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Protein

Adenosylhomocysteinase 2

Gene

AHCYL1

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

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).By similarity6 Publications

Catalytic activityi

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

Cofactori

NAD(+)1 PublicationNote: Binds 1 NAD(+) per subunit.1 Publication

Pathway:iL-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 (AHCYL2), Adenosylhomocysteinase (AHCYL1), Adenosylhomocysteinase (AHCY), Adenosylhomocysteinase (AHCY), Adenosylhomocysteinase, Adenosylhomocysteinase 2 (AHCYL1), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551SubstrateBy similarity
Binding sitei229 – 2291SubstrateBy similarity
Binding sitei254 – 2541SubstrateBy similarity
Binding sitei284 – 2841SubstrateBy similarity
Binding sitei288 – 2881SubstrateBy similarity
Binding sitei341 – 3411NAD1 Publication
Binding sitei376 – 3761NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi318 – 3225NAD1 Publication
Nucleotide bindingi397 – 3993NAD1 Publication

GO - Molecular functioni

GO - Biological processi

  • angiotensin-activated signaling pathway Source: UniProtKB
  • mRNA polyadenylation Source: UniProtKB
  • one-carbon metabolic process Source: UniProtKB-KW
  • positive regulation of sodium ion transport Source: UniProtKB
  • protein export from nucleus Source: Ensembl
  • regulation of anion transport Source: Ensembl
  • regulation of ion transmembrane transporter activity Source: UniProtKB
  • regulation of mRNA 3'-end processing Source: UniProtKB
  • response to calcium ion Source: UniProtKB
  • S-adenosylmethionine cycle Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NAD, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_111064. DAG and IP3 signaling.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_15426. PLC beta mediated events.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_18325. Regulation of insulin secretion.
REACT_188329. CLEC7A (Dectin-1) induces NFAT activation.
REACT_264273. VEGFR2 mediated cell proliferation.
UniPathwayiUPA00314; UER00076.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosylhomocysteinase 2 (EC:3.3.1.1)
Short name:
AdoHcyase 2
Alternative name(s):
DC-expressed AHCY-like molecule
IP(3)Rs binding protein released with IP(3)
Short name:
IRBIT
S-adenosyl-L-homocysteine hydrolase 2
S-adenosylhomocysteine hydrolase-like protein 1Imported
Gene namesi
Name:AHCYL1Imported
Synonyms:DCAL, IRBIT, XPVKONAImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:344. AHCYL1.

Subcellular locationi

  • Endoplasmic reticulum By similarity
  • Cytoplasmcytosol By similarity
  • Microsome By similarity
  • Apical cell membrane By similarity

  • Note: Associates with membranes when phosphorylated, probably through interaction with ITPR1.By similarity

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: GO_Central
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521T → A: No effect on interaction with SLC4A4. 1 Publication
Mutagenesisi58 – 581T → A: No effect on interaction with SLC4A4. 1 Publication
Mutagenesisi62 – 621S → A: No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 2 Publications
Mutagenesisi64 – 641S → A: No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 3 Publications
Mutagenesisi66 – 661S → A: Slightly decreases interaction with ITPR1. Slightly decreases phosphorylation. No effect on interaction with SLC4A4. Abolishes interaction with FIP1L1. 3 Publications
Mutagenesisi68 – 681S → 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 Publications
Mutagenesisi70 – 701S → A: Highly decreases interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Abolishes interaction with FIP1L1. 3 Publications
Mutagenesisi71 – 711S → 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 Publications
Mutagenesisi72 – 721T → A: Highly decreases interaction with ITPR1. Slightly increases phosphorylation. No effect on interaction with SLC4A4. Highly decreases interaction with FIP1L1. 3 Publications
Mutagenesisi74 – 741S → 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 Publications
Mutagenesisi76 – 761S → G: No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 3 Publications
Mutagenesisi77 – 771S → A: Highly decreases interaction with ITPR1. Slightly decreases phosphorylation. Strongly decreases interaction with SLC4A4. Abolishes interaction with FIP1L1. 3 Publications
Mutagenesisi80 – 801S → A: No effect on interaction with SLC4A4. Highly decreases interaction with FIP1L1. 3 Publications
Mutagenesisi82 – 821T → A: No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Decreases interaction with FIP1L1. 3 Publications
Mutagenesisi84 – 841S → A: Slightly decreases interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Decreases interaction with FIP1L1. 3 Publications
Mutagenesisi85 – 851S → A: Slightly decreases interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Decreases interaction with FIP1L1. 3 Publications
Mutagenesisi90 – 901S → A: No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 3 Publications
Mutagenesisi97 – 971T → A: No effect on interaction with ITPR1. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1. 3 Publications

Organism-specific databases

PharmGKBiPA24637.

