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Protein

Heterochromatin protein 1-binding protein 3

Gene

HP1BP3

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

Functioni

Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity (PubMed:24830416). Mediates chromatin condensation during hypoxia, leading to increased tumor cell viability, radio-resistance, chemo-resistance and self-renewal(PubMed:25100860).2 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • nucleosome binding Source: UniProtKB

GO - Biological processi

  • cellular response to hypoxia Source: UniProtKB
  • heterochromatin organization Source: UniProtKB
  • nucleosome assembly Source: InterPro
  • regulation of cell proliferation Source: UniProtKB
  • regulation of nucleus size Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterochromatin protein 1-binding protein 3
Alternative name(s):
Protein HP1-BP741 Publication
Gene namesi
Name:HP1BP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24973. HP1BP3.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB
  • nucleosome Source: InterPro
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671673.

Polymorphism and mutation databases

BioMutaiHP1BP3.
DMDMi74743691.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 553552Heterochromatin protein 1-binding protein 3PRO_0000339642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei142 – 1421Phosphoserine2 Publications
Modified residuei155 – 1551Phosphoserine1 Publication
Modified residuei156 – 1561Phosphoserine1 Publication
Modified residuei190 – 1901N6-acetyllysineBy similarity
Modified residuei248 – 2481Phosphoserine2 Publications
Modified residuei249 – 2491Phosphoserine2 Publications
Modified residuei441 – 4411Phosphoserine1 Publication
Modified residuei442 – 4421Phosphoserine1 Publication
Modified residuei446 – 4461Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5SSJ5.
PaxDbiQ5SSJ5.
PRIDEiQ5SSJ5.

PTM databases

PhosphoSiteiQ5SSJ5.

Expressioni

Gene expression databases

BgeeiQ5SSJ5.
CleanExiHS_HP1BP3.
ExpressionAtlasiQ5SSJ5. baseline and differential.
GenevisibleiQ5SSJ5. HS.

Organism-specific databases

HPAiHPA028215.
HPA054295.

Interactioni

Subunit structurei

Interacts (via PxVxL motif) with CBX5 (via Trp-174).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MEOX2A4D1273EBI-2880687,EBI-10172134

Protein-protein interaction databases

BioGridi119128. 63 interactions.
IntActiQ5SSJ5. 10 interactions.
MINTiMINT-4719917.

Structurei

Secondary structure

1
553
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi161 – 17515Combined sources
Helixi180 – 19011Combined sources
Helixi194 – 1974Combined sources
Turni198 – 2025Combined sources
Helixi203 – 21412Combined sources
Turni224 – 2263Combined sources
Turni231 – 2344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQPNMR-A153-237[»]
ProteinModelPortaliQ5SSJ5.
SMRiQ5SSJ5. Positions 153-237, 255-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SSJ5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini157 – 23276H15 1PROSITE-ProRule annotationAdd
BLAST
Domaini255 – 33076H15 2PROSITE-ProRule annotationAdd
BLAST
Domaini337 – 41377H15 3PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi255 – 2595PxVxL motif1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi454 – 553100Lys-richAdd
BLAST

Domaini

A central region that included the first H15 (linker histone H1/H5 globular) domain binds at the entry/exit site of the nucleosomal DNA.1 Publication

Sequence similaritiesi

Contains 3 H15 (linker histone H1/H5 globular) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG285312.
GeneTreeiENSGT00510000047652.
HOVERGENiHBG097678.
InParanoidiQ5SSJ5.
OMAiASMKQRG.
OrthoDBiEOG75QR72.
PhylomeDBiQ5SSJ5.
TreeFamiTF106395.

Family and domain databases

Gene3Di1.10.10.10. 3 hits.
InterProiIPR005818. Histone_H1/H5_H15.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 3 hits.
[Graphical view]
SMARTiSM00526. H15. 3 hits.
[Graphical view]
PROSITEiPS51504. H15. 3 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5SSJ5-1) [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
MATDTSQGEL VHPKALPLIV GAQLIHADKL GEKVEDSTMP IRRTVNSTRE
60 70 80 90 100
TPPKSKLAEG EEEKPEPDIS SEESVSTVEE QENETPPATS SEAEQPKGEP
110 120 130 140 150
ENEEKEENKS SEETKKDEKD QSKEKEKKVK KTIPSWATLS ASQLARAQKQ
160 170 180 190 200
TPMASSPRPK MDAILTEAIK ACFQKSGASV VAIRKYIIHK YPSLELERRG
210 220 230 240 250
YLLKQALKRE LNRGVIKQVK GKGASGSFVV VQKSRKTPQK SRNRKNRSSA
260 270 280 290 300
VDPEPQVKLE DVLPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL
310 320 330 340 350
LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI
360 370 380 390 400
AAMNEPKTCS TTALKKYVLE NHPGTNSNYQ MHLLKKTLQK CEKNGWMEQI
410 420 430 440 450
SGKGFSGTFQ LCFPYYPSPG VLFPKKEPDD SRDEDEDEDE SSEEDSEDEE
460 470 480 490 500
PPPKRRLQKK TPAKSPGKAA SVKQRGSKPA PKVSAAQRGK ARPLPKKAPP
510 520 530 540 550
KAKTPAKKTR PSSTVIKKPS GGSSKKPATS ARKEVKLPGK GKSTMKKSFR

