HJURP_HUMAN
ID HJURP_HUMAN Reviewed; 748 AA.
AC Q8NCD3; A8IRH5; B4DWR0; B4DZV4; Q9BUT2; Q9NSL8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Holliday junction recognition protein;
DE AltName: Full=14-3-3-associated AKT substrate;
DE AltName: Full=Fetal liver-expressing gene 1 protein;
DE AltName: Full=Up-regulated in lung cancer 9;
GN Name=HJURP; Synonyms=FAKTS, FLEG1 {ECO:0000312|EMBL:BAD36741.1}, URLC9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION
RP WITH MSH5 AND NBN, DNA-BINDING, TISSUE SPECIFICITY, AND VARIANTS LYS-76;
RP GLY-199 AND CYS-295.
RX PubMed=17823411; DOI=10.1158/0008-5472.can-07-1307;
RA Kato T., Sato N., Hayama S., Yamabuki T., Ito T., Miyamoto M., Kondo S.,
RA Nakamura Y., Daigo Y.;
RT "Activation of Holliday junction recognizing protein involved in the
RT chromosomal stability and immortality of cancer cells.";
RL Cancer Res. 67:8544-8553(2007).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD36741.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-76; GLY-199 AND
RP CYS-295.
RA Koike N., Sumii M., Ikura T., Masuda Y., Wakida K., Uchida T., Asahara T.,
RA Usui T., Shimamoto F., Chayama K., Fukumoto M., Kamiya K.;
RT "Impaired cytoplasmic localization and nuclear accumulation of a novel gene
RT product, hFLEG1, associated with hepatocellular carcinoma development.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:BAC11221.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP LYS-76; GLY-199; CYS-295; CYS-549; PHE-691 AND GLY-723.
RC TISSUE=Esophagus, Teratocarcinoma {ECO:0000312|EMBL:BAC11221.1}, and
RC Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5] {ECO:0000312|EMBL:AAH01940.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LYS-76 AND
RP CYS-295.
RC TISSUE=Lung {ECO:0000312|EMBL:AAH01940.2};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-748.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CENPA.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [9] {ECO:0000305}
RP INTERACTION WITH 14-3-3 PROTEINS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PHOSPHORYLATION AT SER-486, AND MUTAGENESIS OF SER-486.
RX PubMed=17256767; DOI=10.1002/prot.21288;
RA Luhn P., Wang H., Marcus A.I., Fu H.;
RT "Identification of FAKTS as a novel 14-3-3-associated nuclear protein.";
RL Proteins 67:479-489(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-448; SER-473 AND
RP SER-642, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CENPA.
RX PubMed=19410544; DOI=10.1016/j.cell.2009.02.039;
RA Foltz D.R., Jansen L.E.T., Bailey A.O., Yates J.R. III, Bassett E.A.,
RA Wood S., Black B.E., Cleveland D.W.;
RT "Centromere-specific assembly of CENP-A nucleosomes is mediated by HJURP.";
RL Cell 137:472-484(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CENPA.
RX PubMed=19410545; DOI=10.1016/j.cell.2009.02.040;
RA Dunleavy E.M., Roche D., Tagami H., Lacoste N., Ray-Gallet D., Nakamura Y.,
RA Daigo Y., Nakatani Y., Almouzni-Pettinotti G.;
RT "HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-
RT A at centromeres.";
RL Cell 137:485-497(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-140 AND SER-473, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-595, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-201; SER-211;
RP SER-448; SER-473; SER-486; SER-496 AND SER-642, VARIANT [LARGE SCALE
RP ANALYSIS] GLY-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP SUBUNIT.
RX PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
RA Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M., Syed S.H.,
RA Lone I.N., Boopathi R., Fontaine E., Papai G., Tachiwana H., Gautier T.,
RA Skoufias D., Padmanabhan K., Bednar J., Kurumizaka H., Schultz P.,
RA Angelov D., Hamiche A., Dimitrov S.;
RT "The flexible ends of CENP-A nucleosome are required for mitotic
RT fidelity.";
RL Mol. Cell 63:674-685(2016).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-354; LYS-581 AND LYS-586, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-80 IN COMPLEX WITH CENPA AND
RP HISTONE H4, AND SUBUNIT.
RX PubMed=21478274; DOI=10.1101/gad.2045111;
RA Hu H., Liu Y., Wang M., Fang J., Huang H., Yang N., Li Y., Wang J., Yao X.,
RA Shi Y., Li G., Xu R.M.;
RT "Structure of a CENP-A-histone H4 heterodimer in complex with chaperone
RT HJURP.";
RL Genes Dev. 25:901-906(2011).
CC -!- FUNCTION: Centromeric protein that plays a central role in the
CC incorporation and maintenance of histone H3-like variant CENPA at
CC centromeres. Acts as a specific chaperone for CENPA and is required for
CC the incorporation of newly synthesized CENPA molecules into nucleosomes
CC at replicated centromeres. Prevents CENPA-H4 tetramerization and
CC prevents premature DNA binding by the CENPA-H4 tetramer. Directly binds
CC Holliday junctions. {ECO:0000269|PubMed:19410544,
CC ECO:0000269|PubMed:19410545}.
