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Entry version 212 (18 Sep 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Adenosylhomocysteinase

Gene

AHCY

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

NAD+2 PublicationsNote: Binds 1 NAD+ per subunit.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-homocysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine.
Proteins known to be involved in this subpathway in this organism are:
  1. Adenosylhomocysteinase (AHCYL1), Adenosylhomocysteinase (AHCYL1), Adenosylhomocysteinase, Adenosylhomocysteinase (AHCY), Adenosylhomocysteinase, Adenosylhomocysteinase (AHCY), Adenosylhomocysteinase (FGFR2-AHCYL1), Adenosylhomocysteinase 3 (AHCYL2)
This subpathway is part of the pathway L-homocysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine, the pathway L-homocysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei57SubstrateBy similarity1
Binding sitei131SubstrateBy similarity1
Binding sitei156SubstrateBy similarity1
Binding sitei186SubstrateBy similarity1
Binding sitei190SubstrateBy similarity1
Binding sitei243NAD2 Publications1
Binding sitei248NAD2 Publications1
Binding sitei346NAD2 Publications1
Binding sitei353NAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi157 – 159NAD2 Publications3
Nucleotide bindingi222 – 227NAD2 Publications6
Nucleotide bindingi299 – 301NAD2 Publications3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processOne-carbon metabolism
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS02273-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.3.1.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-156581 Methylation
R-HSA-1614635 Sulfur amino acid metabolism
R-HSA-2408508 Metabolism of ingested SeMet, Sec, MeSec into H2Se
R-HSA-5578997 Defective AHCY causes Hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD)

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P23526

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00314;UER00076

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Adenosylhomocysteinase (EC:3.3.1.1)
Short name:
AdoHcyase
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AHCY
Synonyms:SAHH
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:343 AHCY

Online Mendelian Inheritance in Man (OMIM)

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MIMi
180960 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P23526

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05858849R → C in HMAHCHD. 2 PublicationsCorresponds to variant dbSNP:rs369428934Ensembl.1
Natural variantiVAR_05858986D → G in HMAHCHD. 2 PublicationsCorresponds to variant dbSNP:rs773162208Ensembl.1
Natural variantiVAR_05859089A → V in HMAHCHD. 1 PublicationCorresponds to variant dbSNP:rs755222515EnsemblClinVar.1
Natural variantiVAR_058591143Y → C in HMAHCHD. 2 PublicationsCorresponds to variant dbSNP:rs121918608EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
191

MalaCards human disease database

More...
MalaCardsi
AHCY
MIMi613752 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000101444

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
88618 Psychomotor retardation due to S-adenosylhomocysteine hydrolase deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24636

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2664

Drug and drug target database

More...
DrugBanki
DB03216 (1'R,2'S)-9-(2-Hydroxy-3'-Keto-Cyclopenten-1-yl)Adenine
DB03273 3'-Oxo-Adenosine
DB09130 Copper
DB03769 D-Eritadenine
DB02325 Isopropyl alcohol

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1233

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
AHCY

Domain mapping of disease mutations (DMDM)

More...
DMDMi
20141702

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001169022 – 432AdenosylhomocysteinaseAdd BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine1 Publication1
Modified residuei183PhosphoserineCombined sources1
Modified residuei193PhosphotyrosineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P23526

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P23526

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P23526

MaxQB - The MaxQuant DataBase

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MaxQBi
P23526

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P23526

PeptideAtlas

More...
PeptideAtlasi
P23526

PRoteomics IDEntifications database

More...
PRIDEi
P23526

ProteomicsDB human proteome resource

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ProteomicsDBi
27374
54126 [P23526-1]

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00012007

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P23526

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P23526

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P23526

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000101444 Expressed in 95 organ(s), highest expression level in body of pancreas

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P23526 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P23526 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA041225
HPA044675

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
106696, 90 interactors

Database of interacting proteins

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DIPi
DIP-50557N

Protein interaction database and analysis system

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IntActi
P23526, 32 interactors

Molecular INTeraction database

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MINTi
P23526

STRING: functional protein association networks

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STRINGi
9606.ENSP00000217426

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P23526

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P23526

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P23526

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1370 Eukaryota
COG0499 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182981

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000227987

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P23526

KEGG Orthology (KO)

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KOi
K01251

Identification of Orthologs from Complete Genome Data

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OMAi
QSTWDGI

Database of Orthologous Groups

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OrthoDBi
900867at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P23526

TreeFam database of animal gene trees

More...
TreeFami
TF300415

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00401 SAHH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1480, 2 hits

HAMAP database of protein families

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HAMAPi
MF_00563 AdoHcyase, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR042172 Adenosylhomocyst_ase-like_sf
IPR000043 Adenosylhomocysteinase-like
IPR015878 Ado_hCys_hydrolase_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020082 S-Ado-L-homoCys_hydrolase_CS

