PBIP1_RAT
ID PBIP1_RAT Reviewed; 722 AA.
AC A2VD12;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 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 MRNA].
RC TISSUE=Lung;
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-559, AND
RP 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: 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 (between AA 190-218). {ECO:0000250}.
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DR EMBL; BC129100; AAI29101.1; -; mRNA.
DR RefSeq; NP_001094446.1; NM_001100976.1.
DR RefSeq; XP_006232731.1; XM_006232669.2.
DR AlphaFoldDB; A2VD12; -.
DR SMR; A2VD12; -.
DR BioGRID; 259689; 1.
DR STRING; 10116.ENSRNOP00000028058; -.
DR GlyGen; A2VD12; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; A2VD12; -.
DR PhosphoSitePlus; A2VD12; -.
DR PaxDb; A2VD12; -.
DR PeptideAtlas; A2VD12; -.
DR PRIDE; A2VD12; -.
DR Ensembl; ENSRNOT00000028057; ENSRNOP00000028058; ENSRNOG00000020673.
DR GeneID; 310644; -.
DR KEGG; rno:310644; -.
DR UCSC; RGD:1305180; rat.
DR CTD; 57326; -.
DR RGD; 1305180; Pbxip1.
DR eggNOG; ENOG502QRIW; Eukaryota.
DR GeneTree; ENSGT00940000162147; -.
DR HOGENOM; CLU_024505_0_0_1; -.
DR InParanoid; A2VD12; -.
DR OMA; LMQQPKG; -.
DR OrthoDB; 640123at2759; -.
DR PhylomeDB; A2VD12; -.
DR TreeFam; TF333202; -.
DR PRO; PR:A2VD12; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000020673; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; A2VD12; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0061975; P:articular cartilage development; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:1901148; P:gene expression involved in extracellular matrix organization; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0097043; P:histone H3-K56 acetylation; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; ISO:RGD.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..722
FT /note="Pre-B-cell leukemia transcription factor-interacting
FT protein 1"
FT /id="PRO_0000306117"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 266..346
FT /evidence="ECO:0000255"
FT COILED 373..401
FT /evidence="ECO:0000255"
FT MOTIF 482..502
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 686..711
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 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TVI8"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 722 AA; 80276 MW; B4E4E3512702B53D CRC64;
MASCPDSDNS WVLAGSETLP VETLGPESRV DPESEEAPQA LQDSSKADGK ESAGTLNGEE
MLFQTESSQG EGAALPEESE AKGALGGDDG HGTKRPGDTA VQEDLQETPM VTSLGPDTQD
LERNIHPQNL PSSPRAVWKE HGCSSSDDDT DVDVEGLRRR RGREPSPPQP TAAVDGEDQA
KGEGIGELGI SLNMCFLGAL VLLGLGILLF SGALLEPETE PVEEAELQVF PETELVQTVG
NRQDEVEQLQ ASVPPDSVPS LQSMGLLLDK LAKENQDIRL LQAQLQAQKE ELQSLLHQPK
GLEEENARLR EALQQGKTSH QALESELQQL RARLQGLEAN CVRGVDGVCL NWGGSPQGGK
ATTEQGHKGQ EPDTSLLEQH KQLEAEAKAL RQELQKQWQL LGSVHRNLQR GLQDAGQGAP
AHAGLAELGH MLAQTLQGLE SQGINTGRSS NDSEAWHQKK PRFQHPREWS GREKWRGGQR
DQKAEHWKLK KEESGQDRKK SWRDEGREFT GHWKENRPRA EESGSRKDSK RQDPKVHPRK
SGNSHSGERQ KHSWGKDNSP DSVSWEELLR RKYRPPQGCS GVADCARQEG LALFGVELAP
VRQQELASVL REYLARLPWA GQLTKELPLS PAYFGEDGIF RHDRLRFRDF VDALEDSLEE
VALKQTGDDD EVDDFEDFIF SHFFGDKALK RRSKKKEKQP WNHRAVGPRE EHSRHPHHYH
QG
