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UniProtKB/Swiss-Prot entry P02008


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HBAZ_HUMAN
Primary accession number P02008
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 102)
Name and origin of the protein
Protein name Hemoglobin subunit zeta
Synonyms Hemoglobin zeta chain
Zeta-globin
HBAZ
Gene name
Name: HBZ
Synonyms: HBZ2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(82)90311-7; PubMed=6297773 [NCBI, ExPASy, EBI, Israel, Japan]
Proudfoot N.J., Gil A., Maniatis T.;
"The structure of the human zeta-globin gene and a closely linked, nearly identical pseudogene.";
Cell 31:553-563(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6963223 [NCBI, ExPASy, EBI, Israel, Japan]
Cohen-Solal M., Authier B., Deriel J.K., Murnane M.J., Forget B.G.;
"Cloning and nucleotide sequence analysis of human embryonic zeta-globin cDNA.";
DNA 1:355-363(1982).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/ng0397-252; PubMed=9054936 [NCBI, ExPASy, EBI, Israel, Japan]
Flint J., Thomas K., Micklem G., Raynham H., Clark K., Doggett N.A., King A., Higgs D.R.;
"The relationship between chromosome structure and function at a human telomeric region.";
Nat. Genet. 15:252-257(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/hmg/10.4.339; PubMed=11157797 [NCBI, ExPASy, EBI, Israel, Japan]
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.";
Hum. Mol. Genet. 10:339-352(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Spleen;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-142.
PubMed=6179844 [NCBI, ExPASy, EBI, Israel, Japan]
Aschauer H., Sanguansermsri T., Braunitzer G.;
"Human embryonic haemoglobins. The primary structure of the zeta chains.";
Hoppe-Seyler's Z. Physiol. Chem. 362:1159-1162(1981).
[7]
PROTEIN SEQUENCE OF 2-142.
DOI=10.1073/pnas.78.10.6076; PubMed=6171809 [NCBI, ExPASy, EBI, Israel, Japan]
Clegg J.B., Gagnon J.;
"Structure of the zeta chain of human embryonic hemoglobin.";
Proc. Natl. Acad. Sci. U.S.A. 78:6076-6080(1981).
[8]
ACETYLATION AT SER-2.
PubMed=6172357 [NCBI, ExPASy, EBI, Israel, Japan]
Aschauer H., Schaefer W., Sanguansermsri T., Braunitzer G.;
"Human embryonic haemoglobins. Ac-Ser-Leu-Thr-is the N-terminal sequence of the zeta-chains.";
Hoppe-Seyler's Z. Physiol. Chem. 362:1657-1659(1981).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J00182; AAB59406.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24173; AAA61306.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z84721; CAB06552.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006462; AAK61214.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027892; AAH27892.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00217473; -.
PIR A90832; HZHU.
RefSeq NP_005323.1; -.
UniGene Hs.585357
3D structure databases
PDB
1JEB; X-ray; 2.10 A; A/C=2-141.[ExPASy / RCSB / EBI]
PDBsum 1JEB; -.
ModBase P02008.
Protein-protein interaction databases
IntAct P02008; 1.
Organism-specific databases
GeneCards GC16P000142; -.
H-InvDB HIX0059559; -.
HGNC HGNC:4835; HBZ.
GenAtlas HBZ.
MIM 142310; gene. [NCBI / EBI]
Orphanet 846; Alpha-thalassemia.
93615; Hemoglobin Constant Spring.
93616; Hemoglobin H disease.
163596; Hydrops fetalis of Barts.
PharmGKB PA29212; -.
Gene expression databases
ArrayExpress P02008; -.
Bgee P02008; -.
CleanEx HS_HBZ; -.
GermOnline ENSG00000130656; Homo sapiens.
Ontologies
GO
GO:0005833; Cellular component: hemoglobin complex (traceable author statement from ProtInc).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0019825; Molecular function: oxygen binding (inferred from electronic annotation from InterPro).
GO:0005344; Molecular function: oxygen transporter activity (traceable author statement from ProtInc).
GO:0015671; Biological process: oxygen transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000971; Globin_subset.
IPR002338; Haemoglobin_a.
IPR002340; Haemoglobin_zeta.
Graphical view of domain structure.
Pfam PF00042; Globin; 1.
Pfam graphical view of domain structure.
PRINTS PR00612; ALPHAHAEM.
PR00816; ZETAHAEM.
PROSITE PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P02008; -.
PRIDE P02008; -.
Genome annotation databases
Ensembl ENSG00000130656; Homo sapiens. [Contig view]
GeneID 3050; -.
KEGG hsa:3050; -.
Phylogenomic databases
HOGENOM P02008; -.
HOVERGEN P02008; -.
OMA P02008; LFASYPQ.
Other
NextBio 12075; -.
SOURCE HBZ; Homo sapiens.
ProtoNet P02008.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   142  141     Hemoglobin subunit zeta. PRO_0000052851
METAL   59    59        Iron (heme distal ligand). 
METAL   88    88        Iron (heme proximal ligand). 
MOD_RES   2     2        N-acetylserine. 
HELIX   5    18  14      
HELIX   22    36  15      
HELIX   38    43  6      
HELIX   54    72  19      
TURN   73    75  3      
HELIX   77    80  4      
HELIX   82    90  9      
HELIX   97   113  17      
TURN   115   117  3      
HELIX   120   138  19      
HELIX   139   141  3      
Sequence information
Length: 142 AA [This is the length of the unprocessed precursor] Molecular weight: 15637 Da [This is the MW of the unprocessed precursor] CRC64: B62A9B825743A155 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLTKTERTI IVSMWAKIST QADTIGTETL ERLFLSHPQT KTYFPHFDLH PGSAQLRAHG 

        70         80         90        100        110        120 
SKVVAAVGDA VKSIDDIGGA LSKLSELHAY ILRVDPVNFK LLSHCLLVTL AARFPADFTA 

       130        140 
EAHAAWDKFL SVVSSVLTEK YR 

P02008 in FASTA format

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