VKK
Length:553
Mass (Da):61,207
Last modified:December 21, 2004 - v1
Checksum:iD18B28EE0156F09B
GO
Isoform 2 (identifier: Q5SSJ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Show »
Length:515
Mass (Da):57,211
Checksum:i130AD6B3FFD97525
GO
Isoform 3 (identifier: Q5SSJ5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: Missing.

Show »
Length:401
Mass (Da):44,435
Checksum:i31A31A118D2508B7
GO
Isoform 4 (identifier: Q5SSJ5-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-133: DEKDQSKEKEKKVKKTI → ERADSIHSTLFIIGQNS
     134-553: Missing.

Show »
Length:133
Mass (Da):14,594
Checksum:i87E1DE4A3A8FB907
GO

Sequence cautioni

The sequence AAF14871.1 differs from that shown. Reason: Frameshift at positions 226, 237 and 243. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621V → G in AAF14871 (PubMed:10931946).Curated
Sequence conflicti267 – 2671F → S in BAF83941 (PubMed:14702039).Curated
Sequence conflicti499 – 4991P → S in BAG64972 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 152152Missing in isoform 3. 2 PublicationsVSP_034168Add
BLAST
Alternative sequencei1 – 3838Missing in isoform 2. 1 PublicationVSP_034169Add
BLAST
Alternative sequencei117 – 13317DEKDQ…VKKTI → ERADSIHSTLFIIGQNS in isoform 4. 1 PublicationVSP_034170Add
BLAST
Alternative sequencei134 – 553420Missing in isoform 4. 1 PublicationVSP_034171Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113534 mRNA. Translation: AAF14871.1. Frameshift.
AK023129 mRNA. Translation: BAG51160.1.
AK291252 mRNA. Translation: BAF83941.1.
AK304065 mRNA. Translation: BAG64972.1.
AL833978 mRNA. Translation: CAD38822.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12528.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12530.1.
AL606477 Genomic DNA. Translation: CAI12531.1.
AL606477 Genomic DNA. Translation: CAI12532.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12533.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23387.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23388.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23389.1.
CH471134 Genomic DNA. Translation: EAW94953.1.
BC032139 mRNA. Translation: AAH32139.1.
BC045660 mRNA. Translation: AAH45660.1.
CCDSiCCDS30621.1. [Q5SSJ5-1]
RefSeqiNP_057371.2. NM_016287.3. [Q5SSJ5-1]
XP_005245932.1. XM_005245875.3. [Q5SSJ5-1]
XP_005245933.1. XM_005245876.3. [Q5SSJ5-1]
XP_005245934.1. XM_005245877.3. [Q5SSJ5-1]
XP_005245935.1. XM_005245878.3. [Q5SSJ5-1]
XP_005245936.1. XM_005245879.3. [Q5SSJ5-2]
UniGeneiHs.142442.

Genome annotation databases

EnsembliENST00000312239; ENSP00000312625; ENSG00000127483. [Q5SSJ5-1]
ENST00000375000; ENSP00000364139; ENSG00000127483. [Q5SSJ5-5]
ENST00000375003; ENSP00000364142; ENSG00000127483. [Q5SSJ5-3]
GeneIDi50809.
KEGGihsa:50809.
UCSCiuc001bdv.1. human. [Q5SSJ5-1]
uc001bea.2. human. [Q5SSJ5-2]
uc001beb.3. human. [Q5SSJ5-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113534 mRNA. Translation: AAF14871.1. Frameshift.
AK023129 mRNA. Translation: BAG51160.1.
AK291252 mRNA. Translation: BAF83941.1.
AK304065 mRNA. Translation: BAG64972.1.
AL833978 mRNA. Translation: CAD38822.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12528.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12530.1.
AL606477 Genomic DNA. Translation: CAI12531.1.
AL606477 Genomic DNA. Translation: CAI12532.1.
AL606477, AL663074 Genomic DNA. Translation: CAI12533.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23387.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23388.1.
AL663074, AL606477 Genomic DNA. Translation: CAI23389.1.
CH471134 Genomic DNA. Translation: EAW94953.1.
BC032139 mRNA. Translation: AAH32139.1.
BC045660 mRNA. Translation: AAH45660.1.
CCDSiCCDS30621.1. [Q5SSJ5-1]
RefSeqiNP_057371.2. NM_016287.3. [Q5SSJ5-1]
XP_005245932.1. XM_005245875.3. [Q5SSJ5-1]
XP_005245933.1. XM_005245876.3. [Q5SSJ5-1]
XP_005245934.1. XM_005245877.3. [Q5SSJ5-1]
XP_005245935.1. XM_005245878.3. [Q5SSJ5-1]
XP_005245936.1. XM_005245879.3. [Q5SSJ5-2]
UniGeneiHs.142442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQPNMR-A153-237[»]
ProteinModelPortaliQ5SSJ5.
SMRiQ5SSJ5. Positions 153-237, 255-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119128. 63 interactions.
IntActiQ5SSJ5. 10 interactions.
MINTiMINT-4719917.

