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P22557

- HEM0_HUMAN

UniProt

P22557 - HEM0_HUMAN

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Protein

5-aminolevulinate synthase, erythroid-specific, mitochondrial

Gene
ALAS2, ALASE, ASB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.1 Publication

Cofactori

Pyridoxal phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei163 – 1631Substrate By similarity
Binding sitei280 – 2801Substrate By similarity
Binding sitei299 – 2991Substrate By similarity
Binding sitei332 – 3321Pyridoxal phosphate By similarity
Binding sitei360 – 3601Pyridoxal phosphate By similarity
Binding sitei388 – 3881Pyridoxal phosphate By similarity
Active sitei391 – 3911 By similarity
Binding sitei420 – 4201Pyridoxal phosphate By similarity
Binding sitei421 – 4211Pyridoxal phosphate By similarity
Binding sitei508 – 5081Substrate By similarity

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: UniProtKB
  2. coenzyme binding Source: UniProtKB
  3. glycine binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular iron ion homeostasis Source: UniProtKB
  2. erythrocyte differentiation Source: UniProtKB
  3. heme biosynthetic process Source: UniProtKB
  4. hemoglobin biosynthetic process Source: UniProtKB
  5. oxygen homeostasis Source: UniProtKB
  6. porphyrin-containing compound metabolic process Source: Reactome
  7. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  8. response to hypoxia Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS08311-MONOMER.
ReactomeiREACT_9465. Heme biosynthesis.
UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase, erythroid-specific, mitochondrial (EC:2.3.1.37)
Short name:
ALAS-E
Alternative name(s):
5-aminolevulinic acid synthase 2
Delta-ALA synthase 2
Delta-aminolevulinate synthase 2
Gene namesi
Name:ALAS2
Synonyms:ALASE, ASB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:397. ALAS2.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Anemia, sideroblastic, X-linked (XLSA) [MIM:300751]: A form of sideroblastic anemia that shows a variable hematologic response to pharmacologic doses of pyridoxine. Sideroblastic anemia is characterized by anemia of varying severity, hypochromic peripheral erythrocytes, systemic iron overload secondary to chronic ineffective erythropoiesis, and the presence of bone marrow ringed sideroblasts. Sideroblasts are characterized by iron-loaded mitochondria clustered around the nucleus.
Note: The disease is caused by mutations affecting the gene represented in this entry.9 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti156 – 1561K → E in XLSA; significantly reduced activity. 1 Publication
VAR_066232
Natural varianti159 – 1591D → Y in XLSA. 1 Publication
VAR_018604
Natural varianti170 – 1701R → H in XLSA; significantly increased thermosensitivity. 1 Publication
VAR_066233
Natural varianti199 – 1991Y → H in XLSA. 1 Publication
VAR_012334
Natural varianti204 – 2041R → Q in XLSA; 15% to 35% activity of wild-type. 1 Publication
VAR_012335
Natural varianti218 – 2181R → H in XLSA; significantly increased thermosensitivity. 1 Publication
Corresponds to variant rs185504937 [ dbSNP | Ensembl ].
VAR_066234
Natural varianti242 – 2421E → K in XLSA; significantly reduced activity. 1 Publication
VAR_066235
Natural varianti263 – 2631D → N in XLSA; significantly reduced activity. 1 Publication
VAR_066236
Natural varianti339 – 3391P → L in XLSA; significantly reduced activity. 1 Publication
VAR_066237
Natural varianti375 – 3751R → C in XLSA; significantly reduced activity. 1 Publication
VAR_066238
Natural varianti388 – 3881T → S in XLSA. 1 Publication
VAR_000562
Natural varianti411 – 4111R → C in XLSA; 12% to 25% activity of wild-type. 2 Publications
VAR_000563
Natural varianti411 – 4111R → H in XLSA; significantly reduced activity. 1 Publication
VAR_066239
Natural varianti448 – 4481R → Q in XLSA. 1 Publication
VAR_012336
Natural varianti452 – 4521R → C in XLSA. 2 Publications
VAR_012337
Natural varianti452 – 4521R → G in XLSA; does not affect activity. 1 Publication
VAR_066240
Natural varianti452 – 4521R → H in XLSA. 1 Publication
VAR_066241
Natural varianti476 – 4761I → N in XLSA. 1 Publication
VAR_000564
Natural varianti560 – 5601R → H in XLSA. 1 Publication
VAR_018605
Natural varianti572 – 5721R → H in XLSA; does not affect activity. 1 Publication
VAR_066243
Erythropoietic protoporphyria, X-linked dominant (XLDPT) [MIM:300752]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. XLDPT is characterized biochemically by a high proportion of zinc-protoporphyrin in erythrocytes, in which a mismatch between protoporphyrin production and the heme requirement of differentiating erythroid cells leads to overproduction of protoporphyrin in amounts sufficient to cause photosensitivity and liver disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Gain of function mutations in ALS2 are responsible for XLDPT, but they can also be a possible aggravating factor in congenital erythropoietic porphyria and other erythropoietic disorders caused by mutations in other genes (1 Publication).1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi300751. phenotype.
300752. phenotype.
Orphaneti79278. Erythropoietic protoporphyria.
75563. X-linked sideroblastic anemia.
PharmGKBiPA24689.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4949MitochondrionAdd
BLAST
Chaini50 – 5875385-aminolevulinate synthase, erythroid-specific, mitochondrialPRO_0000001223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei391 – 3911N6-(pyridoxal phosphate)lysine Inferred

