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P02088 (HBB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Hemoglobin subunit beta-1
Alternative name(s):
Beta-1-globin
Hemoglobin beta-1 chain
Hemoglobin beta-major chain
Gene names
Name:Hbb-b1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in oxygen transport from the lung to the various peripheral tissues.

Subunit structure

Heterotetramer of two alpha chains and two beta chains.

Tissue specificity

Red blood cells.

Polymorphism

Inbred mouse strains possess 1 of 4 alleles at the HBB locus: D (diffuse), S (single), P and W1. The D and P alleles are actually closely linked doublets that coordinately express a major and a minor chain, the minor chain being slightly different in the two alleles. The S allele produces only 1 chain, it is characteristic of North American wild mice. The W1 allele is observed mainly in Northwestern China.

Miscellaneous

The D-major sequence is shown. See also the entry for the beta D and P-minor chain.

Sequence similarities

Belongs to the globin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 147146Hemoglobin subunit beta-1
PRO_0000053024

Sites

Metal binding641Iron (heme distal ligand)
Metal binding931Iron (heme proximal ligand)

Amino acid modifications

Modified residue181N6-succinyllysine Ref.12
Modified residue211Phosphoserine Ref.11

Natural variations

Natural variant141C → G in allele S and allele W1.
Natural variant211S → A in allele S.
Natural variant741D → E in allele W1.
Natural variant1351V → M in allele W1.
Natural variant1401T → A in allele S.

Experimental info

Sequence conflict151L → Q in BAB27362. Ref.6
Sequence conflict391T → A in BAB29299. Ref.6
Sequence conflict631A → T in BAB27237. Ref.6
Sequence conflict911E → Q Ref.3
Sequence conflict1091N → S in BAB29299. Ref.6

Secondary structure

................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02088 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8190EAEEFD9036A3

FASTA14715,840
        10         20         30         40         50         60 
MVHLTDAEKA AVSCLWGKVN SDEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNAK 

        70         80         90        100        110        120 
VKAHGKKVIT AFNDGLNHLD SLKGTFASLS ELHCDKLHVD PENFRLLGNM IVIVLGHHLG 