Polymorphism and mutation databases

BioMutaiAHCYL1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 530529Adenosylhomocysteinase 2PRO_0000116908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei40 – 401N6-acetyllysineBy similarity
Modified residuei68 – 681Phosphoserine2 Publications
Modified residuei71 – 711Phosphoserine2 Publications
Modified residuei74 – 741Phosphoserine1 Publication
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei391 – 3911Phosphoserine1 Publication
Isoform 2 (identifier: O43865-2)
Modified residuei1 – 11N-acetylmethionine1 Publication

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

MaxQBiO43865.
PaxDbiO43865.
PeptideAtlasiO43865.
PRIDEiO43865.

PTM databases

PhosphoSiteiO43865.

Miscellaneous databases

PMAP-CutDBO43865.

Expressioni

Tissue specificityi

Expressed in dendritic cells.1 Publication

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

BgeeiO43865.
CleanExiHS_AHCYL1.
ExpressionAtlasiO43865. baseline and differential.
GenevisibleiO43865. HS.

Organism-specific databases

HPAiHPA042589.

Interactioni

Subunit structurei

Forms multimers (PubMed:16793548). Forms heterotmultimers 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

Binary interactionsi

WithEntry#Exp.IntActNotes
BIDP559573EBI-2371423,EBI-519672
BIDP55957-23EBI-2371423,EBI-10215147
CDKN2CP427733EBI-2371423,EBI-711290
DACH1Q9UI36-27EBI-2371423,EBI-10186082
GEMP550405EBI-2371423,EBI-744104
MEOX2A4D1273EBI-2371423,EBI-10172134
PPLO604373EBI-2371423,EBI-368321
PSMD9O002333EBI-2371423,EBI-750973
SLC23A1Q9UHI73EBI-2371423,EBI-1759386
SOX30O949933EBI-2371423,EBI-742973
tatP046085EBI-2371423,EBI-6164389From a different organism.
ZNF165Q53Z405EBI-2371423,EBI-10186058

Protein-protein interaction databases

BioGridi115987. 127 interactions.
IntActiO43865. 19 interactions.
STRINGi9606.ENSP00000358814.

Structurei

Secondary structure

1
530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi113 – 12412Combined sources
Helixi128 – 13710Combined sources
Turni142 – 1454Combined sources
Beta strandi147 – 1526Combined sources
Helixi156 – 16712Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi177 – 1804Combined sources
Helixi184 – 19310Combined sources
Beta strandi196 – 1983Combined sources
Helixi205 – 21612Combined sources
Beta strandi224 – 2318Combined sources
Helixi232 – 2409Combined sources
Helixi242 – 2454Combined sources
Beta strandi249 – 2535Combined sources
Helixi256 – 26510Combined sources
Turni266 – 2694Combined sources
Beta strandi275 – 2773Combined sources
Helixi282 – 29312Combined sources
Helixi299 – 3057Combined sources
Beta strandi313 – 3175Combined sources
Helixi321 – 33313Combined sources
Beta strandi336 – 3405Combined sources
Helixi344 – 3529Combined sources
Helixi360 – 3623Combined sources
Turni363 – 3664Combined sources
Beta strandi368 – 3725Combined sources
Helixi382 – 3876Combined sources
Beta strandi392 – 3965Combined sources
Turni400 – 4034Combined sources
Helixi406 – 4094Combined sources
Beta strandi415 – 4206Combined sources
Beta strandi423 – 4275Combined sources
Beta strandi433 – 4375Combined sources
Helixi438 – 4403Combined sources
Helixi444 – 4463Combined sources
Helixi452 – 47120Combined sources
Beta strandi479 – 4824Combined sources
Helixi486 – 49611Combined sources
Helixi497 – 5004Combined sources
Helixi509 – 5146Combined sources
Beta strandi519 – 5213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTGX-ray2.64A/B89-530[»]
ProteinModelPortaliO43865.
SMRiO43865. Positions 101-530.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43865.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 9228PEST1 PublicationAdd
BLAST
Regioni281 – 448168NAD bindingBy similarityAdd
BLAST
Regioni520 – 53011PDZ-bindingBy similarityAdd
BLAST

