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Protein

S-adenosylhomocysteine hydrolase-like protein 1

Gene

AHCYL1

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

Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3- and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5-trisphosphate competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1 (PubMed:16793548). When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates of ITPR1 to interact with CFTR and SLC26A6 mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (By similarity). Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3- secretion (PubMed:16769890). Inhibits the effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and CFTR through dephosphorylation (By similarity). Mediates the induction of SLC9A3 surface expression produced by Angiotensin-2 (PubMed:20584908). Depending on the cell type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-dependent calcium inhibition (PubMed:18829453). May modulate the polyadenylation state of specific mRNAs, both by controlling the subcellular location of FIP1L1 and by inhibiting PAPOLA activity, in response to a stimulus that alters its phosphorylation state (PubMed:19224921). Acts as a (dATP)-dependent inhibitor of ribonucleotide reductase large subunit RRM1, controlling the endogenous dNTP pool and ensuring normal cell cycle progression (PubMed:25237103). In vitro does not exhibit any S-adenosyl-L-homocysteine hydrolase activity (By similarity).By similarity6 Publications

Miscellaneous

Ablation of expression in HeLa cells causes imbalanced dNTP pools and altered cell cycle progression.1 Publication

Caution

In spite of its similarity with AHCY, which catalyzes the reversible hydrolysis of S-adenosyl-L-homocysteine to adenosine and homocysteine, recombinant AHCYL1 expressed in bacteria shows no hydrolysase activity, nor does it affect the enzyme activity of AHCY.By similarity

<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+1 PublicationNote: Binds 1 NAD+ per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei155SubstrateBy similarity1
Binding sitei229SubstrateBy similarity1
Binding sitei254SubstrateBy similarity1
Binding sitei284SubstrateBy similarity1
Binding sitei288SubstrateBy similarity1
Binding sitei341NAD1 Publication1
Binding sitei376NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi318 – 322NAD1 Publication5
Nucleotide bindingi397 – 399NAD1 Publication3

<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

  • identical protein binding Source: IntAct
  • RNA binding Source: UniProtKB-KW

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 functionRNA-binding
Biological processOne-carbon metabolism
LigandNAD

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-112043 PLC beta mediated events
R-HSA-1489509 DAG and IP3 signaling
R-HSA-2029485 Role of phospholipids in phagocytosis
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-422356 Regulation of insulin secretion
R-HSA-5218921 VEGFR2 mediated cell proliferation
R-HSA-5578775 Ion homeostasis
R-HSA-5607763 CLEC7A (Dectin-1) induces NFAT activation
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O43865

<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:
S-adenosylhomocysteine hydrolase-like protein 1Imported
Alternative name(s):
DC-expressed AHCY-like molecule
IP(3)Rs binding protein released with IP(3)
Short name:
IRBIT
Putative adenosylhomocysteinase 2
S-adenosyl-L-homocysteine hydrolase 2
Short name:
AdoHcyase 2
<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:AHCYL1Imported
Synonyms:DCAL, IRBIT, XPVKONAImported
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000168710.17

Human Gene Nomenclature Database

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HGNCi
HGNC:344 AHCYL1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
607826 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O43865

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi52T → A: No effect on interaction with SLC4A4. 1 Publication1
Mutagenesisi58T → A: No effect on interaction with SLC4A4. 1 Publication1
Mutagenesisi62S → A: No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 2 Publications1
Mutagenesisi64S → A: No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 3 Publications1
Mutagenesisi66S → A: Slightly decreases interaction with ITPR1. Slightly decreases phosphorylation. No effect on interaction with SLC4A4. Abolishes interaction with FIP1L1. 3 Publications1
Mutagenesisi68S → A: Abolishes interaction with ITPR1. Highly decreases phosphorylation. No effect on formation of multimers. Abolishes interaction with SLC4A4. Abolishes interaction with FIP1L1. Highly decreases interaction with SLC9A3. Highly decreases interaction with SLC9A3; when associated whith A-71 and A-74. 4 Publications1
Mutagenesisi70S → A: Highly decreases interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Abolishes interaction with FIP1L1. 3 Publications1
Mutagenesisi71S → A: Abolishes interaction with ITPR1. Highly decreases phosphorylation. Abolishes interaction with SLC4A4. Abolishes interaction with FIP1L1. Highly decreases interaction with SLC9A3; when associated whith A-68 and A-74. 4 Publications1
Mutagenesisi72T → A: Highly decreases interaction with ITPR1. Slightly increases phosphorylation. No effect on interaction with SLC4A4. Highly decreases interaction with FIP1L1. 3 Publications1
Mutagenesisi74S → G: Abolishes interaction with ITPR1. Slightly decreases phosphorylation. Strongly decreases interaction with SLC4A4. Abolishes interaction with FIP1L1. Highly decreases interaction with SLC9A3; when associated whith A-68 and A-71. 4 Publications1
Mutagenesisi76S → G: No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 3 Publications1
Mutagenesisi77S → A: Highly decreases interaction with ITPR1. Slightly decreases phosphorylation. Strongly decreases interaction with SLC4A4. Abolishes interaction with FIP1L1. 3 Publications1
Mutagenesisi80S → A: No effect on interaction with SLC4A4. Highly decreases interaction with FIP1L1. 3 Publications1
Mutagenesisi82T → A: No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Decreases interaction with FIP1L1. 3 Publications1
Mutagenesisi84S → A: Slightly decreases interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Decreases interaction with FIP1L1. 3 Publications1
Mutagenesisi85S → A: Slightly decreases interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Decreases interaction with FIP1L1. 3 Publications1
Mutagenesisi90S → A: No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 3 Publications1
Mutagenesisi97T → A: No effect on interaction with ITPR1. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 3 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
10768

