PAX5_HUMAN
ID PAX5_HUMAN Reviewed; 391 AA.
AC Q02548; A3QVP6; A3QVP7; A3QVP8; C0KTF6; C0KTF7; C0KTF8; C0KTF9; C0KTG0;
AC O75933; Q5SFM2; Q6S728; Q6S729; Q6S730; Q6S731; Q6S732;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Paired box protein Pax-5;
DE AltName: Full=B-cell-specific transcription factor;
DE Short=BSAP;
GN Name=PAX5;
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).
RX PubMed=1516825; DOI=10.1101/gad.6.9.1589;
RA Adams B., Doerfler P., Aguzzi A., Kozmik Z., Urbanek P., Maurer-Fogy I.,
RA Busslinger M.;
RT "Pax-5 encodes the transcription factor BSAP and is expressed in B
RT lymphocytes, the developing CNS, and adult testis.";
RL Genes Dev. 6:1589-1607(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), AND ALTERNATIVE
RP SPLICING.
RX PubMed=15385562; DOI=10.1074/jbc.m407171200;
RA Robichaud G.A., Nardini M., Laflamme M., Cuperlovic-Culf M.,
RA Ouellette R.J.;
RT "Human Pax-5 C-terminal isoforms possess distinct transactivation
RT properties and are differentially modulated in normal and malignant B
RT cells.";
RL J. Biol. Chem. 279:49956-49963(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 8; 9; 10 AND 11).
RX PubMed=19725825; DOI=10.1111/j.1365-2141.2009.07859.x;
RA Arseneau J.R., Laflamme M., Lewis S.M., Maicas E., Ouellette R.J.;
RT "Multiple isoforms of PAX5 are expressed in both lymphomas and normal B-
RT cells.";
RL Br. J. Haematol. 147:328-338(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-333 (ISOFORM 1), CHROMOSOMAL TRANSLOCATION
RP WITH ZNF521, CHROMOSOMAL TRANSLOCATION WITH FOXP1, AND CHROMOSOMAL
RP TRANSLOCATION WITH ETV6.
RX PubMed=17344859; DOI=10.1038/nature05690;
RA Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E.,
RA Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X., Pui C.-H.,
RA Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R.;
RT "Genome-wide analysis of genetic alterations in acute lymphoblastic
RT leukaemia.";
RL Nature 446:758-764(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-197.
RX PubMed=9742255; DOI=10.1093/nar/26.19.4497;
RA Verkoczy L.K., Berinstein N.L.;
RT "Isolation of genes negatively or positively co-expressed with human
RT recombination activating gene 1 (RAG1) by differential display PCR (DD RT-
RT PCR).";
RL Nucleic Acids Res. 26:4497-4507(1998).
RN [9]
RP INTERACTION WITH TBP AND RB1.
RX PubMed=10197586;
RA Eberhard D., Busslinger M.;
RT "The partial homeodomain of the transcription factor Pax-5 (BSAP) is an
RT interaction motif for the retinoblastoma and TATA-binding proteins.";
RL Cancer Res. 59:1716-1724(1999).
RN [10]
RP INTERACTION WITH TLE4, AND FUNCTION.
RX PubMed=10811620; DOI=10.1093/emboj/19.10.2292;
RA Eberhard D., Jimenez G., Heavey B., Busslinger M.;
RT "Transcriptional repression by Pax5 (BSAP) through interaction with
RT corepressors of the Groucho family.";
RL EMBO J. 19:2292-2303(2000).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR VIRUS
RP PROTEIN BZLF1 (MICROBIAL INFECTION).
RX PubMed=23678172; DOI=10.1128/jvi.00546-13;
RA Raver R.M., Panfil A.R., Hagemeier S.R., Kenney S.C.;
RT "The B-cell-specific transcription factor and master regulator Pax5
RT promotes Epstein-Barr virus latency by negatively regulating the viral
RT immediate early protein BZLF1.";
RL J. Virol. 87:8053-8063(2013).
