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Q3TEA8 (HP1B3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterochromatin protein 1-binding protein 3
Gene names
Name:Hp1bp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of heterochromatin, may be involved in chromatin structure and function. Ref.4

Subunit structure

Interacts with CBX5. Ref.4

Subcellular location

Nucleus By similarity. Chromosome By similarity.

Sequence similarities

Contains 3 H15 (linker histone H1/H5 globular) domains.

Sequence caution

The sequence BAC35912.1 differs from that shown. Reason: Frameshift at positions 13 and 313.

Ontologies

Keywords
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3TEA8-1)

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.
Isoform 2 (identifier: Q3TEA8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     67-79: Missing.
Isoform 3 (identifier: Q3TEA8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-38: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 554553Heterochromatin protein 1-binding protein 3
PRO_0000339643

Regions

Domain159 – 23476H15 1
Domain255 – 33076H15 2
Domain337 – 41377H15 3
Compositional bias59 – 12870Glu-rich
Compositional bias432 – 44110Poly-Asp
Compositional bias455 – 554100Lys-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue61Phosphoserine By similarity
Modified residue1441Phosphoserine By similarity
Modified residue1571Phosphoserine By similarity
Modified residue1581Phosphoserine By similarity
Modified residue1921N6-acetyllysine Ref.5
Modified residue2491Phosphoserine By similarity
Modified residue4431Phosphoserine By similarity
Modified residue4441Phosphoserine By similarity
Modified residue4471Phosphoserine By similarity

Natural variations

Alternative sequence2 – 3837Missing in isoform 3.
VSP_034174
Alternative sequence67 – 7913Missing in isoform 2.
VSP_034175

Experimental info

Sequence conflict681D → N in BAE36164. Ref.1
Sequence conflict1101N → S in CAA67961. Ref.4
Sequence conflict1101N → S in AAH20024. Ref.3
Sequence conflict1111K → E in BAB23683. Ref.1
Sequence conflict1741C → S in CAM18860. Ref.2
Sequence conflict1741C → S in CAM18863. Ref.2
Sequence conflict1971G → D in CAA67961. Ref.4
Sequence conflict1971G → D in AAH04053. Ref.3
Sequence conflict1971G → D in AAH20024. Ref.3
Sequence conflict2191R → K in CAA67961. Ref.4
Sequence conflict2191R → K in AAH04053. Ref.3
Sequence conflict2191R → K in AAH20024. Ref.3
Sequence conflict2471Missing in BAC25794. Ref.1
Sequence conflict4031K → R in BAE38604. Ref.1
Sequence conflict4361E → D in AAH04053. Ref.3
Sequence conflict4361E → D in AAH20024. Ref.3
Sequence conflict440 – 4412Missing in AAH04053. Ref.3
Sequence conflict5471K → E in BAE36164. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: A49C4F7C42D1BE64

FASTA55460,867
        10         20         30         40         50         60 
MATDMSQGEL IHPKALPLIV GAQLIHADKL GEKAEDTTMP IRRAVNSTRE TPPKSKLAEG 

        70         80         90        100        110        120 
EEEKPEPDGS SEESISTVEE QENETPPATS SEAEQPKGEP ESGEKEENNN KSAEEPKKDE 

       130        140        150        160        170        180 
KDQSKEKEKK VKKTIPAWAT LSASQLARAQ RQTPMASSPR PKMDAILTEA IKACFQKTGA 

       190        200        210        220        230        240 
SVVAIRKYII HKYPSLGLER RGYLLKQALK RELNRGVIRQ VKGKGASGSF VVVQKSKPPQ 

       250        260        270        280        290        300 
KSKNRKKGSA LDPEPQVKLE DVLPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL 

       310        320        330        340        350        360 
LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI AAMNEPKTCS 

       370        380        390        400        410        420 
TTALKKYVLE NHPGANSNYQ MHLLKKTLQK CEKNGWLEQI SGKGFSGTFQ LSFPYYPSPG 

       430        440        450        460        470        480 
VLFPKKESGG SDDEDEDDDD DESSEDSEDE EPPPKRSLQK KTPAKSQGKT ASMKQRGSKP 

       490        500        510        520        530        540 
ARKVPAAQRG KVRPLPKKAP PKAKTPARKA RPSPSVIKKP SGSSSRKPIA SARKEAKLPG 

       550 
KGKSAMKKSF KTKK 

« Hide

Isoform 2 [UniParc].

