PSIP1_HUMAN
ID PSIP1_HUMAN Reviewed; 530 AA.
AC O75475; D3DRI9; O00256; O95368; Q6P391; Q86YB9; Q9NZI3; Q9UER6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=PC4 and SFRS1-interacting protein;
DE AltName: Full=CLL-associated antigen KW-7;
DE AltName: Full=Dense fine speckles 70 kDa protein;
DE Short=DFS 70;
DE AltName: Full=Lens epithelium-derived growth factor;
DE AltName: Full=Transcriptional coactivator p75/p52;
GN Name=PSIP1; Synonyms=DFS70, LEDGF, PSIP2;
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] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 4-39 AND
RP 76-89, TISSUE SPECIFICITY, AND INTERACTION WITH IFRD1.
RC TISSUE=Cervix carcinoma;
RX PubMed=9822615; DOI=10.1093/emboj/17.22.6723;
RA Ge H., Si Y., Roeder R.G.;
RT "Isolation of cDNAs encoding novel transcription coactivators p52 and p75
RT reveals an alternate regulatory mechanism of transcriptional activation.";
RL EMBO J. 17:6723-6729(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lens;
RX PubMed=10623627; DOI=10.1006/bbrc.1999.1979;
RA Singh D.P., Ohguro N., Kikuchi T., Sueno T., Reddy V.N., Yuge K.,
RA Chylack L.T. Jr., Shinohara T.;
RT "Lens epithelium-derived growth factor: effects on growth and survival of
RT lens epithelial cells, keratinocytes, and fibroblasts.";
RL Biochem. Biophys. Res. Commun. 267:373-381(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=10721720; DOI=10.1016/s0378-1119(99)00506-5;
RA Singh D.P., Kimura A., Chylack L.T. Jr., Shinohara T.;
RT "Lens epithelium-derived growth factor (LEDGF/p75) and p52 are derived from
RT a single gene by alternative splicing.";
RL Gene 242:265-273(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Leukemia;
RX PubMed=12200376; DOI=10.1182/blood-2002-02-0513;
RA Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M.,
RA Barrett P., Gribben J.G.;
RT "Identification of tumor-associated antigens in chronic lymphocytic
RT leukemia by SEREX.";
RL Blood 100:2123-2131(2002).
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.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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 180-530 (ISOFORM 1).
RX PubMed=10856157; DOI=10.1067/mai.2000.107039;
RA Ochs R.L., Muro Y., Si Y., Ge H., Chan E.K.L., Tan E.M.;
RT "Autoantibodies to DFS 70 kd/transcription coactivator p75 in atopic
RT dermatitis and other conditions.";
RL J. Allergy Clin. Immunol. 105:1211-1220(2000).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15642333; DOI=10.1016/j.exer.2004.08.022;
RA Chylack L.T. Jr., Fu L., Mancini R., Martin-Rehrmann M.D., Saunders A.J.,
RA Konopka G., Tian D., Hedley-Whyte E.T., Folkerth R.D., Goldstein L.E.;
RT "Lens epithelium-derived growth factor (LEDGF/p75) expression in fetal and
RT adult human brain.";
RL Exp. Eye Res. 79:941-948(2004).
RN [10]
RP INTERACTION WITH HUMAN HIV-1 INTEGRASE (ISOFORM 1) (MICROBIAL INFECTION).
RX PubMed=15475359; DOI=10.1074/jbc.m408508200;
RA Llano M., Delgado S., Vanegas M., Poeschla E.M.;
RT "Lens epithelium-derived growth factor/p75 prevents proteasomal degradation
RT of HIV-1 integrase.";
RL J. Biol. Chem. 279:55570-55577(2004).
RN [11]
RP INTERACTION WITH HUMAN HIV-1 AND HIV-2 INTEGRASE (ISOFORM 1) (MICROBIAL
RP INFECTION).
