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 27-MAR-2024, entry version 157. 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; GN 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 Q8NCD3-1; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 130. DR CORUM; Q8NCD3; -. DR DIP; DIP-53282N; -. DR IntAct; Q8NCD3; 28. DR MINT; Q8NCD3; -. DR STRING; 9606.ENSP00000414109; -. DR GlyConnect; 2048; 3 N-Linked glycans (1 site). DR GlyCosmos; Q8NCD3; 1 site, 6 glycans. DR GlyGen; Q8NCD3; 2 sites, 6 N-linked glycans (1 site), 1 O-linked glycan (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; 9606-ENSP00000414109; -. DR PeptideAtlas; Q8NCD3; -. DR ProteomicsDB; 72875; -. [Q8NCD3-1] DR ProteomicsDB; 72876; -. [Q8NCD3-2] DR ProteomicsDB; 72877; -. [Q8NCD3-3] DR Pumba; Q8NCD3; -. DR Antibodypedia; 2018; 191 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 AGR; HGNC:25444; -. 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; 4638446at2759; -. 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; 716 hits in 1169 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 119 other cell types or tissues. DR ExpressionAtlas; Q8NCD3; baseline and differential. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. 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: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 Gene3D; 6.10.250.2320; -; 1. DR IDEAL; IID00283; -. DR InterPro; IPR022102; HJURP_C. DR InterPro; IPR021052; HJURP_central_dom. DR InterPro; IPR018465; Scm3/HJURP. DR PANTHER; PTHR15992; HOLLIDAY JUNCTION RECOGNITION PROTEIN; 1. DR PANTHER; PTHR15992:SF5; HOLLIDAY JUNCTION RECOGNITION PROTEIN; 1. DR Pfam; PF12347; HJURP_C; 2. DR Pfam; PF12346; HJURP_mid; 1. DR Pfam; PF10384; Scm3; 1. DR Genevisible; Q8NCD3; HS. 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 //