The PANTHER Classification System

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PANTHERi
PTHR23420 PTHR23420, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF05221 AdoHcyase, 1 hit
PF00670 AdoHcyase_NAD, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001109 Ad_hcy_hydrolase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00996 AdoHcyase, 1 hit
SM00997 AdoHcyase_NAD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00936 ahcY, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00738 ADOHCYASE_1, 1 hit
PS00739 ADOHCYASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P23526-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
        10         20         30         40         50
MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMRERYS ASKPLKGARI
60 70 80 90 100
AGCLHMTVET AVLIETLVTL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY
110 120 130 140 150
AWKGETDEEY LWCIEQTLYF KDGPLNMILD DGGDLTNLIH TKYPQLLPGI
160 170 180 190 200
RGISEETTTG VHNLYKMMAN GILKVPAINV NDSVTKSKFD NLYGCRESLI
210 220 230 240 250
DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI ITEIDPINAL
260 270 280 290 300
QAAMEGYEVT TMDEACQEGN IFVTTTGCID IILGRHFEQM KDDAIVCNIG
310 320 330 340 350
HFDVEIDVKW LNENAVEKVN IKPQVDRYRL KNGRRIILLA EGRLVNLGCA
360 370 380 390 400
MGHPSFVMSN SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG
410 420 430
KLNVKLTKLT EKQAQYLGMS CDGPFKPDHY RY
Length:432
Mass (Da):47,716
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2833C025F969553E
GO
Isoform 2 (identifier: P23526-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Note: No experimental confirmation available.
Show »
Length:404
Mass (Da):44,659
Checksum:i4AF904249AD2F35F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti249A → V in BAG53495 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05228638R → W1 PublicationCorresponds to variant dbSNP:rs13043752EnsemblClinVar.1
Natural variantiVAR_05858849R → C in HMAHCHD. 2 PublicationsCorresponds to variant dbSNP:rs369428934Ensembl.1
Natural variantiVAR_05858986D → G in HMAHCHD. 2 PublicationsCorresponds to variant dbSNP:rs773162208Ensembl.1
Natural variantiVAR_00693486D → N1 Publication1
Natural variantiVAR_05859089A → V in HMAHCHD. 1 PublicationCorresponds to variant dbSNP:rs755222515EnsemblClinVar.1
Natural variantiVAR_058591143Y → C in HMAHCHD. 2 PublicationsCorresponds to variant dbSNP:rs121918608EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0454041 – 28Missing in isoform 2. 1 PublicationAdd BLAST28

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M61831 mRNA Translation: AAA51681.1
M61832 mRNA Translation: AAA51682.1
BT006697 mRNA Translation: AAP35343.1
AK097610 mRNA Translation: BAG53495.1
AK290422 mRNA Translation: BAF83111.1
AL356299 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW76279.1
CH471077 Genomic DNA Translation: EAW76280.1
BC010018 mRNA Translation: AAH10018.1
BC011606 mRNA Translation: AAH11606.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS13233.1 [P23526-1]
CCDS54457.1 [P23526-2]

Protein sequence database of the Protein Information Resource

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PIRi
A43629

NCBI Reference Sequences

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RefSeqi
NP_000678.1, NM_000687.3 [P23526-1]
NP_001155238.1, NM_001161766.1 [P23526-2]
NP_001309013.1, NM_001322084.1 [P23526-2]
NP_001309014.1, NM_001322085.1 [P23526-2]
XP_005260374.1, XM_005260317.2 [P23526-2]
XP_011526961.1, XM_011528659.1 [P23526-2]
XP_016883197.1, XM_017027708.1
XP_016883198.1, XM_017027709.1 [P23526-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000217426; ENSP00000217426; ENSG00000101444 [P23526-1]
ENST00000538132; ENSP00000442820; ENSG00000101444 [P23526-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
191

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:191

UCSC genome browser

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UCSCi
uc002xai.4 human [P23526-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61831 mRNA Translation: AAA51681.1
M61832 mRNA Translation: AAA51682.1
BT006697 mRNA Translation: AAP35343.1
AK097610 mRNA Translation: BAG53495.1
AK290422 mRNA Translation: BAF83111.1
AL356299 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW76279.1
CH471077 Genomic DNA Translation: EAW76280.1
BC010018 mRNA Translation: AAH10018.1
BC011606 mRNA Translation: AAH11606.1
CCDSiCCDS13233.1 [P23526-1]
CCDS54457.1 [P23526-2]
PIRiA43629
RefSeqiNP_000678.1, NM_000687.3 [P23526-1]
NP_001155238.1, NM_001161766.1 [P23526-2]
NP_001309013.1, NM_001322084.1 [P23526-2]
NP_001309014.1, NM_001322085.1 [P23526-2]
XP_005260374.1, XM_005260317.2 [P23526-2]
XP_011526961.1, XM_011528659.1 [P23526-2]
XP_016883197.1, XM_017027708.1
XP_016883198.1, XM_017027709.1 [P23526-1]

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A7AX-ray2.80A/B1-432[»]
1LI4X-ray2.01A1-432[»]
3NJ4X-ray2.50A/B/C/D1-432[»]
4PFJX-ray2.30A/B1-432[»]
4PGFX-ray2.59A/B1-432[»]
4YVFX-ray2.70A/B1-432[»]
5W49X-ray2.40A/B4-432[»]
5W4BX-ray2.65A/B/C/D/E/F4-432[»]
SMRiP23526
ModBaseiSearch...

