PBIP1_HUMAN
ID PBIP1_HUMAN Reviewed; 731 AA.
AC Q96AQ6; Q5T174; Q5T176; Q9H8X6; Q9HA02; Q9HD85;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INTERACTION WITH PBX1; PBX2 AND PBX3, AND VARIANT
RP ASP-357.
RX PubMed=10825160; DOI=10.1074/jbc.m001323200;
RA Abramovich C., Shen W.-F., Pineault N., Imren S., Montpetit B., Largman C.,
RA Humphries R.K.;
RT "Functional cloning and characterization of a novel nonhomeodomain protein
RT that inhibits the binding of PBX1-HOX complexes to DNA.";
RL J. Biol. Chem. 275:26172-26177(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ASP-357.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [6]
RP FUNCTION, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12360403; DOI=10.1038/sj.onc.1205784;
RA Abramovich C., Chavez E.A., Lansdorp P.M., Humphries R.K.;
RT "Functional characterization of multiple domains involved in the
RT subcellular localization of the hematopoietic Pbx interacting protein
RT (HPIP).";
RL Oncogene 21:6766-6771(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-147; SER-148 AND
RP THR-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ESR1, AND MUTAGENESIS OF
RP 615-LEU--LEU-619.
RX PubMed=17043237; DOI=10.1073/pnas.0607445103;
RA Manavathi B., Acconcia F., Rayala S.K., Kumar R.;
RT "An inherent role of microtubule network in the action of nuclear
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15981-15986(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-147 AND SER-148, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-129, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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. {ECO:0000269|PubMed:10825160,
CC ECO:0000269|PubMed:12360403, ECO:0000269|PubMed:17043237}.
CC -!- SUBUNIT: Interacts with TEX11 (By similarity). Interacts with ESR1,
CC PBX1, PBX2 and PBX3. {ECO:0000250, ECO:0000269|PubMed:10825160,
CC ECO:0000269|PubMed:17043237}.
CC -!- INTERACTION:
CC Q96AQ6; P49069: CAMLG; NbExp=3; IntAct=EBI-740845, EBI-1748958;
CC Q96AQ6; P24863: CCNC; NbExp=3; IntAct=EBI-740845, EBI-395261;
CC Q96AQ6; Q9UER7: DAXX; NbExp=3; IntAct=EBI-740845, EBI-77321;
CC Q96AQ6; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-740845, EBI-745369;
CC Q96AQ6; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-740845, EBI-10172181;
CC Q96AQ6; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-740845, EBI-746969;
CC Q96AQ6; Q96IK5: GMCL1; NbExp=5; IntAct=EBI-740845, EBI-2548508;
CC Q96AQ6; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-740845, EBI-12012928;
CC Q96AQ6; O95447: LCA5L; NbExp=3; IntAct=EBI-740845, EBI-8473670;
CC Q96AQ6; Q99750: MDFI; NbExp=4; IntAct=EBI-740845, EBI-724076;
CC Q96AQ6; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-740845, EBI-399246;
CC Q96AQ6; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-740845, EBI-10288852;
CC Q96AQ6; Q8NI37: PPTC7; NbExp=3; IntAct=EBI-740845, EBI-9089276;
CC Q96AQ6; O43765: SGTA; NbExp=4; IntAct=EBI-740845, EBI-347996;
CC Q96AQ6; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-740845, EBI-10173939;
CC Q96AQ6; Q9Y3C0: WASHC3; NbExp=4; IntAct=EBI-740845, EBI-712969;
CC Q96AQ6-1; P03372: ESR1; NbExp=3; IntAct=EBI-15606280, EBI-78473;
CC Q96AQ6-1; P03372-1: ESR1; NbExp=5; IntAct=EBI-15606280, EBI-15606245;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12360403, ECO:0000269|PubMed:17043237}. Nucleus
CC {ECO:0000269|PubMed:10825160, ECO:0000269|PubMed:12360403}.
CC Note=Shuttles between the nucleus and the cytosol (PubMed:12360403).
