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PC4 and SFRS1-interacting protein (Lens epithelium-derived growth factor) (mLEDGF)

 PSIP1_MOUSE             Reviewed;         528 AA.
Q99JF8; A2BI10; A2BI11; Q3TEJ7; Q3TTD7; Q3UTA1; Q80WQ7; Q99JF7;
Q99LR4; Q9CT03;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 138.
RecName: Full=PC4 and SFRS1-interacting protein;
AltName: Full=Lens epithelium-derived growth factor;
Short=mLEDGF;
Name=Psip1; Synonyms=Ledgf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
Bashein A.M., Brady G.;
Thesis (2000), University of Manchester, United Kingdom.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Yu L.;
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Limb, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-248.
STRAIN=C57BL/6J, and NOD; TISSUE=Egg, Embryo, Testis, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-176; SER-272
AND SER-274, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-176; SER-272
AND SER-274, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-106; THR-115;
THR-122; SER-129; THR-141; SER-176; SER-270; THR-271; SER-272; SER-274
AND SER-520, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
CITRULLINATION AT ARG-515.
PubMed=24463520; DOI=10.1038/nature12942;
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P.,
Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P.,
Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B.,
Kouzarides T.;
"Citrullination regulates pluripotency and histone H1 binding to
chromatin.";
Nature 507:104-108(2014).
-!- FUNCTION: Transcriptional coactivator involved in neuroepithelial
stem cell differentiation and neurogenesis. Involved in particular
in lens epithelial cell gene regulation and stress responses. May
play an important role in lens epithelial to fiber cell terminal
differentiation. May play a protective role during stress-induced
apoptosis (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with IFRD1/PC4. Interacts POGZ and CDCA7L (By
similarity). Murine leukemia virus (MLV) integrase does not
interact with PSIP1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Ledgfa, p75;
IsoId=Q99JF8-1; Sequence=Displayed;
Name=2; Synonyms=Ledgfb, p52;
IsoId=Q99JF8-2; Sequence=VSP_014299, VSP_014300;
Note=Ref.4 (AAH52177) sequence is in conflict in positions:
324:HQTTCNLQ->QLKALIQ. {ECO:0000305};
-!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
-!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ308965; CAC34944.1; -; mRNA.
EMBL; AJ308966; CAC34945.1; -; mRNA.
EMBL; AF339082; AAO32949.1; -; mRNA.
EMBL; AF339083; AAO32950.1; -; mRNA.
EMBL; BX682545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002260; AAH02260.1; -; mRNA.
EMBL; BC043079; AAH43079.1; -; mRNA.
EMBL; BC052177; AAH52177.1; -; mRNA.
EMBL; AK011572; BAB27707.3; -; mRNA.
EMBL; AK139598; BAE24079.1; -; mRNA.
EMBL; AK161426; BAE36388.1; -; mRNA.
EMBL; AK169600; BAE41251.1; -; mRNA.
CCDS; CCDS18299.1; -. [Q99JF8-1]
CCDS; CCDS71412.1; -. [Q99JF8-2]
RefSeq; NP_001277456.1; NM_001290527.1. [Q99JF8-2]
RefSeq; NP_598709.1; NM_133948.5. [Q99JF8-1]
UniGene; Mm.105331; -.
UniGene; Mm.260943; -.
UniGene; Mm.448301; -.
UniGene; Mm.451848; -.
ProteinModelPortal; Q99JF8; -.
SMR; Q99JF8; -.
BioGrid; 221716; 3.
IntAct; Q99JF8; 3.
MINT; Q99JF8; -.
STRING; 10090.ENSMUSP00000030207; -.
iPTMnet; Q99JF8; -.
PhosphoSitePlus; Q99JF8; -.
EPD; Q99JF8; -.
PaxDb; Q99JF8; -.
PeptideAtlas; Q99JF8; -.
PRIDE; Q99JF8; -.
Ensembl; ENSMUST00000030207; ENSMUSP00000030207; ENSMUSG00000028484. [Q99JF8-1]
Ensembl; ENSMUST00000107215; ENSMUSP00000102833; ENSMUSG00000028484. [Q99JF8-2]
GeneID; 101739; -.
KEGG; mmu:101739; -.