RN [12]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=27181361; DOI=10.1016/j.bbrc.2016.05.067;
RA Inagaki Y., Hayakawa F., Hirano D., Kojima Y., Morishita T., Yasuda T.,
RA Naoe T., Kiyoi H.;
RT "PAX5 tyrosine phosphorylation by SYK co-operatively functions with its
RT serine phosphorylation to cancel the PAX5-dependent repression of BLIMP1: A
RT mechanism for antigen-triggered plasma cell differentiation.";
RL Biochem. Biophys. Res. Commun. 475:176-181(2016).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH EPSTEIN-BARR VIRUS PROTEIN
RP EBNA1 (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=31941781; DOI=10.1128/jvi.02028-19;
RA Liu C.D., Lee H.L., Peng C.W.;
RT "B Cell-Specific Transcription Activator PAX5 Recruits p300 To Support
RT EBNA1-Driven Transcription.";
RL J. Virol. 94:0-0(2020).
RN [14]
RP FUNCTION.
RX PubMed=32612238; DOI=10.1038/s41586-020-2454-y;
RA Hill L., Ebert A., Jaritz M., Wutz G., Nagasaka K., Tagoh H.,
RA Kostanova-Poliakova D., Schindler K., Sun Q., Boenelt P., Fischer M.,
RA Peters J.M., Busslinger M.;
RT "Wapl repression by Pax5 promotes V gene recombination by Igh loop
RT extrusion.";
RL Nature 584:142-147(2020).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-149 IN COMPLEX WITH MOUSE ETS1
RP AND DNA.
RX PubMed=11779502; DOI=10.1016/s1097-2765(01)00410-5;
RA Garvie C.W., Hagman J., Wolberger C.;
RT "Structural studies of Ets-1/Pax5 complex formation on DNA.";
RL Mol. Cell 8:1267-1276(2001).
RN [16]
RP VARIANT ALL3 SER-183, VARIANTS ARG-24; GLY-26; GLN-34; VAL-53; GLY-59;
RP ASN-66; ARG-75; ARG-80; THR-139; ILE-151; VAL-183; LEU-213; THR-301 AND
RP VAL-338, AND CHARACTERIZATION OF VARIANT ALL3 SER-183.
RX PubMed=24013638; DOI=10.1038/ng.2754;
RA Shah S., Schrader K.A., Waanders E., Timms A.E., Vijai J., Miething C.,
RA Wechsler J., Yang J., Hayes J., Klein R.J., Zhang J., Wei L., Wu G.,
RA Rusch M., Nagahawatte P., Ma J., Chen S.C., Song G., Cheng J., Meyers P.,
RA Bhojwani D., Jhanwar S., Maslak P., Fleisher M., Littman J., Offit L.,
RA Rau-Murthy R., Fleischut M.H., Corines M., Murali R., Gao X.,
RA Manschreck C., Kitzing T., Murty V.V., Raimondi S.C., Kuiper R.P.,
RA Simons A., Schiffman J.D., Onel K., Plon S.E., Wheeler D.A., Ritter D.,
RA Ziegler D.S., Tucker K., Sutton R., Chenevix-Trench G., Li J.,
RA Huntsman D.G., Hansford S., Senz J., Walsh T., Lee M., Hahn C.N.,
RA Roberts K.G., King M.C., Lo S.M., Levine R.L., Viale A., Socci N.D.,
RA Nathanson K.L., Scott H.S., Daly M., Lipkin S.M., Lowe S.W., Downing J.R.,
RA Altshuler D., Sandlund J.T., Horwitz M.S., Mullighan C.G., Offit K.;
RT "A recurrent germline PAX5 mutation confers susceptibility to pre-B cell
RT acute lymphoblastic leukemia.";
RL Nat. Genet. 45:1226-1231(2013).
