PATZ1_HUMAN
ID PATZ1_HUMAN Reviewed; 687 AA.
AC Q9HBE1; Q9HBE2; Q9HBE3; Q9P1A9; Q9UDU0; Q9Y529;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=POZ-, AT hook-, and zinc finger-containing protein 1;
DE AltName: Full=BTB/POZ domain zinc finger transcription factor;
DE AltName: Full=Protein kinase A RI subunit alpha-associated protein;
DE AltName: Full=Zinc finger and BTB domain-containing protein 19;
DE AltName: Full=Zinc finger protein 278;
DE AltName: Full=Zinc finger sarcoma gene protein;
GN Name=PATZ1; Synonyms=PATZ, RIAZ, ZBTB19, ZNF278, ZSG;
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 4), SUBCELLULAR LOCATION, FUNCTION, AND
RP INTERACTION WITH RNF4.
RX PubMed=10713105; DOI=10.1074/jbc.275.11.7894;
RA Fedele M., Benvenuto G., Pero R., Majello B., Battista S., Lembo F.,
RA Vollono E., Day P.M., Santoro M., Lania L., Bruni C.B., Fusco A.,
RA Chiatiotti L.;
RT "A novel member of the BTB/POZ family, PATZ, associates with the RNF4 RING
RT finger protein and acts as a transcriptional repressor.";
RL J. Biol. Chem. 275:7894-7901(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND CHROMOSOMAL
RP TRANSLOCATION WITH EWSR1.
RX PubMed=10949935; DOI=10.1038/sj.onc.1203762;
RA Mastrangelo T., Modena P., Tornielli S., Bullrich F., Testi A.,
RA Mezzelani A., Radice P., Azzarelli A., Pilotti S., Croce C., Pierotti M.,
RA Sozzi G.;
RT "A novel zinc finger gene is fused to EWS in small round cell tumor.";
RL Oncogene 19:3799-3804(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3).
RA Chin K.-V., Yang W.-L., Kudoh K.;
RT "Novel cAMP signalling via the regulatory subunit of the cAMP-dependent
RT protein kinase.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Collins J.E., Huckle E.J.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Colon;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [10]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=25755280; DOI=10.1128/mcb.01475-14;
RA Keskin N., Deniz E., Eryilmaz J., Un M., Batur T., Ersahin T.,
RA Cetin Atalay R., Sakaguchi S., Ellmeier W., Erman B.;
RT "PATZ1 Is a DNA Damage-Responsive Transcription Factor That Inhibits p53
RT Function.";
RL Mol. Cell. Biol. 35:1741-1753(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-272, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP FUNCTION.
RX PubMed=31875552; DOI=10.1016/j.celrep.2019.11.089;
RA Andersen L., Guelich A.F., Alteneder M., Preglej T., Orola M.J., Dhele N.,
RA Stolz V., Schebesta A., Hamminger P., Hladik A., Floess S., Krausgruber T.,
RA Faux T., Andrabi S.B.A., Huehn J., Knapp S., Sparwasser T., Bock C.,
RA Laiho A., Elo L.L., Rasool O., Lahesmaa R., Sakaguchi S., Ellmeier W.;
RT "The Transcription Factor MAZR/PATZ1 Regulates the Development of FOXP3+
RT Regulatory T Cells.";
RL Cell Rep. 29:4447-4459(2019).
RN [13]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=31060775; DOI=10.1016/j.bbrc.2019.04.175;
RA Aziati I.D., Yoshida T., Hamano A., Maeda K., Takeuchi H., Yamaoka S.;
RT "PATZ1 is required for efficient HIV-1 infection.";
RL Biochem. Biophys. Res. Commun. 514:538-544(2019).
RN [14]
RP STRUCTURE BY NMR OF 359-437.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of zinc finger domains in zinc finger protein 278.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Transcriptional regulator that plays a role in many
CC biological processes such as embryogenesis, senescence, T-cell
CC development or neurogenesis (PubMed:10713105, PubMed:25755280,
CC PubMed:31875552). Interacts with the TP53 protein to control genes that
CC are important in proliferation and in the DNA-damage response.