RX PubMed=15749713; DOI=10.1074/jbc.m411681200;
RA Busschots K., Vercammen J., Emiliani S., Benarous R., Engelborghs Y.,
RA Christ F., Debyser Z.;
RT "The interaction of LEDGF/p75 with integrase is lentiviral-specific and
RT promotes DNA binding.";
RL J. Biol. Chem. 280:17841-17847(2005).
RN [12]
RP INTERACTION WITH HUMAN HIV-1 INTEGRASE (ISOFORM 1) (MICROBIAL INFECTION),
RP AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=15797927; DOI=10.1242/jcs.02299;
RA Vanegas M., Llano M., Delgado S., Thompson D., Peretz M., Poeschla E.M.;
RT "Identification of the LEDGF/p75 HIV-1 integrase-interaction domain and NLS
RT reveals NLS-independent chromatin tethering.";
RL J. Cell Sci. 118:1733-1743(2005).
RN [13]
RP INTERACTION WITH SFRS1, AND SUBCELLULAR LOCATION.
RX PubMed=9885563; DOI=10.1016/s1097-2765(00)80290-7;
RA Ge H., Si Y., Wolffe A.P.;
RT "A novel transcriptional coactivator, p52, functionally interacts with the
RT essential splicing factor ASF/SF2.";
RL Mol. Cell 2:751-759(1998).
RN [14]
RP CHROMOSOMAL TRANSLOCATION WITH NUP98.
RX PubMed=15725483; DOI=10.1016/j.leukres.2004.09.002;
RA Morerio C., Acquila M., Rosanda C., Rapella A., Tassano E., Micalizzi C.,
RA Panarello C.;
RT "t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute myeloid
RT leukemia.";
RL Leuk. Res. 29:467-470(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-437, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-141; SER-273;
RP SER-275; SER-434; SER-443; SER-522 AND THR-527, AND IDENTIFICATION BY MASS
RP 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP INTERACTION WITH POGZ; HIV-1 INTEGRASE (MICROBIAL INFECTION) AND CDCA7L,
RP AND MUTAGENESIS OF LYS-360; ILE-365; ASP-366; VAL-370; PHE-406 AND VAL-408.
RX PubMed=19244240; DOI=10.1074/jbc.m807781200;
RA Bartholomeeusen K., Christ F., Hendrix J., Rain J.C., Emiliani S.,
RA Benarous R., Debyser Z., Gijsbers R., De Rijck J.;
RT "Lens epithelium-derived growth factor/p75 interacts with the transposase-
RT derived DDE domain of PogZ.";
RL J. Biol. Chem. 284:11467-11477(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-167; SER-177;
RP SER-273 AND SER-275, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-122; THR-141;
RP SER-206; SER-273; SER-275; SER-434 AND THR-527, AND IDENTIFICATION BY MASS
RP 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 [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-141; SER-177;
RP SER-206; SER-275 AND THR-527, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-122; SER-129;
RP SER-273; SER-275; SER-434 AND SER-514, AND IDENTIFICATION BY MASS
RP 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-122; SER-129;
RP SER-271; THR-272; SER-273 AND SER-275, AND IDENTIFICATION BY MASS
RP 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 [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75, AND IDENTIFICATION BY MASS
RP 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 [29]
RP STRUCTURE BY NMR OF 347-471, SUBUNIT, MUTAGENESIS OF ILE-365; ASP-366;
RP PHE-406 AND VAL-408, DOMAIN IBD, AND INTERACTION WITH HIV-1 INTEGRASE
RP (MICROBIAL INFECTION).
RX PubMed=15895093; DOI=10.1038/nsmb937;
RA Cherepanov P., Sun Z.-Y., Rahman S., Maertens G., Wagner G., Engelman A.;
RT "Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75.";
RL Nat. Struct. Mol. Biol. 12:526-532(2005).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 347-442 IN COMPLEX WITH HUMAN
RP HIV-1 INTEGRASE.
