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Protein

Ubinuclein-1

Gene

UBN1

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

Functioni

Acts as a novel regulator of senescence. Involved in the formation of senescence-associated heterochromatin foci (SAHF), which represses expression of proliferation-promoting genes. Binds to proliferation-promoting genes. May be required for replication-independent chromatin assembly.2 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • DNA replication-independent nucleosome assembly Source: UniProtKB
  • negative regulation of phosphatase activity Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Names & Taxonomyi

Protein namesi
Recommended name:
Ubinuclein-1
Alternative name(s):
HIRA-binding protein
Protein VT4
Ubiquitously expressed nuclear protein
Gene namesi
Name:UBN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:12506. UBN1.

Subcellular locationi

  • Nucleusnucleoplasm
  • NucleusPML body
  • Cell junctiontight junction

  • Note: Localized as a nuclear speckled-like pattern in proliferating primary fibroblasts. Colocalizes with HIRA, PML and SP100 in PML bodies of senescent cells. Colocalizes with TJP1 and CLDN1. Detected along the upper granular cell layer of epidermis. When overexpressed, accumulates in the nucleus in cells showing defective cytokinesis.

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: ProtInc
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Nucleus, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381F → E: Strongly diminishes interaction with HIRA; when associated with E-139 and L-140.
Mutagenesisi139 – 1391I → E: Strongly diminishes interaction with HIRA; when associated with E-138 and L-140.
Mutagenesisi140 – 1401D → L: Strongly diminishes interaction with HIRA; when associated with E-138 and L-139.
Mutagenesisi160 – 1601F → E: Strongly diminishes interaction with HIRA. 1 Publication
Mutagenesisi162 – 1621I → E: Strongly diminishes interaction with HIRA. 1 Publication

Organism-specific databases

PharmGKBiPA37153.

Polymorphism and mutation databases

DMDMi116242836.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11341134Ubinuclein-1PRO_0000065712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731PhosphoserineCombined sources
Modified residuei175 – 1751PhosphoserineCombined sources
Modified residuei222 – 2221N6-acetyllysineCombined sources
Modified residuei323 – 3231PhosphoserineCombined sources
Modified residuei336 – 3361PhosphoserineCombined sources
Modified residuei338 – 3381PhosphoserineCombined sources
Modified residuei493 – 4931PhosphoserineCombined sources
Modified residuei660 – 6601PhosphoserineCombined sources
Modified residuei677 – 6771PhosphoserineCombined sources
Modified residuei1025 – 10251PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NPG3.
MaxQBiQ9NPG3.
PaxDbiQ9NPG3.
PeptideAtlasiQ9NPG3.
PRIDEiQ9NPG3.

PTM databases

iPTMnetiQ9NPG3.

Expressioni

Tissue specificityi

Ubiquitous. Also expressed in numerous tumors and cancer cell lines.2 Publications

Gene expression databases

BgeeiQ9NPG3.
CleanExiHS_UBN1.
ExpressionAtlasiQ9NPG3. baseline and differential.
GenevisibleiQ9NPG3. HS.

Interactioni

Subunit structurei

Component of a complex that includes at least ASF1A, CABIN1, HIRA, histone H3.3 and UBN1. Interacts with Epstein-Barr virus BZLF1. Interacts with HIRA (via WD repeat domain); the interaction is direct. Interacts with ASF1A, CEBPA, TJP1, TJP2 and TJP3.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIRAP5419810EBI-2880187,EBI-372342

Protein-protein interaction databases

BioGridi118934. 13 interactions.
IntActiQ9NPG3. 8 interactions.
MINTiMINT-6944820.
STRINGi9606.ENSP00000262376.