CC -!- FUNCTION: Transcription factor that plays an essential role in
CC commitment of lymphoid progenitors to the B-lymphocyte lineage
CC (PubMed:10811620, PubMed:27181361). Fulfills a dual role by repressing
CC B-lineage inappropriate genes and simultaneously activating B-lineage-
CC specific genes (PubMed:10811620, PubMed:27181361). In turn, regulates
CC cell adhesion and migration, induces V(H)-to-D(H)J(H) recombination,
CC facilitates pre-B-cell receptor signaling and promotes development to
CC the mature B-cell stage (PubMed:32612238). Repression of the cohesin-
CC release factor WAPL causes global changes of the chromosomal
CC architecture in pro-B cells to facilitate the generation of a diverse
CC antibody repertoire (PubMed:32612238). {ECO:0000269|PubMed:10811620,
CC ECO:0000269|PubMed:27181361, ECO:0000269|PubMed:32612238}.
CC -!- FUNCTION: (Microbial infection) Plays an essential role in the
CC maintenance of Epstein-Barr virus genome copy number within the host
CC cell by promoting EBNA1/oriP-dependent binding and transcription
CC (PubMed:31941781). Participates also in the inhibition of lytic EBV
CC reactivation by modulating viral BZLF1 activity (PubMed:23678172).
CC {ECO:0000269|PubMed:23678172, ECO:0000269|PubMed:31941781}.
CC -!- SUBUNIT: Interacts with ETS1; this interaction alters PAX5 DNA-binding
CC properties (PubMed:11779502). Binds DNA as a monomer (PubMed:11779502).
CC Interacts with TBP; this interaction allows PAX5 to interact with the
CC basal transcription machinery (PubMed:10197586). Interacts with RB1
CC (PubMed:10197586). Interacts with TLE4 (PubMed:10811620). Interacts
CC with DAXX (By similarity). {ECO:0000250|UniProtKB:Q02650,
CC ECO:0000269|PubMed:10197586, ECO:0000269|PubMed:10811620,
CC ECO:0000269|PubMed:11779502}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus) with Epstein-
CC Barr virus protein BZLF1 (via C-terminus); this interaction inhibits
CC BZLF1-mediated lytic viral reactivation (PubMed:23678172). Interacts
CC also with EBNA1; this interaction promotes EBNA1-dependent
CC transcription (PubMed:31941781). {ECO:0000269|PubMed:23678172,
CC ECO:0000269|PubMed:31941781}.
CC -!- INTERACTION:
CC Q02548; Q8WYK0: ACOT12; NbExp=3; IntAct=EBI-296331, EBI-11954993;
CC Q02548; O75934: BCAS2; NbExp=3; IntAct=EBI-296331, EBI-1050106;
CC Q02548; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-296331, EBI-8643161;
CC Q02548; P24863: CCNC; NbExp=3; IntAct=EBI-296331, EBI-395261;
CC Q02548; Q00526: CDK3; NbExp=3; IntAct=EBI-296331, EBI-1245761;
CC Q02548; Q96Q77: CIB3; NbExp=3; IntAct=EBI-296331, EBI-10292696;
CC Q02548; P61024: CKS1B; NbExp=3; IntAct=EBI-296331, EBI-456371;
CC Q02548; P68400: CSNK2A1; NbExp=3; IntAct=EBI-296331, EBI-347804;
CC Q02548; Q8TB03: CXorf38; NbExp=3; IntAct=EBI-296331, EBI-12024320;
CC Q02548; Q86UW9: DTX2; NbExp=3; IntAct=EBI-296331, EBI-740376;
CC Q02548; P23142-4: FBLN1; NbExp=3; IntAct=EBI-296331, EBI-11956479;
CC Q02548; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-296331, EBI-11427343;
CC Q02548; Q6ISB3: GRHL2; NbExp=3; IntAct=EBI-296331, EBI-10219092;
