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Holliday junction recognition protein (14-3-3-associated AKT substrate) (Fetal liver-expressing gene 1 protein) (Up-regulated in lung cancer 9)

 HJURP_HUMAN             Reviewed;         748 AA.
Q8NCD3; A8IRH5; B4DWR0; B4DZV4; Q9BUT2; Q9NSL8;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
25-OCT-2017, entry version 121.
RecName: Full=Holliday junction recognition protein;
AltName: Full=14-3-3-associated AKT substrate;
AltName: Full=Fetal liver-expressing gene 1 protein;
AltName: Full=Up-regulated in lung cancer 9;
Name=HJURP;
Synonyms=FAKTS, FLEG1 {ECO:0000312|EMBL:BAD36741.1}, URLC9;
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), SUBCELLULAR LOCATION,
INTERACTION WITH MSH5 AND NBN, DNA-BINDING, TISSUE SPECIFICITY, AND
VARIANTS LYS-76; GLY-199 AND CYS-295.
PubMed=17823411; DOI=10.1158/0008-5472.CAN-07-1307;
Kato T., Sato N., Hayama S., Yamabuki T., Ito T., Miyamoto M.,
Kondo S., Nakamura Y., Daigo Y.;
"Activation of Holliday junction recognizing protein involved in the
chromosomal stability and immortality of cancer cells.";
Cancer Res. 67:8544-8553(2007).
[2] {ECO:0000305, ECO:0000312|EMBL:BAD36741.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-76; GLY-199
AND CYS-295.
Koike N., Sumii M., Ikura T., Masuda Y., Wakida K., Uchida T.,
Asahara T., Usui T., Shimamoto F., Chayama K., Fukumoto M., Kamiya K.;
"Impaired cytoplasmic localization and nuclear accumulation of a novel
gene product, hFLEG1, associated with hepatocellular carcinoma
development.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000312|EMBL:BAC11221.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
VARIANTS LYS-76; GLY-199; CYS-295; CYS-549; PHE-691 AND GLY-723.
TISSUE=Esophagus, Teratocarcinoma {ECO:0000312|EMBL:BAC11221.1}, and
Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5] {ECO:0000312|EMBL:AAH01940.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
LYS-76 AND CYS-295.
TISSUE=Lung {ECO:0000312|EMBL:AAH01940.2};
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-748.
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CENPA.
PubMed=16622419; DOI=10.1038/ncb1397;
Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
Cleveland D.W.;
"The human CENP-A centromeric nucleosome-associated complex.";
Nat. Cell Biol. 8:458-469(2006).
[9] {ECO:0000305}
INTERACTION WITH 14-3-3 PROTEINS, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, PHOSPHORYLATION AT SER-486, AND MUTAGENESIS OF SER-486.
PubMed=17256767; DOI=10.1002/prot.21288;
Luhn P., Wang H., Marcus A.I., Fu H.;
"Identification of FAKTS as a novel 14-3-3-associated nuclear
protein.";
Proteins 67:479-489(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-448; SER-473
AND SER-642, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CENPA.
PubMed=19410544; DOI=10.1016/j.cell.2009.02.039;
Foltz D.R., Jansen L.E.T., Bailey A.O., Yates J.R. III, Bassett E.A.,
Wood S., Black B.E., Cleveland D.W.;
"Centromere-specific assembly of CENP-A nucleosomes is mediated by
HJURP.";
Cell 137:472-484(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND INTERACTION WITH CENPA.
PubMed=19410545; DOI=10.1016/j.cell.2009.02.040;
Dunleavy E.M., Roche D., Tagami H., Lacoste N., Ray-Gallet D.,
Nakamura Y., Daigo Y., Nakatani Y., Almouzni-Pettinotti G.;
"HJURP is a cell-cycle-dependent maintenance and deposition factor of
CENP-A at centromeres.";
Cell 137:485-497(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-140 AND
SER-473, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-595, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-201; SER-211;
SER-448; SER-473; SER-486; SER-496 AND SER-642, VARIANT [LARGE SCALE
ANALYSIS] GLY-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
SUBUNIT.
PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M.,
Syed S.H., Lone I.N., Boopathi R., Fontaine E., Papai G.,
Tachiwana H., Gautier T., Skoufias D., Padmanabhan K., Bednar J.,
Kurumizaka H., Schultz P., Angelov D., Hamiche A., Dimitrov S.;
"The flexible ends of CENP-A nucleosome are required for mitotic
fidelity.";
Mol. Cell 63:674-685(2016).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-354; LYS-581 AND LYS-586,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-80 IN COMPLEX WITH CENPA
AND HISTONE H4, AND SUBUNIT.
PubMed=21478274; DOI=10.1101/gad.2045111;
Hu H., Liu Y., Wang M., Fang J., Huang H., Yang N., Li Y., Wang J.,
Yao X., Shi Y., Li G., Xu R.M.;
"Structure of a CENP-A-histone H4 heterodimer in complex with
chaperone HJURP.";
Genes Dev. 25:901-906(2011).
-!- FUNCTION: Centromeric protein that plays a central role in the
incorporation and maintenance of histone H3-like variant CENPA at
centromeres. Acts as a specific chaperone for CENPA and is
required for the incorporation of newly synthesized CENPA
molecules into nucleosomes at replicated centromeres. Prevents
CENPA-H4 tetramerization and prevents premature DNA binding by the
CENPA-H4 tetramer. Directly binds Holliday junctions.
{ECO:0000269|PubMed:19410544, ECO:0000269|PubMed:19410545}.
-!- SUBUNIT: Interacts with CENPA (via CATD domain); the interaction
is direct and specific for CENPA since it does not interact with
H3.1- or H3.3-containing nucleosomes (PubMed:16622419,
PubMed:19410544, PubMed:19410545). Heterotrimer composed of HJURP,
CENPA and histone H4, where HJURP interacts with the dimer formed
by CENPA and histone H4 and prevents tetramerization of CENPA and
H4 (PubMed:21478274). Identified in a centromere complex
containing histones H2A, H2B and H4, and at least CENPA, CENPB,
CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1
(PubMed:27499292). Interacts with 14-3-3 family members in a
phosphorylation-dependent manner (PubMed:17256767). Interacts with
MSH5 and NBN (PubMed:17823411). {ECO:0000269|PubMed:16622419,
ECO:0000269|PubMed:17256767, ECO:0000269|PubMed:17823411,
ECO:0000269|PubMed:19410544, ECO:0000269|PubMed:19410545,
ECO:0000269|PubMed:21478274, ECO:0000269|PubMed:27499292}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-719429, EBI-719429;
P49450:CENPA; NbExp=15; IntAct=EBI-719429, EBI-1751979;
P49450-1:CENPA; NbExp=3; IntAct=EBI-719429, EBI-15826012;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome, centromere.
Note=Localizes in centromeres during late telophase and early G1,
when CENPA nucleosomes are assembled. Localizes to nucleolus
during S phase, nucleolus site being often related to storage.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8NCD3-1; Sequence=Displayed;
Name=2;
IsoId=Q8NCD3-2; Sequence=VSP_037468;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8NCD3-3; Sequence=VSP_037467;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: According to PubMed:17256767, highly expressed
in the thymus with lower levels in the placenta, small intestine,
liver, skeletal muscle, and colon. According to PubMed:17823411,
highly expressed in testis, and at a relatively lower level in
thymus and bone marrow. Significantly overexpressed in many lung
cancer samples, compared with normal lung.
{ECO:0000269|PubMed:17256767, ECO:0000269|PubMed:17823411}.
-!- SEQUENCE CAUTION:
Sequence=CAB82391.2; Type=Erroneous termination; Positions=437; Note=Translated as Arg.; Evidence={ECO:0000305};
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EMBL; AB101211; BAF82039.1; -; mRNA.
EMBL; AB162218; BAD36741.1; -; mRNA.
EMBL; AK301643; BAG63122.1; -; mRNA.
EMBL; AK303109; BAG64216.1; -; mRNA.
EMBL; AK074809; BAC11221.1; -; mRNA.
EMBL; AC005538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001940; AAH01940.2; -; mRNA.
EMBL; AL162048; CAB82391.2; ALT_SEQ; mRNA.
CCDS; CCDS33406.1; -. [Q8NCD3-1]
CCDS; CCDS63166.1; -. [Q8NCD3-3]
CCDS; CCDS63167.1; -. [Q8NCD3-2]
PIR; T47163; T47163.
RefSeq; NP_001269891.1; NM_001282962.1. [Q8NCD3-2]
RefSeq; NP_001269892.1; NM_001282963.1. [Q8NCD3-3]
RefSeq; NP_060880.3; NM_018410.4. [Q8NCD3-1]
UniGene; Hs.532968; -.
PDB; 3R45; X-ray; 2.60 A; C=1-80.
PDBsum; 3R45; -.
ProteinModelPortal; Q8NCD3; -.
SMR; Q8NCD3; -.
BioGrid; 120635; 25.
DIP; DIP-53282N; -.
IntAct; Q8NCD3; 15.
MINT; MINT-1402926; -.
STRING; 9606.ENSP00000414109; -.
iPTMnet; Q8NCD3; -.
PhosphoSitePlus; Q8NCD3; -.
BioMuta; HJURP; -.
DMDM; 239938642; -.
EPD; Q8NCD3; -.
MaxQB; Q8NCD3; -.
PaxDb; Q8NCD3; -.
PeptideAtlas; Q8NCD3; -.
PRIDE; Q8NCD3; -.
Ensembl; ENST00000411486; ENSP00000414109; ENSG00000123485. [Q8NCD3-1]
Ensembl; ENST00000432087; ENSP00000407208; ENSG00000123485. [Q8NCD3-2]
Ensembl; ENST00000441687; ENSP00000401944; ENSG00000123485. [Q8NCD3-3]
GeneID; 55355; -.
KEGG; hsa:55355; -.
UCSC; uc002vvg.5; human. [Q8NCD3-1]
CTD; 55355; -.
DisGeNET; 55355; -.
EuPathDB; HostDB:ENSG00000123485.11; -.
GeneCards; HJURP; -.
H-InvDB; HIX0002938; -.
HGNC; HGNC:25444; HJURP.
HPA; HPA008436; -.
HPA; HPA027261; -.
MIM; 612667; gene.
neXtProt; NX_Q8NCD3; -.
OpenTargets; ENSG00000123485; -.
PharmGKB; PA162390937; -.
eggNOG; ENOG410IW66; Eukaryota.
eggNOG; ENOG4111C4D; LUCA.
GeneTree; ENSGT00390000005575; -.
HOGENOM; HOG000112909; -.
HOVERGEN; HBG062573; -.
InParanoid; Q8NCD3; -.
OMA; YAGMLHS; -.
OrthoDB; EOG091G071S; -.
PhylomeDB; Q8NCD3; -.
TreeFam; TF336293; -.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
ChiTaRS; HJURP; human.
GenomeRNAi; 55355; -.
PRO; PR:Q8NCD3; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000123485; -.
CleanEx; HS_HJURP; -.
ExpressionAtlas; Q8NCD3; baseline and differential.
Genevisible; Q8NCD3; HS.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; IMP:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0051101; P:regulation of DNA binding; IDA:UniProtKB.
GO; GO:0043254; P:regulation of protein complex assembly; IDA:UniProtKB.
InterPro; IPR021052; HJURP.
InterPro; IPR022102; HJURP_C.
InterPro; IPR018465; Scm3/HJURP.
Pfam; PF12347; HJURP_C; 2.
Pfam; PF12346; HJURP_mid; 1.
Pfam; PF10384; Scm3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Centromere; Chaperone;
Chromosome; Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 748 Holliday junction recognition protein.
/FTId=PRO_0000287433.
MOD_RES 123 123 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PG16}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 486 486 Phosphoserine; by PKB/AKT1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17256767}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 595 595 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 642 642 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 354 354 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 581 581 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 586 586 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 81 165 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037467.
VAR_SEQ 81 134 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037468.
VARIANT 4 4 T -> A (in dbSNP:rs2302154).
/FTId=VAR_056912.
VARIANT 76 76 E -> K (in dbSNP:rs2286430).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17823411,
ECO:0000269|Ref.2}.
/FTId=VAR_057946.
VARIANT 199 199 R -> G (in dbSNP:rs3806589).
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17823411,
ECO:0000269|Ref.2}.
/FTId=VAR_057947.
VARIANT 295 295 S -> C (in dbSNP:rs3732215).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17823411,
ECO:0000269|Ref.2}.
/FTId=VAR_057948.
VARIANT 548 548 S -> T (in dbSNP:rs17863822).
/FTId=VAR_056913.
VARIANT 549 549 S -> C (in dbSNP:rs3821238).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_056914.
VARIANT 568 568 E -> D (in dbSNP:rs3771333).
/FTId=VAR_056915.
VARIANT 691 691 S -> F (in dbSNP:rs12582).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_056916.
VARIANT 723 723 E -> G (in dbSNP:rs10511).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_057949.
MUTAGEN 486 486 S->A: Loss of phosphorylation by AKT1 and
binding to YWHAG.
{ECO:0000269|PubMed:17256767}.
CONFLICT 613 613 S -> C (in Ref. 3; BAG63122).
{ECO:0000305}.
CONFLICT 733 733 E -> G (in Ref. 3; BAG63122).
{ECO:0000305}.
HELIX 16 40 {ECO:0000244|PDB:3R45}.
STRAND 49 51 {ECO:0000244|PDB:3R45}.
TURN 52 55 {ECO:0000244|PDB:3R45}.
STRAND 56 59 {ECO:0000244|PDB:3R45}.
STRAND 62 65 {ECO:0000244|PDB:3R45}.
STRAND 70 73 {ECO:0000244|PDB:3R45}.
SEQUENCE 748 AA; 83539 MW; DE7F1410F9A748D5 CRC64;
MLGTLRAMEG EDVEDDQLLQ KLRASRRRFQ RRMQRLIEKY NQPFEDTPVV QMATLTYETP
QGLRIWGGRL IKERNEGEIQ DSSMKPADRT DGSVQAAAWG PELPSHRTVL GADSKSGEVD
ATSDQEESVA WALAPAVPQS PLKNELRRKY LTQVDILLQG AEYFECAGNR AGRDVRVTPL
PSLASPAVPA PGYCSRISRK SPGDPAKPAS SPREWDPLHP SSTDMALVPR NDSLSLQETS
SSSFLSSQPF EDDDICNVTI SDLYAGMLHS MSRLLSTKPS SIISTKTFIM QNWNSRRRHR
YKSRMNKTYC KGARRSQRSS KENFIPCSEP VKGTGALRDC KNVLDVSCRK TGLKLEKAFL
EVNRPQIHKL DPSWKERKVT PSKYSSLIYF DSSATYNLDE ENRFRTLKWL ISPVKIVSRP
TIRQGHGENR QREIEIRFDQ LHREYCLSPR NQPRRMCLPD SWAMNMYRGG PASPGGLQGL
ETRRLSLPSS KAKAKSLSEA FENLGKRSLE AGRCLPKSDS SSSLPKTNPT HSATRPQQTS
DLHVQGNSSG IFRKSVSPSK TLSVPDKEVP GHGRNRYDEI KEEFDKLHQK YCLKSPGQMT
VPLCIGVSTD KASMEVRYQT EGFLGKLNPD PHFQGFQKLP SSPLGCRKSL LGSTAIEAPS
STCVARAITR DGTRDHQFPA KRPRLSEPQG SGRQGNSLGA SDGVDNTVRP GDQGSSSQPN
SEERGENTSY RMEEKSDFML EKLETKSV


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