ID   Q5T4E8_HUMAN            Unreviewed;       789 AA.
AC   Q5T4E8;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=PR domain zinc finger protein 1 {ECO:0000256|PIRNR:PIRNR013212};
DE            EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR013212};
GN   Name=PRDM1 {ECO:0000313|EMBL:ABK41898.1};
GN   ORFNames=hCG_33515 {ECO:0000313|EMBL:EAW48420.1};
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 {ECO:0000313|EMBL:ABK41898.1};
RN   [1] {ECO:0000313|EMBL:EAW48420.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW48420.1}
RP   NUCLEOTIDE SEQUENCE.
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   [3] {ECO:0000313|EMBL:ABK41898.1}
RP   NUCLEOTIDE SEQUENCE.
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.
CC   -!- FUNCTION: Transcription factor that mediates a transcriptional program
CC       in various innate and adaptive immune tissue-resident lymphocyte T cell
CC       types such as tissue-resident memory T (Trm), natural killer (trNK) and
CC       natural killer T (NKT) cells and negatively regulates gene expression
CC       of proteins that promote the egress of tissue-resident T-cell
CC       populations from non-lymphoid organs. Plays a role in the development,
CC       retention and long-term establishment of adaptive and innate tissue-
CC       resident lymphocyte T cell types in non-lymphoid organs, such as the
CC       skin and gut, but also in other nonbarrier tissues like liver and
CC       kidney, and therefore may provide immediate immunological protection
CC       against reactivating infections or viral reinfection. Binds
CC       specifically to the PRDI element in the promoter of the beta-interferon
CC       gene. Drives the maturation of B-lymphocytes into Ig secreting cells.
CC       Associates with the transcriptional repressor ZNF683 to chromatin at
CC       gene promoter regions. {ECO:0000256|PIRNR:PIRNR013212}.
CC   -!- SUBUNIT: Interacts with PRMT5. Interacts with FBXO10. Interacts with
CC       FBXO11. {ECO:0000256|PIRNR:PIRNR013212}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR013212}.
CC       Cytoplasm {ECO:0000256|PIRNR:PIRNR013212}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000256|PIRNR:PIRNR013212}.
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DR   EMBL; EF064715; ABK41898.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48420.1; -; Genomic_DNA.
DR   RefSeq; XP_011534365.1; XM_011536063.2.
DR   RefSeq; XP_016866676.1; XM_017011187.1.
DR   AlphaFoldDB; Q5T4E8; -.
DR   SMR; Q5T4E8; -.
DR   MaxQB; Q5T4E8; -.
DR   Antibodypedia; 19038; 731 antibodies from 39 providers.
DR   DNASU; 639; -.
DR   GeneID; 639; -.
DR   UCSC; uc063qim.1; human.
DR   CTD; 639; -.
DR   VEuPathDB; HostDB:ENSG00000057657; -.
DR   HOGENOM; CLU_007033_2_1_1; -.
DR   OrthoDB; 2880949at2759; -.
DR   BioGRID-ORCS; 639; 35 hits in 1191 CRISPR screens.
DR   ChiTaRS; PRDM1; human.
DR   GenomeRNAi; 639; -.
DR   ExpressionAtlas; Q5T4E8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045165; P:cell fate commitment; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd19187; PR-SET_PRDM1; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR016608; PRDM1.
DR   InterPro; IPR044413; PRDM1_PR-SET.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR16515:SF26; PR DOMAIN ZINC FINGER PROTEIN 1; 1.
DR   Pfam; PF21549; PRDM2_PR; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   PIRSF; PIRSF013212; PRDM1; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          48..165
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          539..566
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          567..594
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          595..622
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          623..650
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          288..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  87991 MW;  6A1FEBEAD309BC7D CRC64;
     MKMDMEDADM TLWTEAEFEE KCTYIVNDHP WDSGADGGTS VQAEASLPRN LLFKYATNSE
     EVIGVMSKEY IPKGTRFGPL IGEIYTNDTV PKNANRKYFW RIYSRGELHH FIDGFNEEKS
     NWMRYVNPAH SPREQNLAAC QNGMNIYFYT IKPIPANQEL LVWYCRDFAE RLHYPYPGEL
     TMMNLTQTQS SLKQPSTEKN ELCPKNVPKR EYSVKEILKL DSNPSKGKDL YRSNISPLTS
     EKDLDDFRRR GSPEMPFYPR VVYPIRAPLP EDFLKASLAY GIERPTYITR SPIPSSTTPS
     PSARSSPDQS LKSSSPHSSP GNTVSPVGPG SQEHRDSYAY LNASYGTEGL GSYPGYAPLP
     HLPPAFIPSY NAHYPKFLLP PYGMNCNGLS AVSSMNGINN FGLFPRLCPV YSNLLGGGSL
     PHPMLNPTSL PSSLPSDGAR RLLQPEHPRE VLVPAPHSAF SFTGAAASMK DKACSPTSGS
     PTAGTAATAE HVVQPKATSA AMAAPSSDEA MNLIKNKRNM TGYKTLPYPL KKQNGKIKYE
     CNVCAKTFGQ LSNLKVHLRV HSGERPFKCQ TCNKGFTQLA HLQKHYLVHT GEKPHECQVC
     HKRFSSTSNL KTHLRLHSGE KPYQCKVCPA KFTQFVHLKL HKRLHTRERP HKCSQCHKNY
     IHLCSLKVHL KGNCAAAPAP GLPLEDLTRI NEEIEKFDIS DNADRLEDVE DDISVISVVE
     KEILAVVRKE KEETGLKVSL QRNMGNGLLS SGCSLYESSD LPLMKLPPSN PLPLVPVKVK
     QETVEPMDP
//