PSIP1_RAT
ID PSIP1_RAT Reviewed; 528 AA.
AC Q812D1; Q7TNY0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=PC4 and SFRS1-interacting protein;
DE AltName: Full=Lens epithelium-derived growth factor;
GN Name=Psip1; Synonyms=Ledgf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Yu L.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-106; THR-122;
RP SER-129; SER-176 AND SER-274, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ledgfa;
CC IsoId=Q812D1-1; Sequence=Displayed;
CC Name=2; Synonyms=Ledgfb;
CC IsoId=Q812D1-2; Sequence=VSP_014301, VSP_014302;
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q99JF8}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR EMBL; AF339084; AAO32951.1; -; mRNA.
DR EMBL; AF372090; AAP97282.1; -; mRNA.
DR RefSeq; NP_786941.1; NM_175765.2. [Q812D1-1]
DR AlphaFoldDB; Q812D1; -.
DR BMRB; Q812D1; -.
DR SMR; Q812D1; -.
DR STRING; 10116.ENSRNOP00000016130; -.
DR iPTMnet; Q812D1; -.
DR PhosphoSitePlus; Q812D1; -.
DR jPOST; Q812D1; -.
DR PaxDb; Q812D1; -.
DR PRIDE; Q812D1; -.
DR GeneID; 313323; -.
DR KEGG; rno:313323; -.
DR UCSC; RGD:631439; rat. [Q812D1-1]
DR CTD; 11168; -.
DR RGD; 631439; Psip1.
DR eggNOG; KOG1904; Eukaryota.
DR InParanoid; Q812D1; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; Q812D1; -.
DR PRO; PR:Q812D1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Citrullination; Coiled coil; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..528
FT /note="PC4 and SFRS1-interacting protein"
FT /id="PRO_0000191710"
FT DOMAIN 7..64
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 86..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..415
FT /note="Integrase-binding domain (IBD)"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT REGION 444..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 304..332
FT /evidence="ECO:0000255"
FT COILED 369..393
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 207..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
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:22673903"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 515
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75475"
FT MOD_RES 525
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"
FT VAR_SEQ 324..331
FT /note="QQTKDEGK -> HQTTCNLQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014301"
FT VAR_SEQ 332..528
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014302"
FT CONFLICT 273
FT /note="D -> Y (in Ref. 1; AAP97282)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="H -> N (in Ref. 1; AAP97282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59639 MW; 8E0C2887842F6125 CRC64;
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP
YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQVSTK QSNASSDVEA EEKETSVSKE
DTDQEEKASN EDVTKAADIT TPKAARRGRK RKAEKQVDTE EAGVVTAATA SNVKASPKRG
RPAATEVKIP KPRGRPKVVK QPCPSESDMV IDEDKSKKKG PEEKPPKKQL KKEEEGQKEE
EKPRKEPDKK EGKKEVESKR KNLAKPGVTS TSDSEEDDDQ EGEKKRKGGR HFQAAHRRNM
LKGQHEKEAA DRKRKQEEQM ETEQQTKDEG KKPEVKKVEK KRETSMDSRL QRIHAEIKNS
LKIDNLDVNR CIEALDELAS LQVTMQQAQK HTEMITTLKK IRRFKVSQVI MEKSTMLYNK
FKNMFLVGEG DSVITQVLNK SLAEQRQHEE ANKTKDQGKK GPNKKLEKEQ TGTKSLNGGS
DAQESNHPQH NGDSAEESKD SREAGSKTKT PGEEREAEVS LKESTLDN
