000281513.10; ENSP00000281513.5; ENSG00000151779.13. [A2RRP1-1]
DR GeneID; 51594; -.
DR KEGG; hsa:51594; -.
DR MANE-Select; ENST00000281513.10; ENSP00000281513.5; NM_015909.4; NP_056993.2.
DR UCSC; uc002rcc.3; human. [A2RRP1-1]
DR CTD; 51594; -.
DR DisGeNET; 51594; -.
DR GeneCards; NBAS; -.
DR HGNC; HGNC:15625; NBAS.
DR HPA; ENSG00000151779; Low tissue specificity.
DR MalaCards; NBAS; -.
DR MIM; 608025; gene.
DR MIM; 614800; phenotype.
DR MIM; 616483; phenotype.
DR neXtProt; NX_A2RRP1; -.
DR OpenTargets; ENSG00000151779; -.
DR Orphanet; 464724; Fever-associated acute infantile liver failure syndrome.
DR Orphanet; 391677; Short stature-optic atrophy-Pelger-Huet anomaly syndrome.
DR PharmGKB; PA164723457; -.
DR VEuPathDB; HostDB:ENSG00000151779; -.
DR eggNOG; KOG1797; Eukaryota.
DR GeneTree; ENSGT00390000012474; -.
DR HOGENOM; CLU_001315_0_0_1; -.
DR InParanoid; A2RRP1; -.
DR OMA; WWADGAV; -.
DR PhylomeDB; A2RRP1; -.
DR TreeFam; TF313901; -.
DR PathwayCommons; A2RRP1; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; A2RRP1; -.
DR SIGNOR; A2RRP1; -.
DR BioGRID-ORCS; 51594; 444 hits in 1088 CRISPR screens.
DR ChiTaRS; NBAS; human.
DR GenomeRNAi; 51594; -.
DR Pharos; A2RRP1; Tbio.
DR PRO; PR:A2RRP1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; A2RRP1; protein.
DR Bgee; ENSG00000151779; Expressed in calcaneal tendon and 197 other tissues.
DR ExpressionAtlas; A2RRP1; baseline and differential.
DR Genevisible; A2RRP1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070939; C:Dsl1/NZR complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR029145; NBAS_N.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR013244; Sec39_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF15492; Nbas_N; 1.
DR Pfam; PF08314; Sec39; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Disease variant; Dwarfism;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..2371
FT /note="NBAS subunit of NRZ tethering complex"
FT /id="PRO_0000292806"
FT REPEAT 130..169
FT /note="WD 1"
FT REPEAT 316..355
FT /note="WD 2"
FT REGION 1..1035
FT /note="Interaction with USE1"
FT /evidence="ECO:0000269|PubMed:19369418"
FT REGION 1036..2371
FT /note="Interaction with ZW10 and RINT1"
FT /evidence="ECO:0000269|PubMed:19369418,
FT ECO:0000269|PubMed:20462495"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1057
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 860..979
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026445"
FT VARIANT 44
FT /note="Q -> E (in dbSNP:rs77081203)"
FT /evidence="ECO:0000269|PubMed:20577004"
FT /id="VAR_068954"
FT VARIANT 95
FT /note="A -> V (probable disease-associated variant found in
FT patients with a multisystem disease involving liver, eye,
FT immune system, connective tissue and bone)"
FT /evidence="ECO:0000269|PubMed:26286438"
FT /id="VAR_074643"
FT VARIANT 137
FT /note="R -> W (probable disease-associated variant found in
