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Protein

Holliday junction recognition protein

Gene

HJURP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • histone binding Source: UniProtKB
  • identical protein binding Source: IntAct

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • CENP-A containing nucleosome assembly Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • regulation of DNA binding Source: UniProtKB
  • regulation of protein complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Names & Taxonomyi

Protein namesi
Recommended name:
Holliday junction recognition protein
Alternative name(s):
14-3-3-associated AKT substrate
Fetal liver-expressing gene 1 protein
Up-regulated in lung cancer 9
Gene namesi
Name:HJURP
Synonyms:FAKTS, FLEG1Imported, URLC9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:25444. HJURP.

Subcellular locationi

  • Nucleusnucleolus
  • Chromosomecentromere

  • 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.

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB
  • cytoplasm Source: HPA
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi486 – 4861S → A: Loss of phosphorylation by AKT1 and binding to YWHAG. 1 Publication

Organism-specific databases

PharmGKBiPA162390937.

Polymorphism and mutation databases

BioMutaiHJURP.
DMDMi239938642.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 748748Holliday junction recognition proteinPRO_0000287433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei123 – 1231PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineCombined sources
Modified residuei185 – 1851PhosphoserineCombined sources
Modified residuei412 – 4121PhosphoserineBy similarity
Modified residuei448 – 4481PhosphoserineCombined sources
Modified residuei473 – 4731PhosphoserineCombined sources
Modified residuei486 – 4861Phosphoserine; by PKB/AKT11 Publication
Modified residuei595 – 5951PhosphoserineCombined sources
Modified residuei642 – 6421PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8NCD3.
MaxQBiQ8NCD3.
PaxDbiQ8NCD3.
PRIDEiQ8NCD3.

PTM databases

iPTMnetiQ8NCD3.
PhosphoSiteiQ8NCD3.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ8NCD3.
CleanExiHS_HJURP.
ExpressionAtlasiQ8NCD3. baseline and differential.
GenevisibleiQ8NCD3. HS.

Organism-specific databases

HPAiHPA008436.
HPA027261.

Interactioni

Subunit structurei

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. 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. Interacts with 14-3-3 family members in a phosphorylation-dependent manner. Interacts with MSH5 and NBN.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-719429,EBI-719429
CENPAP4945015EBI-719429,EBI-1751979

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi120635. 23 interactions.
DIPiDIP-53282N.
IntActiQ8NCD3. 7 interactions.
MINTiMINT-1402926.
STRINGi9606.ENSP00000414109.

Structurei

Secondary structure

1
748
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 4025Combined sources
Beta strandi49 – 513Combined sources
Turni52 – 554Combined sources
Beta strandi56 – 594Combined sources
Beta strandi62 – 654Combined sources
Beta strandi70 – 734Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R45X-ray2.60C1-80[»]
ProteinModelPortaliQ8NCD3.
SMRiQ8NCD3. Positions 14-74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IW66. Eukaryota.
ENOG4111C4D. LUCA.
GeneTreeiENSGT00390000005575.
HOGENOMiHOG000112909.
HOVERGENiHBG062573.
InParanoidiQ8NCD3.
OMAiYAGMLHS.
OrthoDBiEOG7N8ZVF.
PhylomeDBiQ8NCD3.
TreeFamiTF336293.

Family and domain databases

InterProiIPR021052. HJURP.
IPR022102. HJURP_C.
IPR018465. Scm3/HJURP.
[Graphical view]
PfamiPF12347. HJURP_C. 2 hits.
PF12346. HJURP_mid. 1 hit.
PF10384. Scm3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NCD3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLGTLRAMEG EDVEDDQLLQ KLRASRRRFQ RRMQRLIEKY NQPFEDTPVV
60 70 80 90 100
QMATLTYETP QGLRIWGGRL IKERNEGEIQ DSSMKPADRT DGSVQAAAWG
110 120 130 140 150
PELPSHRTVL GADSKSGEVD ATSDQEESVA WALAPAVPQS PLKNELRRKY
160 170 180 190 200
LTQVDILLQG AEYFECAGNR AGRDVRVTPL PSLASPAVPA PGYCSRISRK
210 220 230 240 250
SPGDPAKPAS SPREWDPLHP SSTDMALVPR NDSLSLQETS SSSFLSSQPF
260 270 280 290 300
EDDDICNVTI SDLYAGMLHS MSRLLSTKPS SIISTKTFIM QNWNSRRRHR
310 320 330 340 350
YKSRMNKTYC KGARRSQRSS KENFIPCSEP VKGTGALRDC KNVLDVSCRK
360 370 380 390 400
TGLKLEKAFL EVNRPQIHKL DPSWKERKVT PSKYSSLIYF DSSATYNLDE
410 420 430 440 450
ENRFRTLKWL ISPVKIVSRP TIRQGHGENR QREIEIRFDQ LHREYCLSPR
460 470 480 490 500
NQPRRMCLPD SWAMNMYRGG PASPGGLQGL ETRRLSLPSS KAKAKSLSEA
510 520 530 540 550
FENLGKRSLE AGRCLPKSDS SSSLPKTNPT HSATRPQQTS DLHVQGNSSG
560 570 580 590 600
IFRKSVSPSK TLSVPDKEVP GHGRNRYDEI KEEFDKLHQK YCLKSPGQMT
610 620 630 640 650
VPLCIGVSTD KASMEVRYQT EGFLGKLNPD PHFQGFQKLP SSPLGCRKSL
660 670 680 690 700
LGSTAIEAPS STCVARAITR DGTRDHQFPA KRPRLSEPQG SGRQGNSLGA
710 720 730 740
SDGVDNTVRP GDQGSSSQPN SEERGENTSY RMEEKSDFML EKLETKSV
Length:748
Mass (Da):83,539
Last modified:June 16, 2009 - v2
Checksum:iDE7F1410F9A748D5
GO
Isoform 2 (identifier: Q8NCD3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-134: Missing.

