NIBA1_MOUSE
ID NIBA1_MOUSE Reviewed; 926 AA.
AC Q3UW53; A0PJB3; Q3TD68; Q6PE79; Q9ESL7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein Niban 1 {ECO:0000305};
DE AltName: Full=Protein FAM129A;
DE AltName: Full=Protein Niban {ECO:0000303|PubMed:11011112};
GN Name=Niban1 {ECO:0000312|MGI:MGI:2137237};
GN Synonyms=Fam129a {ECO:0000312|MGI:MGI:2137237},
GN Niban {ECO:0000303|PubMed:11011112};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAE23066.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23066.1}, and
RC NOD {ECO:0000312|EMBL:BAE41736.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE41736.1},
RC Epididymis {ECO:0000312|EMBL:BAE23066.1}, and
RC Testis {ECO:0000312|EMBL:BAC26641.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|EMBL:AAH21332.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH58234.2}, and
RC FVB/N-3 {ECO:0000312|EMBL:AAH21332.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH21332.1}, and
RC Olfactory epithelium {ECO:0000312|EMBL:AAH58234.2};
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 [3] {ECO:0000305, ECO:0000312|EMBL:BAB17052.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-926.
RX PubMed=11011112; DOI=10.1111/j.1349-7006.2000.tb01027.x;
RA Majima S., Kajino K., Fukuda T., Otsuka F., Hino O.;
RT "A novel gene 'Niban' upregulated in renal carcinogenesis: cloning by the
RT cDNA-amplified fragment length polymorphism approach.";
RL Jpn. J. Cancer Res. 91:869-874(2000).
RN [4] {ECO:0000305}
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17588536; DOI=10.1016/j.bbrc.2007.06.021;
RA Sun G.D., Kobayashi T., Abe M., Tada N., Adachi H., Shiota A., Totsuka Y.,
RA Hino O.;
RT "The endoplasmic reticulum stress-inducible protein Niban regulates
RT eIF2alpha and S6K1/4E-BP1 phosphorylation.";
RL Biochem. Biophys. Res. Commun. 360:181-187(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; SER-581; SER-595 AND
RP SER-601, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulates phosphorylation of a number of proteins involved in
CC translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be
CC involved in the endoplasmic reticulum stress response.
CC {ECO:0000269|PubMed:17588536}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN0}.
CC Membrane {ECO:0000250|UniProtKB:Q9BZQ8}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9BZQ8}.
CC -!- INDUCTION: By endoplasmic reticulum stress-inducing agents such as
CC tunicamycin and thapsigargin in liver, kidney and cerebrum.
CC {ECO:0000269|PubMed:17588536}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotypic abnormalities but mice show
CC increased phosphorylation of Eif2a and decreased phosphorylation of
CC Eif4ebp1 and Rps6kb1. {ECO:0000269|PubMed:17588536}.
CC -!- MISCELLANEOUS: 'Niban' means 'second' in Japanese.
CC {ECO:0000269|PubMed:11011112}.
CC -!- SIMILARITY: Belongs to the Niban family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21332.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH58234.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI37844.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB17052.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC26641.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK029847; BAC26641.1; ALT_SEQ; mRNA.
DR EMBL; AK136597; BAE23066.1; -; mRNA.
DR EMBL; AK170347; BAE41736.1; -; mRNA.
DR EMBL; BC021332; AAH21332.1; ALT_SEQ; mRNA.
DR EMBL; BC058234; AAH58234.2; ALT_INIT; mRNA.
DR EMBL; BC137843; AAI37844.1; ALT_INIT; mRNA.
DR EMBL; AB049355; BAB17052.1; ALT_INIT; mRNA.
DR CCDS; CCDS48393.1; -.
DR RefSeq; NP_071301.2; NM_022018.3.
DR RefSeq; XP_006529839.1; XM_006529776.3.
DR AlphaFoldDB; Q3UW53; -.
DR SMR; Q3UW53; -.
DR BioGRID; 211004; 5.
DR IntAct; Q3UW53; 1.
DR STRING; 10090.ENSMUSP00000115822; -.
DR iPTMnet; Q3UW53; -.
DR PhosphoSitePlus; Q3UW53; -.
DR EPD; Q3UW53; -.
DR jPOST; Q3UW53; -.
DR MaxQB; Q3UW53; -.
DR PaxDb; Q3UW53; -.
DR PeptideAtlas; Q3UW53; -.