FT patients with a multisystem disease involving liver, eye,
FT immune system, connective tissue and bone;
FT dbSNP:rs368085185)"
FT /evidence="ECO:0000269|PubMed:26286438"
FT /id="VAR_074644"
FT VARIANT 187
FT /note="Missing (in ILFS2)"
FT /evidence="ECO:0000269|PubMed:26073778"
FT /id="VAR_074645"
FT VARIANT 197..2371
FT /note="Missing (in ILFS2; unknown pathological
FT significance; dbSNP:rs1131692171)"
FT /evidence="ECO:0000269|PubMed:28629372"
FT /id="VAR_085212"
FT VARIANT 202
FT /note="Missing (in ILFS2)"
FT /evidence="ECO:0000269|PubMed:26073778"
FT /id="VAR_074646"
FT VARIANT 227
FT /note="H -> P (in ILFS2; unknown pathological significance;
FT dbSNP:rs748880753)"
FT /evidence="ECO:0000269|PubMed:28576691"
FT /id="VAR_085213"
FT VARIANT 243
FT /note="I -> V (in dbSNP:rs13029846)"
FT /evidence="ECO:0000269|PubMed:15815621"
FT /id="VAR_057611"
FT VARIANT 348
FT /note="P -> S (in ILFS2)"
FT /evidence="ECO:0000269|PubMed:26073778"
FT /id="VAR_074647"
FT VARIANT 396
FT /note="W -> R (probable disease-associated variant found in
FT patients with a multisystem disease involving liver, eye,
FT immune system, connective tissue and bone)"
FT /evidence="ECO:0000269|PubMed:26286438"
FT /id="VAR_074648"
FT VARIANT 501..2371
FT /note="Missing (found in a patient with a multisystem
FT disease involving liver, eye, immune system, connective
FT tissue and bone; unknown pathological significance;
FT dbSNP:rs759960319)"
FT /evidence="ECO:0000269|PubMed:30825388"
FT /id="VAR_085214"
FT VARIANT 583..2371
FT /note="Missing (in ILFS2; unknown pathological
FT significance; dbSNP:rs770446752)"
FT /evidence="ECO:0000269|PubMed:28576691"
FT /id="VAR_085215"
FT VARIANT 655
FT /note="K -> R (in dbSNP:rs4668909)"
FT /evidence="ECO:0000269|PubMed:12706883,
FT ECO:0000269|PubMed:15815621"
FT /id="VAR_057612"
FT VARIANT 678..2371
FT /note="Missing (found in a patient with a multisystem
FT disease involving liver, eye, immune system, connective
FT tissue and bone; unknown pathological significance; reduced
FT protein expression levels in fibroblasts)"
FT /evidence="ECO:0000269|PubMed:27789416"
FT /id="VAR_085216"
FT VARIANT 777
FT /note="P -> H (in ILFS2)"
FT /evidence="ECO:0000269|PubMed:26073778"
FT /id="VAR_074649"
FT VARIANT 803
FT /note="E -> K (in ILFS2; unknown pathological significance;
FT dbSNP:rs781408707)"
FT /evidence="ECO:0000269|PubMed:28629372"
FT /id="VAR_085217"
FT VARIANT 842
FT /note="V -> F (in ILFS2; dbSNP:rs1085307944)"
FT /evidence="ECO:0000269|PubMed:26073778"
FT /id="VAR_074650"
FT VARIANT 903
FT /note="L -> R (in ILFS2; unknown pathological significance;
FT dbSNP:rs368196005)"
FT /evidence="ECO:0000269|PubMed:26073778,
FT ECO:0000269|PubMed:32146038"
FT /id="VAR_074651"
FT VARIANT 941
FT /note="R -> H (in ILFS2; unknown pathological significance;
FT dbSNP:rs781766556)"