Proteomic databases

MaxQBiP22557.
PaxDbiP22557.
PRIDEiP22557.

PTM databases

PhosphoSiteiP22557.

Expressioni

Tissue specificityi

Erythroid specific.

Gene expression databases

ArrayExpressiP22557.
BgeeiP22557.
CleanExiHS_ALAS2.
GenevestigatoriP22557.

Organism-specific databases

HPAiHPA001638.

Interactioni

Subunit structurei

Homodimer. Interacts with SUCLA2.1 Publication

Protein-protein interaction databases

BioGridi106714. 2 interactions.
IntActiP22557. 1 interaction.
STRINGi9606.ENSP00000332369.

Structurei

3D structure databases

ProteinModelPortaliP22557.
SMRiP22557. Positions 1-49, 151-540.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
HOVERGENiHBG005954.
InParanoidiP22557.
KOiK00643.
OMAiHYLQSIN.
PhylomeDBiP22557.
TreeFamiTF300724.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR015118. 5aminolev_synth_preseq.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P22557-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MVTAAMLLQC CPVLARGPTS LLGKVVKTHQ FLFGIGRCPI LATQGPNCSQ    50
IHLKATKAGG DSPSWAKGHC PFMLSELQDG KSKIVQKAAP EVQEDVKAFK 100
TDLPSSLVSV SLRKPFSGPQ EQEQISGKVT HLIQNNMPGN YVFSYDQFFR 150
DKIMEKKQDH TYRVFKTVNR WADAYPFAQH FSEASVASKD VSVWCSNDYL 200
GMSRHPQVLQ ATQETLQRHG AGAGGTRNIS GTSKFHVELE QELAELHQKD 250
SALLFSSCFV ANDSTLFTLA KILPGCEIYS DAGNHASMIQ GIRNSGAAKF 300
VFRHNDPDHL KKLLEKSNPK IPKIVAFETV HSMDGAICPL EELCDVSHQY 350
GALTFVDEVH AVGLYGSRGA GIGERDGIMH KIDIISGTLG KAFGCVGGYI 400
ASTRDLVDMV RSYAAGFIFT TSLPPMVLSG ALESVRLLKG EEGQALRRAH 450
QRNVKHMRQL LMDRGLPVIP CPSHIIPIRV GNAALNSKLC DLLLSKHGIY 500
VQAINYPTVP RGEELLRLAP SPHHSPQMME DFVEKLLLAW TAVGLPLQDV 550
SVAACNFCRR PVHFELMSEW ERSYFGNMGP QYVTTYA 587
Length:587
Mass (Da):64,633
Last modified:January 23, 2002 - v2
Checksum:iFD821BE245C440B5
GO
Isoform 2 (identifier: P22557-2) [UniParc]FASTAAdd to Basket

Also known as: Delta4

The sequence of this isoform differs from the canonical sequence as follows:
     102-138: Missing.

Note: Constitutes 35-45% of erythrocytes ALAS2 mRNAs. Catalytic activity is 70% of isoform 1 activity.

Show »
Length:550
Mass (Da):60,589
Checksum:iBB28A593D343264F
GO
Isoform 3 (identifier: P22557-3) [UniParc]FASTAAdd to Basket

Also known as: F143M

The sequence of this isoform differs from the canonical sequence as follows:
     1-142: Missing.
     143-143: F → M

Note: Catalytic activity is 80% of isoform 1 activity.

Show »
Length:445
Mass (Da):49,395
Checksum:i3304747E4DE0CC2E
GO
Isoform 4 (identifier: P22557-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRGGEVALGWNKKKRLFCEDFRFKM
     102-138: Missing.

Show »
Length:574
Mass (Da):63,487
Checksum:i7F5E13D5F36738CD
GO

Sequence cautioni

The sequence CAA39795.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti156 – 1561K → E in XLSA; significantly reduced activity. 1 Publication
VAR_066232
Natural varianti159 – 1591D → Y in XLSA. 1 Publication
VAR_018604
Natural varianti170 – 1701R → H in XLSA; significantly increased thermosensitivity. 1 Publication
VAR_066233
Natural varianti199 – 1991Y → H in XLSA. 1 Publication
VAR_012334
Natural varianti204 – 2041R → Q in XLSA; 15% to 35% activity of wild-type. 1 Publication
VAR_012335
Natural varianti218 – 2181R → H in XLSA; significantly increased thermosensitivity. 1 Publication
Corresponds to variant rs185504937 [ dbSNP | Ensembl ].
VAR_066234
Natural varianti242 – 2421E → K in XLSA; significantly reduced activity. 1 Publication
VAR_066235
Natural varianti263 – 2631D → N in XLSA; significantly reduced activity. 1 Publication
VAR_066236
Natural varianti339 – 3391P → L in XLSA; significantly reduced activity. 1 Publication
VAR_066237
Natural varianti375 – 3751R → C in XLSA; significantly reduced activity. 1 Publication
VAR_066238
Natural varianti388 – 3881T → S in XLSA. 1 Publication
VAR_000562
Natural varianti411 – 4111R → C in XLSA; 12% to 25% activity of wild-type. 2 Publications
VAR_000563
Natural varianti411 – 4111R → H in XLSA; significantly reduced activity. 1 Publication
VAR_066239
Natural varianti448 – 4481R → Q in XLSA. 1 Publication
VAR_012336
Natural varianti452 – 4521R → C in XLSA. 2 Publications
VAR_012337
Natural varianti452 – 4521R → G in XLSA; does not affect activity. 1 Publication
VAR_066240
Natural varianti452 – 4521R → H in XLSA. 1 Publication
VAR_066241
Natural varianti476 – 4761I → N in XLSA. 1 Publication
VAR_000564
Natural varianti520 – 5201P → L.1 Publication
Corresponds to variant rs201062903 [ dbSNP | Ensembl ].
VAR_066242
Natural varianti560 – 5601R → H in XLSA. 1 Publication
VAR_018605
Natural varianti572 – 5721R → H in XLSA; does not affect activity. 1 Publication
VAR_066243
Natural varianti586 – 5861Y → F Rare variant found in a congenital erythropoietic porphyria patient that also carries UROS mutations R-73R and Q-248; increased enzyme activity. 1 Publication
Corresponds to variant rs139596860 [ dbSNP | Ensembl ].
VAR_066244

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 142142Missing in isoform 3. VSP_042851Add
BLAST
Alternative sequencei1 – 11M → MRGGEVALGWNKKKRLFCED FRFKM in isoform 4. VSP_047330
Alternative sequencei102 – 13837Missing in isoform 2 and isoform 4. VSP_042852Add
BLAST
Alternative sequencei143 – 1431F → M in isoform 3. VSP_042853

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821S → F in CAA39795. 1 Publication
Sequence conflicti221 – 2211A → V in AAH30230. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56352 mRNA. Translation: CAA39795.1. Different initiation.
X60364 mRNA. Translation: CAA42916.1.
AF068624 Genomic DNA. Translation: AAC39838.1.
AK290565 mRNA. Translation: BAF83254.1.
AK291589 mRNA. Translation: BAF84278.1.
AK313118 mRNA. Translation: BAG35939.1.
Z83821 Genomic DNA. No translation available.
AL020991 Genomic DNA. Translation: CAA15886.1.
AL020991 Genomic DNA. Translation: CAX15017.1.
CH471154 Genomic DNA. Translation: EAW93211.1.
CH471154 Genomic DNA. Translation: EAW93213.1.
BC030230 mRNA. Translation: AAH30230.2.
CCDSiCCDS14366.1. [P22557-1]
CCDS35303.1. [P22557-2]
CCDS43960.1. [P22557-4]
PIRiS16347. SYHUAE.
RefSeqiNP_000023.2. NM_000032.4. [P22557-1]
NP_001033056.1. NM_001037967.3. [P22557-2]
NP_001033057.1. NM_001037968.3. [P22557-4]
UniGeneiHs.522666.
Hs.555936.