PTM databases

PhosphoSiteiQ5SSJ5.

Polymorphism and mutation databases

BioMutaiHP1BP3.
DMDMi74743691.

Proteomic databases

MaxQBiQ5SSJ5.
PaxDbiQ5SSJ5.
PRIDEiQ5SSJ5.

Protocols and materials databases

DNASUi50809.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312239; ENSP00000312625; ENSG00000127483. [Q5SSJ5-1]
ENST00000375000; ENSP00000364139; ENSG00000127483. [Q5SSJ5-5]
ENST00000375003; ENSP00000364142; ENSG00000127483. [Q5SSJ5-3]
GeneIDi50809.
KEGGihsa:50809.
UCSCiuc001bdv.1. human. [Q5SSJ5-1]
uc001bea.2. human. [Q5SSJ5-2]
uc001beb.3. human. [Q5SSJ5-5]

Organism-specific databases

CTDi50809.
GeneCardsiGC01M021069.
HGNCiHGNC:24973. HP1BP3.
HPAiHPA028215.
HPA054295.
MIMi616072. gene.
neXtProtiNX_Q5SSJ5.
PharmGKBiPA142671673.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285312.
GeneTreeiENSGT00510000047652.
HOVERGENiHBG097678.
InParanoidiQ5SSJ5.
OMAiASMKQRG.
OrthoDBiEOG75QR72.
PhylomeDBiQ5SSJ5.
TreeFamiTF106395.

Miscellaneous databases

ChiTaRSiHP1BP3. human.
EvolutionaryTraceiQ5SSJ5.
GeneWikiiHP1BP3.
GenomeRNAii50809.
NextBioi53250.
PROiQ5SSJ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SSJ5.
CleanExiHS_HP1BP3.
ExpressionAtlasiQ5SSJ5. baseline and differential.
GenevisibleiQ5SSJ5. HS.

Family and domain databases

Gene3Di1.10.10.10. 3 hits.
InterProiIPR005818. Histone_H1/H5_H15.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 3 hits.
[Graphical view]
SMARTiSM00526. H15. 3 hits.
[Graphical view]
PROSITEiPS51504. H15. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hypothalamus.
  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] (ISOFORMS 1 AND 2).
    Tissue: Teratocarcinoma and Trachea.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 3 AND 4).
    Tissue: Brain and Testis.
  7. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 132-146; 176-184; 275-282; 284-291; 294-302 AND 312-329, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "The middle region of an HP1-binding protein, HP1-BP74, associates with linker DNA at the entry/exit site of nucleosomal DNA."
    Hayashihara K., Uchiyama S., Shimamoto S., Kobayashi S., Tomschik M., Wakamatsu H., No D., Sugahara H., Hori N., Noda M., Ohkubo T., Zlatanova J., Matsunaga S., Fukui K.
    J. Biol. Chem. 285:6498-6507(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBX5, DOMAIN, SUBCELLULAR LOCATION, STRUCTURE BY NMR OF 153-237.
  14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-142; SER-155; SER-156; SER-248 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-441; SER-442 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Profiling of the chromatin-associated proteome identifies HP1BP3 as a novel regulator of cell cycle progression."
    Dutta B., Ren Y., Hao P., Sim K.H., Cheow E., Adav S., Tam J.P., Sze S.K.
    Mol. Cell. Proteomics 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION.
  19. "Quantitative profiling of chromatome dynamics reveals a novel role for HP1BP3 in hypoxia-induced oncogenesis."
    Dutta B., Ren Y., Lim S.K., Tam J.P., Sze S.K.
    Mol. Cell. Proteomics 13:3236-3249(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.

Entry informationi

Entry nameiHP1B3_HUMAN
AccessioniPrimary (citable) accession number: Q5SSJ5
Secondary accession number(s): A6NI71
, A8K5D7, B3KMZ8, B4E210, Q05BI0, Q5SSJ6, Q5SWC6, Q6PIM9, Q8NDF0, Q9UHY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: December 21, 2004
Last modified: June 24, 2015
This is version 111 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.