NIBA2_MOUSE
ID NIBA2_MOUSE Reviewed; 749 AA.
AC Q8R1F1; Q3TCV6; Q3U8I3; Q3UC84; Q3UDW4; Q3UIE4; Q543S7; Q8BQ71; Q8CC78;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein Niban 2 {ECO:0000305};
DE AltName: Full=Meg-3;
DE AltName: Full=Niban-like protein 1;
DE AltName: Full=Protein FAM129B;
GN Name=Niban2 {ECO:0000312|MGI:MGI:2442910};
GN Synonyms=Fam129b {ECO:0000303|PubMed:21148485};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Adipose tissue, Cecum, Dendritic cell, Embryonic heart,
RC Embryonic spinal ganglion, and Macrophage;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647; SER-650; SER-695 AND
RP SER-699, 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).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21148485; DOI=10.1074/jbc.m110.175273;
RA Chen S., Evans H.G., Evans D.R.;
RT "FAM129B/MINERVA, a novel adherens junction-associated protein, suppresses
RT apoptosis in HeLa cells.";
RL J. Biol. Chem. 286:10201-10209(2011).
CC -!- FUNCTION: May play a role in apoptosis suppression. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21148485}.
CC Cell junction, adherens junction {ECO:0000250}. Membrane
CC {ECO:0000250|UniProtKB:Q96TA1}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q96TA1}. Note=In exponentially growing cells,
CC exclusively cytoplasmic. Cell membrane localization is observed when
CC cells reach confluency and during telophase (By similarity).
CC Phosphorylation may play a role in relocalization to the membrane (By
CC similarity). {ECO:0000250}.
CC -!- PTM: As apoptosis proceeds, degraded via an proteasome-independent
CC pathway, probably by caspases. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Niban family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28456.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK033735; BAC28456.1; ALT_INIT; mRNA.
DR EMBL; AK046583; BAC32795.1; -; mRNA.
DR EMBL; AK051396; BAC34625.1; -; mRNA.
DR EMBL; AK146953; BAE27562.1; -; mRNA.
DR EMBL; AK149888; BAE29147.1; -; mRNA.
DR EMBL; AK150642; BAE29730.1; -; mRNA.
DR EMBL; AK152207; BAE31035.1; -; mRNA.
DR EMBL; AK153489; BAE32037.1; -; mRNA.
DR EMBL; AK170512; BAE41849.1; -; mRNA.
DR EMBL; AL845471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08584.1; -; Genomic_DNA.
DR EMBL; BC024639; AAH24639.1; -; mRNA.
DR EMBL; BC027843; AAH27843.1; -; mRNA.
DR CCDS; CCDS15934.1; -.
DR RefSeq; NP_666231.1; NM_146119.2.
DR AlphaFoldDB; Q8R1F1; -.
DR SMR; Q8R1F1; -.
DR BioGRID; 230679; 2.
DR IntAct; Q8R1F1; 1.
DR STRING; 10090.ENSMUSP00000028135; -.
DR iPTMnet; Q8R1F1; -.
DR PhosphoSitePlus; Q8R1F1; -.
DR SwissPalm; Q8R1F1; -.
DR EPD; Q8R1F1; -.
DR jPOST; Q8R1F1; -.
DR MaxQB; Q8R1F1; -.
DR PaxDb; Q8R1F1; -.
DR PeptideAtlas; Q8R1F1; -.
DR PRIDE; Q8R1F1; -.
DR ProteomicsDB; 293656; -.
DR Antibodypedia; 17013; 133 antibodies from 28 providers.
DR Ensembl; ENSMUST00000028135; ENSMUSP00000028135; ENSMUSG00000026796.
DR GeneID; 227737; -.
DR KEGG; mmu:227737; -.
DR UCSC; uc008jhc.2; mouse.
DR CTD; 64855; -.
DR MGI; MGI:2442910; Niban2.
DR VEuPathDB; HostDB:ENSMUSG00000026796; -.
DR eggNOG; ENOG502QV2S; Eukaryota.
DR GeneTree; ENSGT00940000154149; -.
DR HOGENOM; CLU_009718_1_1_1; -.
DR InParanoid; Q8R1F1; -.
DR OMA; TPIDWGE; -.
DR OrthoDB; 138545at2759; -.
DR PhylomeDB; Q8R1F1; -.
DR TreeFam; TF333351; -.
DR BioGRID-ORCS; 227737; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Fam129b; mouse.
DR PRO; PR:Q8R1F1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R1F1; protein.
DR Bgee; ENSMUSG00000026796; Expressed in gastrula and 217 other tissues.
DR ExpressionAtlas; Q8R1F1; baseline and differential.
DR Genevisible; Q8R1F1; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0032274; P:gonadotropin secretion; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR026088; Niban-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR14392; PTHR14392; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasm; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT CHAIN 2..749
FT /note="Protein Niban 2"
FT /id="PRO_0000213122"
FT DOMAIN 68..192
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 589..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B4F7E8"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT CONFLICT 81
FT /note="D -> G (in Ref. 1; BAE31035)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="P -> A (in Ref. 1; BAC28456)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="H -> L (in Ref. 1; BAE29147)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="V -> E (in Ref. 1; BAC34625)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="P -> Q (in Ref. 1; BAE27562)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="F -> S (in Ref. 1; BAE41849)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="T -> A (in Ref. 1; BAE29147)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="A -> G (in Ref. 1; BAE27562)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="D -> V (in Ref. 1; BAE29730)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="E -> K (in Ref. 1; BAE41849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 749 AA; 84819 MW; DB578DEA188492C8 CRC64;
MGDVLSTHLD DARRQHIAEK TEKILTEFLR FYEDQYGVSL FNSMRHEIEG TGPPQAQLLW
RKVPLDERII FSGNLFQYQE DNKKWRNRFS LVPHNYGLVL YENKVAYERQ IPPRAVINSA
GYKVLTSVDQ YLELVGNSLP GTTSKSGSTP ILKCPTQFPL ILWHPYARHY YFCMMTEAEQ
DKWQAVLQDC VRHCNNGIPE NSKVEGPAFT DAIRMYRQSK EQYGTWEMLC GNEVQILSNL
VMEELGPALK AELGPRLKGK PQERQRQWIQ ISDAVYRLVF EQAKVHFEDV LCKLQRARPA
MEAVIRTDMD QIITSKEHLA SKIRAFILPK AEVCVRNHVQ PYIPSILEAL MVPTSQGFTE
VRDVFFKEVT DMNLNVINEG GIDKLGEYME KLSQLAYHPL KMQSCYEKME PLRLDGLQQR
FDVSSTSVFK QRAQIHMREQ MDNAVYTFET LLHQELGKGP TKEELCKSIQ RILERVLKKY
DYDSSSVRKR FFREALLQIT IPFLLKKLAP TCKSELPRFQ ELIFEDFARF ILVENTYEEV
VLQTVMKDIL QAVKEAAVQR KHNLYRDSMV LHNSDPNLHL LAEGTPIDWG EQYGDSGDSG
GGDSGGSPCP SEAATLTEKR RRAKQVMSVV QDEESGLPFE AGVEPPSPAS PDSVTELRGL
LAQDLQAESS PPASPLLNGA PVQESSQPVA VPEASPPASP LRHLPPGKAV DLEPPKPSDQ
ETGEQVSSPG SRPPIHTTTE DSAGVQTEF
