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   27-MAR-2024, entry version 154.
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,
RC   Pancreas, 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   iPTMnet; Q8R1F1; -.
DR   PhosphoSitePlus; Q8R1F1; -.
DR   SwissPalm; Q8R1F1; -.
DR   EPD; Q8R1F1; -.
DR   jPOST; Q8R1F1; -.
DR   MaxQB; Q8R1F1; -.
DR   PaxDb; 10090-ENSMUSP00000028135; -.
DR   PeptideAtlas; Q8R1F1; -.
DR   ProteomicsDB; 293656; -.
DR   Pumba; Q8R1F1; -.
DR   Antibodypedia; 17013; 164 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000028135.15; ENSMUSP00000028135.9; ENSMUSG00000026796.17.
DR   GeneID; 227737; -.
DR   KEGG; mmu:227737; -.
DR   UCSC; uc008jhc.2; mouse.
DR   AGR; MGI:2442910; -.
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; GTPIDWG; -.
DR   OrthoDB; 5482508at2759; -.
DR   PhylomeDB; Q8R1F1; -.
DR   TreeFam; TF333351; -.
DR   BioGRID-ORCS; 227737; 2 hits in 76 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 220 other cell types or tissues.
DR   ExpressionAtlas; Q8R1F1; baseline and differential.
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 DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR026088; Niban-like.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR14392; NIBAN FAMILY MEMBER; 1.
DR   PANTHER; PTHR14392:SF2; PROTEIN NIBAN 2; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   Genevisible; Q8R1F1; MM.
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
//