CC Mechanistically, the interaction inhibits the DNA binding and
CC transcriptional activity of TP53/p53 (PubMed:25755280). Part of the
CC transcriptional network modulating regulatory T-cell development and
CC controls the generation of the regulatory T-cell pool under homeostatic
CC conditions (PubMed:31875552). {ECO:0000269|PubMed:10713105,
CC ECO:0000269|PubMed:25755280, ECO:0000269|PubMed:31875552}.
CC -!- FUNCTION: (Microbial infection) Plays a positive role in viral cDNA
CC synthesis. {ECO:0000269|PubMed:31060775}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with RNF4
CC (PubMed:10713105). Interacts (via C-terminus) with TP53; this
CC interaction inhibits TP53 ability to activate transcription
CC (PubMed:25755280). {ECO:0000250|UniProtKB:Q5NBY9,
CC ECO:0000269|PubMed:10713105, ECO:0000269|PubMed:25755280}.
CC -!- INTERACTION:
CC Q9HBE1-4; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-11022007, EBI-12318443;
CC Q9HBE1-4; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-11022007, EBI-357530;
CC Q9HBE1-4; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-11022007, EBI-12102070;
CC Q9HBE1-4; P54252: ATXN3; NbExp=3; IntAct=EBI-11022007, EBI-946046;
CC Q9HBE1-4; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-11022007, EBI-11983447;
CC Q9HBE1-4; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-11022007, EBI-953896;
CC Q9HBE1-4; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-11022007, EBI-718615;
CC Q9HBE1-4; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-11022007, EBI-11976299;
CC Q9HBE1-4; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-11022007, EBI-744556;
CC Q9HBE1-4; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11022007, EBI-742887;
CC Q9HBE1-4; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-11022007, EBI-11523759;
CC Q9HBE1-4; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11022007, EBI-3867333;
CC Q9HBE1-4; Q15038: DAZAP2; NbExp=3; IntAct=EBI-11022007, EBI-724310;
CC Q9HBE1-4; G5E9A7: DMWD; NbExp=3; IntAct=EBI-11022007, EBI-10976677;
CC Q9HBE1-4; Q92997: DVL3; NbExp=3; IntAct=EBI-11022007, EBI-739789;
CC Q9HBE1-4; O00167-2: EYA2; NbExp=3; IntAct=EBI-11022007, EBI-12807776;
CC Q9HBE1-4; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-11022007, EBI-11978259;
CC Q9HBE1-4; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-11022007, EBI-12193763;
CC Q9HBE1-4; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-11022007, EBI-5916454;
CC Q9HBE1-4; O95872: GPANK1; NbExp=3; IntAct=EBI-11022007, EBI-751540;
CC Q9HBE1-4; P52597: HNRNPF; NbExp=3; IntAct=EBI-11022007, EBI-352986;
CC Q9HBE1-4; P31943: HNRNPH1; NbExp=6; IntAct=EBI-11022007, EBI-351590;
CC Q9HBE1-4; Q16082: HSPB2; NbExp=3; IntAct=EBI-11022007, EBI-739395;
CC Q9HBE1-4; O43464: HTRA2; NbExp=3; IntAct=EBI-11022007, EBI-517086;
CC Q9HBE1-4; P42858: HTT; NbExp=3; IntAct=EBI-11022007, EBI-466029;
CC Q9HBE1-4; Q8NA54: IQUB; NbExp=3; IntAct=EBI-11022007, EBI-10220600;
CC Q9HBE1-4; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-11022007, EBI-1055254;
CC Q9HBE1-4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-11022007, EBI-10975473;