RX PubMed=16260736; DOI=10.1073/pnas.0506924102;
RA Cherepanov P., Ambrosio A.L.B., Rahman S., Ellenberger T., Engelman A.;
RT "Structural basis for the recognition between HIV-1 integrase and
RT transcriptional coactivator p75.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17308-17313(2005).
RN [31] {ECO:0007744|PDB:3U88}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 347-435 IN COMPLEX WITH KMT2A AND
RP MEN1, AND INTERACTION WITH KMT2A-MENIN COMPLEX.
RX PubMed=22327296; DOI=10.1038/nature10806;
RA Huang J., Gurung B., Wan B., Matkar S., Veniaminova N.A., Wan K.,
RA Merchant J.L., Hua X., Lei M.;
RT "The same pocket in menin binds both MLL and JUND but has opposite effects
RT on transcription.";
RL Nature 482:542-546(2012).
RN [32] {ECO:0007744|PDB:2MTN}
RP STRUCTURE BY NMR OF 337-442 IN COMPLEX WITH KMT2A, INTERACTION WITH KMT2A;
RP KMT2A-MEN1 COMPLEX AND FUSION PROTEIN KMT2A-MLLT3, AND INTERACTION WITH
RP HIV-1 INTEGRASE (MICROBIAL INFECTION).
RX PubMed=25305204; DOI=10.1182/blood-2014-01-550079;
RA Murai M.J., Pollock J., He S., Miao H., Purohit T., Yokom A., Hess J.L.,
RA Muntean A.G., Grembecka J., Cierpicki T.;
RT "The same site on the integrase-binding domain of lens epithelium-derived
RT growth factor is a therapeutic target for MLL leukemia and HIV.";
RL Blood 124:3730-3737(2014).
RN [33] {ECO:0007744|PDB:2MSR}
RP STRUCTURE BY NMR OF 344-426 IN COMPLEX WITH KMT2A, INTERACTION WITH KMT2A;
RP CDCA7L AND POGZ, INTERACTION WITH HIV-1 INTEGRASE (MICROBIAL INFECTION),
RP AND MUTAGENESIS OF ASP-366; LEU-368; ARG-404; ARG-405 AND LYS-407.
RX PubMed=25082813; DOI=10.1158/0008-5472.can-13-3602;
RA Cermakova K., Tesina P., Demeulemeester J., El Ashkar S., Mereau H.,
RA Schwaller J., Rezacova P., Veverka V., De Rijck J.;
RT "Validation and structural characterization of the LEDGF/p75-MLL interface
RT as a new target for the treatment of MLL-dependent leukemia.";
RL Cancer Res. 74:5139-5151(2014).
RN [34] {ECO:0007744|PDB:5YI9, ECO:0007744|PDB:6EMO, ECO:0007744|PDB:6EMP, ECO:0007744|PDB:6EMQ, ECO:0007744|PDB:6EMR}
RP STRUCTURE BY NMR OF 345-443 IN COMPLEX WITH KMT2A; CDCA7L; POGZ AND IWS1,
RP AND INTERACTION WITH KMT2A; CDCA7L; POGZ; IWS1; MED1 AND DBF4.
RX PubMed=29997176; DOI=10.1073/pnas.1803909115;
RA Sharma S., Cermakova K., De Rijck J., Demeulemeester J., Fabry M.,
RA El Ashkar S., Van Belle S., Lepsik M., Tesina P., Duchoslav V., Novak P.,
RA Hubalek M., Srb P., Christ F., Rezacova P., Hodges H.C., Debyser Z.,
RA Veverka V.;
RT "Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-
RT dependent phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E7053-E7062(2018).
