HJURP_MOUSE
ID HJURP_MOUSE Reviewed; 667 AA.
AC Q6PG16; Q6BCZ4; Q8C9A7;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Holliday junction recognition protein;
DE AltName: Full=Fetal liver expressing gene 1 protein homolog;
DE Short=mFleg1;
GN Name=Hjurp; Synonyms=Fleg1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q8NCD3}.
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. Heterotrimer composed of HJURP, CENPA and
CC histone H4, where HJURP interacts with the dimer formed by CENPA and
CC histone H4 and prevents tetramerization of CENPA and H4. Identified in
CC a centromere complex containing histones H2A, H2B and H4, and at least
CC CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1.
CC Interacts with 14-3-3 family members in a phosphorylation-dependent
CC manner. Interacts with MSH5 and NBN. {ECO:0000250|UniProtKB:Q8NCD3}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PG16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PG16-2; Sequence=VSP_037516;
CC Name=3;
CC IsoId=Q6PG16-3; Sequence=VSP_037515;
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DR EMBL; AB162219; BAD36742.1; -; mRNA.
DR EMBL; AK042589; BAC31301.1; -; mRNA.
DR EMBL; BC057309; AAH57309.1; -; mRNA.
DR EMBL; BC131919; AAI31920.1; -; mRNA.
DR CCDS; CCDS15144.1; -. [Q6PG16-1]
DR RefSeq; NP_766093.1; NM_172505.4.
DR RefSeq; NP_941054.2; NM_198652.2.
DR RefSeq; XP_006529783.1; XM_006529720.3.
DR AlphaFoldDB; Q6PG16; -.
DR SMR; Q6PG16; -.
DR BioGRID; 237854; 3.
DR STRING; 10090.ENSMUSP00000054263; -.
DR iPTMnet; Q6PG16; -.
DR PhosphoSitePlus; Q6PG16; -.
DR EPD; Q6PG16; -.
DR jPOST; Q6PG16; -.
DR MaxQB; Q6PG16; -.
DR PaxDb; Q6PG16; -.
DR PRIDE; Q6PG16; -.
DR ProteomicsDB; 273143; -. [Q6PG16-1]
DR ProteomicsDB; 273144; -. [Q6PG16-2]
DR ProteomicsDB; 273145; -. [Q6PG16-3]
DR DNASU; 381280; -.
DR GeneID; 212427; -.
DR GeneID; 381280; -.
DR KEGG; mmu:212427; -.
DR KEGG; mmu:381280; -.
DR CTD; 55355; -.
DR MGI; MGI:2685821; Hjurp.
DR eggNOG; ENOG502SJZT; Eukaryota.
DR InParanoid; Q6PG16; -.
DR OrthoDB; 426984at2759; -.
DR PhylomeDB; Q6PG16; -.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR BioGRID-ORCS; 212427; 4 hits in 17 CRISPR screens.
DR BioGRID-ORCS; 381280; 24 hits in 71 CRISPR screens.
DR ChiTaRS; Hjurp; mouse.
DR PRO; PR:Q6PG16; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6PG16; protein.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0051101; P:regulation of DNA binding; ISO:MGI.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:MGI.
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 Alternative splicing; Cell cycle; Centromere; Chaperone; Chromosome;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..667
FT /note="Holliday junction recognition protein"
FT /id="PRO_0000378154"
FT REGION 78..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..301
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCD3"
FT VAR_SEQ 74..149
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_037515"
FT VAR_SEQ 286..302
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037516"
FT CONFLICT 12
FT /note="H -> Q (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="K -> N (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="S -> R (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="R -> T (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="E -> G (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="D -> N (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="P -> L (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="P -> H (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="S -> F (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="V -> G (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="S -> C (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="Y -> D (in Ref. 1; BAD36742, 2; BAC31301 and 3;
FT AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="A -> P (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 635..636
FT /note="DS -> EP (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="C -> R (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
FT CONFLICT 657..659
FT /note="FHD -> SHN (in Ref. 2; BAC31301 and 3; AAI31920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 74199 MW; 258747B28A1123C9 CRC64;
MESMGRQDRR LHQQLKESSS RFQTLMKRLI AKYNQPFEDD PLVEMRTLTY ETPQGLRVWG
GKLMKKEDKE YTQVIDRLNG QAPEGDSESS GADTSLEENW PSCSSAMREA SGDPRQRQPA
VPGNTLETDL RRKYLTQVDI LPQDEEYFKN AEKRGGKDTV MTWVPSVTSS VTPASGCQDA
ISAKSSGGPE VSALSSRGQG PSYPCPADMA IVARSDGLSL LGTSSNSVSS QSFEVDDLCN
VTISDLYEGM MHSMSRLLRS KPSCIISTKT YINQSWKLRR RPSRKQGLHK NRTHCPRSKP
SQRSARKGPA SCSEPGKEAG ILRDYGNLLH VAPHKTGLEL KSVSLEGSKR QVHKSSPAWK
ELQMMPQKDL DLNRERENRV MTLQWLISPV KVVPRPRMLP SQVEKWYREI KIKFDKLHQE
YCLSSGKQPR LTDPTESWAV DVYRSGSKSP GSRQDVETCR PSSPFGREKT ERPGEALEDL
RGNGKSVKTK SCLLRSCPSP EGSPSRSPSH SQLSSGLQEH NSEPTGKAVW PSTAISAPSI
GSPGCGKDNY YELKKEFNRL YQKYCLSPQR AKVTSCGRVS PMKAAAALPC QSEHLKRLNP
DSPQQSSQKR SISPGCHRRV LQDSTAQTAS TLVRDSWLPT KRCKLSYPVA CAHQAKFHDT
SGASGWP