CC Q9HBE1-4; Q13351: KLF1; NbExp=3; IntAct=EBI-11022007, EBI-8284732;
CC Q9HBE1-4; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-11022007, EBI-9478422;
CC Q9HBE1-4; Q14525: KRT33B; NbExp=3; IntAct=EBI-11022007, EBI-1049638;
CC Q9HBE1-4; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-11022007, EBI-10176379;
CC Q9HBE1-4; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-11022007, EBI-11953846;
CC Q9HBE1-4; Q3LI76: KRTAP15-1; NbExp=5; IntAct=EBI-11022007, EBI-11992140;
CC Q9HBE1-4; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-11022007, EBI-12811111;
CC Q9HBE1-4; Q3LI72: KRTAP19-5; NbExp=5; IntAct=EBI-11022007, EBI-1048945;
CC Q9HBE1-4; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-11022007, EBI-12805508;
CC Q9HBE1-4; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-11022007, EBI-10241353;
CC Q9HBE1-4; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-11022007, EBI-9996449;
CC Q9HBE1-4; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-11022007, EBI-3957694;
CC Q9HBE1-4; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-11022007, EBI-12111050;
CC Q9HBE1-4; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11022007, EBI-11962084;
CC Q9HBE1-4; P02545: LMNA; NbExp=3; IntAct=EBI-11022007, EBI-351935;
CC Q9HBE1-4; P25791-3: LMO2; NbExp=3; IntAct=EBI-11022007, EBI-11959475;
CC Q9HBE1-4; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-11022007, EBI-2341787;
CC Q9HBE1-4; Q8IV03: LURAP1L; NbExp=3; IntAct=EBI-11022007, EBI-12898559;
CC Q9HBE1-4; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-11022007, EBI-741037;
CC Q9HBE1-4; Q99750: MDFI; NbExp=3; IntAct=EBI-11022007, EBI-724076;
CC Q9HBE1-4; P35548: MSX2; NbExp=3; IntAct=EBI-11022007, EBI-6447480;
CC Q9HBE1-4; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-11022007, EBI-10271199;
CC Q9HBE1-4; P0CG21: NHLRC4; NbExp=3; IntAct=EBI-11022007, EBI-12868744;
CC Q9HBE1-4; O43482: OIP5; NbExp=3; IntAct=EBI-11022007, EBI-536879;
CC Q9HBE1-4; Q99471: PFDN5; NbExp=3; IntAct=EBI-11022007, EBI-357275;
CC Q9HBE1-4; O43189: PHF1; NbExp=3; IntAct=EBI-11022007, EBI-530034;
CC Q9HBE1-4; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-11022007, EBI-10293968;
CC Q9HBE1-4; O75864: PPP1R37; NbExp=3; IntAct=EBI-11022007, EBI-5235692;
CC Q9HBE1-4; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-11022007, EBI-3957793;
CC Q9HBE1-4; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-11022007, EBI-11320284;
CC Q9HBE1-4; O60260-5: PRKN; NbExp=3; IntAct=EBI-11022007, EBI-21251460;
CC Q9HBE1-4; P41219: PRPH; NbExp=3; IntAct=EBI-11022007, EBI-752074;
CC Q9HBE1-4; P60891: PRPS1; NbExp=3; IntAct=EBI-11022007, EBI-749195;
CC Q9HBE1-4; P86480: PRR20D; NbExp=3; IntAct=EBI-11022007, EBI-12754095;
CC Q9HBE1-4; P98175: RBM10; NbExp=3; IntAct=EBI-11022007, EBI-721525;
CC Q9HBE1-4; Q93062-3: RBPMS; NbExp=6; IntAct=EBI-11022007, EBI-740343;
CC Q9HBE1-4; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-11022007, EBI-11987469;
CC Q9HBE1-4; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-11022007, EBI-746118;
