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

 HDGR2_HUMAN             Reviewed;         671 AA.
Q7Z4V5; I3L080; K7EQZ6; Q96GI5; Q9BW08;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Hepatoma-derived growth factor-related protein 2;
Short=HRP-2;
AltName: Full=Hepatoma-derived growth factor 2;
Short=HDGF-2;
Name=HDGFL2 {ECO:0000312|HGNC:HGNC:14680}; Synonyms=HDGF2, HDGFRP2;
ORFNames=UNQ785/PRO1604;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yu L.;
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 103-671 (ISOFORM 1).
TISSUE=Kidney, and Muscle;
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633 AND SER-634, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH IWS1.
PubMed=25689719; DOI=10.1016/j.bbrc.2015.02.042;
Gao K., Xu C., Jin X., Wumaier R., Ma J., Peng J., Wang Y., Tang Y.,
Yu L., Zhang P.;
"HDGF-related protein-2 (HRP-2) acts as an oncogene to promote cell
growth in hepatocellular carcinoma.";
Biochem. Biophys. Res. Commun. 458:849-855(2015).
[10]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-93 IN COMPLEX WITH HISTONE
H3 PEPTIDE, AND INTERACTION WITH HISTONE H3.
PubMed=21720545; DOI=10.1371/journal.pone.0018919;
Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L.,
Qiu W., Wang Y., Min J.;
"Structural and histone binding ability characterizations of human
PWWP domains.";
PLoS ONE 6:E18919-E18919(2011).
-!- FUNCTION: Involved in cellular growth control, through the
regulation of cyclin D1 expression. {ECO:0000269|PubMed:25689719}.
-!- SUBUNIT: Interacts with HDGF (By similarity). Interacts with
trimethylated 'Lys-36' of histone H3 (H3K36me3). Interacts with
trimethylated 'Lys-79' of histone H3 (H3K79me3), but has higher
affinity for H3K36me3. Interacts with IWS1 (PubMed:25689719).
{ECO:0000250|UniProtKB:Q3UMU9, ECO:0000269|PubMed:21720545,
ECO:0000269|PubMed:25689719}.
-!- INTERACTION:
Q15554:TERF2; NbExp=2; IntAct=EBI-1049136, EBI-706637;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3UMU9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q7Z4V5-1; Sequence=Displayed;
Name=2;
IsoId=Q7Z4V5-2; Sequence=VSP_031116;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q7Z4V5-3; Sequence=VSP_047329;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q7Z4V5-4; Sequence=VSP_047329, VSP_031116;
-!- TISSUE SPECIFICITY: Widely expressed. High expression is found in
heart, skeletal muscle, ovary and testis. Overexpression is
frequently observed in hepatocellular carcinoma samples.
{ECO:0000269|PubMed:25689719}.
-!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF294267; AAP97281.1; -; mRNA.
EMBL; AY358600; AAQ88963.1; -; mRNA.
EMBL; AC011498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471139; EAW69215.1; -; Genomic_DNA.
EMBL; CH471139; EAW69216.1; -; Genomic_DNA.
EMBL; BC000755; AAH00755.1; -; mRNA.
EMBL; BC009449; AAH09449.1; -; mRNA.
CCDS; CCDS42472.1; -. [Q7Z4V5-1]
CCDS; CCDS59336.1; -. [Q7Z4V5-2]
RefSeq; NP_001001520.1; NM_001001520.2. [Q7Z4V5-1]
RefSeq; NP_116020.1; NM_032631.3. [Q7Z4V5-2]
UniGene; Hs.43071; -.
PDB; 3EAE; X-ray; 2.24 A; A/B=1-93.
PDB; 3QBY; X-ray; 1.95 A; A/B/C=1-93.
PDB; 3QJ6; X-ray; 2.30 A; A=1-93.
PDBsum; 3EAE; -.
PDBsum; 3QBY; -.
PDBsum; 3QJ6; -.
ProteinModelPortal; Q7Z4V5; -.
SMR; Q7Z4V5; -.
BioGrid; 124221; 44.
IntAct; Q7Z4V5; 20.
MINT; MINT-5005346; -.
STRING; 9606.ENSP00000301284; -.
iPTMnet; Q7Z4V5; -.
PhosphoSitePlus; Q7Z4V5; -.
SwissPalm; Q7Z4V5; -.
BioMuta; HDGFRP2; -.
DMDM; 74738715; -.
EPD; Q7Z4V5; -.
MaxQB; Q7Z4V5; -.
PaxDb; Q7Z4V5; -.
PeptideAtlas; Q7Z4V5; -.
PRIDE; Q7Z4V5; -.
