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Hepatoma-derived growth factor-related protein 2 (HRP-2)

 HDGR2_MOUSE             Reviewed;         669 AA.
Q3UMU9; D6CHX5; O35540; Q3UIH6; Q99L92;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
30-AUG-2017, entry version 102.
RecName: Full=Hepatoma-derived growth factor-related protein 2;
Short=HRP-2;
Name=Hdgfl2; Synonyms=Hdgfrp2;
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] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=9299445; DOI=10.1006/bbrc.1997.7233;
Izumoto Y., Kuroda T., Harada H., Kishimoto T., Nakamura H.;
"Hepatoma-derived growth factor belongs to a gene family in mice
showing significant homology in the amino terminus.";
Biochem. Biophys. Res. Commun. 238:26-32(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING,
FUNCTION, INTERACTION WITH HDGF, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=22212508; DOI=10.1111/j.1742-4658.2011.08464.x;
Thakar K., Votteler I., Kelkar D., Shidore T., Gupta S., Kelm S.,
Dietz F.;
"Interaction of HRP-2 isoforms with HDGF: chromatin binding of a
specific heteromer.";
FEBS J. 279:737-751(2012).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Heart, Lung, and Spleen;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Teratocarcinoma;
PubMed=17622165; DOI=10.1021/pr070122r;
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
"A differential phosphoproteomic analysis of retinoic acid-treated P19
cells.";
J. Proteome Res. 6:3174-3186(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; SER-450 AND
SER-635, 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-366 AND SER-367, 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-366 AND SER-367, 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-366; SER-450; SER-620;
SER-628; SER-629; SER-635; SER-640; SER-659; SER-661 AND SER-669,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 (ISOFORM 4), 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).
-!- FUNCTION: Involved in cellular growth control, through the
regulation of cyclin D1 expression (By similarity). Associates
with chromatin. Isoform 1 and isoform 3 bind to condensed
chromatin in mitotic cells. Isoform 4 binds to non-condensed
chromatin in the presence of HDGF. {ECO:0000250|UniProtKB:Q7Z4V5,
ECO:0000269|PubMed:22212508}.
-!- SUBUNIT: Interacts with HDGF (PubMed:22212508). Isoform 4
selectively interacts with HDGF (N-terminally processed form).
Interacts with trimethylated 'Lys-36' of histone H3 (H3K36me3).
Interacts with trimethylated 'Lys-79' of histone H3 (H3K79me3),
but has higher affinity for H3K36me3 (By similarity). Interacts
with IWS1 (By similarity). {ECO:0000250|UniProtKB:Q7Z4V5,
ECO:0000269|PubMed:22212508}.
-!- INTERACTION:
P51859:Hdgf; NbExp=4; IntAct=EBI-7627961, EBI-2943087;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22212508}.
Note=Isoform 4 displays a punctate pattern and colocalizes with N-
terminally processed HDFG.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Isoform a;
IsoId=Q3UMU9-1; Sequence=Displayed;
Name=2;
IsoId=Q3UMU9-2; Sequence=VSP_031118, VSP_031119;
Note=No experimental confirmation available. Contains a
phosphoserine at position 619. {ECO:0000244|PubMed:21183079};
Name=3; Synonyms=Isoform b;
IsoId=Q3UMU9-3; Sequence=VSP_031117;
Name=4; Synonyms=Isoform c;
IsoId=Q3UMU9-4; Sequence=VSP_047648, VSP_031119;
Note=Contains a phosphoserine at position 567.
{ECO:0000244|PubMed:21183079};
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:22212508}.
-!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D63850; BAA22896.1; -; mRNA.
EMBL; FN687734; CBK52221.2; -; mRNA.
EMBL; AK143616; BAE25467.1; -; mRNA.
EMBL; AK144669; BAE25999.1; -; mRNA.
EMBL; AK146813; BAE27453.1; -; mRNA.
EMBL; AK146918; BAE27530.1; -; mRNA.
EMBL; BC003741; AAH03741.1; -; mRNA.
CCDS; CCDS28894.1; -. [Q3UMU9-1]
PIR; JC5662; JC5662.
RefSeq; NP_001291713.1; NM_001304784.2. [Q3UMU9-3]
RefSeq; NP_001291714.1; NM_001304785.2. [Q3UMU9-2]
RefSeq; NP_001317982.1; NM_001331053.1.
RefSeq; NP_032259.1; NM_008233.4. [Q3UMU9-1]
UniGene; Mm.12966; -.
UniGene; Mm.279188; -.
ProteinModelPortal; Q3UMU9; -.
SMR; Q3UMU9; -.