CC Q02548; O14964: HGS; NbExp=3; IntAct=EBI-296331, EBI-740220;
CC Q02548; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-296331, EBI-2549423;
CC Q02548; O15347: HMGB3; NbExp=3; IntAct=EBI-296331, EBI-2214136;
CC Q02548; P31273: HOXC8; NbExp=3; IntAct=EBI-296331, EBI-1752118;
CC Q02548; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-296331, EBI-6426443;
CC Q02548; PRO_0000390949 [Q03164]: KMT2A; NbExp=2; IntAct=EBI-296331, EBI-2610266;
CC Q02548; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-296331, EBI-10171774;
CC Q02548; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-296331, EBI-1043191;
CC Q02548; Q6P4E2: LARP4; NbExp=3; IntAct=EBI-296331, EBI-12079790;
CC Q02548; Q5SW96: LDLRAP1; NbExp=3; IntAct=EBI-296331, EBI-747813;
CC Q02548; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-296331, EBI-2341787;
CC Q02548; P45984: MAPK9; NbExp=3; IntAct=EBI-296331, EBI-713568;
CC Q02548; Q969S2: NEIL2; NbExp=3; IntAct=EBI-296331, EBI-10281234;
CC Q02548; Q13952-2: NFYC; NbExp=3; IntAct=EBI-296331, EBI-11956831;
CC Q02548; Q96IV0: NGLY1; NbExp=3; IntAct=EBI-296331, EBI-6165879;
CC Q02548; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-296331, EBI-9057006;
CC Q02548; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-296331, EBI-10171633;
CC Q02548; P43351: RAD52; NbExp=3; IntAct=EBI-296331, EBI-706448;
CC Q02548; Q9UBE0: SAE1; NbExp=3; IntAct=EBI-296331, EBI-743154;
CC Q02548; Q9UDX3: SEC14L4; NbExp=3; IntAct=EBI-296331, EBI-10320311;
CC Q02548; Q99469: STAC; NbExp=3; IntAct=EBI-296331, EBI-2652799;
CC Q02548; Q86UE8: TLK2; NbExp=3; IntAct=EBI-296331, EBI-1047967;
CC Q02548; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-296331, EBI-10180829;
CC Q02548; Q14CS0: UBXN2B; NbExp=3; IntAct=EBI-296331, EBI-1993619;
CC Q02548; O94888: UBXN7; NbExp=3; IntAct=EBI-296331, EBI-1993627;
CC Q02548; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-296331, EBI-17634549;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31941781}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=1;
CC IsoId=Q02548-1; Sequence=Displayed;
CC Name=2; Synonyms=delta9;
CC IsoId=Q02548-2; Sequence=VSP_044121;
CC Name=3; Synonyms=delta78;
CC IsoId=Q02548-3; Sequence=VSP_044117, VSP_044118, VSP_044120;
CC Name=4; Synonyms=delta789;
CC IsoId=Q02548-4; Sequence=VSP_044116, VSP_044120;
CC Name=5; Synonyms=delta8;
CC IsoId=Q02548-5; Sequence=VSP_044115;
CC Name=6; Synonyms=delta7;
CC IsoId=Q02548-6; Sequence=VSP_044119;
CC Name=7;
CC IsoId=Q02548-7; Sequence=VSP_047830;
CC Name=8;
CC IsoId=Q02548-8; Sequence=VSP_047828;
CC Name=9;
CC IsoId=Q02548-9; Sequence=VSP_047828, VSP_044121;
CC Name=10;
CC IsoId=Q02548-10; Sequence=VSP_047827, VSP_047831;
CC Name=11;
CC IsoId=Q02548-11; Sequence=VSP_047829, VSP_047832;
CC -!- DEVELOPMENTAL STAGE: Expressed at early B-cell differentiation, in the
CC developing CNS and in adult testis.
CC -!- PTM: O-glycosylated. {ECO:0000305}.
CC -!- PTM: Phosphorylated by SYK. This phosphorylation plays an important
CC role in the abolition of BLIMP1 repression by PAX5 in order to trigger
CC plasma cell differentiation. {ECO:0000269|PubMed:27181361}.