CC Q9HBE1-4; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-11022007, EBI-10226430;
CC Q9HBE1-4; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-11022007, EBI-10269374;
CC Q9HBE1-4; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-11022007, EBI-12275818;
CC Q9HBE1-4; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-11022007, EBI-8463848;
CC Q9HBE1-4; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-11022007, EBI-11959123;
CC Q9HBE1-4; Q13148: TARDBP; NbExp=3; IntAct=EBI-11022007, EBI-372899;
CC Q9HBE1-4; Q08117-2: TLE5; NbExp=5; IntAct=EBI-11022007, EBI-11741437;
CC Q9HBE1-4; Q63HR2: TNS2; NbExp=3; IntAct=EBI-11022007, EBI-949753;
CC Q9HBE1-4; Q13077: TRAF1; NbExp=3; IntAct=EBI-11022007, EBI-359224;
CC Q9HBE1-4; Q12933: TRAF2; NbExp=3; IntAct=EBI-11022007, EBI-355744;
CC Q9HBE1-4; Q15654: TRIP6; NbExp=3; IntAct=EBI-11022007, EBI-742327;
CC Q9HBE1-4; Q86WV8: TSC1; NbExp=3; IntAct=EBI-11022007, EBI-12806590;
CC Q9HBE1-4; O76024: WFS1; NbExp=3; IntAct=EBI-11022007, EBI-720609;
CC Q9HBE1-4; Q9NZC7-5: WWOX; NbExp=5; IntAct=EBI-11022007, EBI-12040603;
CC Q9HBE1-4; O00308: WWP2; NbExp=3; IntAct=EBI-11022007, EBI-743923;
CC Q9HBE1-4; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-11022007, EBI-10188476;
CC Q9HBE1-4; Q15915: ZIC1; NbExp=3; IntAct=EBI-11022007, EBI-11963196;
CC Q9HBE1-4; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-11022007, EBI-11962760;
CC Q9HBE1-4; G4XUV3; NbExp=3; IntAct=EBI-11022007, EBI-10177989;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10713105}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=C;
CC IsoId=Q9HBE1-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9HBE1-2; Sequence=VSP_008799, VSP_008800;
CC Name=3; Synonyms=A;
CC IsoId=Q9HBE1-3; Sequence=VSP_008801;
CC Name=4; Synonyms=Short;
CC IsoId=Q9HBE1-4; Sequence=VSP_008802, VSP_008800;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Note=A chromosomal aberration involving PATZ1 is associated
CC with small round cell sarcoma. Translocation t(1;22)(p36.1;q12) with
CC EWSR1. {ECO:0000269|PubMed:10949935}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB51404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF119256; AAF32518.1; -; mRNA.
DR EMBL; AF254082; AAG09031.1; -; mRNA.
DR EMBL; AF254083; AAG09032.1; -; mRNA.
DR EMBL; AF254084; AAG09033.1; -; mRNA.
DR EMBL; AF254085; AAG09034.1; -; mRNA.
DR EMBL; AY028384; AAK19024.1; -; mRNA.
DR EMBL; AL096880; CAB51404.1; ALT_INIT; mRNA.
DR EMBL; CR456613; CAG30499.1; -; mRNA.
DR EMBL; AC005003; AAF01349.1; -; Genomic_DNA.
DR EMBL; BC021091; AAH21091.1; -; mRNA.
DR CCDS; CCDS13894.1; -. [Q9HBE1-1]
DR CCDS; CCDS13895.1; -. [Q9HBE1-3]
DR CCDS; CCDS13896.1; -. [Q9HBE1-4]
DR CCDS; CCDS46691.1; -. [Q9HBE1-2]
DR RefSeq; NP_055138.2; NM_014323.2. [Q9HBE1-1]
DR RefSeq; NP_114439.1; NM_032050.1. [Q9HBE1-3]
DR RefSeq; NP_114440.1; NM_032051.1. [Q9HBE1-4]
DR RefSeq; NP_114441.1; NM_032052.1. [Q9HBE1-2]
DR PDB; 2EPP; NMR; -; A=286-338.
DR PDB; 2EPQ; NMR; -; A=380-411.
DR PDB; 2EPR; NMR; -; A=350-384.
DR PDB; 2EPS; NMR; -; A=408-445.
DR PDB; 2YT9; NMR; -; A=355-436.