UCSC; uc008tkw.2; mouse. [Q99JF8-1]
UCSC; uc008tkx.2; mouse. [Q99JF8-2]
CTD; 11168; -.
MGI; MGI:2142116; Psip1.
eggNOG; KOG1904; Eukaryota.
eggNOG; ENOG410Y5WD; LUCA.
GeneTree; ENSGT00530000063013; -.
HOVERGEN; HBG108300; -.
InParanoid; Q99JF8; -.
OMA; GNLELWK; -.
OrthoDB; EOG091G045X; -.
PhylomeDB; Q99JF8; -.
TreeFam; TF105385; -.
ChiTaRS; Psip1; mouse.
PRO; PR:Q99JF8; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028484; Expressed in 299 organ(s), highest expression level in brain.
CleanEx; MM_PSIP1; -.
ExpressionAtlas; Q99JF8; baseline and differential.
Genevisible; Q99JF8; MM.
GO; GO:0005720; C:nuclear heterochromatin; ISS:UniProtKB.
GO; GO:0034399; C:nuclear periphery; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0035327; C:transcriptionally active chromatin; ISS:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0097100; F:supercoiled DNA binding; ISS:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0000395; P:mRNA 5'-splice site recognition; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0009408; P:response to heat; IDA:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd05834; HDGF_related; 1.
Gene3D; 1.20.930.10; -; 1.
InterPro; IPR035496; HDGF-rel_PWWP.
InterPro; IPR036218; HIVI-bd_sf.
InterPro; IPR021567; LEDGF_IBD.
InterPro; IPR000313; PWWP_dom.
InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
InterPro; IPR017859; Treacle-like_TCS.
Pfam; PF11467; LEDGF; 1.
Pfam; PF00855; PWWP; 1.
PRINTS; PR01503; TREACLE.
SMART; SM00293; PWWP; 1.
SUPFAM; SSF140576; SSF140576; 1.
PROSITE; PS50812; PWWP; 1.
1: Evidence at protein level;
Alternative splicing; Citrullination; Coiled coil; Complete proteome;
DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 528 PC4 and SFRS1-interacting protein.
/FTId=PRO_0000191709.
DOMAIN 7 64 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
COILED 306 332 {ECO:0000255}.
COILED 369 393 {ECO:0000255}.
MOTIF 146 156 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:Q812D1}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 115 115 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 122 122 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000250|UniProtKB:O75475}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 271 271 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000250|UniProtKB:O75475}.
MOD_RES 435 435 Phosphothreonine.
{ECO:0000250|UniProtKB:O75475}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:O75475}.
MOD_RES 515 515 Citrulline.
{ECO:0000269|PubMed:24463520}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 525 525 Phosphothreonine.
{ECO:0000250|UniProtKB:O75475}.
CROSSLNK 75 75 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O75475}.
VAR_SEQ 324 331 QQNKDEGK -> HQTTCNLQ (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1, ECO:0000303|Ref.2}.
/FTId=VSP_014299.
VAR_SEQ 332 528 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1, ECO:0000303|Ref.2}.
/FTId=VSP_014300.
SEQUENCE 528 AA; 59697 MW; 4A9AE28245843AB6 CRC64;
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP
YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQASTK QSNASSDVEV EEKETNVSKE
DTDQEEKASN EDVTKAVDIT TPKAARRGRK RKAEKQVDTE EAGMVTAATA SNVKASPKRG
RPAATEVKIP KPRGRPKVVK QPCPSDGDMV IDEDKSKKKG PEEKQPKKQL KKEEEGQKEE
EKPRKEPDKK EGKKEVESKR KNLAKPGVTS TSDSEDEDDQ EGEKKRKGGR NFQAAHRRNM
LKGQHEKEAG DRKRKQEEQM ETEQQNKDEG KKPEVKKVEK KRETSMDSRL QRIHAEIKNS
LKIDNLDVNR CIEALDELAS LQVTMQQAQK HTEMITTLKK IRRFKVSQVI MEKSTMLYNK
FKNMFLVGEG DSVITQVLNK SLAEQRQHEE ANKTKDQGKK GPNKKLEKEP TGTKSLNGGS
DAQESNHPQH NGDSNEDGKD SREASSKTKP PGEEREAEIS LKESTLDN


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