CC Mainly localized in the cytoplasm, associated with microtubules
CC (PubMed:10825160, PubMed:12360403). Detected in small amounts in the
CC nucleus (PubMed:10825160).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96AQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AQ6-2; Sequence=VSP_028418;
CC Name=3;
CC IsoId=Q96AQ6-3; Sequence=VSP_028419;
CC -!- TISSUE SPECIFICITY: Expressed in early hematopoietic precursors.
CC {ECO:0000269|PubMed:10825160}.
CC -!- DOMAIN: The C-terminal domain (AA 443-731) contains a nuclear export
CC signal.
CC -!- DOMAIN: Association to the cytoskeleton through a N-terminal leucine
CC rich-domain (AA 190-218).
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DR EMBL; AF221521; AAG02026.1; -; mRNA.
DR EMBL; AK022497; BAB14059.1; -; mRNA.
DR EMBL; AK023219; BAB14471.1; -; mRNA.
DR EMBL; AL451085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53175.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53176.1; -; Genomic_DNA.
DR EMBL; BC016852; AAH16852.1; -; mRNA.
DR CCDS; CCDS1074.1; -. [Q96AQ6-1]
DR CCDS; CCDS81382.1; -. [Q96AQ6-2]
DR RefSeq; NP_001304663.1; NM_001317734.1. [Q96AQ6-2]
DR RefSeq; NP_001304664.1; NM_001317735.1.
DR RefSeq; NP_065385.2; NM_020524.3. [Q96AQ6-1]
DR AlphaFoldDB; Q96AQ6; -.
DR SMR; Q96AQ6; -.
DR BioGRID; 121486; 250.
DR DIP; DIP-46922N; -.
DR IntAct; Q96AQ6; 63.
DR MINT; Q96AQ6; -.
DR STRING; 9606.ENSP00000357448; -.
DR GlyConnect; 1622; 3 N-Linked glycans (1 site).
DR GlyGen; Q96AQ6; 2 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q96AQ6; -.
DR PhosphoSitePlus; Q96AQ6; -.
DR SwissPalm; Q96AQ6; -.
DR BioMuta; PBXIP1; -.
DR DMDM; 74751749; -.
DR EPD; Q96AQ6; -.
DR jPOST; Q96AQ6; -.
DR MassIVE; Q96AQ6; -.
DR MaxQB; Q96AQ6; -.
DR PaxDb; Q96AQ6; -.
DR PeptideAtlas; Q96AQ6; -.
DR PRIDE; Q96AQ6; -.
DR ProteomicsDB; 75987; -. [Q96AQ6-1]
DR ProteomicsDB; 75988; -. [Q96AQ6-2]
DR ProteomicsDB; 75989; -. [Q96AQ6-3]
DR Antibodypedia; 1813; 176 antibodies from 27 providers.
DR DNASU; 57326; -.
DR Ensembl; ENST00000368463.8; ENSP00000357448.3; ENSG00000163346.17. [Q96AQ6-1]
DR Ensembl; ENST00000368465.5; ENSP00000357450.1; ENSG00000163346.17. [Q96AQ6-2]
DR GeneID; 57326; -.
DR KEGG; hsa:57326; -.
DR MANE-Select; ENST00000368463.8; ENSP00000357448.3; NM_020524.4; NP_065385.2.
DR UCSC; uc001ffr.4; human. [Q96AQ6-1]
DR CTD; 57326; -.
DR DisGeNET; 57326; -.
DR GeneCards; PBXIP1; -.
DR HGNC; HGNC:21199; PBXIP1.
DR HPA; ENSG00000163346; Low tissue specificity.
DR MIM; 618819; gene.
DR neXtProt; NX_Q96AQ6; -.
DR OpenTargets; ENSG00000163346; -.
DR PharmGKB; PA134956095; -.
DR VEuPathDB; HostDB:ENSG00000163346; -.
DR eggNOG; ENOG502QRIW; Eukaryota.
DR GeneTree; ENSGT00940000162147; -.
