NIBA2_RAT
ID NIBA2_RAT Reviewed; 747 AA.
AC B4F7E8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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|RGD:1307018}; Synonyms=Fam129b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-641; SER-645;
RP SER-648; SER-672; SER-693 AND SER-697, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role in apoptosis suppression. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell junction,
CC 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}.
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DR EMBL; CH474001; EDL93203.1; -; Genomic_DNA.
DR EMBL; BC168248; AAI68248.1; -; mRNA.
DR RefSeq; NP_001103355.1; NM_001109885.1.
DR AlphaFoldDB; B4F7E8; -.
DR SMR; B4F7E8; -.
DR STRING; 10116.ENSRNOP00000021689; -.
DR iPTMnet; B4F7E8; -.
DR PhosphoSitePlus; B4F7E8; -.
DR jPOST; B4F7E8; -.
DR PaxDb; B4F7E8; -.
DR PeptideAtlas; B4F7E8; -.
DR PRIDE; B4F7E8; -.
DR Ensembl; ENSRNOT00000021689; ENSRNOP00000021689; ENSRNOG00000015845.
DR GeneID; 362115; -.
DR KEGG; rno:362115; -.
DR UCSC; RGD:1307018; rat.
DR CTD; 64855; -.
DR RGD; 1307018; Niban2.
DR eggNOG; ENOG502QV2S; Eukaryota.
DR GeneTree; ENSGT00940000154149; -.
DR HOGENOM; CLU_009718_1_1_1; -.
DR InParanoid; B4F7E8; -.
DR OMA; TPIDWGE; -.
DR OrthoDB; 138545at2759; -.
DR TreeFam; TF333351; -.
DR PRO; PR:B4F7E8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000015845; Expressed in lung and 19 other tissues.
DR Genevisible; B4F7E8; RN.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0032274; P:gonadotropin secretion; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
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..747
FT /note="Protein Niban 2"
FT /id="PRO_0000412856"
FT DOMAIN 68..192
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 589..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..747
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 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q96TA1"
SQ SEQUENCE 747 AA; 84731 MW; CE5CFDA3C47A2EE7 CRC64;
MGDVLSTHLD DARRQNIAEK TEKILREFLR FYEDQYGVSL FNSMRHEIEG TGPPQAQLLW
RKVPLDERII FSGNLFQYQE DNKKWRNRFS LVPHNYGLVL YENKVAYERQ IPPRAVINSA
GYKVLTSLDQ YLELVGNSLP GTTSKSGSTP ILKCPTQFPL ILWHPYARHY YFCMMTEAEQ
DKWQAVLQDC VRHCNNGIPE NSKVEGPAFT DAIRMYRQSK EQYGTWEMLC GNEVQILSNL
VMEELGPALK TELGPRLKGK PQERQRQWIQ ISDAVYRLVF EQAKVHFEEV LCKLQLARPA
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 KHNLYRDSVV LHNSDPNLHL LAEGAPIDWG EQYGDGGDGS
DSGGSPCPSE AATLTEKRRR AKQVVSVVQD EESGLPFEAG SEPPSPASPD NVTELRGLLA
QDLQAESSPP ASPLLNGAPV QESPQPMTVL EASPPASPLR HLPPGKAVDL EPPKPSDQET
GEKVSSPGSR PPIHTTTEDS AGVQTEF