CC -!- SUBUNIT: Interacts with CENPA (via CATD domain); the interaction is
CC direct and specific for CENPA since it does not interact with H3.1- or
CC H3.3-containing nucleosomes (PubMed:16622419, PubMed:19410544,
CC PubMed:19410545). Heterotrimer composed of HJURP, CENPA and histone H4,
CC where HJURP interacts with the dimer formed by CENPA and histone H4 and
CC prevents tetramerization of CENPA and H4 (PubMed:21478274). Identified
CC in a centromere complex containing histones H2A, H2B and H4, and at
CC least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1
CC (PubMed:27499292). Interacts with 14-3-3 family members in a
CC phosphorylation-dependent manner (PubMed:17256767). Interacts with MSH5
CC and NBN (PubMed:17823411). {ECO:0000269|PubMed:16622419,
CC ECO:0000269|PubMed:17256767, ECO:0000269|PubMed:17823411,
CC ECO:0000269|PubMed:19410544, ECO:0000269|PubMed:19410545,
CC ECO:0000269|PubMed:21478274, ECO:0000269|PubMed:27499292}.
CC -!- INTERACTION:
CC Q8NCD3; P49450: CENPA; NbExp=15; IntAct=EBI-719429, EBI-1751979;
CC Q8NCD3; P49450-1: CENPA; NbExp=3; IntAct=EBI-719429, EBI-15826012;
CC Q8NCD3; Q8NCD3: HJURP; NbExp=4; IntAct=EBI-719429, EBI-719429;
CC Q8NCD3; O00629: KPNA4; NbExp=4; IntAct=EBI-719429, EBI-396343;
CC Q8NCD3-1; P49450: CENPA; NbExp=2; IntAct=EBI-15825976, EBI-1751979;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome, centromere.
CC Note=Localizes in centromeres during late telophase and early G1, when
CC CENPA nucleosomes are assembled. Localizes to nucleolus during S phase,
CC nucleolus site being often related to storage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NCD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NCD3-2; Sequence=VSP_037468;
CC Name=3;
CC IsoId=Q8NCD3-3; Sequence=VSP_037467;
CC -!- TISSUE SPECIFICITY: According to PubMed:17256767, highly expressed in
CC the thymus with lower levels in the placenta, small intestine, liver,
CC skeletal muscle, and colon. According to PubMed:17823411, highly
CC expressed in testis, and at a relatively lower level in thymus and bone
CC marrow. Significantly overexpressed in many lung cancer samples,
CC compared with normal lung. {ECO:0000269|PubMed:17256767,
CC ECO:0000269|PubMed:17823411}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82391.2; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB101211; BAF82039.1; -; mRNA.
DR EMBL; AB162218; BAD36741.1; -; mRNA.
DR EMBL; AK301643; BAG63122.1; -; mRNA.
DR EMBL; AK303109; BAG64216.1; -; mRNA.
DR EMBL; AK074809; BAC11221.1; -; mRNA.
DR EMBL; AC005538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001940; AAH01940.2; -; mRNA.
DR EMBL; AL162048; CAB82391.2; ALT_SEQ; mRNA.
DR CCDS; CCDS33406.1; -. [Q8NCD3-1]
DR CCDS; CCDS63166.1; -. [Q8NCD3-3]
DR CCDS; CCDS63167.1; -. [Q8NCD3-2]
DR PIR; T47163; T47163.
DR RefSeq; NP_001269891.1; NM_001282962.1. [Q8NCD3-2]
DR RefSeq; NP_001269892.1; NM_001282963.1. [Q8NCD3-3]
DR RefSeq; NP_060880.3; NM_018410.4. [Q8NCD3-1]
DR PDB; 3R45; X-ray; 2.60 A; C=1-80.
DR PDBsum; 3R45; -.
DR AlphaFoldDB; Q8NCD3; -.
DR SMR; Q8NCD3; -.
DR BioGRID; 120635; 116.
DR CORUM; Q8NCD3; -.
DR DIP; DIP-53282N; -.
DR IntAct; Q8NCD3; 22.
DR MINT; Q8NCD3; -.
DR STRING; 9606.ENSP00000414109; -.
DR GlyConnect; 2048; 3 N-Linked glycans (1 site).
DR GlyGen; Q8NCD3; 1 site, 6 N-linked glycans (1 site).
DR iPTMnet; Q8NCD3; -.
DR MetOSite; Q8NCD3; -.
DR PhosphoSitePlus; Q8NCD3; -.
DR BioMuta; HJURP; -.
DR DMDM; 239938642; -.
DR EPD; Q8NCD3; -.
DR jPOST; Q8NCD3; -.
DR MassIVE; Q8NCD3; -.
DR MaxQB; Q8NCD3; -.
DR PaxDb; Q8NCD3; -.