DR HOGENOM; CLU_024505_0_0_1; -.
DR InParanoid; Q96AQ6; -.
DR OMA; LMQQPKG; -.
DR OrthoDB; 640123at2759; -.
DR PhylomeDB; Q96AQ6; -.
DR TreeFam; TF333202; -.
DR PathwayCommons; Q96AQ6; -.
DR SignaLink; Q96AQ6; -.
DR BioGRID-ORCS; 57326; 22 hits in 1085 CRISPR screens.
DR ChiTaRS; PBXIP1; human.
DR GenomeRNAi; 57326; -.
DR Pharos; Q96AQ6; Tbio.
DR PRO; PR:Q96AQ6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96AQ6; protein.
DR Bgee; ENSG00000163346; Expressed in saphenous vein and 206 other tissues.
DR ExpressionAtlas; Q96AQ6; baseline and differential.
DR Genevisible; Q96AQ6; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0061975; P:articular cartilage development; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:1901148; P:gene expression involved in extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IEP:UniProtKB.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IEA:Ensembl.
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 Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..731
FT /note="Pre-B-cell leukemia transcription factor-interacting
FT protein 1"
FT /id="PRO_0000306115"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..348
FT /evidence="ECO:0000255"
FT COILED 377..417
FT /evidence="ECO:0000255"
FT MOTIF 485..505
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 695..720
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2VD12"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028418"
FT VAR_SEQ 566..634
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028419"
FT VARIANT 356
FT /note="G -> D (in dbSNP:rs2061690)"
FT /id="VAR_051263"
FT VARIANT 357
FT /note="G -> D (in dbSNP:rs2061690)"
FT /evidence="ECO:0000269|PubMed:10825160,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_035265"
FT MUTAGEN 615..619
FT /note="LASLL->AASAA: Reduces interaction with ESR1."
FT /evidence="ECO:0000269|PubMed:17043237"
FT CONFLICT 139
FT /note="I -> F (in Ref. 2; BAB14059)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="M -> I (in Ref. 1; AAG02026 and 2; BAB14471)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="L -> P (in Ref. 2; BAB14059)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="A -> P (in Ref. 1; AAG02026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 80643 MW; D9AB1F22A12E178D CRC64;
MASCPDSDNS WVLAGSESLP VETLGPASRM DPESERALQA PHSPSKTDGK ELAGTMDGEG
TLFQTESPQS GSILTEETEV KGTLEGDVCG VEPPGPGDTV VQGDLQETTV VTGLGPDTQD
LEGQSPPQSL PSTPKAAWIR EEGRCSSSDD DTDVDMEGLR RRRGREAGPP QPMVPLAVEN
QAGGEGAGGE LGISLNMCLL GALVLLGLGV LLFSGGLSES ETGPMEEVER QVLPDPEVLE
AVGDRQDGLR EQLQAPVPPD SVPSLQNMGL LLDKLAKENQ DIRLLQAQLQ AQKEELQSLM
HQPKGLEEEN AQLRGALQQG EAFQRALESE LQQLRARLQG LEADCVRGPD GVCLSGGRGP
QGDKAIREQG PREQEPELSF LKQKEQLEAE AQALRQELER QRRLLGSVQQ DLERSLQDAS
RGDPAHAGLA ELGHRLAQKL QGLENWGQDP GVSANASKAW HQKSHFQNSR EWSGKEKWWD
GQRDRKAEHW KHKKEESGRE RKKNWGGQED REPAGRWKEG RPRVEESGSK KEGKRQGPKE
PPRKSGSFHS SGEKQKQPRW REGTKDSHDP LPSWAELLRP KYRAPQGCSG VDECARQEGL
TFFGTELAPV RQQELASLLR TYLARLPWAG QLTKELPLSP AFFGEDGIFR HDRLRFRDFV
DALEDSLEEV AVQQTGDDDE VDDFEDFIFS HFFGDKALKK RSGKKDKHSQ SPRAAGPREG
HSHSHHHHHR G