CC -!- DISEASE: Note=A chromosomal aberration involving PAX5 is a cause of
CC acute lymphoblastic leukemia. Translocation t(9;18)(p13;q11.2) with
CC ZNF521. Translocation t(9;3)(p13;p14.1) with FOXP1. Translocation
CC t(9;12)(p13;p13) with ETV6. {ECO:0000269|PubMed:17344859}.
CC -!- DISEASE: Leukemia, acute lymphoblastic, 3 (ALL3) [MIM:613065]: A
CC subtype of acute leukemia, a cancer of the white blood cells. Acute
CC lymphoblastic anemia is a malignant disease of bone marrow and the most
CC common malignancy diagnosed in children. The malignant cells are
CC lymphoid precursor cells (lymphoblasts) that are arrested in an early
CC stage of development. The lymphoblasts replace the normal marrow
CC elements, resulting in a marked decrease in the production of normal
CC blood cells. Consequently, anemia, thrombocytopenia, and neutropenia
CC occur to varying degrees. The lymphoblasts also proliferate in organs
CC other than the marrow, particularly the liver, spleen, and lymphnodes.
CC {ECO:0000269|PubMed:24013638}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PAX5ID62.html";
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DR EMBL; M96944; AAA58397.1; -; mRNA.
DR EMBL; AY463952; AAR27590.1; -; mRNA.
DR EMBL; AY463953; AAR27591.1; -; mRNA.
DR EMBL; AY463954; AAR27592.1; -; mRNA.
DR EMBL; AY463955; AAR27593.1; -; mRNA.
DR EMBL; AY463956; AAR27594.1; -; mRNA.
DR EMBL; AY463957; AAR27595.1; -; mRNA.
DR EMBL; FJ626421; ACM91604.1; -; mRNA.
DR EMBL; FJ626422; ACM91605.1; -; mRNA.
DR EMBL; FJ626423; ACM91606.1; -; mRNA.
DR EMBL; FJ626424; ACM91607.1; -; mRNA.
DR EMBL; FJ626425; ACM91608.1; -; mRNA.
DR EMBL; EF064717; ABK41900.1; -; Genomic_DNA.
DR EMBL; AL161781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58294.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58295.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58296.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58297.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58298.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58299.1; -; Genomic_DNA.
DR EMBL; DQ841178; ABI30005.1; ALT_TERM; mRNA.
DR EMBL; DQ845345; ABI33104.1; ALT_TERM; mRNA.
DR EMBL; DQ845346; ABI33105.1; ALT_TERM; mRNA.
DR EMBL; AF080573; AAC35286.1; -; mRNA.
DR CCDS; CCDS65041.1; -. [Q02548-10]
DR CCDS; CCDS65042.1; -. [Q02548-9]
DR CCDS; CCDS65043.1; -. [Q02548-8]
DR CCDS; CCDS65044.1; -. [Q02548-4]
DR CCDS; CCDS65045.1; -. [Q02548-3]
DR CCDS; CCDS65046.1; -. [Q02548-7]
DR CCDS; CCDS65047.1; -. [Q02548-6]
DR CCDS; CCDS65048.1; -. [Q02548-2]
DR CCDS; CCDS6607.1; -. [Q02548-1]
DR PIR; A44063; A44063.
DR RefSeq; NP_001267476.1; NM_001280547.1. [Q02548-6]
DR RefSeq; NP_001267477.1; NM_001280548.1. [Q02548-2]
DR RefSeq; NP_001267478.1; NM_001280549.1.
DR RefSeq; NP_001267479.1; NM_001280550.1.
DR RefSeq; NP_001267481.1; NM_001280552.1. [Q02548-7]
DR RefSeq; NP_001267482.1; NM_001280553.1. [Q02548-9]
DR RefSeq; NP_001267483.1; NM_001280554.1. [Q02548-8]
DR RefSeq; NP_001267484.1; NM_001280555.1. [Q02548-10]
DR RefSeq; NP_001267485.1; NM_001280556.1.