       130        140 
KDFTPAAQAA FQKVVAGVAT ALAHKYH 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the BALB/c mouse beta-globin complex."
Shehee W.R., Loeb D.D., Adey N.B., Burton F.H., Casavant N.C., Cole P., Davies C.J., McGraw R.A., Schichman S.A., Severynse D.M., Voliva C.F., Weyter F.W., Wisely G.B., Edgell M.H., Hutchison C.A. III
J. Mol. Biol. 205:41-62(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The evolution and sequence comparison of two recently diverged mouse chromosomal beta-globin genes."
Konkel D.A., Maizel J.V. Jr., Leder P.
Cell 18:865-873(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[3]"Comparison of total sequence of a cloned rabbit beta-globin gene and its flanking regions with a homologous mouse sequence."
van Ooyen A., van den Berg J., Mantei N., Weissmann C.
Science 206:337-344(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Evolution of the mouse beta-globin genes: a recent gene conversion in the Hbbs haplotype."
Erhart M.A., Simons K.S., Weaver S.
Mol. Biol. Evol. 2:304-320(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE S).
Strain: C57BL/10.
[5]"Nucleotide sequences of the mouse globin beta gene cDNAs in a wild derived new haplotype Hbb(w1)."
Ueda Y., Miyashita N., Imai K., Yamaguchi Y., Takamura K., Notohara M., Shiroishi T., Kawashima T., Ning L., Wang C., Wu X., Moriwaki K.
Mamm. Genome 10:879-882(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELES P AND W1).
[6]"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].
Strain: C57BL/6J and NOD.
Tissue: Head, Heart, Kidney, Liver, Placenta, Spleen, Stomach and Thymus.
[7]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 19-41; 32-60 AND 67-145, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[8]"Characterization and kinetics of synthesis of 15S beta-globin RNA, a putative precursor of beta-globin mRNA."
Curtis P.J., Mantei N., Weissmann C.
Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 86-109.
[9]"Comparison of cloned rabbit and mouse beta-globin genes showing strong evolutionary divergence of two homologous pairs of introns."
van den Berg J., van Ooyen A., Mantei N., Schamboeck A., Grosveld G., Flavell R.A., Weissmann C.
Nature 276:37-44(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-44 AND 100-115.
[10]"Intervening sequence of DNA identified in the structural portion of a mouse beta-globin gene."
Tilghman S.M., Tiemeier D.C., Seidman J.G., Peterlin B.M., Sullivan M., Maizel J.V. Jr., Leder P.
Proc. Natl. Acad. Sci. U.S.A. 75:725-729(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-105.
[11]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"The role of beta chains in the control of the hemoglobin oxygen binding function: chimeric human/mouse proteins, structure, and function."
Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.
Biochemistry 40:15669-15675(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[14]"Mouse haemoglobin beta chains. Comparative sequence data on adult major and minor beta chains from two species, Mus musculus and Mus cervicolor."
Gilman J.G.
Biochem. J. 159:43-53(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALLELIC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14061 Genomic DNA. Translation: CAA32224.1.
J00413 Genomic DNA. Translation: AAA37791.1.
AB020013 mRNA. Translation: BAA77353.1.
AB020015 mRNA. Translation: BAA77355.1.
AK002258 mRNA. Translation: BAB21971.1.
AK002394 mRNA. Translation: BAB22067.1.
AK003096 mRNA. Translation: BAB22562.1.
AK003472 mRNA. Translation: BAB22806.1.
AK005442 mRNA. Translation: BAB24036.1.
AK005490 mRNA. Translation: BAB24075.1.
AK005496 mRNA. Translation: BAB24080.1.
AK010873 mRNA. Translation: BAB27237.1.
AK010902 mRNA. Translation: BAB27255.1.
AK010980 mRNA. Translation: BAB27302.1.
AK010981 mRNA. Translation: BAB27303.1.
AK010991 mRNA. Translation: BAB27310.1.
AK010993 mRNA. Translation: BAB27312.1.
AK011006 mRNA. Translation: BAB27325.1.
AK011013 mRNA. Translation: BAB27331.1.
AK011016 mRNA. Translation: BAB27334.1.
AK011027 mRNA. Translation: BAB27343.1.
AK011033 mRNA. Translation: BAB27347.1.
AK011050 mRNA. Translation: BAB27360.1.
AK011052 mRNA. Translation: BAB27361.1.
AK011053 mRNA. Translation: BAB27362.1.
AK011057 mRNA. Translation: BAB27365.1.
AK011067 mRNA. Translation: BAB27374.1.
AK011069 mRNA. Translation: BAB27376.1.
AK011075 mRNA. Translation: BAB27380.1.
AK011077 mRNA. Translation: BAB27382.1.
AK011083 mRNA. Translation: BAB27387.1.
AK011102 mRNA. Translation: BAB27399.1.
AK012551 mRNA. Translation: BAB28311.1.
AK014364 mRNA. Translation: BAB29299.1.
AK027903 mRNA. Translation: BAC25655.1.
AK027904 mRNA. Translation: BAC25656.1.
AK028067 mRNA. Translation: BAC25734.1.
AK088149 mRNA. Translation: BAC40173.1.
AK133714 mRNA. Translation: BAE21794.1.
AK147001 mRNA. Translation: BAE27598.1.
AK160629 mRNA. Translation: BAE35926.1.
AK161021 mRNA. Translation: BAE36152.1.
AK165490 mRNA. Translation: BAE38217.1.
AK167615 mRNA. Translation: BAE39668.1.
AK168412 mRNA. Translation: BAE40327.1.
AK168477 mRNA. Translation: BAE40366.1.
AK168562 mRNA. Translation: BAE40435.1.
AK168584 mRNA. Translation: BAE40453.1.
AK168819 mRNA. Translation: BAE40646.1.
AK168826 mRNA. Translation: BAE40653.1.
AK168846 mRNA. Translation: BAE40669.1.
M19236 mRNA. Translation: AAA37788.1.
M10828 Genomic DNA. Translation: AAA37786.1.
M10830, M10829 Genomic DNA. Translation: AAA37787.1.
M10688 Genomic DNA. Translation: AAA37790.1.
PIRHBMS. A90790.
RefSeqNP_001188320.1. NM_001201391.1.
NP_001265090.1. NM_001278161.1.
NP_032246.2. NM_008220.5.
UniGeneMm.288567.
Mm.467412.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEBX-ray2.10B/D2-147[»]
3HRWX-ray2.80B/D2-147[»]
ProteinModelPortalP02088.
SMRP02088. Positions 2-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200219. 3 interactions.
IntActP02088. 11 interactions.
MINTMINT-4097231.

PTM databases

PhosphoSiteP02088.

2D gel databases

REPRODUCTION-2DPAGEIPI00553333.
P02088.
SWISS-2DPAGEP02088.

Proteomic databases

PaxDbP02088.
PRIDEP02088.

Protocols and materials databases

DNASU15129.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100503605.
101488143.
15129.
KEGGmmu:100503605.
mmu:101488143.
mmu:15129.

Organism-specific databases

CTD100503605.
101488143.
15129.
MGIMGI:96021. Hbb-b1.

Phylogenomic databases

eggNOGNOG269316.
HOVERGENHBG009709.
InParanoidP02088.
KOK13823.
PhylomeDBP02088.

Gene expression databases

CleanExMM_HBB-B1.
GenevestigatorP02088.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]
PANTHERPTHR11442:SF7. PTHR11442:SF7. 1 hit.
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00814. BETAHAEM.
SUPFAMSSF46458. SSF46458. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHbb-b1. mouse.
EvolutionaryTraceP02088.
NextBio287582.
PROP02088.
SOURCESearch...

Entry information

Entry nameHBB1_MOUSE
AccessionPrimary (citable) accession number: P02088
Secondary accession number(s): Q54AI0 expand/collapse secondary AC list , Q91V86, Q9CRZ2, Q9CXH5, Q9CY12, Q9CY54, Q9R0S6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 143 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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