Genome annotation databases

EnsembliENST00000330807; ENSP00000332369; ENSG00000158578. [P22557-1]
ENST00000335854; ENSP00000337131; ENSG00000158578. [P22557-2]
ENST00000396198; ENSP00000379501; ENSG00000158578. [P22557-4]
GeneIDi212.
KEGGihsa:212.
UCSCiuc004dua.4. human. [P22557-1]
uc004dub.4. human.
uc004dud.4. human. [P22557-2]

Polymorphism databases

DMDMi20141346.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56352 mRNA. Translation: CAA39795.1 . Different initiation.
X60364 mRNA. Translation: CAA42916.1 .
AF068624 Genomic DNA. Translation: AAC39838.1 .
AK290565 mRNA. Translation: BAF83254.1 .
AK291589 mRNA. Translation: BAF84278.1 .
AK313118 mRNA. Translation: BAG35939.1 .
Z83821 Genomic DNA. No translation available.
AL020991 Genomic DNA. Translation: CAA15886.1 .
AL020991 Genomic DNA. Translation: CAX15017.1 .
CH471154 Genomic DNA. Translation: EAW93211.1 .
CH471154 Genomic DNA. Translation: EAW93213.1 .
BC030230 mRNA. Translation: AAH30230.2 .
CCDSi CCDS14366.1. [P22557-1 ]
CCDS35303.1. [P22557-2 ]
CCDS43960.1. [P22557-4 ]
PIRi S16347. SYHUAE.
RefSeqi NP_000023.2. NM_000032.4. [P22557-1 ]
NP_001033056.1. NM_001037967.3. [P22557-2 ]
NP_001033057.1. NM_001037968.3. [P22557-4 ]
UniGenei Hs.522666.
Hs.555936.

3D structure databases

ProteinModelPortali P22557.
SMRi P22557. Positions 1-49, 151-540.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106714. 2 interactions.
IntActi P22557. 1 interaction.
STRINGi 9606.ENSP00000332369.

Chemistry

DrugBanki DB00145. Glycine.

PTM databases

PhosphoSitei P22557.

Polymorphism databases

DMDMi 20141346.

Proteomic databases

MaxQBi P22557.
PaxDbi P22557.
PRIDEi P22557.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330807 ; ENSP00000332369 ; ENSG00000158578 . [P22557-1 ]
ENST00000335854 ; ENSP00000337131 ; ENSG00000158578 . [P22557-2 ]
ENST00000396198 ; ENSP00000379501 ; ENSG00000158578 . [P22557-4 ]
GeneIDi 212.
KEGGi hsa:212.
UCSCi uc004dua.4. human. [P22557-1 ]
uc004dub.4. human.
uc004dud.4. human. [P22557-2 ]

Organism-specific databases

CTDi 212.
GeneCardsi GC0XM055053.
GeneReviewsi ALAS2.
HGNCi HGNC:397. ALAS2.
HPAi HPA001638.
MIMi 300751. phenotype.
300752. phenotype.
301300. gene.
neXtProti NX_P22557.
Orphaneti 79278. Erythropoietic protoporphyria.
75563. X-linked sideroblastic anemia.
PharmGKBi PA24689.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0156.
HOGENOMi HOG000221020.
HOVERGENi HBG005954.
InParanoidi P22557.
KOi K00643.
OMAi HYLQSIN.
PhylomeDBi P22557.
TreeFami TF300724.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00375 .
BioCyci MetaCyc:HS08311-MONOMER.
Reactomei REACT_9465. Heme biosynthesis.

Miscellaneous databases

ChiTaRSi ALAS2. human.
GeneWikii ALAS2.
GenomeRNAii 212.
NextBioi 852.
PROi P22557.
SOURCEi Search...