Note: No experimental confirmation available.
Show »
Length:694
Mass (Da):77,971
Checksum:iCF6B285E45EDACC0
GO
Isoform 3 (identifier: Q8NCD3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-165: Missing.

Note: No experimental confirmation available.
Show »
Length:663
Mass (Da):74,372
Checksum:i714B1621C5107AC6
GO

Sequence cautioni

The sequence CAB82391.2 differs from that shown. Reason: Erroneous termination at position 437. Translated as Arg.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti613 – 6131S → C in BAG63122 (PubMed:14702039).Curated
Sequence conflicti733 – 7331E → G in BAG63122 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41T → A.
Corresponds to variant rs2302154 [ dbSNP | Ensembl ].
VAR_056912
Natural varianti76 – 761E → K.4 Publications
Corresponds to variant rs2286430 [ dbSNP | Ensembl ].
VAR_057946
Natural varianti199 – 1991R → G.3 Publications
Corresponds to variant rs3806589 [ dbSNP | Ensembl ].
VAR_057947
Natural varianti295 – 2951S → C.4 Publications
Corresponds to variant rs3732215 [ dbSNP | Ensembl ].
VAR_057948
Natural varianti548 – 5481S → T.
Corresponds to variant rs17863822 [ dbSNP | Ensembl ].
VAR_056913
Natural varianti549 – 5491S → C.1 Publication
Corresponds to variant rs3821238 [ dbSNP | Ensembl ].
VAR_056914
Natural varianti568 – 5681E → D.
Corresponds to variant rs3771333 [ dbSNP | Ensembl ].
VAR_056915
Natural varianti691 – 6911S → F.1 Publication
Corresponds to variant rs12582 [ dbSNP | Ensembl ].
VAR_056916
Natural varianti723 – 7231E → G.1 Publication
Corresponds to variant rs10511 [ dbSNP | Ensembl ].
VAR_057949

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei81 – 16585Missing in isoform 3. 1 PublicationVSP_037467Add
BLAST
Alternative sequencei81 – 13454Missing in isoform 2. 1 PublicationVSP_037468Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB101211 mRNA. Translation: BAF82039.1.
AB162218 mRNA. Translation: BAD36741.1.
AK301643 mRNA. Translation: BAG63122.1.
AK303109 mRNA. Translation: BAG64216.1.
AK074809 mRNA. Translation: BAC11221.1.
AC005538 Genomic DNA. No translation available.
BC001940 mRNA. Translation: AAH01940.2.
AL162048 mRNA. Translation: CAB82391.2. Sequence problems.
CCDSiCCDS33406.1. [Q8NCD3-1]
CCDS63166.1. [Q8NCD3-3]
CCDS63167.1. [Q8NCD3-2]
PIRiT47163.
RefSeqiNP_001269891.1. NM_001282962.1. [Q8NCD3-2]
NP_001269892.1. NM_001282963.1. [Q8NCD3-3]
NP_060880.3. NM_018410.4. [Q8NCD3-1]
UniGeneiHs.532968.

Genome annotation databases

EnsembliENST00000411486; ENSP00000414109; ENSG00000123485. [Q8NCD3-1]
ENST00000432087; ENSP00000407208; ENSG00000123485. [Q8NCD3-2]
ENST00000441687; ENSP00000401944; ENSG00000123485. [Q8NCD3-3]
GeneIDi55355.
KEGGihsa:55355.
UCSCiuc002vvg.5. human. [Q8NCD3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB101211 mRNA. Translation: BAF82039.1.
AB162218 mRNA. Translation: BAD36741.1.
AK301643 mRNA. Translation: BAG63122.1.
AK303109 mRNA. Translation: BAG64216.1.
AK074809 mRNA. Translation: BAC11221.1.
AC005538 Genomic DNA. No translation available.
BC001940 mRNA. Translation: AAH01940.2.
AL162048 mRNA. Translation: CAB82391.2. Sequence problems.
CCDSiCCDS33406.1. [Q8NCD3-1]
CCDS63166.1. [Q8NCD3-3]
CCDS63167.1. [Q8NCD3-2]
PIRiT47163.
RefSeqiNP_001269891.1. NM_001282962.1. [Q8NCD3-2]
NP_001269892.1. NM_001282963.1. [Q8NCD3-3]
NP_060880.3. NM_018410.4. [Q8NCD3-1]
UniGeneiHs.532968.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R45X-ray2.60C1-80[»]
ProteinModelPortaliQ8NCD3.
SMRiQ8NCD3. Positions 14-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120635. 23 interactions.
DIPiDIP-53282N.
IntActiQ8NCD3. 7 interactions.
MINTiMINT-1402926.
STRINGi9606.ENSP00000414109.