Open Targets

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OpenTargetsi
ENSG00000168710

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24637

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3751646

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
AHCYL1

<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 methionineiRemovedCombined sources
<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_00001169082 – 530S-adenosylhomocysteine hydrolase-like protein 1Add BLAST529

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-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei40N6-acetyllysineBy similarity1
Modified residuei68Phosphoserine2 Publications1
Modified residuei71Phosphoserine2 Publications1
Modified residuei74Phosphoserine1 Publication1
Modified residuei77Phosphoserine1 Publication1
Modified residuei84PhosphoserineBy similarity1
Modified residuei391PhosphoserineCombined sources1
Isoform 2 (identifier: O43865-2)
Modified residuei1N-acetylmethionineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated at Ser/Thr residues between Ser-68 and Thr-72 in the PEST region: required for interaction with dATP-bound RRM1 and ITPR1. Phosphorylation at Ser-68 by PRKD1 and CAMK4 is required for further phosphorylations by CSNK1A1 (PubMed:16793548). Phosphorylation is induced by oxidative stress (PubMed:19224921). Probably phosphorylated by CAMK2A; phosphorylation at Ser-68 may be required for interaction with SLC9A3 (PubMed:20584908).1 Publication3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O43865

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O43865

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O43865

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

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PaxDbi
O43865

PeptideAtlas

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PeptideAtlasi
O43865

PRoteomics IDEntifications database

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PRIDEi
O43865

ProteomicsDB human proteome resource

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ProteomicsDBi
49211
49212 [O43865-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O43865

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

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PhosphoSitePlusi
O43865

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
O43865

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in dendritic cells.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expression increases markedly during activation of blood and skin DC (Langerhans cells), but is diminished in terminally differentiated tonsil DC.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000168710 Expressed in 241 organ(s), highest expression level in hypothalamus

CleanEx database of gene expression profiles

More...
CleanExi
HS_AHCYL1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O43865 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43865 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA042589

<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

Forms multimers (PubMed:16793548). Forms heteromultimers with AHCYL2 (via the C-terminal region) (PubMed:19220705). Interacts (when phosphorylated) with ITPR1 (when not phosphorylated); the interaction suppresses inositol 1,4,5-trisphosphate binding to ITPR1 (PubMed:16793548). Interacts with CFTR and SLC26A6; the interactions take place once AHCYL1 is released from ITPR1 and increase CFTR and SLC26A6 activities (By similarity). Interacts with RRM1; in a phosphorylation- and (dATP)-dependent manner. Interacts (via PEST domain when phosphorylated) with SLC4A4 isoform 1 but not isoform 2; the interaction increases SLC4A4 isoform 1 activity (PubMed:16769890). Interacts (when phosphorylated) with SLC9A3; the interaction is required for SLC9A3 apical location and activity (PubMed:18829453, PubMed:20584908). Interacts (when phosphorylated) with FIP1L1; the interaction is direct and associates AHCYL1 with the CPSF complex and RNA (PubMed:19224921). Interacts with PAPOLA (PubMed:19224921).By similarity7 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)

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BioGridi
115987, 193 interactors

Protein interaction database and analysis system

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IntActi
O43865, 40 interactors

Molecular INTeraction database

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MINTi
O43865

STRING: functional protein association networks

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STRINGi
9606.ENSP00000358814

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O43865

<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

1530
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

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
3MTGX-ray2.64A/B89-530[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O43865

