PBIP1_BOVIN
ID PBIP1_BOVIN Reviewed; 727 AA.
AC A6QLY7; Q0V8Q4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Pre-B-cell leukemia transcription factor-interacting protein 1;
DE AltName: Full=Hematopoietic PBX-interacting protein;
GN Name=PBXIP1; Synonyms=HPIP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of pre-B-cell leukemia transcription factors (BPXs)
CC function. Inhibits the binding of PBX1-HOX complex to DNA and blocks
CC the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-
CC alpha (ESR1) to microtubules and allows them to influence estrogen
CC receptors-alpha signaling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ESR1, PBX1, PBX2 and PBX3. Interacts with TEX11
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q96AQ6}. Nucleus {ECO:0000250|UniProtKB:Q96AQ6}.
CC Note=Shuttles between the nucleus and the cytosol. Mainly localized in
CC the cytoplasm, associated with microtubules. Detected in small amounts
CC in the nucleus. {ECO:0000250|UniProtKB:Q96AQ6}.
CC -!- DOMAIN: The C-terminal domain (AA 443-731) contains a nuclear export
CC signal. {ECO:0000250}.
CC -!- DOMAIN: Association to the cytoskeleton through a N-terminal leucine
CC rich-domain (AA 190-218). {ECO:0000250}.
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DR EMBL; BT026164; ABG67003.1; -; mRNA.
DR EMBL; BC148133; AAI48134.1; -; mRNA.
DR RefSeq; NP_001068733.1; NM_001075265.1.
DR AlphaFoldDB; A6QLY7; -.
DR SMR; A6QLY7; -.
DR BioGRID; 163129; 1.
DR STRING; 9913.ENSBTAP00000005980; -.
DR PaxDb; A6QLY7; -.
DR PRIDE; A6QLY7; -.
DR GeneID; 506485; -.
DR KEGG; bta:506485; -.
DR CTD; 57326; -.
DR eggNOG; ENOG502QRIW; Eukaryota.
DR HOGENOM; CLU_024505_0_0_1; -.
DR InParanoid; A6QLY7; -.
DR OrthoDB; 640123at2759; -.
DR TreeFam; TF333202; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:2001106; P:regulation of Rho guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR InterPro; IPR033589; PBXIP1.
DR PANTHER; PTHR28638:SF1; PTHR28638:SF1; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..727
FT /note="Pre-B-cell leukemia transcription factor-interacting
FT protein 1"
FT /id="PRO_0000306114"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 269..353
FT /evidence="ECO:0000255"
FT COILED 380..421
FT /evidence="ECO:0000255"
FT MOTIF 488..506
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 696..719
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2VD12"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT CONFLICT 82
FT /note="Missing (in Ref. 1; ABG67003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 80258 MW; 14F9A8057E5E85C9 CRC64;
MASCPDSDNS WVLAGSESLP VETLGPESGN DPESERAPRA PQSPSRAAAE ESAGTLDGGE
TVSQNESSKS GPILSEEAEA KQGVLEGDDP GVESPGPGDT EAQGDLEETP EVVGLEPDSQ
DLEDQSPHRS LPSSPKTAWI REEAHHSSSD DDTDVDVEGL RRRRGREPGT PQPAATLGVE
DQVQGEGAGG QLGISLNMCL LGSLVLLGLG VLLFGGLSES ESGPLEEVDL QVLPDVESDT
EMLEAVGDGQ DGLQQLQTSE VLDSVPSLQN MALLLDKLAK ENQDIRLLQA QLQAQKEELQ
SLMRQPKGLE EENARLRGAL QQGEASQRAL ESELQQLRAQ LQGLEADCVQ GADGLCLQWG
RGPQAGQVTK EQGPTGQEPS PGFLEQKKQL EAEAQALRQE LERQRRLLGS VQQDLERSLK
EAGRGDPARA GLAELGHRLA QKLRGLENWG QHPGVPANVS EAWHQKPHFQ NSREPSGKEK
WWDRQGDWKT EHWKHKKEAS GREKSWRGEE DRELVGRRKE GKPRVEEWAG KKDGKQQRSK
EPPRKSGRPH PSGERQKHPR WKEGAKDRHD PLPLWAELSR HKYQAPQGCS GVHECARQEG
LAFFGIELAP VRQQELASLL RTYLARLPWA GPLTEELPLS PAYFGEDGIF RHDRLRFRDF
VDALEDQLEE VAVRQTGDDD AVDDFEDFIF SHFFGDKALK KRSGKKDKHL QNRVVGPREE
HSPHRQG
