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 05-OCT-2010, entry version 58. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RP VARIANT ASP-357. RX MEDLINE=20408961; PubMed=10825160; DOI=10.1074/jbc.M001323200; RA Abramovich C., Shen W.-F., Pineault N., Imren S., Montpetit B., RA Largman C., Humphries R.K.; RT "Functional cloning and characterization of a novel nonhomeodomain RT protein 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ESR1, AND MUTAGENESIS RP OF 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-146; SER-147; RP SER-148 AND THR-152, AND MASS SPECTROMETRY. 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=19007248; DOI=10.1021/ac801708p; RA Wang B., Malik R., Nigg E.A., Korner R.; RT "Evaluation of the low-specificity protease elastase for large-scale RT phosphoproteome analysis."; RL Anal. Chem. 80:9526-9533(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-147 AND RP SER-148, AND MASS SPECTROMETRY. 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). CC -!- FUNCTION: Regulator of pre-B-cell leukemia transcription factors CC (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA CC and blocks the transcriptional activity of E2A-PBX1. Tethers CC estrogen receptor-alpha (ESR1) to microtubules and allows them to CC influence estrogen receptors-alpha signaling. CC -!- SUBUNIT: Interacts with ESR1, PBX1, PBX2 and PBX3. CC -!- INTERACTION: CC Q9Y3C0:CCDC53; NbExp=2; IntAct=EBI-740845, EBI-712969; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. CC Note=Shuttles between the nucleus and the cytosol. Mainly CC localized in the cytoplasm, associated with microtubules. Detected CC in small amounts in the nucleus. 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 -!- DOMAIN: The C-terminal domain (AA 443-731) contains a nuclear CC export signal. CC -!- DOMAIN: Association to the cytoskeleton through a N-terminal CC leucine rich-domain (AA 190-218). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF221521; AAG02026.1; -; mRNA. DR EMBL; AK022497; BAB14059.1; -; mRNA. DR EMBL; AK023219; BAB14471.1; -; mRNA. DR EMBL; AL451085; CAI13238.1; -; Genomic_DNA. DR EMBL; AL451085; CAI13239.1; -; Genomic_DNA. DR EMBL; AL451085; CAI13240.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53175.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53176.1; -; Genomic_DNA. DR EMBL; BC016852; AAH16852.1; -; mRNA. DR IPI; IPI00220556; -. DR IPI; IPI00332106; -. DR IPI; IPI00645060; -. DR RefSeq; NP_065385.2; -. DR UniGene; Hs.505806; -. DR ProteinModelPortal; Q96AQ6; -. DR IntAct; Q96AQ6; 13. DR MINT; MINT-1438383; -. DR STRING; Q96AQ6; -. DR PhosphoSite; Q96AQ6; -. DR PRIDE; Q96AQ6; -. DR Ensembl; ENST00000368463; ENSP00000357448; ENSG00000163346. DR GeneID; 57326; -. DR KEGG; hsa:57326; -. DR UCSC; uc001ffr.1; human. DR UCSC; uc001ffs.1; human. DR CTD; 57326; -. DR GeneCards; GC01M154916; -. DR H-InvDB; HIX0001107; -. DR HGNC; HGNC:21199; PBXIP1. DR HPA; HPA006949; -. DR PharmGKB; PA134956095; -. DR HOGENOM; HBG126255; -. DR HOVERGEN; HBG108234; -. DR InParanoid; Q96AQ6; -. DR OMA; ARLPWAG; -. DR PhylomeDB; Q96AQ6; -. DR NextBio; 63434; -. DR ArrayExpress; Q96AQ6; -. DR Bgee; Q96AQ6; -. DR CleanEx; HS_PBXIP1; -. DR Genevestigator; Q96AQ6; -. DR GO; GO:0005829; C:cytosol; NAS:UniProtKB. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; NAS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB. DR GO; GO:0007275; P:multicellular organismal development; NAS:UniProtKB. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; KW Cytoskeleton; Microtubule; Nucleus; Phosphoprotein; Polymorphism. FT CHAIN 1 731 Pre-B-cell leukemia transcription factor- FT interacting protein 1. FT /FTId=PRO_0000306115. FT COILED 270 348 Potential. FT COILED 377 417 Potential. FT MOTIF 485 505 Nuclear localization signal (Potential). FT MOTIF 695 720 Nuclear localization signal (Potential). FT COMPBIAS 160 165 Poly-Arg. FT COMPBIAS 721 729 His-rich. FT MOD_RES 43 43 Phosphoserine. FT MOD_RES 45 45 Phosphoserine. FT MOD_RES 146 146 Phosphoserine. FT MOD_RES 147 147 Phosphoserine. FT MOD_RES 148 148 Phosphoserine. FT MOD_RES 152 152 Phosphothreonine. FT VAR_SEQ 1 29 Missing (in isoform 2). FT /FTId=VSP_028418. FT VAR_SEQ 566 634 Missing (in isoform 3). FT /FTId=VSP_028419. FT VARIANT 356 356 G -> D (in dbSNP:rs2061690). FT /FTId=VAR_051263. FT VARIANT 357 357 G -> D (in dbSNP:rs2061690). FT /FTId=VAR_035265. FT MUTAGEN 615 619 LASLL->AASAA: Reduces interaction with FT ESR1. FT CONFLICT 139 139 I -> F (in Ref. 2; BAB14059). FT CONFLICT 268 268 M -> I (in Ref. 1; AAG02026 and 2; FT BAB14471). FT CONFLICT 381 381 L -> P (in Ref. 2; BAB14059). FT CONFLICT 595 595 A -> P (in Ref. 1; AAG02026). 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 //