DR PeptideAtlas; Q8NCD3; -.
DR PRIDE; Q8NCD3; -.
DR ProteomicsDB; 72875; -. [Q8NCD3-1]
DR ProteomicsDB; 72876; -. [Q8NCD3-2]
DR ProteomicsDB; 72877; -. [Q8NCD3-3]
DR Antibodypedia; 2018; 154 antibodies from 29 providers.
DR DNASU; 55355; -.
DR Ensembl; ENST00000411486.7; ENSP00000414109.1; ENSG00000123485.12. [Q8NCD3-1]
DR Ensembl; ENST00000432087.5; ENSP00000407208.1; ENSG00000123485.12. [Q8NCD3-2]
DR Ensembl; ENST00000441687.5; ENSP00000401944.1; ENSG00000123485.12. [Q8NCD3-3]
DR GeneID; 55355; -.
DR KEGG; hsa:55355; -.
DR MANE-Select; ENST00000411486.7; ENSP00000414109.1; NM_018410.5; NP_060880.3.
DR UCSC; uc002vvg.5; human. [Q8NCD3-1]
DR CTD; 55355; -.
DR DisGeNET; 55355; -.
DR GeneCards; HJURP; -.
DR HGNC; HGNC:25444; HJURP.
DR HPA; ENSG00000123485; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 612667; gene.
DR neXtProt; NX_Q8NCD3; -.
DR OpenTargets; ENSG00000123485; -.
DR PharmGKB; PA162390937; -.
DR VEuPathDB; HostDB:ENSG00000123485; -.
DR eggNOG; ENOG502SJZT; Eukaryota.
DR GeneTree; ENSGT00390000005575; -.
DR InParanoid; Q8NCD3; -.
DR OMA; YGQWASS; -.
DR OrthoDB; 426984at2759; -.
DR PhylomeDB; Q8NCD3; -.
DR TreeFam; TF336293; -.
DR PathwayCommons; Q8NCD3; -.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR SignaLink; Q8NCD3; -.
DR SIGNOR; Q8NCD3; -.
DR BioGRID-ORCS; 55355; 685 hits in 1089 CRISPR screens.
DR ChiTaRS; HJURP; human.
DR GenomeRNAi; 55355; -.
DR Pharos; Q8NCD3; Tbio.
DR PRO; PR:Q8NCD3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NCD3; protein.
DR Bgee; ENSG00000123485; Expressed in ventricular zone and 118 other tissues.
DR ExpressionAtlas; Q8NCD3; baseline and differential.
DR Genevisible; Q8NCD3; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0051101; P:regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IDA:UniProtKB.
DR IDEAL; IID00283; -.
DR InterPro; IPR022102; HJURP_C.
DR InterPro; IPR021052; HJURP_central_dom.
DR InterPro; IPR018465; Scm3/HJURP.
DR Pfam; PF12347; HJURP_C; 2.
DR Pfam; PF12346; HJURP_mid; 1.
DR Pfam; PF10384; Scm3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Centromere; Chaperone;
KW Chromosome; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..748
FT /note="Holliday junction recognition protein"
FT /id="PRO_0000287433"
FT REGION 191..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PG16"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 486
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:17256767,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 581
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 586
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 81..165
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037467"
FT VAR_SEQ 81..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037468"
FT VARIANT 4
FT /note="T -> A (in dbSNP:rs2302154)"
FT /id="VAR_056912"
FT VARIANT 76
FT /note="E -> K (in dbSNP:rs2286430)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17823411,
FT ECO:0000269|Ref.2"
FT /id="VAR_057946"
FT VARIANT 199
FT /note="R -> G (in dbSNP:rs3806589)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17823411, ECO:0000269|Ref.2,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_057947"
FT VARIANT 295
FT /note="S -> C (in dbSNP:rs3732215)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17823411,
FT ECO:0000269|Ref.2"
FT /id="VAR_057948"
FT VARIANT 548
FT /note="S -> T (in dbSNP:rs17863822)"
FT /id="VAR_056913"
FT VARIANT 549
FT /note="S -> C (in dbSNP:rs3821238)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_056914"
FT VARIANT 568
FT /note="E -> D (in dbSNP:rs3771333)"
FT /id="VAR_056915"
FT VARIANT 691
FT /note="S -> F (in dbSNP:rs12582)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_056916"
FT VARIANT 723
FT /note="E -> G (in dbSNP:rs10511)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_057949"
FT MUTAGEN 486
FT /note="S->A: Loss of phosphorylation by AKT1 and binding to
FT YWHAG."
FT /evidence="ECO:0000269|PubMed:17256767"
FT CONFLICT 613
FT /note="S -> C (in Ref. 3; BAG63122)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="E -> G (in Ref. 3; BAG63122)"
FT /evidence="ECO:0000305"
FT HELIX 16..40
FT /evidence="ECO:0007829|PDB:3R45"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3R45"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:3R45"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3R45"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3R45"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3R45"
SQ 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