Checksum: 2F19451E819E2EB7
Show »

FASTA54159,548
Isoform 3 [UniParc].

Checksum: 95FCF9349FACFC4E
Show »

FASTA51756,972

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Cerebellum, Liver, Lung, Skin and Thymus.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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).
Strain: FVB/N.
Tissue: Mammary tumor.
[4]"A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors."
le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P.
EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-324, FUNCTION, INTERACTION WITH CBX5.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004938 mRNA. Translation: BAB23683.1.
AK028181 mRNA. Translation: BAC25794.1.
AK043260 mRNA. Translation: BAC31507.1.
AK075725 mRNA. Translation: BAC35912.1. Frameshift.
AK161041 mRNA. Translation: BAE36164.1.
AK166161 mRNA. Translation: BAE38604.1.
AK169740 mRNA. Translation: BAE41340.1.
AL807249 Genomic DNA. Translation: CAM18860.1.
AL807249 Genomic DNA. Translation: CAM18863.1.
BC004053 mRNA. Translation: AAH04053.1.
BC020024 mRNA. Translation: AAH20024.1.
X99642 mRNA. Translation: CAA67961.1.
CCDSCCDS38927.1. [Q3TEA8-1]
CCDS51334.1. [Q3TEA8-3]
RefSeqNP_001116368.1. NM_001122896.2.
NP_001116369.1. NM_001122897.2. [Q3TEA8-1]
NP_001272407.1. NM_001285478.1. [Q3TEA8-1]
NP_001272408.1. NM_001285479.1.
NP_001272409.1. NM_001285480.1.
NP_001272410.1. NM_001285481.1. [Q3TEA8-2]
NP_034600.2. NM_010470.3. [Q3TEA8-1]
XP_006538631.1. XM_006538568.1. [Q3TEA8-1]
XP_006538632.1. XM_006538569.1.
XP_006538633.1. XM_006538570.1.
UniGeneMm.348429.
Mm.399941.

3D structure databases

ProteinModelPortalQ3TEA8.
SMRQ3TEA8. Positions 155-237, 248-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200401. 4 interactions.
IntActQ3TEA8. 2 interactions.
MINTMINT-4128252.

PTM databases

PhosphoSiteQ3TEA8.

Proteomic databases

MaxQBQ3TEA8.
PaxDbQ3TEA8.
PRIDEQ3TEA8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030541; ENSMUSP00000030541; ENSMUSG00000028759. [Q3TEA8-1]
ENSMUST00000097836; ENSMUSP00000095447; ENSMUSG00000028759.
ENSMUST00000165861; ENSMUSP00000132614; ENSMUSG00000028759. [Q3TEA8-1]
GeneID15441.
KEGGmmu:15441.
UCSCuc008vkg.2. mouse. [Q3TEA8-1]
uc008vki.2. mouse. [Q3TEA8-2]

Organism-specific databases

CTD50809.
MGIMGI:109369. Hp1bp3.

Phylogenomic databases

eggNOGNOG285312.
GeneTreeENSGT00510000047652.
HOVERGENHBG097678.
OrthoDBEOG75QR72.
PhylomeDBQ3TEA8.
TreeFamTF106395.

Gene expression databases

ArrayExpressQ3TEA8.
BgeeQ3TEA8.
GenevestigatorQ3TEA8.

Family and domain databases

Gene3D1.10.10.10. 3 hits.
InterProIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00538. Linker_histone. 3 hits.
[Graphical view]
PRINTSPR00624. HISTONEH5.
SMARTSM00526. H15. 3 hits.
[Graphical view]
PROSITEPS51504. H15. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHP1BP3. mouse.
NextBio288226.
PROQ3TEA8.
SOURCESearch...

Entry information

Entry nameHP1B3_MOUSE
AccessionPrimary (citable) accession number: Q3TEA8
Secondary accession number(s): A2AM64 expand/collapse secondary AC list , A2AM68, Q3TM38, Q3TU07, Q61688, Q8BT17, Q8C6H2, Q8C911, Q8VE06, Q99KR0, Q9DBI1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot