PBIP1_MOUSE
ID PBIP1_MOUSE Reviewed; 727 AA.
AC Q3TVI8; Q3TD91; Q3TWL9; Q8R319;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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-143 AND SER-164, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH TEX11.
RX PubMed=22383461; DOI=10.1210/me.2011-1263;
RA Yu Y.H., Siao F.P., Hsu L.C., Yen P.H.;
RT "TEX11 modulates germ cell proliferation by competing with estrogen
RT receptor beta for the binding to HPIP.";
RL Mol. Endocrinol. 26:630-642(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 (By similarity).
CC Interacts with TEX11. {ECO:0000250, ECO:0000269|PubMed:22383461}.
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; AK028858; BAC26157.1; -; mRNA.
DR EMBL; AK159422; BAE35070.1; -; mRNA.
DR EMBL; AK159448; BAE35092.1; -; mRNA.
DR EMBL; AK159633; BAE35247.1; -; mRNA.
DR EMBL; AK160103; BAE35630.1; -; mRNA.
DR EMBL; AK170318; BAE41713.1; -; mRNA.
DR EMBL; BC026838; AAH26838.1; -; mRNA.
DR EMBL; BC027771; AAH27771.1; -; mRNA.
DR EMBL; BC034200; AAH34200.1; -; mRNA.
DR CCDS; CCDS17510.1; -.
DR RefSeq; NP_666243.1; NM_146131.2.
DR RefSeq; XP_006501416.1; XM_006501353.1.
DR AlphaFoldDB; Q3TVI8; -.
DR SMR; Q3TVI8; -.
DR BioGRID; 230856; 6.
DR IntAct; Q3TVI8; 2.
DR STRING; 10090.ENSMUSP00000040429; -.
DR GlyConnect; 2599; 5 N-Linked glycans (1 site).
DR GlyGen; Q3TVI8; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; Q3TVI8; -.
DR PhosphoSitePlus; Q3TVI8; -.
DR EPD; Q3TVI8; -.
DR jPOST; Q3TVI8; -.
DR MaxQB; Q3TVI8; -.
DR PaxDb; Q3TVI8; -.
DR PeptideAtlas; Q3TVI8; -.
DR PRIDE; Q3TVI8; -.
DR ProteomicsDB; 287962; -.
DR Antibodypedia; 1813; 176 antibodies from 27 providers.
DR DNASU; 229534; -.
DR Ensembl; ENSMUST00000038942; ENSMUSP00000040429; ENSMUSG00000042613.
DR GeneID; 229534; -.
DR KEGG; mmu:229534; -.
DR UCSC; uc008pzr.2; mouse.
DR CTD; 57326; -.
DR MGI; MGI:2441670; Pbxip1.
DR VEuPathDB; HostDB:ENSMUSG00000042613; -.
DR eggNOG; ENOG502QRIW; Eukaryota.
DR GeneTree; ENSGT00940000162147; -.
DR HOGENOM; CLU_024505_0_0_1; -.
DR InParanoid; Q3TVI8; -.
DR OMA; LMQQPKG; -.
DR OrthoDB; 640123at2759; -.
DR PhylomeDB; Q3TVI8; -.
DR TreeFam; TF333202; -.
DR BioGRID-ORCS; 229534; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pbxip1; mouse.
DR PRO; PR:Q3TVI8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3TVI8; protein.
DR Bgee; ENSMUSG00000042613; Expressed in aorta tunica media and 253 other tissues.
DR ExpressionAtlas; Q3TVI8; baseline and differential.
DR Genevisible; Q3TVI8; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0061975; P:articular cartilage development; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:1901148; P:gene expression involved in extracellular matrix organization; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:MGI.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IMP:MGI.
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..727
FT /note="Pre-B-cell leukemia transcription factor-interacting
FT protein 1"
FT /id="PRO_0000306116"
FT REGION 1..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..350
FT /evidence="ECO:0000255"
FT COILED 377..405
FT /evidence="ECO:0000255"
FT MOTIF 486..506
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 691..716
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 97..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2VD12"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96AQ6"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2VD12"
FT CONFLICT 120
FT /note="E -> G (in Ref. 1; BAE35247)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="W -> R (in Ref. 1; BAE35630/BAE41713/BAE35247)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="R -> H (in Ref. 1; BAE41713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 81164 MW; D33539CF495B9222 CRC64;
MASCPDSDNS WVLAGSENLP VETLGPEPRM DPESEGASQA LRDSSKADGK ELAGTLDGEE
KLFQTESSQR ETAVLTESAA KGTLGADGHG TEAPGDTVVQ EDSQETPVAT SLGPDTQDLE
SEIHPQNLPS SPRAVWKEHR CSSSDDDTDV DVEGLRRRRG REPSSSQPVV PVDVEDQAKG
EGIGGELGIS LNMCFLGALV LLGLGILLFS GTLLEPETGP MEEAELQVFP ETGPETELVE
TLGNRQDEIE HLQASSVPPD SVPSLQSMGF LLDKLAKENQ DIRLLQAQLQ AQKEELQSLL
HQPKGLEEEN ARLREALQQG KTSHQALESE LQQLRARLQG LEANCVRGVD GVCLNWGGDP
QDGKATKEQG HKGQEPDPSL LEQHKQLEAE AKALRQELQR QWQLLGSVHW DLQRGLRDAG
RGAPAHPGLA ELGHMLAQTL QDLENQGINT GRSPNDSEAW HQKKPHTQSP REWGGKEKWR
GGQRDQKAEH WKPRKEESGQ ERQRSWRDEG REHTGRWRED RLRADESGSR KDSKRQDPKV
HPRKDGNSHS VERQKHSWGK DNSPDALSSW EELLRRKYRP PQGCSGVADC ARQEGLALFG
VELAPVRQQE LASVLREYLS RLPWAGQLTK QLPLSPAYFG EDGIFRHDRL RFRDFVDALE
DSLEEVALKQ TGDDDEVDDF EDFVFGHFFG DKALKKRSRK KEKHSWNPRV VGPREEHSRH
PHHYHQG