CC -!- FUNCTION: Transcriptional coactivator involved in neuroepithelial stem
CC cell differentiation and neurogenesis. Involved in particular in lens
CC epithelial cell gene regulation and stress responses. May play an
CC important role in lens epithelial to fiber cell terminal
CC differentiation. May play a protective role during stress-induced
CC apoptosis. Isoform 2 is a more general and stronger transcriptional
CC coactivator. Isoform 2 may also act as an adapter to coordinate pre-
CC mRNA splicing. Cellular cofactor for lentiviral integration.
CC {ECO:0000269|PubMed:15642333}.
CC -!- SUBUNIT: Monomer (PubMed:15895093). Interacts with IFRD1/PC4
CC (PubMed:9822615). Isoform 2 interacts with SFRS1 (PubMed:9885563).
CC Isoform 1 interacts (via IBD domain) with POGZ (via IBM motif) and
CC CDCA7L (via IBM motifs) (PubMed:19244240, PubMed:25082813,
CC PubMed:29997176). Interacts (via IBD domain) with KMT2A (via IBM
CC motifs) with a moderate affinity whereas interacts with the KMT2A-MEN1
CC complex with a greater affinity; MEN1 enhances interaction of KMT2A
CC with PSIP1 (PubMed:22327296, PubMed:25305204, PubMed:25082813,
CC PubMed:29997176). Interacts with fusion protein KMT2A-MLLT3
CC (PubMed:25305204). Interacts (via IBD domain) with IWS1 (via IBM
CC motif), MED1 (via IBM motif) and DBF4 (via IBM motifs)
CC (PubMed:29997176). {ECO:0000269|PubMed:15895093,
CC ECO:0000269|PubMed:16260736, ECO:0000269|PubMed:19244240,
CC ECO:0000269|PubMed:22327296, ECO:0000269|PubMed:25082813,
CC ECO:0000269|PubMed:25305204, ECO:0000269|PubMed:29997176,
CC ECO:0000269|PubMed:9822615, ECO:0000269|PubMed:9885563}.
CC -!- SUBUNIT: [Isoform 1]: (Microbial infection) Interacts (via IBD domain)
CC with human HIV-1 integrase protein (HIV-1 IN), determining its nuclear
CC localization, its tight association with chromatin and its protection
CC from the proteasome. {ECO:0000269|PubMed:15475359,
CC ECO:0000269|PubMed:15749713, ECO:0000269|PubMed:15797927,
CC ECO:0000269|PubMed:15895093, ECO:0000269|PubMed:19244240,
CC ECO:0000269|PubMed:25082813, ECO:0000269|PubMed:25305204}.
CC -!- SUBUNIT: [Isoform 1]: (Microbial infection) Interacts with HIV-2 IN.
CC {ECO:0000269|PubMed:15749713}.
CC -!- INTERACTION:
CC O75475; Q99708: RBBP8; NbExp=4; IntAct=EBI-1801773, EBI-745715;
CC O75475; P63165: SUMO1; NbExp=4; IntAct=EBI-1801773, EBI-80140;
CC O75475; P04585: gag-pol; Xeno; NbExp=21; IntAct=EBI-1801773, EBI-3989067;
CC O75475-1; PRO_0000042447 [P04585]: gag-pol; Xeno; NbExp=2; IntAct=EBI-5279836, EBI-9872653;
CC O75475-1; PRO_0000042402 [P12497]: gag-pol; Xeno; NbExp=3; IntAct=EBI-5279836, EBI-10131955;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15642333,
CC ECO:0000269|PubMed:9885563}. Note=Remains chromatin-associated
CC throughout the cell cycle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=p75, PSIP1;
CC IsoId=O75475-1; Sequence=Displayed;
CC Name=2; Synonyms=p52, PSIP2;
CC IsoId=O75475-2; Sequence=VSP_014297, VSP_014298;
CC Name=3;
CC IsoId=O75475-3; Sequence=VSP_044435;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in the
CC thymus. Expressed in fetal and adult brain. Expressed in neurons, but
CC not astrocytes. Markedly elevated in fetal as compared to adult brain.