DR RefSeq; NP_057953.1; NM_016734.2. [Q02548-1]
DR PDB; 1K78; X-ray; 2.25 A; A/E/I=1-149.
DR PDB; 1MDM; X-ray; 2.80 A; A=1-149.
DR PDBsum; 1K78; -.
DR PDBsum; 1MDM; -.
DR AlphaFoldDB; Q02548; -.
DR SMR; Q02548; -.
DR BioGRID; 111113; 57.
DR ELM; Q02548; -.
DR IntAct; Q02548; 43.
DR STRING; 9606.ENSP00000350844; -.
DR iPTMnet; Q02548; -.
DR PhosphoSitePlus; Q02548; -.
DR BioMuta; PAX5; -.
DR DMDM; 417449; -.
DR MassIVE; Q02548; -.
DR MaxQB; Q02548; -.
DR PaxDb; Q02548; -.
DR PeptideAtlas; Q02548; -.
DR PRIDE; Q02548; -.
DR ProteomicsDB; 58109; -. [Q02548-1]
DR ProteomicsDB; 67344; -.
DR ProteomicsDB; 67345; -.
DR ProteomicsDB; 67346; -.
DR ProteomicsDB; 7578; -.
DR ProteomicsDB; 7579; -.
DR ProteomicsDB; 7580; -.
DR ProteomicsDB; 7581; -.
DR ProteomicsDB; 7582; -.
DR Antibodypedia; 3668; 966 antibodies from 49 providers.
DR DNASU; 5079; -.
DR Ensembl; ENST00000358127.9; ENSP00000350844.4; ENSG00000196092.14. [Q02548-1]
DR Ensembl; ENST00000377840.6; ENSP00000367071.2; ENSG00000196092.14. [Q02548-5]
DR Ensembl; ENST00000377847.6; ENSP00000367078.2; ENSG00000196092.14. [Q02548-7]
DR Ensembl; ENST00000377852.7; ENSP00000367083.2; ENSG00000196092.14. [Q02548-6]
DR Ensembl; ENST00000377853.6; ENSP00000367084.2; ENSG00000196092.14. [Q02548-2]
DR Ensembl; ENST00000414447.5; ENSP00000412188.1; ENSG00000196092.14. [Q02548-8]
DR Ensembl; ENST00000446742.5; ENSP00000404687.1; ENSG00000196092.14. [Q02548-10]
DR Ensembl; ENST00000520281.5; ENSP00000430773.1; ENSG00000196092.14. [Q02548-9]
DR Ensembl; ENST00000523493.5; ENSP00000431038.1; ENSG00000196092.14. [Q02548-11]
DR GeneID; 5079; -.
DR KEGG; hsa:5079; -.
DR MANE-Select; ENST00000358127.9; ENSP00000350844.4; NM_016734.3; NP_057953.1.
DR UCSC; uc003zzo.3; human. [Q02548-1]
DR CTD; 5079; -.
DR DisGeNET; 5079; -.
DR GeneCards; PAX5; -.
DR HGNC; HGNC:8619; PAX5.
DR HPA; ENSG00000196092; Tissue enriched (lymphoid).
DR MalaCards; PAX5; -.
DR MIM; 167414; gene.
DR MIM; 613065; phenotype.
DR neXtProt; NX_Q02548; -.
DR OpenTargets; ENSG00000196092; -.
DR Orphanet; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality.
DR PharmGKB; PA32959; -.
DR VEuPathDB; HostDB:ENSG00000196092; -.
DR eggNOG; KOG3862; Eukaryota.
DR GeneTree; ENSGT00940000159636; -.
DR HOGENOM; CLU_019281_1_3_1; -.
DR InParanoid; Q02548; -.
DR OMA; IXIQESP; -.
DR OrthoDB; 592933at2759; -.