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

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SMRi
O43865

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O43865

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni65 – 92PEST1 PublicationAdd BLAST28
Regioni281 – 448NAD bindingBy similarityAdd BLAST168
Regioni520 – 530PDZ-bindingBy similarityAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PEST region is essential for the interaction with ITPR1, and, when phosphorylated, is also the RRM1-binding region. The PDZ-binding region is required for maximal interaction with ITPR1 and is also responsible for the IP3-insensitive interaction with ITPR1 (By similarity).By similarity1 Publication

<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

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GeneTreei
ENSGT00940000153650

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000227986

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005041

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O43865

KEGG Orthology (KO)

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KOi
K01251

Identification of Orthologs from Complete Genome Data

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OMAi
DRCVNVD

Database of Orthologous Groups

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OrthoDBi
371693at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O43865

TreeFam database of animal gene trees

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TreeFami
TF300415

Family and domain databases

Conserved Domains Database

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CDDi
cd00401 SAHH, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
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

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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

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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>.<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: O43865-1) [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
        10         20         30         40         50
MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE
60 70 80 90 100
FTKFPTKTGR RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK
110 120 130 140 150
GSSNFCVKNI KQAEFGRREI EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG
160 170 180 190 200
CTHITAQTAV LIETLCALGA QCRWSACNIY STQNEVAAAL AEAGVAVFAW
210 220 230 240 250
KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK YPNVFKKIRG
260 270 280 290 300
IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG
310 320 330 340 350
LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA
360 370 380 390 400
CMDGFRVVKL NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS
410 420 430 440 450
NTEIDVTSLR TPELTWERVR SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV
460 470 480 490 500
PTFVLSITAT TQALALIELY NAPEGRYKQD VYLLPKKMDE YVASLHLPSF
510 520 530
DAHLTELTDD QAKYLGLNKN GPFKPNYYRY
Length:530
Mass (Da):58,951
Last modified:April 4, 2006 - v2
<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:i974D23361A245D04
GO
Isoform 2 (identifier: O43865-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Note: Derived from EST data.Combined sources
Show »
Length:483
Mass (Da):53,753
Checksum:i18DFC7E74697E1D4
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC01960 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BI460083 differs from that shown. Reason: Frameshift at several positions.Curated
The sequence CAB43223 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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 conflicti94K → M in T19009 (PubMed:7782076).Curated1
Sequence conflicti99S → F in T19009 (PubMed:7782076).Curated1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0217511 – 47Missing in isoform 2. 5 PublicationsAdd BLAST47

Sequence databases

Select the link destinations:

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

More...
DDBJi
Links Updated
AF315687 mRNA Translation: AAL26869.1
AL036027 mRNA No translation available.
AK303690 mRNA Translation: BAG64680.1
AK316110 mRNA Translation: BAH14481.1
AL049954 mRNA Translation: CAB43223.2 Different initiation.
AL772411 Genomic DNA Translation: CAH70965.1
AL772411 Genomic DNA Translation: CAH70966.1
CH471122 Genomic DNA Translation: EAW56426.1
BC007576 mRNA Translation: AAH07576.3
BC010681 mRNA Translation: AAH10681.3
BC016942 mRNA Translation: AAH16942.3
BC065254 mRNA Translation: AAH65254.2
BC095476 mRNA Translation: AAH95476.2
BC110896 mRNA Translation: AAI10897.2
BI460083 mRNA No translation available.
U82761 mRNA Translation: AAC01960.1 Different initiation.
AU279527 mRNA No translation available.
T19009 mRNA No translation available.
BK005418 mRNA Translation: DAA05763.1
BK005417 mRNA Translation: DAA05762.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS55620.1 [O43865-2]
CCDS818.1 [O43865-1]

Protein sequence database of the Protein Information Resource

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PIRi
T08681

NCBI Reference Sequences

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RefSeqi
NP_001229602.1, NM_001242673.1 [O43865-2]
NP_001229603.1, NM_001242674.1 [O43865-2]
NP_001229604.1, NM_001242675.1 [O43865-2]
NP_001229605.1, NM_001242676.1 [O43865-2]
NP_006612.2, NM_006621.5 [O43865-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.743973

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000359172; ENSP00000352092; ENSG00000168710 [O43865-2]
ENST00000369799; ENSP00000358814; ENSG00000168710 [O43865-1]
ENST00000393614; ENSP00000377238; ENSG00000168710 [O43865-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
10768