CC In the adult brain, expressed in the subventricular zone (SVZ), in
CC hippocampus, and undetectable elsewhere. In the fetal brain, expressed
CC in the germinal neuroepithelium and cortical plate regions.
CC {ECO:0000269|PubMed:15642333, ECO:0000269|PubMed:9822615}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q99JF8}.
CC -!- DISEASE: Note=A chromosomal aberration involving PSIP1 is associated
CC with pediatric acute myeloid leukemia (AML) with intermediate
CC characteristics between M2-M3 French-American-British (FAB) subtypes.
CC Translocation t(9;11)(p22;p15) with NUP98. The chimeric transcript is
CC an in-frame fusion of NUP98 exon 8 to PSIP1 exon 4.
CC {ECO:0000269|PubMed:15725483}.
CC -!- MISCELLANEOUS: [Isoform 1]: Less active than isoform 2 as
CC transcriptional coactivator, but more abundant in cells.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PSIP1ID405ch9q22.html";
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DR EMBL; AF098483; AAC97946.1; -; mRNA.
DR EMBL; AF098482; AAC97945.1; -; mRNA.
DR EMBL; AF063020; AAC25167.1; -; mRNA.
DR EMBL; AF199339; AAF25870.1; -; Genomic_DNA.
DR EMBL; AF199339; AAF25871.1; -; Genomic_DNA.
DR EMBL; AF432220; AAL99926.1; -; mRNA.
DR EMBL; AL359998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL441925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58677.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58678.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58679.1; -; Genomic_DNA.
DR EMBL; BC044568; AAH44568.2; -; mRNA.
DR EMBL; BC064135; AAH64135.1; -; mRNA.
DR EMBL; U94319; AAB52589.1; -; mRNA.
DR CCDS; CCDS6479.1; -. [O75475-1]
DR CCDS; CCDS6480.1; -. [O75475-2]
DR CCDS; CCDS83348.1; -. [O75475-3]
DR PIR; JC7168; JC7168.
DR RefSeq; NP_001121689.1; NM_001128217.2. [O75475-1]
DR RefSeq; NP_001304827.1; NM_001317898.1. [O75475-3]
DR RefSeq; NP_001304829.1; NM_001317900.1.
DR RefSeq; NP_066967.3; NM_021144.3. [O75475-2]
DR RefSeq; NP_150091.2; NM_033222.4. [O75475-1]
DR PDB; 1Z9E; NMR; -; A=347-471.
DR PDB; 2B4J; X-ray; 2.02 A; C/D=347-442.
DR PDB; 2M16; NMR; -; A=1-93.
DR PDB; 2MSR; NMR; -; B=344-426.
DR PDB; 2MTN; NMR; -; A=337-442.
DR PDB; 2N3A; NMR; -; B=348-426.
DR PDB; 3F9K; X-ray; 3.20 A; C/G/K/O/S/W/a/e/i/m/q/u=347-435.
DR PDB; 3HPG; X-ray; 3.28 A; G/H/I/J/K/L=347-435.
DR PDB; 3HPH; X-ray; 2.64 A; E/F/G/H=348-435.
DR PDB; 3U88; X-ray; 3.00 A; C/D=347-435.
DR PDB; 3ZEH; NMR; -; A=3-100.
DR PDB; 4FU6; X-ray; 2.10 A; A=1-135.
DR PDB; 5N88; X-ray; 1.70 A; D=347-425, E=347-424.
DR PDB; 5OYM; X-ray; 2.05 A; A/B/C/D/E/F/G/H=345-431.
DR PDB; 5YI9; NMR; -; A=345-442.
DR PDB; 6EMO; NMR; -; A=345-442.
DR PDB; 6EMP; NMR; -; A=345-442.
DR PDB; 6EMQ; NMR; -; A=345-443.
DR PDB; 6EMR; NMR; -; A=345-442.
DR PDB; 6S01; EM; 3.20 A; K=1-530.
