P02088 (HBB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hemoglobin subunit beta-1

Alternative name(s):
Beta-1-globin
Hemoglobin beta-1 chain
Hemoglobin beta-major chain

Gene names

Name:

Hbb-b1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	hemoglobin complex Inferred from electronic annotation. Source: InterPro
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 147

146

Hemoglobin subunit beta-1

PRO_0000053024

Sites

Metal binding

64

1

Iron (heme distal ligand)

Metal binding

93

1

Iron (heme proximal ligand)

Amino acid modifications

Modified residue

45

1

Phosphoserine Ref.11 Ref.12

Modified residue

81

1

Phosphoserine Ref.12 Ref.13

Natural variations

Natural variant

14

1

C → G in allele S and allele W1.

Natural variant

21

1

S → A in allele S.

Natural variant

74

1

D → E in allele W1.

Natural variant

135

1

V → M in allele W1.

Natural variant

140

1

T → A in allele S.

Experimental info

Sequence conflict

15

1

L → Q in BAB27362. Ref.6

Sequence conflict

39

1

T → A in BAB29299. Ref.6

Sequence conflict

63

1

A → T in BAB27237. Ref.6

Sequence conflict

91

1

E → Q Ref.3

Sequence conflict

109

1

N → S in BAB29299. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

147

Helix Strand Turn

Details...

Helix

6 – 18

13

Helix

21 – 35

15

Helix

37 – 42

6

Helix

52 – 56

5

Helix

59 – 77

19

Helix

82 – 94

13

Turn

95 – 97

3

Helix

102 – 119

18

Helix

120 – 122

3

Helix

125 – 143

19

Sequences

	Sequence		Length	Mass (Da)
	P02088 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 8190EAEEFD9036A3	FASTA	147	15,840
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, MASS SPECTROMETRY. Tissue: Embryonic brain.
[12]	"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-45 AND SER-81, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, MASS SPECTROMETRY. Tissue: Melanoma.
[14]	"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).
[15]	"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.

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.

IPI

IPI00762198.

PIR

HBMS. A90790.

RefSeq

NP_001188320.1. NM_001201391.1.
NP_032246.2. NM_008220.4.

UniGene

Mm.288567.
Mm.467412.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JEB	X-ray	2.10	B/D	2-147	[»]
3HRW	X-ray	2.80	B/D	2-147	[»]

ProteinModelPortal

P02088.

SMR

P02088. Positions 2-147.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02088. 5 interactions.

PTM databases

PhosphoSite

P02088.

2D gel databases

REPRODUCTION-2DPAGE

IPI00553333.
P02088.

SWISS-2DPAGE

P02088.

Proteomic databases

PaxDb

P02088.

PRIDE

P02088.

Protocols and materials databases

DNASU

15129.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

100503605.
15129.

KEGG

mmu:100503605.
mmu:15129.

Organism-specific databases

CTD

100503605.
15129.

MGI

MGI:96021. Hbb-b1.

Phylogenomic databases

eggNOG

NOG269316.

HOVERGEN

HBG009709.

InParanoid

P02088.

KO

K13823.

OrthoDB

EOG4THVVF.

Gene expression databases

CleanEx

MM_HBB-B1.

Genevestigator

P02088.

GermOnline

ENSMUSG00000052305. Mus musculus.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00814. BETAHAEM.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

Hbb-b1. mouse.

EvolutionaryTrace

P02088.

NextBio

287582.

SOURCE

Search...

Entry information

Entry name

HBB1_MOUSE

Accession

Primary (citable) accession number: P02088
Secondary accession number(s): Q54AI0 , 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 3, 2013
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program