NIBA1_RAT
ID NIBA1_RAT Reviewed; 937 AA.
AC Q9ESN0;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 93.
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|RGD:71088}; Synonyms=Fam129a, Niban {ECO:0000305};
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] {ECO:0000305, ECO:0000312|EMBL:BAB15951.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Renal cell carcinoma {ECO:0000312|EMBL:BAB15951.1};
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 [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14990989; DOI=10.1038/sj.onc.1207468;
RA Adachi H., Majima S., Kon S., Kobayashi T., Kajino K., Mitani H.,
RA Hirayama Y., Shiina H., Igawa M., Hino O.;
RT "Niban gene is commonly expressed in the renal tumors: a new candidate
RT marker for renal carcinogenesis.";
RL Oncogene 23:3495-3500(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; SER-581; SER-601 AND
RP SER-768, AND IDENTIFICATION BY MASS 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: 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q3UW53}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14990989}. Membrane
CC {ECO:0000250|UniProtKB:Q9BZQ8}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9BZQ8}.
CC -!- TISSUE SPECIFICITY: Detected in brain, lung, spleen and skeletal
CC muscle. Expressed in small renal tumors but not in normal kidney.
CC {ECO:0000269|PubMed:11011112, ECO:0000269|PubMed:14990989}.
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=BAB15951.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046718; BAB15951.1; ALT_INIT; mRNA.
DR RefSeq; NP_071578.2; NM_022242.2.
DR AlphaFoldDB; Q9ESN0; -.
DR SMR; Q9ESN0; -.
DR IntAct; Q9ESN0; 1.
DR STRING; 10116.ENSRNOP00000003320; -.
DR iPTMnet; Q9ESN0; -.
DR PhosphoSitePlus; Q9ESN0; -.
DR PaxDb; Q9ESN0; -.
DR PRIDE; Q9ESN0; -.
DR Ensembl; ENSRNOT00000003320; ENSRNOP00000003320; ENSRNOG00000002403.
DR GeneID; 63912; -.
DR KEGG; rno:63912; -.
DR UCSC; RGD:71088; rat.
DR CTD; 116496; -.
DR RGD; 71088; Niban1.
DR eggNOG; ENOG502QVNR; Eukaryota.
DR GeneTree; ENSGT00940000154149; -.
DR HOGENOM; CLU_009718_0_1_1; -.
DR InParanoid; Q9ESN0; -.
DR OMA; PKCRILP; -.
DR OrthoDB; 164866at2759; -.
DR PhylomeDB; Q9ESN0; -.
DR TreeFam; TF333351; -.
DR PRO; PR:Q9ESN0; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002403; Expressed in esophagus and 18 other tissues.
DR Genevisible; Q9ESN0; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS: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..937
FT /note="Protein Niban 1"
FT /id="PRO_0000355584"
FT REGION 584..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZQ8"
SQ SEQUENCE 937 AA; 103465 MW; E923CED974F3169A CRC64;
MGGSASSQLD EGKCAYIRGK TEASIKNFSP YYSRQYSVAF CNHVRSEVEQ QRDLTSQFLK
TKPPLEPGTV LYEAELSQFA EDIRKWKDRY VVVKNDFAVE SYENKEAYQR GAVPKSRILP
AGGKVLTSEE EYSLLSDKHF PDPTASSEKN SQPFLVLPKA FPVYLWQPYL RHGYFCFHEA
AEQQKFSALL NDCIRHLNHD YMKQTTFEAQ AFLEAVQFFR QEKGHYGAWE VITGDEVQIL
SKLVMEELLP TLQTDLLPKL KGKKNDRKRA WFGLLEEAYN LVQHQVSEGL SALKEECRAL
TKDLEGTIRS DMDQIVNSKN FLTGKIRAMV AQPAENRCGE SVQPFLASIL EELMGPVSSG
FSEVRALFEK EVDELSQSFH TTQDGAQLKE CLDQLMKLPL DSVKMEPCYT KVTLLPERLL
DLQSRFRFPH VDLVVQRTQN YMQELMENAV FTFEQLLSPY LQGEASRTAV AIEKVKLRVL
KQYDYDSSTI RKKIFQEALI QITLPTVQKA LASTCKPELQ KYEQFIFADH TNMIHVENIY
EEILYQILLD ETLKVITEAA ILKKHNLFED NMALPSESVS SLTDLKTSMG SNQASPARGA
SAILPGAPGD EAPGSEVFQG PEEKQQQPGV PGSLAREESA SISGSSPPSG EDGQVSVSGV
DNSAGNPLSA DNSAGPLSSH LSEAEAGEPP KDEETAHKRP ESSAVPGSLR ELKELLTVTV
FVESAPEIGN DTLNGTPVPQ EDKKEEEEEE ESKIHPEASG PAAIQQDSCE ESEVREREAH
PMPLEAEAPG VNLGTLPEGR GPTSQSTGEG LTENTSCLGP IEEPSEAQGP TEEVLLATVS
TQDSTEAGGE AVHSVTVTPQ EDATLSSNPI CPVENNEGPQ VSEDQEVLGG NDSPALAMDT
EQINDAHVYE CHWEVEDAPS ADILDVHDCD VGSPGEW