DR PDB; 6TRJ; X-ray; 1.30 A; A=345-430.
DR PDB; 6TVM; NMR; -; A/B=345-467.
DR PDB; 6ZV0; NMR; -; A=345-431.
DR PDB; 7OUF; EM; 3.00 A; C/F=1-325.
DR PDB; 7OUG; EM; 3.10 A; C/F=1-325.
DR PDB; 7OUH; EM; 3.50 A; C/F=1-325.
DR PDB; 7PEL; EM; 3.34 A; C/F=1-325.
DR PDBsum; 1Z9E; -.
DR PDBsum; 2B4J; -.
DR PDBsum; 2M16; -.
DR PDBsum; 2MSR; -.
DR PDBsum; 2MTN; -.
DR PDBsum; 2N3A; -.
DR PDBsum; 3F9K; -.
DR PDBsum; 3HPG; -.
DR PDBsum; 3HPH; -.
DR PDBsum; 3U88; -.
DR PDBsum; 3ZEH; -.
DR PDBsum; 4FU6; -.
DR PDBsum; 5N88; -.
DR PDBsum; 5OYM; -.
DR PDBsum; 5YI9; -.
DR PDBsum; 6EMO; -.
DR PDBsum; 6EMP; -.
DR PDBsum; 6EMQ; -.
DR PDBsum; 6EMR; -.
DR PDBsum; 6S01; -.
DR PDBsum; 6TRJ; -.
DR PDBsum; 6TVM; -.
DR PDBsum; 6ZV0; -.
DR PDBsum; 7OUF; -.
DR PDBsum; 7OUG; -.
DR PDBsum; 7OUH; -.
DR PDBsum; 7PEL; -.
DR AlphaFoldDB; O75475; -.
DR BMRB; O75475; -.
DR SMR; O75475; -.
DR BioGRID; 116339; 146.
DR CORUM; O75475; -.
DR DIP; DIP-46656N; -.
DR IntAct; O75475; 40.
DR MINT; O75475; -.
DR STRING; 9606.ENSP00000370109; -.
DR BindingDB; O75475; -.
DR ChEMBL; CHEMBL3988590; -.
DR Allergome; 2120; Hom s DSF70.
DR GlyGen; O75475; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; O75475; -.
DR MetOSite; O75475; -.
DR PhosphoSitePlus; O75475; -.
DR SwissPalm; O75475; -.
DR BioMuta; PSIP1; -.
DR EPD; O75475; -.
DR jPOST; O75475; -.
DR MassIVE; O75475; -.
DR MaxQB; O75475; -.
DR PaxDb; O75475; -.
DR PeptideAtlas; O75475; -.
DR PRIDE; O75475; -.
DR ProteomicsDB; 50037; -. [O75475-1]
DR ProteomicsDB; 50038; -. [O75475-2]
DR TopDownProteomics; O75475-1; -. [O75475-1]
DR TopDownProteomics; O75475-2; -. [O75475-2]
DR ABCD; O75475; 2 sequenced antibodies.
DR Antibodypedia; 4436; 239 antibodies from 32 providers.
DR DNASU; 11168; -.
DR Ensembl; ENST00000380715.5; ENSP00000370091.1; ENSG00000164985.15. [O75475-3]
DR Ensembl; ENST00000380716.8; ENSP00000370092.4; ENSG00000164985.15. [O75475-2]
DR Ensembl; ENST00000380733.9; ENSP00000370109.4; ENSG00000164985.15. [O75475-1]
DR Ensembl; ENST00000380738.8; ENSP00000370114.4; ENSG00000164985.15. [O75475-1]
DR Ensembl; ENST00000397519.6; ENSP00000380653.2; ENSG00000164985.15. [O75475-2]
DR GeneID; 11168; -.
DR KEGG; hsa:11168; -.
DR MANE-Select; ENST00000380733.9; ENSP00000370109.4; NM_033222.5; NP_150091.2.