Structurei

Secondary structure

1
1134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi123 – 1275Combined sources
Turni128 – 1314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZBJX-ray2.25D122-148[»]
ProteinModelPortaliQ9NPG3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 166166Sufficient for interaction with HIRAAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili479 – 54264Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi181 – 26181Lys-richAdd
BLAST
Compositional biasi862 – 1042181Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the ubinuclein family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IPMD. Eukaryota.
ENOG410XREY. LUCA.
GeneTreeiENSGT00530000063595.
HOGENOMiHOG000154753.
HOVERGENiHBG059815.
InParanoidiQ9NPG3.
KOiK17492.
OMAiRRIMGPR.
OrthoDBiEOG75B866.
PhylomeDBiQ9NPG3.
TreeFamiTF326088.

Family and domain databases

InterProiIPR014840. HRD.
IPR026936. Ubinuclein-1.
IPR026947. UBN_middle_dom.
[Graphical view]
PANTHERiPTHR21669:SF12. PTHR21669:SF12. 2 hits.
PfamiPF08729. HUN. 1 hit.
PF14075. UBN_AB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NPG3-1) [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
MSEPHRVQFT SLPGSLNPAF LKKSRKEEAG AGEQHQDCEP AAAAVRITLT
60 70 80 90 100
LFEPDHKRCP EFFYPELVKN IRGKVKGLQP GDKKKDLSDP FNDEEKERHK
110 120 130 140 150
VEALARKFEE KYGGKKRRKD RIQDLIDMGY GYDESDSFID NSEAYDELVP
160 170 180 190 200
ASLTTKYGGF YINSGTLQFR QASESEDDFI KEKKKKSPKK RKLKEGGEKI
210 220 230 240 250
KKKKKDDTYD KEKKSKKSKF SKAGFTALNA SKEKKKKKYS GALSVKEMLK
260 270 280 290 300
KFQKEKEAQK KREEEHKPVA VPSAEAQGLR ELEGASDPLL SLFGSTSDND
310 320 330 340 350
LLQAATAMDS LTDLDLEHLL SESPEGSPFR DMDDGSDSLG VGLDQEFRQP
360 370 380 390 400
SSLPEGLPAP LEKRVKELAQ AARAAEGESR QKFFTQDING ILLDIEAQTR
410 420 430 440 450
ELSSQVRSGV YAYLASFLPC SKDALLKRAR KLHLYEQGGR LKEPLQKLKE
460 470 480 490 500
AIGRAMPEQM AKYQDECQAH TQAKVAKMLE EEKDKEQRDR ICSDEEEDEE
510 520 530 540 550
KGGRRIMGPR KKFQWNDEIR ELLCQVVKIK LESQDLERNN KAQAWEDCVK
560 570 580 590 600
GFLDAEVKPL WPKGWMQART LFKESRRGHG HLTSILAKKK VMAPSKIKVK
610 620 630 640 650
ESSTKPDKKV SVPSGQIGGP IALPSDHQTG GLSIGASSRE LPSQASGGLA
660 670 680 690 700
NPPPVNLEDS LDEDLIRNPA SSVEAVSKEL AALNSRAAGN SEFTLPAPSK
710 720 730 740 750
APAEKVGGVL CTEEKRNFAK PSPSAPPPAS SLQSPLNFLA EQALALGQSS
760 770 780 790 800
QEKKPESSGY KELSCQAPLN KGLPEVHQSK AKHHSLPRTS HGPQVAVPVP
810 820 830 840 850
GPQVKVFHAG TQQQKNFTPP SPFANKLQGP KASPTQCHRS LLQLVKTAAK
860 870 880 890 900
GQGFHPSAPA TSGGLSASSS SSHKTPASSS SALSHPAKPH SVSSAGSSYK
910 920 930 940 950
NNPFASSISK HGVSSGSSSS GGTPVQSSVS GSLVPGIQPP SVGQATSRPV
960 970 980 990 1000
PSSAGKKMPV SQKLTLVAPP GGPNGDSSGG TQGVAKLLTS PSLKPSAVSS
1010 1020 1030 1040 1050
VTSSTSLSKG ASGTVLLAGS SLMASPYKSS SPKLSGAMSS NSLGIITPVP
1060 1070 1080 1090 1100
IPVHVLSFSA DSSAKAGVSK DAIVTGPAPG SFHHGLGHSL LAGLHSSPPH
1110 1120 1130
AAPLPHAAVP THIPQSLPGA SQLHGKGPAV PRKL
Length:1,134
Mass (Da):121,520
Last modified:October 17, 2006 - v2
Checksum:i8DE68C63D4E8E01B
GO
Isoform 2 (identifier: Q9NPG3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1090-1119: Missing.