DR PhylomeDB; Q02548; -.
DR TreeFam; TF315397; -.
DR PathwayCommons; Q02548; -.
DR Reactome; R-HSA-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR SignaLink; Q02548; -.
DR SIGNOR; Q02548; -.
DR BioGRID-ORCS; 5079; 24 hits in 1098 CRISPR screens.
DR ChiTaRS; PAX5; human.
DR EvolutionaryTrace; Q02548; -.
DR GeneWiki; PAX5; -.
DR GenomeRNAi; 5079; -.
DR Pharos; Q02548; Tbio.
DR PRO; PR:Q02548; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q02548; protein.
DR Bgee; ENSG00000196092; Expressed in buccal mucosa cell and 116 other tissues.
DR ExpressionAtlas; Q02548; baseline and differential.
DR Genevisible; Q02548; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030183; P:B cell differentiation; TAS:ProtInc.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl.
DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR CDD; cd00131; PAX; 1.
DR DisProt; DP00969; -.
DR Gene3D; 1.10.10.10; -; 2.
DR IDEAL; IID00067; -.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR043182; PAIRED_DNA-bd_dom.
DR InterPro; IPR001523; Paired_dom.
DR InterPro; IPR022130; Pax2_C.
DR InterPro; IPR043565; PAX_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR45636; PTHR45636; 1.
DR Pfam; PF00292; PAX; 1.
DR Pfam; PF12403; Pax2_C; 1.
DR PRINTS; PR00027; PAIREDBOX.
DR SMART; SM00351; PAX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00034; PAIRED_1; 1.
DR PROSITE; PS51057; PAIRED_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement;
KW Developmental protein; Differentiation; Disease variant; DNA-binding;
KW Glycoprotein; Neurogenesis; Nucleus; Paired box; Proto-oncogene;
KW Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..391
FT /note="Paired box protein Pax-5"
FT /id="PRO_0000050183"
FT DNA_BIND 16..142
FT /note="Paired"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 19..75
FT /note="PAI subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 94..142
FT /note="RED subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT REGION 182..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 158..159
FT /note="Breakpoint for translocation to form PAX5-ETV6"
FT SITE 260..261
FT /note="Breakpoint for translocation to form PAX5-FOXP1"
FT SITE 303..304
FT /note="Breakpoint for translocation to form PAX5-ZNF521"
FT VAR_SEQ 71..136
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:19725825"
FT /id="VSP_047827"
FT VAR_SEQ 159..201
FT /note="Missing (in isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:19725825"
FT /id="VSP_047828"
FT VAR_SEQ 261..391
FT /note="TTEYSAMASLAGGLDDMKANLASPTPADIGSSVPGPQSYPIVTGRDLASTTL
FT PGYPPHVPPAGQGSYSAPTLTGMVPGSEFSGSPYSHPQYSSYNDSWRFPNPGLLGSPYY
FT YSAAARGAAPPAAATAYDRH -> AVTWRARPSPGTLHTSPPLDRAATQHRR (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15385562"
FT /id="VSP_044115"
FT VAR_SEQ 261..315
FT /note="TTEYSAMASLAGGLDDMKANLASPTPADIGSSVPGPQSYPIVTGRDLASTTL
FT PGY -> APPIIIALPPEE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15385562"
FT /id="VSP_044116"
FT VAR_SEQ 261..307
FT /note="TTEYSAMASLAGGLDDMKANLASPTPADIGSSVPGPQSYPIVTGRDL -> W
FT CPVLMRQYLVQPQAVLFQAVTWRARPSPGTLHTSPPLDRAATQHRR (in isoform
FT 11)"
FT /evidence="ECO:0000303|PubMed:19725825"
FT /id="VSP_047829"
FT VAR_SEQ 261..282
FT /note="TTEYSAMASLAGGLDDMKANLA -> GVSFPGVPTATLSIPRTTTPGG (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15385562"
FT /id="VSP_044117"
FT VAR_SEQ 286..315
FT /note="PADIGSSVPGPQSYPIVTGRDLASTTLPGY -> RGCLAPPIIIALPPEE
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15385562"
FT /id="VSP_044118"
FT VAR_SEQ 304..366
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:19725825"
FT /id="VSP_047830"