DR UCSC; uc003zlv.6; human. [O75475-1]
DR CTD; 11168; -.
DR DisGeNET; 11168; -.
DR GeneCards; PSIP1; -.
DR HGNC; HGNC:9527; PSIP1.
DR HPA; ENSG00000164985; Low tissue specificity.
DR MIM; 603620; gene.
DR neXtProt; NX_O75475; -.
DR OpenTargets; ENSG00000164985; -.
DR PharmGKB; PA33872; -.
DR VEuPathDB; HostDB:ENSG00000164985; -.
DR eggNOG; KOG1904; Eukaryota.
DR GeneTree; ENSGT00940000154706; -.
DR HOGENOM; CLU_034054_1_0_1; -.
DR InParanoid; O75475; -.
DR OMA; NLRVGMN; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; O75475; -.
DR TreeFam; TF105385; -.
DR PathwayCommons; O75475; -.
DR Reactome; R-HSA-162592; Integration of provirus.
DR Reactome; R-HSA-164843; 2-LTR circle formation.
DR Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
DR Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
DR Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR SignaLink; O75475; -.
DR SIGNOR; O75475; -.
DR BioGRID-ORCS; 11168; 35 hits in 1084 CRISPR screens.
DR ChiTaRS; PSIP1; human.
DR EvolutionaryTrace; O75475; -.
DR GeneWiki; PSIP1; -.
DR GenomeRNAi; 11168; -.
DR Pharos; O75475; Tchem.
DR PRO; PR:O75475; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O75475; protein.
DR Bgee; ENSG00000164985; Expressed in secondary oocyte and 214 other tissues.
DR ExpressionAtlas; O75475; baseline and differential.
DR Genevisible; O75475; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0097100; F:supercoiled DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR CDD; cd05834; HDGF_related; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR IDEAL; IID00408; -.
DR InterPro; IPR035496; HDGF-rel_PWWP.
DR InterPro; IPR036218; HIVI-bd_sf.
DR InterPro; IPR021567; LEDGF_IBD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR Pfam; PF11467; LEDGF; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF140576; SSF140576; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement;
KW Citrullination; Coiled coil; Direct protein sequencing; DNA-binding;
KW Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..530
FT /note="PC4 and SFRS1-interacting protein"
FT /id="PRO_0000191708"
FT DOMAIN 1..64
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 88..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..417
FT /note="Integrase-binding domain (IBD)"
FT /evidence="ECO:0000269|PubMed:15895093"
FT REGION 446..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 306..334
FT /evidence="ECO:0000255"
FT COILED 371..395
FT /evidence="ECO:0000255"
FT MOTIF 146..156
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:15797927"
FT COMPBIAS 88..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q812D1"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JF8"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99JF8"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 272
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 437
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 517
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 527
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 326..530
FT /note="QQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEAL
FT DELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVI
FT TQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGE
FT SNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN -> HFAL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044435"
FT VAR_SEQ 326..333
FT /note="QQNKDEGK -> HQTTCNLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9822615"
FT /id="VSP_014297"
FT VAR_SEQ 334..530
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9822615"
FT /id="VSP_014298"
FT MUTAGEN 360
FT /note="K->A: Reduced interaction with POGZ, CDCA7L and
FT human HIV-1 integrase."
FT /evidence="ECO:0000269|PubMed:19244240"
FT MUTAGEN 365
FT /note="I->A: Loss of interaction with human HIV-1
FT integrase; reduced interaction with POGZ and CDCA7L."
FT /evidence="ECO:0000269|PubMed:15895093,
FT ECO:0000269|PubMed:19244240"
FT MUTAGEN 366
FT /note="D->A: Loss of interaction with human HIV-1
FT integrase; no effect on interaction with CDCA7L and POGZ."