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

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

eggNOGiCOG0499.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227986.
HOVERGENiHBG005041.
InParanoidiO43865.
KOiK01251.
OMAiPVKKQIQ.
OrthoDBiEOG76739S.
PhylomeDBiO43865.
TreeFamiTF300415.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 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
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.1 Publication
Show »
Length:483
Mass (Da):53,753
Checksum:i18DFC7E74697E1D4
GO

Sequence cautioni

The sequence AAC01960.1 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 CAB43223.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941K → M in T19009 (PubMed:7782076).Curated
Sequence conflicti99 – 991S → F in T19009 (PubMed:7782076).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 2. 5 PublicationsVSP_021751Add
BLAST

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.

Genome annotation databases

EnsembliENST00000359172; ENSP00000352092; ENSG00000168710. [O43865-2]
ENST00000369799; ENSP00000358814; ENSG00000168710.
ENST00000393614; ENSP00000377238; ENSG00000168710. [O43865-2]
GeneIDi10768.
KEGGihsa:10768.
UCSCiuc001dyx.3. human. [O43865-1]

Keywords - Coding sequence diversityi

Alternative splicing

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTGX-ray2.64A/B89-530[»]
ProteinModelPortaliO43865.
SMRiO43865. Positions 101-530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115987. 127 interactions.
IntActiO43865. 19 interactions.
STRINGi9606.ENSP00000358814.

PTM databases

PhosphoSiteiO43865.

Polymorphism and mutation databases

BioMutaiAHCYL1.

Proteomic databases

MaxQBiO43865.
PaxDbiO43865.
PeptideAtlasiO43865.
PRIDEiO43865.

Protocols and materials databases

DNASUi10768.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359172; ENSP00000352092; ENSG00000168710. [O43865-2]
ENST00000369799; ENSP00000358814; ENSG00000168710.
ENST00000393614; ENSP00000377238; ENSG00000168710. [O43865-2]
GeneIDi10768.
KEGGihsa:10768.
UCSCiuc001dyx.3. human. [O43865-1]

Organism-specific databases

CTDi10768.
GeneCardsiGC01P110529.
HGNCiHGNC:344. AHCYL1.
HPAiHPA042589.
MIMi607826. gene.
neXtProtiNX_O43865.
PharmGKBiPA24637.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0499.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227986.
HOVERGENiHBG005041.
InParanoidiO43865.
KOiK01251.
OMAiPVKKQIQ.
OrthoDBiEOG76739S.
PhylomeDBiO43865.
TreeFamiTF300415.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.
ReactomeiREACT_111064. DAG and IP3 signaling.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_15426. PLC beta mediated events.
REACT_160158. Role of phospholipids in phagocytosis.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_18325. Regulation of insulin secretion.
REACT_188329. CLEC7A (Dectin-1) induces NFAT activation.
REACT_264273. VEGFR2 mediated cell proliferation.

Miscellaneous databases

ChiTaRSiAHCYL1. human.
EvolutionaryTraceiO43865.
GeneWikiiAHCYL1.
GenomeRNAii10768.
NextBioi40889.
PMAP-CutDBO43865.
PROiO43865.
SOURCEiSearch...

