FUBP1_RAT
ID FUBP1_RAT Reviewed; 639 AA.
AC Q32PX7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Far upstream element-binding protein 1 {ECO:0000250|UniProtKB:Q96AE4, ECO:0000312|EMBL:AAI07943.1};
DE Short=FBP {ECO:0000250|UniProtKB:Q96AE4};
DE Short=FUSE-binding protein 1 {ECO:0000250|UniProtKB:Q96AE4};
GN Name=Fubp1 {ECO:0000312|EMBL:AAI07943.1, ECO:0000312|RGD:1591892};
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:0000312|EMBL:AAI07943.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC TISSUE=Thymus {ECO:0000312|EMBL:AAI07943.1};
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 [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625, AND IDENTIFICATION BY
RP 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 MYC expression by binding to a single-stranded far-
CC upstream element (FUSE) upstream of the MYC promoter. May act both as
CC activator and repressor of transcription (By similarity).
CC {ECO:0000250|UniProtKB:Q96AE4}.
CC -!- SUBUNIT: Found in a complex with PUF60 and far upstream element (FUSE)
CC DNA segment. Interacts with PUF60 and JTV1 (By similarity).
CC {ECO:0000250|UniProtKB:Q96AE4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Ubiquitinated. This targets the protein for proteasome-mediated
CC degradation (By similarity). {ECO:0000250|UniProtKB:Q96AE4}.
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DR EMBL; BC107942; AAI07943.1; -; mRNA.
DR RefSeq; NP_001032742.1; NM_001037653.1.
DR AlphaFoldDB; Q32PX7; -.
DR SMR; Q32PX7; -.
DR IntAct; Q32PX7; 2.
DR STRING; 10116.ENSRNOP00000061544; -.
DR iPTMnet; Q32PX7; -.
DR PhosphoSitePlus; Q32PX7; -.
DR jPOST; Q32PX7; -.
DR PaxDb; Q32PX7; -.
DR PRIDE; Q32PX7; -.
DR GeneID; 654496; -.
DR KEGG; rno:654496; -.
DR CTD; 8880; -.
DR RGD; 1591892; Fubp1.
DR eggNOG; KOG1676; Eukaryota.
DR HOGENOM; CLU_014285_1_0_1; -.
DR InParanoid; Q32PX7; -.
DR OrthoDB; 590738at2759; -.
DR PhylomeDB; Q32PX7; -.
DR PRO; PR:Q32PX7; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q32PX7; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0048588; P:developmental cell growth; ISO:RGD.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; IMP:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0048103; P:somatic stem cell division; ISO:RGD.
DR Gene3D; 3.30.1370.10; -; 4.
DR InterPro; IPR015096; FUBP_C.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF09005; DUF1897; 2.
DR Pfam; PF00013; KH_1; 4.
DR SMART; SM00322; KH; 4.
DR SUPFAM; SSF54791; SSF54791; 4.
DR PROSITE; PS50084; KH_TYPE_1; 4.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT CHAIN 2..639
FT /note="Far upstream element-binding protein 1"
FT /id="PRO_0000365105"
FT DOMAIN 95..159
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 180..246
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 270..334
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 371..438
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 316
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q91WJ8"
FT MOD_RES 354
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 356
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 358
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 427
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96AE4"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 639 AA; 67197 MW; 60ADA3F9BBC3314D CRC64;
MADYSTVPPP SSGSAGGGGG GGVNDAFKDA LQRARQIAAK IGGDAGTSLN SNDYGYGGQK
RPLEDGDQPD AKKVPPQNDS FGAQLPPMHQ QQRSVMTEEY KVPDGMVGFI IGRGGEQISR
IQQESGCKIQ IAPDSGGLPE RSCMLTGTPE SVQSAKRLLD QIVEKGRPAP GFHHGDGPGN
AVQEIMIPAS KAGLVIGKGG ETIKQLQERA GVKMVMIQDG PQNTGADKPL RITGDPYKVQ
QAKEMVLELI RDQGGFREVR NEYGSRIGGN EGIDVPIPRF AVGIVIGRNG EMIKKIQNDA
GVRIQFKPDD GTTPDRIAQI TGPPDRCQHA AEIITDLLRS VQAGNPGGPG PGGRGRGRGQ
GNWNMGPPGG LQEFNFIVPT GKTGLIIGKG GETIKSISQQ SGARIELQRN PPPNADPNMK
LFTIRGTPQQ IDYARQLIEE KIGGPVNPLG PPVPHGPHGV PGPHGPPGPP GPGTPMGPYN
PAPYNPGPPG PAPHGPPAPY APQGWGNAYP HWQQQAPPDP AKAGTDPNSA AWAAYYAHYY
QQQAQPPPAA PAGAPTTTQT NGQGDQQNPA PAGQVDYTKA WEEYYKKMGQ AVPAPAGAPP
GGQPDYSAAW AEYYRQQAAY YAQTSPQGMP QHPPAPQGQ