DR PRIDE; Q3UW53; -.
DR ProteomicsDB; 293655; -.
DR Antibodypedia; 34451; 201 antibodies from 31 providers.
DR Ensembl; ENSMUST00000148810; ENSMUSP00000115822; ENSMUSG00000026483.
DR GeneID; 63913; -.
DR KEGG; mmu:63913; -.
DR UCSC; uc007cyz.2; mouse.
DR CTD; 116496; -.
DR MGI; MGI:2137237; Niban1.
DR VEuPathDB; HostDB:ENSMUSG00000026483; -.
DR eggNOG; ENOG502QVNR; Eukaryota.
DR GeneTree; ENSGT00940000154149; -.
DR HOGENOM; CLU_009718_0_1_1; -.
DR InParanoid; Q3UW53; -.
DR OMA; PKCRILP; -.
DR OrthoDB; 164866at2759; -.
DR PhylomeDB; Q3UW53; -.
DR TreeFam; TF333351; -.
DR BioGRID-ORCS; 63913; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Fam129a; mouse.
DR PRO; PR:Q3UW53; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3UW53; protein.
DR Bgee; ENSMUSG00000026483; Expressed in iris and 190 other tissues.
DR ExpressionAtlas; Q3UW53; baseline and differential.
DR Genevisible; Q3UW53; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR InterPro; IPR026088; Niban-like.
DR PANTHER; PTHR14392; PTHR14392; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome; Stress response; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
FT CHAIN 2..926
FT /note="Protein Niban 1"
FT /id="PRO_0000355583"
FT REGION 604..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN0"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
FT CONFLICT 2..4
FT /note="GGS -> ASA (in Ref. 3; BAB17052)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="R -> G (in Ref. 2; AAH21332)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="P -> Q (in Ref. 1; BAE41736)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="V -> E (in Ref. 2; AAH21332)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="T -> S (in Ref. 2; AAH21332)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="P -> S (in Ref. 2; AAH21332)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="K -> E (in Ref. 2; AAH21332)"
FT /evidence="ECO:0000305"
FT CONFLICT 911
FT /note="V -> L (in Ref. 1; BAE23066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 102649 MW; D41F603AF127673C CRC64;
MGGSASSQLD EGKCAYIRGK TEASIKNFSP YYSRQYSVAF CNHVRSEVEQ QRDLTSQFLK
TKPPLEPGTV LYEAELSQFA EDIRKWKDRY IVIKNDFAVE SYESKEAYQR GAVPKSRILP
AGGKVLTSEE EYSLLSDKHF PDPTASSEKN SQPFVLLPKA FPVYLWQPYL RHGYFCFHEA
AEQQKFSALL NDCIRHLNHD YMKQTTFEAQ AFLEAVQFFR QEKGHYGSWE MTTGDEVQVL
SKLVMEELLP TLQTDLLPKL KGKKNDRKRA WFGLLEEAYN LVQHQVSEGL NALKEECRAL
TKDLEGTIRS DMDQIVTSKN FLTGKIRAMV AQPAEQCCGE SVQPFLASIL EELMGPVSSG
FSEVRALFEK EVDELSQSFH ATQDSAQLKE GLQQLMKLPL DSVKMEPCYT KVTLLPERLL
DLQSRFRFPH VDLVVQRTQN YMQELMENAV FTFEQLLSPY LQGEASRIPV AIEKVKLRVL
KQYDYDSSTI RKKIFQEALI QITLPTVQKA LASTCKPELQ KYEQFIFADH TNMIHVENVY
EEILYEILLD ETLKVITEAA ILKKHNLFED NMALPSESVS SLTDLKTAMG SNQASPARRV
SAILPGAPDN ELPSNEVFQE PEEKKEQPGV PGSLAISASS CPSGGDGQVS VDHSAGGPLT
VENTAGPLSS HLSEVEAGGT LKDEEPTCQS PEPSAVPGSL KELKKLLTVT VSVESAPVVE
NDIHNGTPVP QENIKEEESK IHPEASHPAA IQQDSCEERE VREKEAQPLE AEAPGVDLGI
LPEGRGSTSQ STSGGLTENT SCPGPIEEPF EAQEPAEKVL PAIVSTEDSP QAGGEAEHSV
TVTPQEDATL SSNPICPMES NEVAQASGDQ EVLGGEDSSA LGMDTEQVND THEHACQWLV
EDTLSTDILA VHDFDVSSPE QPSEEW