Ensembl; ENST00000616600; ENSP00000483345; ENSG00000167674. [Q7Z4V5-1]
Ensembl; ENST00000621835; ENSP00000483702; ENSG00000167674. [Q7Z4V5-2]
GeneID; 84717; -.
KEGG; hsa:84717; -.
UCSC; uc032hkd.2; human. [Q7Z4V5-1]
CTD; 84717; -.
DisGeNET; 84717; -.
EuPathDB; HostDB:ENSG00000167674.14; -.
GeneCards; HDGFL2; -.
HGNC; HGNC:14680; HDGFL2.
HPA; HPA042559; -.
HPA; HPA044208; -.
neXtProt; NX_Q7Z4V5; -.
eggNOG; KOG1904; Eukaryota.
eggNOG; ENOG4111PJT; LUCA.
GeneTree; ENSGT00530000063013; -.
HOGENOM; HOG000230488; -.
HOVERGEN; HBG099722; -.
InParanoid; Q7Z4V5; -.
OMA; ANKEVME; -.
OrthoDB; EOG091G045X; -.
PhylomeDB; Q7Z4V5; -.
TreeFam; TF105385; -.
ChiTaRS; HDGFRP2; human.
EvolutionaryTrace; Q7Z4V5; -.
GenomeRNAi; 84717; -.
PMAP-CutDB; Q7Z4V5; -.
PRO; PR:Q7Z4V5; -.
Proteomes; UP000005640; Unplaced.
Bgee; ENSG00000167674; -.
ExpressionAtlas; Q7Z4V5; baseline and differential.
Genevisible; Q7Z4V5; HS.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
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_domain.
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;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 671 Hepatoma-derived growth factor-related
protein 2.
/FTId=PRO_0000317643.
DOMAIN 7 64 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
COILED 521 581 {ECO:0000255}.
COMPBIAS 142 269 Ser-rich.
COMPBIAS 299 307 Poly-Ser.
COMPBIAS 318 391 Arg-rich.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UMU9}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UMU9}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UMU9}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000250|UniProtKB:Q925G1}.
MOD_RES 625 625 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UMU9}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UMU9}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UMU9}.
VAR_SEQ 574 574 K -> KLAGEE (in isoform 3 and isoform 4).
{ECO:0000305}.
/FTId=VSP_047329.
VAR_SEQ 640 640 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031116.
STRAND 10 13 {ECO:0000244|PDB:3QBY}.
STRAND 21 25 {ECO:0000244|PDB:3QBY}.
TURN 28 30 {ECO:0000244|PDB:3EAE}.
STRAND 40 44 {ECO:0000244|PDB:3QBY}.
TURN 45 47 {ECO:0000244|PDB:3QBY}.
STRAND 50 53 {ECO:0000244|PDB:3QBY}.
HELIX 55 57 {ECO:0000244|PDB:3QBY}.
STRAND 58 60 {ECO:0000244|PDB:3QBY}.
HELIX 61 68 {ECO:0000244|PDB:3QBY}.
HELIX 77 86 {ECO:0000244|PDB:3QBY}.
SEQUENCE 671 AA; 74317 MW; 66CA046E0E802741 CRC64;
MPHAFKPGDL VFAKMKGYPH WPARIDDIAD GAVKPPPNKY PIFFFGTHET AFLGPKDLFP
YDKCKDKYGK PNKRKGFNEG LWEIQNNPHA SYSAPPPVSS SDSEAPEANP ADGSDADEDD
EDRGVMAVTA VTATAASDRM ESDSDSDKSS DNSGLKRKTP ALKMSVSKRA RKASSDLDQA
SVSPSEEENS ESSSESEKTS DQDFTPEKKA AVRAPRRGPL GGRKKKKAPS ASDSDSKADS
DGAKPEPVAM ARSASSSSSS SSSSDSDVSV KKPPRGRKPA EKPLPKPRGR KPKPERPPSS
SSSDSDSDEV DRISEWKRRD EARRRELEAR RRREQEEELR RLREQEKEEK ERRRERADRG
EAERGSGGSS GDELREDDEP VKKRGRKGRG RGPPSSSDSE PEAELEREAK KSAKKPQSSS
TEPARKPGQK EKRVRPEEKQ QAKPVKVERT RKRSEGFSMD RKVEKKKEPS VEEKLQKLHS
EIKFALKVDS PDVKRCLNAL EELGTLQVTS QILQKNTDVV ATLKKIRRYK ANKDVMEKAA
EVYTRLKSRV LGPKIEAVQK VNKAGMEKEK AEEKLAGEEL AGEEAPQEKA EDKPSTDLSA
PVNGEATSQK GESAEDKEHE EGRDSEEGPR CGSSEDLHDS VREGPDLDRP GSDRQERERA
RGDSEALDEE S


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