DR PDBsum; 2EPP; -.
DR PDBsum; 2EPQ; -.
DR PDBsum; 2EPR; -.
DR PDBsum; 2EPS; -.
DR PDBsum; 2YT9; -.
DR AlphaFoldDB; Q9HBE1; -.
DR BMRB; Q9HBE1; -.
DR SMR; Q9HBE1; -.
DR BioGRID; 117133; 167.
DR IntAct; Q9HBE1; 107.
DR MINT; Q9HBE1; -.
DR STRING; 9606.ENSP00000266269; -.
DR GlyGen; Q9HBE1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HBE1; -.
DR PhosphoSitePlus; Q9HBE1; -.
DR BioMuta; PATZ1; -.
DR DMDM; 38258840; -.
DR EPD; Q9HBE1; -.
DR jPOST; Q9HBE1; -.
DR MassIVE; Q9HBE1; -.
DR MaxQB; Q9HBE1; -.
DR PaxDb; Q9HBE1; -.
DR PeptideAtlas; Q9HBE1; -.
DR PRIDE; Q9HBE1; -.
DR ProteomicsDB; 81529; -. [Q9HBE1-1]
DR ProteomicsDB; 81530; -. [Q9HBE1-2]
DR ProteomicsDB; 81531; -. [Q9HBE1-3]
DR ProteomicsDB; 81532; -. [Q9HBE1-4]
DR Antibodypedia; 25019; 175 antibodies from 24 providers.
DR DNASU; 23598; -.
DR Ensembl; ENST00000215919.3; ENSP00000215919.3; ENSG00000100105.18. [Q9HBE1-4]
DR Ensembl; ENST00000266269.10; ENSP00000266269.5; ENSG00000100105.18. [Q9HBE1-1]
DR Ensembl; ENST00000351933.8; ENSP00000337520.4; ENSG00000100105.18. [Q9HBE1-3]
DR Ensembl; ENST00000405309.7; ENSP00000384173.3; ENSG00000100105.18. [Q9HBE1-2]
DR GeneID; 23598; -.
DR KEGG; hsa:23598; -.
DR MANE-Select; ENST00000266269.10; ENSP00000266269.5; NM_014323.3; NP_055138.2.
DR UCSC; uc003akp.4; human. [Q9HBE1-1]
DR CTD; 23598; -.
DR DisGeNET; 23598; -.
DR GeneCards; PATZ1; -.
DR HGNC; HGNC:13071; PATZ1.
DR HPA; ENSG00000100105; Low tissue specificity.
DR MIM; 605165; gene.
DR neXtProt; NX_Q9HBE1; -.
DR OpenTargets; ENSG00000100105; -.
DR PharmGKB; PA162398806; -.
DR VEuPathDB; HostDB:ENSG00000100105; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159296; -.
DR HOGENOM; CLU_030477_1_0_1; -.
DR InParanoid; Q9HBE1; -.
DR OMA; KFACGEC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9HBE1; -.
DR TreeFam; TF331686; -.
DR PathwayCommons; Q9HBE1; -.
DR SignaLink; Q9HBE1; -.
DR SIGNOR; Q9HBE1; -.
DR BioGRID-ORCS; 23598; 24 hits in 1138 CRISPR screens.
DR ChiTaRS; PATZ1; human.
DR EvolutionaryTrace; Q9HBE1; -.
DR GeneWiki; PATZ1; -.
DR GenomeRNAi; 23598; -.
DR Pharos; Q9HBE1; Tbio.
DR PRO; PR:Q9HBE1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9HBE1; protein.
DR Bgee; ENSG00000100105; Expressed in ventricular zone and 188 other tissues.
DR ExpressionAtlas; Q9HBE1; baseline and differential.