Show »
Length:1,104
Mass (Da):118,554
Checksum:iB3F257D8DB385A2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191K → N in BAH13219 (PubMed:14702039).Curated
Sequence conflicti276 – 2761A → V in AAF31755 (PubMed:10725330).Curated
Sequence conflicti276 – 2761A → V in AAF31756 (PubMed:10725330).Curated
Sequence conflicti277 – 2771Q → H in BAH13219 (PubMed:14702039).Curated
Sequence conflicti718 – 7181F → L in AAF31755 (PubMed:10725330).Curated
Sequence conflicti718 – 7181F → L in AAF31756 (PubMed:10725330).Curated
Sequence conflicti945 – 9451A → P in AAF31755 (PubMed:10725330).Curated
Sequence conflicti945 – 9451A → P in AAF31756 (PubMed:10725330).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti435 – 4351Y → C.
Corresponds to variant rs35103368 [ dbSNP | Ensembl ].
VAR_051465

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1090 – 111930Missing in isoform 2. 1 PublicationVSP_036971Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF108460 mRNA. Translation: AAF31755.1.
AF108461 mRNA. Translation: AAF31756.1.
AF108459
, AF108454, AF108455, AF108456, AF108457, AF108458 Genomic DNA. Translation: AAF34869.1.
AK300131 mRNA. Translation: BAH13219.1.
AC020663 Genomic DNA. No translation available.
AC027687 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85249.1.
CH471112 Genomic DNA. Translation: EAW85250.1.
U19346 mRNA. Translation: AAA64188.1.
CCDSiCCDS10525.1. [Q9NPG3-1]
CCDS73822.1. [Q9NPG3-2]
PIRiG01628.
RefSeqiNP_001072982.1. NM_001079514.2. [Q9NPG3-1]
NP_001275585.1. NM_001288656.1. [Q9NPG3-2]
UniGeneiHs.440219.

Genome annotation databases

EnsembliENST00000262376; ENSP00000262376; ENSG00000118900. [Q9NPG3-1]
ENST00000396658; ENSP00000379894; ENSG00000118900. [Q9NPG3-1]
ENST00000590769; ENSP00000468740; ENSG00000118900. [Q9NPG3-2]
GeneIDi29855.
KEGGihsa:29855.
UCSCiuc002cyb.5. human. [Q9NPG3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF108460 mRNA. Translation: AAF31755.1.
AF108461 mRNA. Translation: AAF31756.1.
AF108459
, AF108454, AF108455, AF108456, AF108457, AF108458 Genomic DNA. Translation: AAF34869.1.
AK300131 mRNA. Translation: BAH13219.1.
AC020663 Genomic DNA. No translation available.
AC027687 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85249.1.
CH471112 Genomic DNA. Translation: EAW85250.1.
U19346 mRNA. Translation: AAA64188.1.
CCDSiCCDS10525.1. [Q9NPG3-1]
CCDS73822.1. [Q9NPG3-2]
PIRiG01628.
RefSeqiNP_001072982.1. NM_001079514.2. [Q9NPG3-1]
NP_001275585.1. NM_001288656.1. [Q9NPG3-2]
UniGeneiHs.440219.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZBJX-ray2.25D122-148[»]
ProteinModelPortaliQ9NPG3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118934. 13 interactions.
IntActiQ9NPG3. 8 interactions.
MINTiMINT-6944820.
STRINGi9606.ENSP00000262376.

PTM databases

iPTMnetiQ9NPG3.

Polymorphism and mutation databases

DMDMi116242836.