FT /evidence="ECO:0000269|PubMed:32146038"
FT /id="VAR_085218"
FT VARIANT 949
FT /note="V -> L (in dbSNP:rs74727069)"
FT /evidence="ECO:0000269|PubMed:20577004"
FT /id="VAR_068955"
FT VARIANT 984
FT /note="I -> S (in ILFS2; dbSNP:rs140841721)"
FT /evidence="ECO:0000269|PubMed:26073778"
FT /id="VAR_074652"
FT VARIANT 1004..2371
FT /note="Missing (found in a patient with a multisystem
FT disease involving liver, eye, immune system, connective
FT tissue and bone; unknown pathological significance; reduced
FT collagen secretion, diffuse collagen bundles and reduced
FT protein expression in fibroblasts; dbSNP:rs780108348)"
FT /evidence="ECO:0000269|PubMed:27789416"
FT /id="VAR_085219"
FT VARIANT 1004
FT /note="R -> Q (in dbSNP:rs16862653)"
FT /id="VAR_057613"
FT VARIANT 1009
FT /note="C -> S (in dbSNP:rs74411619)"
FT /evidence="ECO:0000269|PubMed:20577004"
FT /id="VAR_068956"
FT VARIANT 1055
FT /note="L -> P (in ILFS2; dbSNP:rs796052121)"
FT /evidence="ECO:0000269|PubMed:26073778"
FT /id="VAR_074653"
FT VARIANT 1178
FT /note="S -> N (in dbSNP:rs35770368)"
FT /id="VAR_057614"
FT VARIANT 1199
FT /note="C -> Y (in ILFS2; unknown pathological significance;
FT dbSNP:rs779982692)"
FT /evidence="ECO:0000269|PubMed:28629372"
FT /id="VAR_085220"
FT VARIANT 1914
FT /note="R -> H (in SOPH; also found in patients with a
FT multisystem disease involving liver, eye, immune system,
FT connective tissue and bone; unknown pathological
FT significance; reduced collagen secretion, diffuse collagen
FT bundles and reduced protein expression in fibroblasts.;
FT dbSNP:rs369698072)"
FT /evidence="ECO:0000269|PubMed:20577004,
FT ECO:0000269|PubMed:27789416"
FT /id="VAR_068957"
FT VARIANT 2074
FT /note="A -> T (in dbSNP:rs6710817)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_057615"
FT CONFLICT 22
FT /note="I -> T (in Ref. 1; AAM93544)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="K -> E (in Ref. 1; AAM93544)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="F -> L (in Ref. 1; AAM93544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1102
FT /note="M -> T (in Ref. 1; AAM93544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1229
FT /note="K -> E (in Ref. 4; AAD18133)"
FT /evidence="ECO:0000305"
FT CONFLICT 1277
FT /note="E -> G (in Ref. 1; AAM93544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1784
FT /note="H -> Y (in Ref. 1; AAM93544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1797
FT /note="G -> S (in Ref. 1; AAM93544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1854
FT /note="L -> S (in Ref. 1; AAM93544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1997
FT /note="E -> D (in Ref. 4; AAD18133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2028
FT /note="P -> L (in Ref. 4; AAD18133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2030
FT /note="D -> N (in Ref. 4; AAD18133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2033
