PSIP1_BOVIN
ID PSIP1_BOVIN Reviewed; 530 AA.
AC Q8MJG1; A7E383; Q0VCL7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=PC4 and SFRS1-interacting protein;
DE AltName: Full=Lens epithelium-derived growth factor;
GN Name=PSIP1; Synonyms=LEDGF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-458.
RC STRAIN=Hereford; TISSUE=Fetal lung, and Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-530.
RC TISSUE=Brain;
RA Adachi N., Singh D.P., Shinohara T.;
RT "Lens epithelium-derived growth factor (LEDGF): sequence conservation among
RT animal species.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:O75475}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with IFRD1/PC4 (By
CC similarity). Interacts (via IBD domain) with POGZ (via IBM motif) and
CC CDCA7L (via IBM motifs) (By similarity). Interacts (via IBD domain)
CC with KMT2A (via IBM motifs) with a moderate affinity whereas interacts
CC with the KMT2A-MEN1 complex with a greater affinity; MEN1 enhances
CC interaction of KMT2A with PSIP1 (By similarity). Interacts (via IBD
CC domain) with IWS1 (via IBM motif), MED1 (via IBM motif) and DBF4 (via
CC IBM motifs) (By similarity). {ECO:0000250|UniProtKB:O75475}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75475}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q99JF8}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI20107.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI51755.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BC120106; AAI20107.1; ALT_SEQ; mRNA.
DR EMBL; BC151754; AAI51755.1; ALT_SEQ; mRNA.
DR EMBL; AF474175; AAM90841.1; -; mRNA.
DR RefSeq; NP_001193405.1; NM_001206476.1.
DR AlphaFoldDB; Q8MJG1; -.
DR BMRB; Q8MJG1; -.
DR SMR; Q8MJG1; -.
DR STRING; 9913.ENSBTAP00000010356; -.
DR PeptideAtlas; Q8MJG1; -.
DR PRIDE; Q8MJG1; -.
DR Ensembl; ENSBTAT00000010356; ENSBTAP00000010356; ENSBTAG00000007872.
DR GeneID; 282011; -.
DR KEGG; bta:282011; -.
DR CTD; 11168; -.
DR VEuPathDB; HostDB:ENSBTAG00000007872; -.
DR VGNC; VGNC:33436; PSIP1.
DR eggNOG; KOG1904; Eukaryota.
DR GeneTree; ENSGT00940000154706; -.
DR InParanoid; Q8MJG1; -.
DR OMA; NLRVGMN; -.
DR OrthoDB; 530959at2759; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000007872; Expressed in spermatocyte and 108 other tissues.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0097100; F:supercoiled DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS: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 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 2: Evidence at transcript level;
KW Citrullination; Coiled coil; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..530
FT /note="PC4 and SFRS1-interacting protein"
FT /id="PRO_0000191706"
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:0000250|UniProtKB:O75475"
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:0000250|UniProtKB:O75475"
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:0000250|UniProtKB:O75475"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99JF8"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 272
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 437
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 517
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 527
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75475"
SQ SEQUENCE 530 AA; 60099 MW; 9AC58DE903FC372F CRC64;
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP
YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQASAK QSNASSDVEV EEKETSVSKE
DTDPEEKASN EDVTKAIDIT TPKAARRGRK RKAEKQVETE EAGVVTTATA SANLKVSPKR
GRPAATEVKI PKPRGRPKMV KQPCPSESDM ITEEDKSKKK GQEEKQPKKQ LKKDEEGQKE
EEKPRKEPDK KEGKKEVESK RKNLAKTGVT STSDSEEEGD DQEGEKKRKG GRNFQTAHRR
NMLKGQHEKE AADRKRKQEE QMETEQQNKD EGKKPEVKKV EKKRETSMDS RLQRIHAEIK
NSLKIDNLDV NRCIEALDEL ASLQVTMQQA QKHTEMITTL KKIRRFKVSQ VIMEKSTMLY
NKFKNMFLVG EGDSVITQVL NKSLAEQRQH EEANKTKDQG KKGPNKKLEK EQTGSKTLNG
GSDAQDSNQP QHNGDSNEES KDNHEASSKK KPSSEERETE ISLKDSTLDN