Proteomic databases

EPDiQ9NPG3.
MaxQBiQ9NPG3.
PaxDbiQ9NPG3.
PeptideAtlasiQ9NPG3.
PRIDEiQ9NPG3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262376; ENSP00000262376; ENSG00000118900. [Q9NPG3-1]
ENST00000396658; ENSP00000379894; ENSG00000118900. [Q9NPG3-1]
ENST00000590769; ENSP00000468740; ENSG00000118900. [Q9NPG3-2]
GeneIDi29855.
KEGGihsa:29855.
UCSCiuc002cyb.5. human. [Q9NPG3-1]

Organism-specific databases

CTDi29855.
GeneCardsiUBN1.
H-InvDBHIX0012793.
HGNCiHGNC:12506. UBN1.
MIMi609771. gene.
neXtProtiNX_Q9NPG3.
PharmGKBiPA37153.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPMD. Eukaryota.
ENOG410XREY. LUCA.
GeneTreeiENSGT00530000063595.
HOGENOMiHOG000154753.
HOVERGENiHBG059815.
InParanoidiQ9NPG3.
KOiK17492.
OMAiRRIMGPR.
OrthoDBiEOG75B866.
PhylomeDBiQ9NPG3.
TreeFamiTF326088.

Enzyme and pathway databases

ReactomeiR-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

ChiTaRSiUBN1. human.
GenomeRNAii29855.
PROiQ9NPG3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPG3.
CleanExiHS_UBN1.
ExpressionAtlasiQ9NPG3. baseline and differential.
GenevisibleiQ9NPG3. HS.

Family and domain databases

InterProiIPR014840. HRD.
IPR026936. Ubinuclein-1.
IPR026947. UBN_middle_dom.
[Graphical view]
PANTHERiPTHR21669:SF12. PTHR21669:SF12. 2 hits.
PfamiPF08729. HUN. 1 hit.
PF14075. UBN_AB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ubinuclein, a novel nuclear protein interacting with cellular and viral transcription factors."
    Aho S., Buisson M., Pajunen T., Ryoo Y.W., Giot J.-F., Gruffat H., Sergeant A., Uitto J.
    J. Cell Biol. 148:1165-1176(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), INTERACTION WITH EPSTEIN-BARR VIRUS BZLF1 AND CEBPA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "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] (ISOFORM 2).
    Tissue: Placenta.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Tesmer V., Babin J., Rajadhyaksha A., Bina M.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 348-691 (ISOFORM 1).
    Tissue: Cervix carcinoma.
  6. "Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis."
    Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.
    Cell 116:51-61(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ASF1A; CABIN1; HIRA AND HISTONE H3.3.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NACos)."
    Aho S., Lupo J., Coly P.-A., Sabine A., Castellazzi M., Morand P., Sergeant A., Manet E., Boyer V., Gruffat H.
    Biol. Cell 101:319-334(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TJP1; TJP2 AND TJP3, SUBCELLULAR LOCATION.
  9. "Human UBN1 is an ortholog of yeast Hpc2p and has an essential role in the HIRA/ASF1a chromatin-remodeling pathway in senescent cells."
    Banumathy G., Somaiah N., Zhang R., Tang Y., Hoffmann J., Andrake M., Ceulemans H., Schultz D., Marmorstein R., Adams P.D.
    Mol. Cell. Biol. 29:758-770(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH ASF1A AND HIRA, SUBCELLULAR LOCATION, MUTAGENESIS OF 138-PHE--ASP-140; PHE-160 AND ILE-162, TISSUE SPECIFICITY.
  10. "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-336; SER-660; SER-677 AND SER-1025, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-336; SER-338 AND SER-660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-493 AND SER-660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiUBN1_HUMAN
AccessioniPrimary (citable) accession number: Q9NPG3
Secondary accession number(s): B7Z6D3
, D3DUE8, Q13079, Q9P1P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 17, 2006
Last modified: June 8, 2016
This is version 117 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 16
    Human chromosome 16: 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
  6. SIMILARITY comments
    Index of protein domains and families

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.