DR Genevisible; Q9HBE1; HS.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00354; HMGI_Y; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..687
FT /note="POZ-, AT hook-, and zinc finger-containing protein
FT 1"
FT /id="PRO_0000047504"
FT DOMAIN 41..130
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DNA_BIND 264..276
FT /note="A.T hook"
FT ZN_FING 292..314
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 413..436
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..464
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..518
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 605..628
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 250..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 446..537
FT /note="TCNASFATRDRLRSHLACHEDKVPCQVCGKYLRAAYMADHLKKHSEGPSNFC
FT SICNRGFSSASYLKVHVKTHHGVPLPQVSRHQEPILNGGA -> VWVGSSSGLPPLEPL
FT PSDLPSWDFAQPALWRSSHSVPDTAFSLSLKKSFPALENLGPAHSSNTLFCPAPPGYLR
FT QGWTTPEGSRAFTQWPVG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10713105,
FT ECO:0000303|PubMed:10949935, ECO:0000303|PubMed:15489334"
FT /id="VSP_008802"
FT VAR_SEQ 503..548
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10949935,
FT ECO:0000303|PubMed:15461802, ECO:0000303|Ref.4"
FT /id="VSP_008801"
FT VAR_SEQ 504..537
FT /note="FSSASYLKVHVKTHHGVPLPQVSRHQEPILNGGA -> LQAPGAHPEWGSSV
FT PLRQDLWQQRRPEMLTSGSD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10949935"
FT /id="VSP_008799"
FT VAR_SEQ 538..687
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10713105,
FT ECO:0000303|PubMed:10949935, ECO:0000303|PubMed:15489334"
FT /id="VSP_008800"
FT VARIANT 685
FT /note="E -> D (in dbSNP:rs2240424)"
FT /id="VAR_052724"
FT CONFLICT 63
FT /note="S -> N (in Ref. 1; AAF32518)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="P -> L (in Ref. 1; AAF32518)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="R -> K (in Ref. 1; AAF32518)"
FT /evidence="ECO:0000305"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:2EPP"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:2EPP"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:2EPP"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:2EPR"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:2EPR"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:2EPR"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:2EPR"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:2EPR"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:2EPQ"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:2EPQ"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2YT9"
FT HELIX 395..405
FT /evidence="ECO:0007829|PDB:2EPQ"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:2YT9"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:2EPS"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:2EPS"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:2EPS"
SQ SEQUENCE 687 AA; 74060 MW; 0F1C59A78C6D110A CRC64;
MERVNDASCG PSGCYTYQVS RHSTEMLHNL NQQRKNGGRF CDVLLRVGDE SFPAHRAVLA
ACSEYFESVF SAQLGDGGAA DGGPADVGGA TAAPGGGAGG SRELEMHTIS SKVFGDILDF
AYTSRIVVRL ESFPELMTAA KFLLMRSVIE ICQEVIKQSN VQILVPPARA DIMLFRPPGT
SDLGFPLDMT NGAALAANSN GIAGSMQPEE EAARAAGAAI AGQASLPVLP GVDRLPMVAG
PLSPQLLTSP FPSVASSAPP LTGKRGRGRP RKANLLDSMF GSPGGLREAG ILPCGLCGKV
FTDANRLRQH EAQHGVTSLQ LGYIDLPPPR LGENGLPISE DPDGPRKRSR TRKQVACEIC
GKIFRDVYHL NRHKLSHSGE KPYSCPVCGL RFKRKDRMSY HVRSHDGSVG KPYICQSCGK
GFSRPDHLNG HIKQVHTSER PHKCQTCNAS FATRDRLRSH LACHEDKVPC QVCGKYLRAA
YMADHLKKHS EGPSNFCSIC NRGFSSASYL KVHVKTHHGV PLPQVSRHQE PILNGGAAFH
CARTYGNKEG QKCSHQDPIE SSDSYGDLSD ASDLKTPEKQ SANGSFSCDM AVPKNKMESD
GEKKYPCPEC GSFFRSKSYL NKHIQKVHVR ALGGPLGDLG PALGSPFSPQ QNMSLLESFG
FQIVQSAFAS SLVDPEVDQQ PMGPEGK