BioGrid; 200267; 1.
IntAct; Q3UMU9; 3.
MINT; MINT-4104792; -.
STRING; 10090.ENSMUSP00000002911; -.
iPTMnet; Q3UMU9; -.
PhosphoSitePlus; Q3UMU9; -.
EPD; Q3UMU9; -.
MaxQB; Q3UMU9; -.
PaxDb; Q3UMU9; -.
PeptideAtlas; Q3UMU9; -.
PRIDE; Q3UMU9; -.
Ensembl; ENSMUST00000002911; ENSMUSP00000002911; ENSMUSG00000002833. [Q3UMU9-1]
GeneID; 15193; -.
KEGG; mmu:15193; -.
UCSC; uc008dau.2; mouse. [Q3UMU9-1]
UCSC; uc008dav.3; mouse. [Q3UMU9-2]
UCSC; uc008daw.2; mouse. [Q3UMU9-3]
UCSC; uc012avq.2; mouse. [Q3UMU9-4]
CTD; 84717; -.
MGI; MGI:1194492; Hdgfl2.
eggNOG; KOG1904; Eukaryota.
eggNOG; ENOG4111PJT; LUCA.
GeneTree; ENSGT00530000063013; -.
HOGENOM; HOG000230488; -.
HOVERGEN; HBG099722; -.
InParanoid; Q3UMU9; -.
OMA; ANKEVME; -.
OrthoDB; EOG091G045X; -.
PhylomeDB; Q3UMU9; -.
TreeFam; TF105385; -.
PRO; PR:Q3UMU9; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000002833; -.
CleanEx; MM_HDGFRP2; -.
Genevisible; Q3UMU9; MM.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
CDD; cd05834; HDGF_related; 1.
InterPro; IPR035496; HDGF-rel_PWWP.
InterPro; IPR021567; LEDGF_IBD.
InterPro; IPR000313; PWWP_dom.
Pfam; PF11467; LEDGF; 1.
Pfam; PF00855; PWWP; 1.
SMART; SM00293; PWWP; 1.
SUPFAM; SSF140576; SSF140576; 1.
PROSITE; PS50812; PWWP; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 669 Hepatoma-derived growth factor-related
protein 2.
/FTId=PRO_0000317644.
DOMAIN 7 64 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
COILED 550 575 {ECO:0000255}.
COMPBIAS 142 271 Ser-rich.
COMPBIAS 322 363 Arg-rich.
MOD_RES 366 366 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000250|UniProtKB:Q925G1}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 628 628 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 629 629 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 661 661 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 669 669 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 66 118 Missing (in isoform 4).
{ECO:0000303|PubMed:22212508}.
/FTId=VSP_047648.
VAR_SEQ 224 225 KK -> KKHPTGYACPQ (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_031117.
VAR_SEQ 226 226 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_031118.
VAR_SEQ 635 635 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:22212508}.
/FTId=VSP_031119.
SEQUENCE 669 AA; 74291 MW; 01228985D4616848 CRC64;
MPHAFKPGDL VFAKMKGYPH WPARIDDIAD GAVKPPPNKY PIFFFGTHET AFLGPKDLFP
YDKCKDKYGK PNKRKGFNEG LWEIQNNPHA SYSAPPPVSS SDSEAPEADL GCGSDVDKDK
ESRRVMTVTA VTTTATSDRM ESDSDSDKSS DHSGLKRKTP VLKVSVSKRA RRASSDLDQA
SVSPSEEDSE SPSESEKTSD QDFTPEKKTA ARPPRRGPLG GRKKKKVPSA SDSDSKADSD
GAKEEPVVTA QPSPSSSSSS SSSSSSDSDV SVKKPPRGRK PAEKPPPKPR GRRPKPERPP
STSSSDSDSD SGEVDRISEW KRRDEERRRE LEARRRREQE EELRRLREQE REEKERRKER
AERGGSSGEE LEDEEPVKKR SRKARGRGTP SSSDSEPEGE LGKEGKKLAK KSQLPGSESA
RKPGQKEKRG RPDEKPRARP VKVERTRKRS EGLSLERKGE KKKEPSVEER LQKLHSEIKF
ALKVDNPDVR KCLSALEELG TLQVTSQILQ KNTDVVATLK KIRRYKANKD VMAKAAEVYT
RLKSRVLGPK VEALQKVNKA GAEKERADNE KLEEQPGEQA PRELAEDEPS TDRSAPVNGE
ATSQKGENME DRAQEDGQDS EDGPRGGSSE ELHDSPRDNS DPAKPGNERQ DHERTRLASE
SANDDNEDS


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