Q9NZD4 (AHSP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-hemoglobin-stabilizing protein

Alternative name(s):
Erythroid differentiation-related factor
Erythroid-associated factor

Gene names

Name:	AHSP
Synonyms:	EDRF, ERAF

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	102 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Act as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia. Ref.6
Subunit structure	Monomer. Forms an heterodimer with free alpha-hemoglobin. Does not bind beta-hemoglobin nor alpha2beta2 hemoglobin A.
Subcellular location	Cytoplasm Ref.6.
Tissue specificity	Expressed in blood and bone marrow. Ref.1 Ref.6
Induction	By GATA1 during erythroid maturation.
Sequence similarities	Belongs to the AHSP family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	hemoglobin metabolic process Non-traceable author statement Ref.6. Source: UniProtKB hemopoiesis Non-traceable author statement Ref.6. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro protein stabilization Inferred from electronic annotation. Source: InterPro
Cellular component	hemoglobin complex Non-traceable author statement Ref.6. Source: UniProtKB
Molecular function	hemoglobin binding Non-traceable author statement Ref.6. Source: UniProtKB unfolded protein binding Non-traceable author statement Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 102

102

Alpha-hemoglobin-stabilizing protein

PRO_0000064509

Natural variations

Natural variant

100

1

P → T.
Corresponds to variant rs36018996 [ dbSNP | Ensembl ].

VAR_050650

Experimental info

Sequence conflict

32

1

V → A in AAL82894. Ref.3

Sequence conflict

87

1

D → N in AAL82894. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

102

Helix Strand Turn

Details...

Helix

5 – 23

19

Helix

27 – 29

3

Helix

34 – 52

19

Turn

53 – 55

3

Helix

60 – 86

27

Sequences

	Sequence		Length	Mass (Da)
	Q9NZD4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 275DDF8BC670EF20	FASTA	102	11,840
	10 20 30 40 50 60 MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN YYRQQVTGEP 70 80 90 100 QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel erythroid-specific marker of transmissible spongiform encephalopathies." Miele G., Manson J., Clinton M. Nat. Med. 7:361-364(2001) [PubMed: 11231637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[3]	Michel U., Schulz-Schaeffer W. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	Finning K., Anstee D. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"An abundant erythroid protein that stabilizes free alpha-haemoglobin." Kihm A.J., Kong Y., Hong W., Russell J.E., Rouda S., Adachi K., Simon M.C., Blobel G.A., Weiss M.J. Nature 417:758-763(2002) [PubMed: 12066189] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"Biophysical characterization of the alpha-globin binding protein alpha-hemoglobin stabilizing protein." Gell D., Kong Y., Eaton S.A., Weiss M.J., Mackay J.P. J. Biol. Chem. 277:40602-40609(2002) [PubMed: 12192002] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin." Feng L., Gell D.A., Zhou S., Gu L., Kong Y., Li J., Hu M., Yan N., Lee C., Rich A.M., Armstrong R.S., Lay P.A., Gow A.J., Weiss M.J., Mackay J.P., Shi Y. Cell 119:629-640(2004) [PubMed: 15550245] [Abstract] Cited for: STRUCTURE BY NMR OF 1-90, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH HBA.
[9]	"NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding." Santiveri C.M., Perez-Canadillas J.M., Vadivelu M.K., Allen M.D., Rutherford T.J., Watkins N.A., Bycroft M. J. Biol. Chem. 279:34963-34970(2004) [PubMed: 15178680] [Abstract] Cited for: STRUCTURE BY NMR OF 2-102 OF WILD TYPE AND MUTANT ALA-30.
[10]	"Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem." Feng L., Zhou S., Gu L., Gell D.A., Mackay J.P., Weiss M.J., Gow A.J., Shi Y. Nature 435:697-701(2005) [PubMed: 15931225] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH HBA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF364517 mRNA. Translation: AAK50856.1.
AF208865 mRNA. Translation: AAF64279.1.
AY072612 Genomic DNA. Translation: AAL82894.1.
AF485325 Genomic DNA. Translation: AAO49381.1.
BC035842 mRNA. Translation: AAH35842.1.

IPI

IPI00010257.

RefSeq

NP_057717.1. NM_016633.2.

UniGene

Hs.274309.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W09	NMR	-	A	3-94	[»]
1W0A	NMR	-	A	3-94	[»]
1W0B	NMR	-	A	2-102	[»]
1XZY	NMR	-	A	1-90	[»]
1Y01	X-ray	2.80	A	1-102	[»]
1Z8U	X-ray	2.40	A/C	1-102	[»]
3IA3	X-ray	3.20	A/C	1-91	[»]
3OVU	X-ray	2.83	A	2-102	[»]

ProteinModelPortal

Q9NZD4.

SMR

Q9NZD4. Positions 2-91.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NZD4. 4 interactions.

MINT

MINT-1427628.

STRING

Q9NZD4.

Polymorphism databases

DMDM

23813669.

Proteomic databases

PeptideAtlas

Q9NZD4.

PRIDE

Q9NZD4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302312; ENSP00000307199; ENSG00000169877.

GeneID

51327.

KEGG

hsa:51327.

UCSC

uc002ecj.1. human.

Organism-specific databases

CTD

51327.

GeneCards

GC16P031540.

H-InvDB

HIX0012995.

HGNC

HGNC:18075. AHSP.

HPA

HPA040940.

MIM

605821. gene.

neXtProt

NX_Q9NZD4.

PharmGKB

PA27842.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000003648.

HOVERGEN

HBG023495.

InParanoid

Q9NZD4.

OMA

GMKEFNV.

OrthoDB

EOG476K1T.

PhylomeDB

Q9NZD4.

Gene expression databases

ArrayExpress

Q9NZD4.

Bgee

Q9NZD4.

CleanEx

HS_ERAF.

Genevestigator

Q9NZD4.

GermOnline

ENSG00000169877. Homo sapiens.

Family and domain databases

InterPro

IPR015317. A_Hb_stabilising_prot.
[Graphical view]

PANTHER

PTHR15914. A_Hb_stabilising_prot. 1 hit.

Pfam

PF09236. AHSP. 1 hit.
[Graphical view]

ProDom

PD285427. A_Hb_stabilising_prot. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF109751. A_Hb_stabilising_prot. 1 hit.

ProtoNet

Search...

Other

NextBio

54729.

SOURCE

Search...

Entry information

Entry name

AHSP_HUMAN

Accession

Primary (citable) accession number: Q9NZD4
Secondary accession number(s): Q8TD01

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.