FT /evidence="ECO:0000269|PubMed:19244240"
FT MUTAGEN 366
FT /note="D->N: Loss of interaction with human HIV-1
FT integrase; no effect on interaction with KMT2A."
FT /evidence="ECO:0000269|PubMed:15895093,
FT ECO:0000269|PubMed:25082813"
FT MUTAGEN 368
FT /note="L->A: Reduced interaction with KMT2A. Significant
FT loss of interaction with KMT2A; when associated with D-
FT 407."
FT /evidence="ECO:0000269|PubMed:25082813"
FT MUTAGEN 370
FT /note="V->A: Reduced interaction with POGZ, CDCA7L and
FT human HIV-1 integrase."
FT /evidence="ECO:0000269|PubMed:19244240"
FT MUTAGEN 404
FT /note="R->D: Significant loss of interaction with KMT2A;
FT when associated with D-405."
FT /evidence="ECO:0000269|PubMed:25082813"
FT MUTAGEN 405
FT /note="R->D: Significant loss of interaction with KMT2A;
FT when associated with D-404."
FT /evidence="ECO:0000269|PubMed:25082813"
FT MUTAGEN 406
FT /note="F->A: Loss of interaction with human HIV-1 integrase
FT and POGZ; reduced interaction with CDCA7L."
FT /evidence="ECO:0000269|PubMed:15895093,
FT ECO:0000269|PubMed:19244240"
FT MUTAGEN 407
FT /note="K->D: Reduced interaction with KMT2A. Significant
FT loss of interaction with KMT2A; when associated with A-
FT 368."
FT /evidence="ECO:0000269|PubMed:25082813"
FT MUTAGEN 408
FT /note="V->A: Reduced interaction with human HIV-1
FT integrase; no effect on interaction with POGZ and CDCA7L."
FT /evidence="ECO:0000269|PubMed:15895093,
FT ECO:0000269|PubMed:19244240"
FT CONFLICT 153..161
FT /note="Missing (in Ref. 7; AAH64135)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="E -> G (in Ref. 1; AAC97946/AAC97945)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="T -> P (in Ref. 8; AAB52589)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="Y -> F (in Ref. 1; AAC97946 and 8; AAB52589)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:4FU6"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:4FU6"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:4FU6"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2M16"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6S01"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:4FU6"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:4FU6"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4FU6"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4FU6"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4FU6"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:4FU6"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:4FU6"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:6TRJ"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:3HPH"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:6TRJ"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:6TRJ"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:6TRJ"
FT HELIX 394..403
FT /evidence="ECO:0007829|PDB:6TRJ"
FT HELIX 410..428
FT /evidence="ECO:0007829|PDB:6TRJ"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5YI9"
FT HELIX 442..452
FT /evidence="ECO:0007829|PDB:6TVM"
SQ SEQUENCE 530 AA; 60103 MW; 4B653D02B1D0E174 CRC64;
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP
YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQAATK QSNASSDVEV EEKETSVSKE
DTDHEEKASN EDVTKAVDIT TPKAARRGRK RKAEKQVETE EAGVVTTATA SVNLKVSPKR
GRPAATEVKI PKPRGRPKMV KQPCPSESDI ITEEDKSKKK GQEEKQPKKQ PKKDEEGQKE
EDKPRKEPDK KEGKKEVESK RKNLAKTGVT STSDSEEEGD DQEGEKKRKG GRNFQTAHRR
NMLKGQHEKE AADRKRKQEE QMETEQQNKD EGKKPEVKKV EKKRETSMDS RLQRIHAEIK
NSLKIDNLDV NRCIEALDEL ASLQVTMQQA QKHTEMITTL KKIRRFKVSQ VIMEKSTMLY
NKFKNMFLVG EGDSVITQVL NKSLAEQRQH EEANKTKDQG KKGPNKKLEK EQTGSKTLNG
GSDAQDGNQP QHNGESNEDS KDNHEASTKK KPSSEERETE ISLKDSTLDN