Gene expression databases

ArrayExpressi P22557.
Bgeei P22557.
CleanExi HS_ALAS2.
Genevestigatori P22557.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR015118. 5aminolev_synth_preseq.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01821. 5aminolev_synth. 1 hit.
PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes."
    Bishop D.F.
    Nucleic Acids Res. 18:7187-7188(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA."
    Cox T.C., Bawden M.J., Martin A., May B.K.
    EMBO J. 10:1891-1902(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene."
    Surinya K.H., Cox T.C., May B.K.
    J. Biol. Chem. 273:16798-16809(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lung, Placenta and Umbilical cord blood.
  5. "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.
    , 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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 4).
    Tissue: Pancreas.
  8. "The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis."
    Cox T.C., Sadlon T.J., Schwarz Q.P., Matthews C.S., Wise P.D., Cox L.L., Bottomley S.S., May B.K.
    Int. J. Biochem. Cell Biol. 36:281-295(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TRANSIT PEPTIDE CLEAVAGE SITE, INTERACTION WITH SUCLA2.
  9. "X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase."
    Cox T.C., Bottomley S.S., Wiley J.S., Bawden M.J., Matthews C.S., May B.K.
    N. Engl. J. Med. 330:675-679(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XLSA SER-388.
  10. "Enzymatic defect in 'X-linked' sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency."
    Cotter P.D., Baumann M., Bishop D.F.
    Proc. Natl. Acad. Sci. U.S.A. 89:4028-4032(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XLSA ASN-476.
  11. "R411C mutation of the ALAS2 gene encodes a pyridoxine-responsive enzyme with low activity."
    Furuyama K., Uno R., Urabe A., Hayashi N., Fujita H., Kondo M., Sassa S., Yamamoto M.
    Br. J. Haematol. 103:839-841(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XLSA CYS-411.
  12. "A novel mutation of the erythroid-specific gamma-aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia."
    Harigae H., Furuyama K., Kudo K., Hayashi N., Yamamoto M., Sassa S., Sasaki T.
    Am. J. Hematol. 62:112-114(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XLSA GLN-204.
  13. "Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis."
    Cotter P.D., May A., Li L., Al-Sabah A.I., Fitzsimons E.J., Cazzola M., Bishop D.F.
    Blood 93:1757-1769(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLSA HIS-199; CYS-411; GLN-448 AND CYS-452.
  14. "Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation."
    Cazzola M., May A., Bergamaschi G., Cerani P., Ferrillo S., Bishop D.F.
    Blood 100:4236-4238(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XLSA HIS-560.
  15. "A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia."
    Hurford M.T., Marshall-Taylor C., Vicki S.L., Zhou J.Z., Silverman L.M., Rezuke W.N., Altman A., Tsongalis G.J.
    Clin. Chim. Acta 321:49-53(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XLSA TYR-159.
  16. "C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload."
    Whatley S.D., Ducamp S., Gouya L., Grandchamp B., Beaumont C., Badminton M.N., Elder G.H., Holme S.A., Anstey A.V., Parker M., Corrigall A.V., Meissner P.N., Hift R.J., Marsden J.T., Ma Y., Mieli-Vergani G., Deybach J.C., Puy H.
    Am. J. Hum. Genet. 83:408-414(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN XLDPT.
  17. "New mutation in erythroid-specific delta-aminolevulinate synthase as the cause of X-linked sideroblastic anemia responsive to pyridoxine."
    Kucerova J., Horvathova M., Mojzikova R., Belohlavkova P., Cermak J., Divoky V.
    Acta Haematol. 125:193-197(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLSA GLU-156; CYS-452 AND HIS-452, CHARACTERIZATION OF VARIANT XLSA GLU-156.
  18. Cited for: VARIANT PHE-586, CHARACTERIZATION OF VARIANT PHE-586, POSSIBLE ROLE AS MODIFIER GENE IN ERYTHROPOIETIC DISORDERS.
  19. "Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations."
    Ducamp S., Kannengiesser C., Touati M., Garcon L., Guerci-Bresler A., Guichard J.F., Vermylen C., Dochir J., Poirel H.A., Fouyssac F., Mansuy L., Leroux G., Tertian G., Girot R., Heimpel H., Matthes T., Talbi N., Deybach J.C.
    , Beaumont C., Puy H., Grandchamp B.
    Hum. Mutat. 32:590-597(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLSA HIS-170; HIS-218; LYS-242; ASN-263; LEU-339; CYS-375; HIS-411; GLY-452 AND HIS-572, VARIANT LEU-520, CHARACTERIZATION OF VARIANTS XLSA HIS-170; HIS-218; LYS-242; ASN-263; LEU-339; CYS-375; HIS-411; GLY-452 AND HIS-572.

Entry informationi

Entry nameiHEM0_HUMAN
AccessioniPrimary (citable) accession number: P22557
Secondary accession number(s): A8K3F0
, A8K6C4, Q13735, Q5JZF5, Q8N6H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2002
Last modified: September 3, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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