FT VAR_SEQ 304..337
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:19725825"
FT /id="VSP_047831"
FT VAR_SEQ 305..349
FT /note="RDLASTTLPGYPPHVPPAGQGSYSAPTLTGMVPGSEFSGSPYSHP -> SEF
FT SGSPYSHP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15385562"
FT /id="VSP_044119"
FT VAR_SEQ 308..391
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:19725825"
FT /id="VSP_047832"
FT VAR_SEQ 319..391
FT /note="VPPAGQGSYSAPTLTGMVPGSEFSGSPYSHPQYSSYNDSWRFPNPGLLGSPY
FT YYSAAARGAAPPAAATAYDRH -> LQPPLPMTVTDPWSQAGTKH (in isoform 3
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15385562"
FT /id="VSP_044120"
FT VAR_SEQ 338..366
FT /note="Missing (in isoform 2 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:15385562,
FT ECO:0000303|PubMed:19725825"
FT /id="VSP_044121"
FT VARIANT 24
FT /note="G -> R (in dbSNP:rs868494257)"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070672"
FT VARIANT 26
FT /note="V -> G (in dbSNP:rs926053251)"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070673"
FT VARIANT 34
FT /note="P -> Q"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070674"
FT VARIANT 53
FT /note="D -> V"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070675"
FT VARIANT 59
FT /note="R -> G"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070676"
FT VARIANT 66
FT /note="S -> N"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070677"
FT VARIANT 75
FT /note="T -> R"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070678"
FT VARIANT 80
FT /note="P -> R"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070679"
FT VARIANT 139
FT /note="I -> T"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070680"
FT VARIANT 151
FT /note="V -> I (in dbSNP:rs115889954)"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070681"
FT VARIANT 183
FT /note="G -> S (in ALL3; confers susceptibility to ALL3;
FT reduced transcription factor activity; dbSNP:rs398123063)"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070682"
FT VARIANT 183
FT /note="G -> V"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070683"
FT VARIANT 213
FT /note="S -> L (in dbSNP:rs137870876)"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070684"
FT VARIANT 301
FT /note="I -> T (in dbSNP:rs372989600)"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070685"
FT VARIANT 322
FT /note="A -> T (in dbSNP:rs34810717)"
FT /id="VAR_034370"
FT VARIANT 338
FT /note="G -> V"
FT /evidence="ECO:0000269|PubMed:24013638"
FT /id="VAR_070686"
FT CONFLICT 99
FT /note="I -> F (in Ref. 8; AAC35286)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..143
FT /note="TKV -> PKL (in Ref. 8; AAC35286)"
FT /evidence="ECO:0000305"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1K78"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1K78"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:1K78"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1K78"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1K78"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:1K78"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1K78"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:1K78"
SQ SEQUENCE 391 AA; 42149 MW; DB37E6EACD9F993A CRC64;
MDLEKNYPTP RTSRTGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV
SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVEKIA EYKRQNPTMF AWEIRDRLLA
ERVCDNDTVP SVSSINRIIR TKVQQPPNQP VPASSHSIVS TGSVTQVSSV STDSAGSSYS
ISGILGITSP SADTNKRKRD EGIQESPVPN GHSLPGRDFL RKQMRGDLFT QQQLEVLDRV
FERQHYSDIF TTTEPIKPEQ TTEYSAMASL AGGLDDMKAN LASPTPADIG SSVPGPQSYP
IVTGRDLAST TLPGYPPHVP PAGQGSYSAP TLTGMVPGSE FSGSPYSHPQ YSSYNDSWRF
PNPGLLGSPY YYSAAARGAA PPAAATAYDR H
