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 27-MAR-2024, entry version 133. 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 DEL; 1004-ARG--VAL-2371 DEL AND HIS-1914, AND RP CHARACTERIZATION OF VARIANTS 678-GLU--VAL-2371 DEL; 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; 123. DR ComplexPortal; CPX-6201; NRZ tethering complex. DR DIP; DIP-56726N; -. DR IntAct; A2RRP1; 30. DR STRING; 9606.ENSP00000281513; -. DR GlyGen; A2RRP1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; A2RRP1; -. DR MetOSite; A2RRP1; -. DR PhosphoSitePlus; A2RRP1; -. DR SwissPalm; A2RRP1; -. DR BioMuta; NBAS; -. DR EPD; A2RRP1; -. DR jPOST; A2RRP1; -. DR MassIVE; A2RRP1; -. DR MaxQB; A2RRP1; -. DR PaxDb; 9606-ENSP00000281513; -. DR PeptideAtlas; A2RRP1; -. DR ProteomicsDB; 478; -. [A2RRP1-1] DR ProteomicsDB; 479; -. [A2RRP1-2] DR Pumba; A2RRP1; -. DR Antibodypedia; 26924; 111 antibodies from 25 providers. DR DNASU; 51594; -. DR Ensembl; ENST00000281513.10; ENSP00000281513.5; ENSG00000151779.14. [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 AGR; HGNC:15625; -. 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; KHMLPAE; -. DR OrthoDB; 7541at2759; -. 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; 458 hits in 1164 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 199 other cell types or tissues. DR ExpressionAtlas; A2RRP1; baseline and differential. 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; IEA:UniProtKB-SubCell. 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; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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 PANTHER; PTHR15922:SF2; NBAS SUBUNIT OF NRZ TETHERING COMPLEX; 1. DR PANTHER; PTHR15922; NEUROBLASTOMA-AMPLIFIED SEQUENCE; 1. DR Pfam; PF15492; Nbas_N; 1. DR Pfam; PF08314; Sec39; 1. DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR Genevisible; A2RRP1; HS. 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 (found in patients with a multisystem disease FT involving liver, eye, immune system, connective tissue and FT bone; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:26286438" FT /id="VAR_074643" FT VARIANT 137 FT /note="R -> W (found in patients with a multisystem disease FT involving liver, eye, immune system, connective tissue and FT bone; likely pathogenic; 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; uncertain significance; FT 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; uncertain 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 (found in patients with a multisystem disease FT involving liver, eye, immune system, connective tissue and FT bone; likely pathogenic)" 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; uncertain significance; FT dbSNP:rs759960319)" FT /evidence="ECO:0000269|PubMed:30825388" FT /id="VAR_085214" FT VARIANT 583..2371 FT /note="Missing (in ILFS2; uncertain significance; FT 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; uncertain significance; reduced protein FT 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; uncertain 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; uncertain 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; uncertain 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; uncertain significance; reduced collagen FT secretion, diffuse collagen bundles and reduced protein FT 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; uncertain significance; FT dbSNP:rs779982692)" FT /evidence="ECO:0000269|PubMed:28629372" FT /id="VAR_085220" FT VARIANT 1914 FT /note="R -> H (in SOPH; uncertain significance; also found FT in patients with a multisystem disease involving liver, FT eye, immune system, connective tissue and bone; uncertain 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 //