Protein-protein interaction databases

BioGridi106696, 90 interactors
DIPiDIP-50557N
IntActiP23526, 32 interactors
MINTiP23526
STRINGi9606.ENSP00000217426

Chemistry databases

BindingDBiP23526
ChEMBLiCHEMBL2664
DrugBankiDB03216 (1'R,2'S)-9-(2-Hydroxy-3'-Keto-Cyclopenten-1-yl)Adenine
DB03273 3'-Oxo-Adenosine
DB09130 Copper
DB03769 D-Eritadenine
DB02325 Isopropyl alcohol

DrugCentral

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DrugCentrali
P23526
GuidetoPHARMACOLOGYi1233

PTM databases

iPTMnetiP23526
PhosphoSitePlusiP23526
SwissPalmiP23526

Polymorphism and mutation databases

BioMutaiAHCY
DMDMi20141702

2D gel databases

REPRODUCTION-2DPAGEiIPI00012007

Proteomic databases

EPDiP23526
jPOSTiP23526
MassIVEiP23526
MaxQBiP23526
PaxDbiP23526
PeptideAtlasiP23526
PRIDEiP23526
ProteomicsDBi27374
54126 [P23526-1]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
191
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217426; ENSP00000217426; ENSG00000101444 [P23526-1]
ENST00000538132; ENSP00000442820; ENSG00000101444 [P23526-2]
GeneIDi191
KEGGihsa:191
UCSCiuc002xai.4 human [P23526-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
191
DisGeNETi191

GeneCards: human genes, protein and diseases

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GeneCardsi
AHCY
HGNCiHGNC:343 AHCY
HPAiHPA041225
HPA044675
MalaCardsiAHCY
MIMi180960 gene
613752 phenotype
neXtProtiNX_P23526
OpenTargetsiENSG00000101444
Orphaneti88618 Psychomotor retardation due to S-adenosylhomocysteine hydrolase deficiency
PharmGKBiPA24636

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1370 Eukaryota
COG0499 LUCA
GeneTreeiENSGT00950000182981
HOGENOMiHOG000227987
InParanoidiP23526
KOiK01251
OMAiQSTWDGI
OrthoDBi900867at2759
PhylomeDBiP23526
TreeFamiTF300415

Enzyme and pathway databases

UniPathwayiUPA00314;UER00076
BioCyciMetaCyc:HS02273-MONOMER
BRENDAi3.3.1.1 2681
ReactomeiR-HSA-156581 Methylation
R-HSA-1614635 Sulfur amino acid metabolism
R-HSA-2408508 Metabolism of ingested SeMet, Sec, MeSec into H2Se
R-HSA-5578997 Defective AHCY causes Hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD)
SABIO-RKiP23526

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
AHCY human
EvolutionaryTraceiP23526

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
191

Pharos

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Pharosi
P23526

Protein Ontology

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PROi
PR:P23526

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000101444 Expressed in 95 organ(s), highest expression level in body of pancreas
ExpressionAtlasiP23526 baseline and differential
GenevisibleiP23526 HS

Family and domain databases

CDDicd00401 SAHH, 1 hit
Gene3Di3.40.50.1480, 2 hits
HAMAPiMF_00563 AdoHcyase, 1 hit
InterProiView protein in InterPro
IPR042172 Adenosylhomocyst_ase-like_sf
IPR000043 Adenosylhomocysteinase-like
IPR015878 Ado_hCys_hydrolase_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR020082 S-Ado-L-homoCys_hydrolase_CS
PANTHERiPTHR23420 PTHR23420, 1 hit
PfamiView protein in Pfam
PF05221 AdoHcyase, 1 hit
PF00670 AdoHcyase_NAD, 1 hit
PIRSFiPIRSF001109 Ad_hcy_hydrolase, 1 hit
SMARTiView protein in SMART
SM00996 AdoHcyase, 1 hit
SM00997 AdoHcyase_NAD, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00936 ahcY, 1 hit
PROSITEiView protein in PROSITE
PS00738 ADOHCYASE_1, 1 hit
PS00739 ADOHCYASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSAHH_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P23526
Secondary accession number(s): A8K307
, B3KUN3, E1P5P2, F5H737, Q96A36
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: September 18, 2019
This is version 212 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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