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:10768

UCSC genome browser

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UCSCi
uc001dyx.4 human [O43865-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF315687 mRNA Translation: AAL26869.1
AL036027 mRNA No translation available.
AK303690 mRNA Translation: BAG64680.1
AK316110 mRNA Translation: BAH14481.1
AL049954 mRNA Translation: CAB43223.2 Different initiation.
AL772411 Genomic DNA Translation: CAH70965.1
AL772411 Genomic DNA Translation: CAH70966.1
CH471122 Genomic DNA Translation: EAW56426.1
BC007576 mRNA Translation: AAH07576.3
BC010681 mRNA Translation: AAH10681.3
BC016942 mRNA Translation: AAH16942.3
BC065254 mRNA Translation: AAH65254.2
BC095476 mRNA Translation: AAH95476.2
BC110896 mRNA Translation: AAI10897.2
BI460083 mRNA No translation available.
U82761 mRNA Translation: AAC01960.1 Different initiation.
AU279527 mRNA No translation available.
T19009 mRNA No translation available.
BK005418 mRNA Translation: DAA05763.1
BK005417 mRNA Translation: DAA05762.1
CCDSiCCDS55620.1 [O43865-2]
CCDS818.1 [O43865-1]
PIRiT08681
RefSeqiNP_001229602.1, NM_001242673.1 [O43865-2]
NP_001229603.1, NM_001242674.1 [O43865-2]
NP_001229604.1, NM_001242675.1 [O43865-2]
NP_001229605.1, NM_001242676.1 [O43865-2]
NP_006612.2, NM_006621.5 [O43865-1]
UniGeneiHs.743973

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MTGX-ray2.64A/B89-530[»]
ProteinModelPortaliO43865
SMRiO43865
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115987, 193 interactors
IntActiO43865, 40 interactors
MINTiO43865
STRINGi9606.ENSP00000358814

Chemistry databases

BindingDBiO43865
ChEMBLiCHEMBL3751646

PTM databases

iPTMnetiO43865
PhosphoSitePlusiO43865

Polymorphism and mutation databases

BioMutaiAHCYL1

Proteomic databases

EPDiO43865
jPOSTiO43865
MaxQBiO43865
PaxDbiO43865
PeptideAtlasiO43865
PRIDEiO43865
ProteomicsDBi49211
49212 [O43865-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10768
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359172; ENSP00000352092; ENSG00000168710 [O43865-2]
ENST00000369799; ENSP00000358814; ENSG00000168710 [O43865-1]
ENST00000393614; ENSP00000377238; ENSG00000168710 [O43865-2]
GeneIDi10768
KEGGihsa:10768
UCSCiuc001dyx.4 human [O43865-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10768
DisGeNETi10768
EuPathDBiHostDB:ENSG00000168710.17

GeneCards: human genes, protein and diseases

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GeneCardsi
AHCYL1
HGNCiHGNC:344 AHCYL1
HPAiHPA042589
MIMi607826 gene
neXtProtiNX_O43865
OpenTargetsiENSG00000168710
PharmGKBiPA24637

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1370 Eukaryota
COG0499 LUCA
GeneTreeiENSGT00940000153650
HOGENOMiHOG000227986
HOVERGENiHBG005041
InParanoidiO43865
KOiK01251
OMAiDRCVNVD
OrthoDBi371693at2759
PhylomeDBiO43865
TreeFamiTF300415

Enzyme and pathway databases

ReactomeiR-HSA-112043 PLC beta mediated events
R-HSA-1489509 DAG and IP3 signaling
R-HSA-2029485 Role of phospholipids in phagocytosis
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-422356 Regulation of insulin secretion
R-HSA-5218921 VEGFR2 mediated cell proliferation
R-HSA-5578775 Ion homeostasis
R-HSA-5607763 CLEC7A (Dectin-1) induces NFAT activation
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
SIGNORiO43865

Miscellaneous databases

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

More...
ChiTaRSi
AHCYL1 human
EvolutionaryTraceiO43865

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
AHCYL1

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

More...
GenomeRNAii
10768
PMAP-CutDBiO43865

Protein Ontology

More...
PROi
PR:O43865

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000168710 Expressed in 241 organ(s), highest expression level in hypothalamus
CleanExiHS_AHCYL1
ExpressionAtlasiO43865 baseline and differential
GenevisibleiO43865 HS

Family and domain databases

CDDicd00401 SAHH, 1 hit
InterProiView protein in InterPro
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

More...
ProtoNeti
Search...

<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 nameiSAHH2_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: O43865
Secondary accession number(s): B4E168
, Q2TAJ6, Q502W8, Q5VSM0, Q6P171, Q96PK4, Q9UG84
<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: December 15, 1998
Last sequence update: April 4, 2006
Last modified: January 16, 2019
This is version 180 of the entry and version 2 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
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