FT /note="P -> T (in Ref. 4; AAD18133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2171
FT /note="A -> T (in Ref. 4; AAD18133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2371 AA; 268571 MW; 54500EFAA487FB94 CRC64;
MAAPESGPAL SPGTAEGEEE TILYDLLVNT EWPPETEVQP RGNQKHGASF IITKAIRDRL
LFLRQYIWYS PAPFLLPDGL VRLVNKQINW HLVLASNGKL LAAVQDQCVE IRSAKDDFTS
IIGKCQVPKD PKPQWRRVAW SYDCTLLAYA ESTGTVRVFD LMGSELFVIS PASSFIGDLS
YAIAGLIFLE YKASAQWSAE LLVINYRGEL RSYLVSVGTN QSYQESHCFS FSSHYPHGIN
TAIYHPGHRL LLVGGCETAE VGMSKASSCG LSAWRVLSGS PYYKQVTNGG DGVTAVPKTL
GLLRMLSVKF YSRQGQEQDG IFKMSLSPDG MLLAAIHFSG KLSIWAIPSL KQQGEWGQNE
QPGYDDLNPD WRLSTEKRKK IKDKESFYPL IDVNWWADSA VTLARCSGAL TVSSVKTLKN
LLGKSCEWFE PSPQVTATHD GGFLSLECEI KLAPKRSRLE TRAGEEDEGE EDSDSDYEIS
AKARYFGYIK QGLYLVTEME RFAPPRKRPR TITKNYRLVS LRSTTPEELY QRKIESEEYE
EALSLAHTYG LDTDLVYQRQ WRKSAVNVAS IQNYLSKIKK RSWVLHECLE RVPENVDAAK
ELLQYGLKGT DLEALLAIGK GADDGRFTLP GEIDIDSISY EELSPPDEEP AKNKKEKELK
KRQELLKLVN FSKLTLEQKE LCRCRRKLLT YLDRLATYEE ILGVPHASEQ RYDAEFFKKF
RNQNIVLSAR TYAQESNVQA LEILFTYHGS DLLPHRLAIL SNFPETTSPH EYSVLLPEAC
FNGDSLMIIP WHEHKHRAKD WCEELACRMV VEPNLQDESE FLYAAQPELL RFRMTQLTVE
KVMDWYQTRA EEIEHYARQV DCALSLIRLG MERNIPGLLV LCDNLVTLET LVYEARCDVT
LTLKELQQMK DIEKLRLLMN SCSEDKYVTS AYQWMVPFLH RCEKQSPGVA NELLKEYLVT
LAKGDLKFPL KIFQHSKPDL QQKIIPDQDQ LMAIALECIY TCERNDQLCL CYDLLECLPE
RGYGDKTEAT TKLHDMVDQL EQILSVSELL EKHGLEKPIS FVKNTQSSSE EARKLMVRLT
RHTGRKQPPV SESHWRTLLQ DMLTMQQNVY TCLDSDACYE IFTESLLCSS RLENIHLAGQ
MMHCSACSEN PPAGIAHKGK PHYRVSYEKS IDLVLAASRE YFNSSTNLTD SCMDLARCCL
QLITDRPPAI QEELDLIQAV GCLEEFGVKI LPLQVRLCPD RISLIKECIS QSPTCYKQST
KLLGLAELLR VAGENPEERR GQVLILLVEQ ALRFHDYKAA SMHCQELMAT GYPKSWDVCS
QLGQSEGYQD LATRQELMAF ALTHCPPSSI ELLLAASSSL QTEILYQRVN FQIHHEGGEN
ISASPLTSKA VQEDEVGVPG SNSADLLRWT TATTMKVLSN TTTTTKAVLQ AVSDGQWWKK
SLTYLRPLQG QKCGGAYQIG TTANEDLEKQ GCHPFYESVI SNPFVAESEG TYDTYQHVPV
ESFAEVLLRT GKLAEAKNKG EVFPTTEVLL QLASEALPND MTLALAYLLA LPQVLDANRC
FEKQSPSALS LQLAAYYYSL QIYARLAPCF RDKCHPLYRA DPKELIKMVT RHVTRHEHEA
WPEDLISLTK QLHCYNERLL DFTQAQILQG LRKGVDVQRF TADDQYKRET ILGLAETLEE
SVYSIAISLA QRYSVSRWEV FMTHLEFLFT DSGLSTLEIE NRAQDLHLFE TLKTDPEAFH
QHMVKYIYPT IGGFDHERLQ YYFTLLENCG CADLGNCAIK PETHIRLLKK FKVVASGLNY
KKLTDENMSP LEALEPVLSS QNILSISKLV PKIPEKDGQM LSPSSLYTIW LQKLFWTGDP
HLIKQVPGSS PEWLHAYDVC MKYFDRLHPG DLITVVDAVT FSPKAVTKLS VEARKEMTRK
AIKTVKHFIE KPRKRNSEDE AQEAKDSKVT YADTLNHLEK SLAHLETLSH SFILSLKNSE
QETLQKYSHL YDLSRSEKEK LHDEAVAICL DGQPLAMIQQ LLEVAVGPLD ISPKDIVQSA
IMKIISALSG GSADLGGPRD PLKVLEGVVA AVHASVDKGE ELVSPEDLLE WLRPFCADDA
WPVRPRIHVL QILGQSFHLT EEDSKLLVFF RTEAILKASW PQRQVDIADI ENEENRYCLF
MELLESSHHE AEFQHLVLLL QAWPPMKSEY VITNNPWVRL ATVMLTRCTM ENKEGLGNEV
LKMCRSLYNT KQMLPAEGVK ELCLLLLNQS LLLPSLKLLL ESRDEHLHEM ALEQITAVTT
VNDSNCDQEL LSLLLDAKLL VKCVSTPFYP RIVDHLLASL QQGRWDAEEL GRHLREAGHE
AEAGSLLLAV RGTHQAFRTF STALRAAQHW V