Gene expression databases

BgeeiO43865.
CleanExiHS_AHCYL1.
ExpressionAtlasiO43865. baseline and differential.
GenevisibleiO43865. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation."
    Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J., Hart D.N., Kato M.
    Immunogenetics 53:993-1001(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "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] (ISOFORM 2).
    Tissue: Kidney and Thalamus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-251 (ISOFORM 2).
    Tissue: Brain, Colon, Eye, Placenta, PNS and Testis.
  7. "Complementation of chromosomal instability in the xeroderma pigmentosum variant by a gene on human chromosome 1 with homology to S-adenosyl homocysteine hydrolase."
    Volpe J.P.G., McDowell M., Jostes R.F., Afzal V., Sadinski W., Trask B.J., Legerski R., Cleaver J.E.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-530 (ISOFORM 1).
    Tissue: Skin.
  8. "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis."
    Imabayashi H., Mori T., Gojo S., Kiyono T., Sugiyama T., Irie R., Isogai T., Hata J., Toyama Y., Umezawa A.
    Exp. Cell Res. 288:35-50(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-164 (ISOFORM 2).
    Tissue: Chondrocyte.
  9. "Characterization of a large population of mRNAs from human testis."
    Pawlak A., Toussaint C., Levy I., Bulle F., Poyard M., Barouki R., Guellaen G.
    Genomics 26:151-158(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-105 (ISOFORM 2).
    Tissue: Testis.
  10. "Suppression and overexpression of adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) influences zebrafish embryo development: a possible role for AHCYL1 in inositol phospholipid signaling."
    Cooper B.J., Key B., Carter A., Angel N.Z., Hart D.N.J., Kato M.
    J. Biol. Chem. 281:22471-22484(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM 2).
  11. "IRBIT suppresses IP3 receptor activity by competing with IP3 for the common binding site on the IP3 receptor."
    Ando H., Mizutani A., Kiefer H., Tsuzurugi D., Michikawa T., Mikoshiba K.
    Mol. Cell 22:795-806(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH ITPR1, PHOSPHORYLATION AT SER-68 AND SER-71, MUTAGENESIS OF SER-64; SER-66; SER-68; SER-70; SER-71; THR-72; SER-74; SER-76; SER-77; SER-80; THR-82; SER-84; SER-85; SER-90 AND THR-97.
  12. "IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein, specifically binds to and activates pancreas-type Na+/HCO3-cotransporter 1 (pNBC1)."
    Shirakabe K., Priori G., Yamada H., Ando H., Horita S., Fujita T., Fujimoto I., Mizutani A., Seki G., Mikoshiba K.
    Proc. Natl. Acad. Sci. U.S.A. 103:9542-9547(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC4A4, MUTAGENESIS OF THR-52; THR-58; SER-62; SER-64; SER-66; SER-68; SER-70; SER-71; THR-72; SER-74; SER-76; SER-77; SER-80; THR-82; SER-84; SER-85; SER-90 AND THR-97.
  13. "IRBIT, inositol 1,4,5-triphosphate (IP3) receptor-binding protein released with IP3, binds Na+/H+ exchanger NHE3 and activates NHE3 activity in response to calcium."
    He P., Zhang H., Yun C.C.
    J. Biol. Chem. 283:33544-33553(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC9A3.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Inositol 1,4,5-triphosphate receptor-binding protein released with inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA 3' processing machinery in a phosphorylation-dependent manner and inhibits polyadenylation."
    Kiefer H., Mizutani A., Iemura S., Natsume T., Ando H., Kuroda Y., Mikoshiba K.
    J. Biol. Chem. 284:10694-10705(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FIP1L1 AND PAPOLA, RNA-BINDING, MUTAGENESIS OF SER-62; SER-64; SER-66; SER-68; SER-70; SER-71; THR-72; SER-74; SER-76; SER-77; SER-80; THR-82; SER-84; SER-85; SER-90 AND THR-97.
  16. "An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage."
    Ando H., Mizutani A., Mikoshiba K.
    J. Neurochem. 109:539-550(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AHCYL2 AND ITPR1, PHOSPHORYLATION AT SER-68; SER-71; SER-74 AND SER-77.
  17. "Activation of Na+/H+ exchanger NHE3 by angiotensin II is mediated by inositol 1,4,5-triphosphate (IP3) receptor-binding protein released with IP3 (IRBIT) and Ca2+/calmodulin-dependent protein kinase II."
    He P., Klein J., Yun C.C.
    J. Biol. Chem. 285:27869-27878(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC9A3, MUTAGENESIS OF SER-68; SER-71 AND SER-74.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes."
    Arnaoutov A., Dasso M.
    Science 345:1512-1515(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 89-530 OF MUTANT ALA-508 IN COMPLEX WITH NAD, COFACTOR, FUNCTION, INTERACTION WITH RRM1, MISCELLANEOUS, PEST REGION, PHOSPHORYLATION.

Entry informationi

Entry nameiSAHH2_HUMAN
AccessioniPrimary (citable) accession number: O43865
Secondary accession number(s): B4E168
, Q2TAJ6, Q502W8, Q5VSM0, Q6P171, Q96PK4, Q9UG84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 4, 2006
Last modified: July 22, 2015
This is version 147 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

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.