PTM databases

iPTMnetiQ8NCD3.
PhosphoSiteiQ8NCD3.

Polymorphism and mutation databases

BioMutaiHJURP.
DMDMi239938642.

Proteomic databases

EPDiQ8NCD3.
MaxQBiQ8NCD3.
PaxDbiQ8NCD3.
PRIDEiQ8NCD3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000411486; ENSP00000414109; ENSG00000123485. [Q8NCD3-1]
ENST00000432087; ENSP00000407208; ENSG00000123485. [Q8NCD3-2]
ENST00000441687; ENSP00000401944; ENSG00000123485. [Q8NCD3-3]
GeneIDi55355.
KEGGihsa:55355.
UCSCiuc002vvg.5. human. [Q8NCD3-1]

Organism-specific databases

CTDi55355.
GeneCardsiHJURP.
H-InvDBHIX0002938.
HGNCiHGNC:25444. HJURP.
HPAiHPA008436.
HPA027261.
MIMi612667. gene.
neXtProtiNX_Q8NCD3.
PharmGKBiPA162390937.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IW66. Eukaryota.
ENOG4111C4D. LUCA.
GeneTreeiENSGT00390000005575.
HOGENOMiHOG000112909.
HOVERGENiHBG062573.
InParanoidiQ8NCD3.
OMAiYAGMLHS.
OrthoDBiEOG7N8ZVF.
PhylomeDBiQ8NCD3.
TreeFamiTF336293.

Enzyme and pathway databases

ReactomeiR-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Miscellaneous databases

ChiTaRSiHJURP. human.
GenomeRNAii55355.
PROiQ8NCD3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NCD3.
CleanExiHS_HJURP.
ExpressionAtlasiQ8NCD3. baseline and differential.
GenevisibleiQ8NCD3. HS.

Family and domain databases

InterProiIPR021052. HJURP.
IPR022102. HJURP_C.
IPR018465. Scm3/HJURP.
[Graphical view]
PfamiPF12347. HJURP_C. 2 hits.
PF12346. HJURP_mid. 1 hit.
PF10384. Scm3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Activation of Holliday junction recognizing protein involved in the chromosomal stability and immortality of cancer cells."
    Kato T., Sato N., Hayama S., Yamabuki T., Ito T., Miyamoto M., Kondo S., Nakamura Y., Daigo Y.
    Cancer Res. 67:8544-8553(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH MSH5 AND NBN, DNA-BINDING, TISSUE SPECIFICITY, VARIANTS LYS-76; GLY-199 AND CYS-295.
  2. "Impaired cytoplasmic localization and nuclear accumulation of a novel gene product, hFLEG1, associated with hepatocellular carcinoma development."
    Koike N., Sumii M., Ikura T., Masuda Y., Wakida K., Uchida T., Asahara T., Usui T., Shimamoto F., Chayama K., Fukumoto M., Kamiya K.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LYS-76; GLY-199 AND CYS-295.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANTS LYS-76; GLY-199; CYS-295; CYS-549; PHE-691 AND GLY-723.
    Tissue: Esophagus, TeratocarcinomaImported and Thymus.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    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.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS LYS-76 AND CYS-295.
    Tissue: LungImported.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-748.
    Tissue: Melanoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CENPA.
  9. "Identification of FAKTS as a novel 14-3-3-associated nuclear protein."
    Luhn P., Wang H., Marcus A.I., Fu H.
    Proteins 67:479-489(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH 14-3-3 PROTEINS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-486, MUTAGENESIS OF SER-486.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-448; SER-473 AND SER-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Centromere-specific assembly of CENP-A nucleosomes is mediated by HJURP."
    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.
    Cell 137:472-484(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPA.
  15. "HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres."
    Dunleavy E.M., Roche D., Tagami H., Lacoste N., Ray-Gallet D., Nakamura Y., Daigo Y., Nakatani Y., Almouzni-Pettinotti G.
    Cell 137:485-497(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPA.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-140 AND SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP."
    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.
    Genes Dev. 25:901-906(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-80 IN COMPLEX WITH CENPA AND HISTONE H4, SUBUNIT.

Entry informationi

Entry nameiHJURP_HUMAN
AccessioniPrimary (citable) accession number: Q8NCD3
Secondary accession number(s): A8IRH5
, B4DWR0, B4DZV4, Q9BUT2, Q9NSL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 16, 2009
Last modified: June 8, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.