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O15347 (HMGB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High mobility group protein B3
Alternative name(s):
High mobility group protein 2a
Short name=HMG-2a
High mobility group protein 4
Short name=HMG-4
Gene names
Name:HMGB3
Synonyms:HMG2A, HMG4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds preferentially single-stranded DNA and unwinds double-stranded DNA By similarity.

Subcellular location

Nucleus By similarity. Chromosome By similarity.

Tissue specificity

Expressed predominantly in placenta.

Sequence similarities

Belongs to the HMGB family.

Contains 2 HMG box DNA-binding domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200High mobility group protein B3
PRO_0000048539

Regions

DNA binding9 – 7971HMG box 1
DNA binding93 – 16169HMG box 2
Compositional bias181 – 20020Asp/Glu-rich (acidic)

Natural variations

Natural variant511T → A.
Corresponds to variant rs16995792 [ dbSNP | Ensembl ].
VAR_049558
Natural variant561E → Q. Ref.6
VAR_064162

Experimental info

Sequence conflict131M → T in CAA71143. Ref.1
Sequence conflict521M → V in CAA71143. Ref.1
Sequence conflict1871E → Q in CAA71143. Ref.1

Secondary structure

............... 200
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15347 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 31C090FAA4D581E6

FASTA20022,980
        10         20         30         40         50         60 
MAKGDPKKPK GKMSAYAFFV QTCREEHKKK NPEVPVNFAE FSKKCSERWK TMSGKEKSKF 

        70         80         90        100        110        120 
DEMAKADKVR YDREMKDYGP AKGGKKKKDP NAPKRPPSGF FLFCSEFRPK IKSTNPGISI 

       130        140        150        160        170        180 
GDVAKKLGEM WNNLNDSEKQ PYITKAAKLK EKYEKDVADY KSKGKFDGAK GPAKVARKKV 

       190        200 
EEEDEEEEEE EEEEEEEEDE 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of human and mouse HMG2a cDNAs: evidence for an HMG2a-specific 3' untranslated region."
Wilke K., Wiemann S., Gaul R., Gong W., Poustka A.
Gene 198:269-274(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Eye.
[4]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Solution structure of the first and second HMG-box domain from high mobility group protein B3."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-164.
[6]"Terminal osseous dysplasia is caused by a single recurrent mutation in the FLNA gene."
Sun Y., Almomani R., Aten E., Celli J., van der Heijden J., Venselaar H., Robertson S.P., Baroncini A., Franco B., Basel-Vanagaite L., Horii E., Drut R., Ariyurek Y., den Dunnen J.T., Breuning M.H.
Am. J. Hum. Genet. 87:146-153(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-56.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10043 mRNA. Translation: CAA71143.1.
AF003626 Genomic DNA. No translation available.
BC070482 mRNA. Translation: AAH70482.1.
CCDSCCDS35428.1.
RefSeqNP_005333.2. NM_005342.2.
XP_005274724.1. XM_005274667.1.
UniGeneHs.19114.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQZNMR-A1-79[»]
2YQINMR-A91-164[»]
ProteinModelPortalO15347.
SMRO15347. Positions 1-164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109392. 18 interactions.
IntActO15347. 1 interaction.
MINTMINT-5002211.
STRING9606.ENSP00000359393.

PTM databases

PhosphoSiteO15347.

Proteomic databases

MaxQBO15347.
PaxDbO15347.
PeptideAtlasO15347.
PRIDEO15347.

Protocols and materials databases

DNASU3149.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325307; ENSP00000359393; ENSG00000029993.
ENST00000448905; ENSP00000442758; ENSG00000029993.
ENST00000593327; ENSP00000472199; ENSG00000269411.
ENST00000595259; ENSP00000472961; ENSG00000269411.
GeneID3149.
KEGGhsa:3149.
UCSCuc004fep.3. human.

Organism-specific databases

CTD3149.
GeneCardsGC0XP150148.
HGNCHGNC:5004. HMGB3.
HPAHPA062583.
MIM300193. gene.
neXtProtNX_O15347.
PharmGKBPA35092.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320947.
HOGENOMHOG000197861.
HOVERGENHBG009000.
InParanoidO15347.
KOK11296.
OMANEKQPYN.
PhylomeDBO15347.
TreeFamTF105371.

Gene expression databases

ArrayExpressO15347.
BgeeO15347.
CleanExHS_HMGB3.
GenevestigatorO15347.

Family and domain databases

Gene3D1.10.30.10. 2 hits.
InterProIPR009071. HMG_box_dom.
IPR017967. HMG_boxA_CS.
[Graphical view]
PfamPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 2 hits.
[Graphical view]
SUPFAMSSF47095. SSF47095. 2 hits.
PROSITEPS00353. HMG_BOX_1. 1 hit.
PS50118. HMG_BOX_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO15347.
GeneWikiHMGB3.
GenomeRNAi3149.
NextBio12480.
PROO15347.
SOURCESearch...

Entry information

Entry nameHMGB3_HUMAN
AccessionPrimary (citable) accession number: O15347
Secondary accession number(s): O95556, Q6NS40
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM