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P23526

- SAHH_HUMAN

UniProt

P23526 - SAHH_HUMAN

Protein

Adenosylhomocysteinase

Gene

AHCY

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    Catalytic activityi

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

    Cofactori

    Binds 1 NAD per subunit.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571SubstrateBy similarity
    Binding sitei131 – 1311SubstrateBy similarity
    Binding sitei156 – 1561SubstrateBy similarity
    Binding sitei186 – 1861SubstrateBy similarity
    Binding sitei190 – 1901SubstrateBy similarity
    Binding sitei243 – 2431NAD2 Publications
    Binding sitei248 – 2481NAD2 Publications
    Binding sitei346 – 3461NAD2 Publications
    Binding sitei353 – 3531NAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi157 – 1593NAD2 Publications
    Nucleotide bindingi222 – 2276NAD2 Publications
    Nucleotide bindingi299 – 3013NAD2 Publications

    GO - Molecular functioni

    1. adenosylhomocysteinase activity Source: UniProtKB

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. methylation Source: Reactome
    3. one-carbon metabolic process Source: UniProtKB-KW
    4. small molecule metabolic process Source: Reactome
    5. sulfur amino acid metabolic process Source: Reactome
    6. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_115639. Sulfur amino acid metabolism.
    REACT_6946. Methylation.
    SABIO-RKP23526.
    UniPathwayiUPA00314; UER00076.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenosylhomocysteinase (EC:3.3.1.1)
    Short name:
    AdoHcyase
    Alternative name(s):
    S-adenosyl-L-homocysteine hydrolase
    Gene namesi
    Name:AHCY
    Synonyms:SAHH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:343. AHCY.

    Subcellular locationi

    Cytoplasm 1 Publication. Melanosome 1 Publication
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. melanosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Hypermethioninemia with S-adenosylhomocysteine hydrolase deficiency (HMAHCHD) [MIM:613752]: A metabolic disorder characterized by hypermethioninemia associated with failure to thrive, mental and motor retardation, facial dysmorphism with abnormal hair and teeth, and myocardiopathy.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491R → C in HMAHCHD. 2 Publications
    VAR_058588
    Natural varianti86 – 861D → G in HMAHCHD. 2 Publications
    VAR_058589
    Natural varianti89 – 891A → V in HMAHCHD. 1 Publication
    VAR_058590
    Natural varianti143 – 1431Y → C in HMAHCHD. 2 Publications
    VAR_058591

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613752. phenotype.
    Orphaneti88618. Psychomotor retardation due to S-adenosylhomocysteine hydrolase deficiency.
    PharmGKBiPA24636.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 432431AdenosylhomocysteinasePRO_0000116902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP23526.
    PaxDbiP23526.
    PeptideAtlasiP23526.
    PRIDEiP23526.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00012007.

    PTM databases

    PhosphoSiteiP23526.

    Expressioni

    Gene expression databases

    ArrayExpressiP23526.
    BgeeiP23526.
    CleanExiHS_AHCY.
    GenevestigatoriP23526.

    Organism-specific databases

    HPAiHPA041225.
    HPA044675.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi106696. 50 interactions.
    IntActiP23526. 13 interactions.
    MINTiMINT-5000523.
    STRINGi9606.ENSP00000217426.

    Structurei

    Secondary structure

    1
    432
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Helixi12 – 143
    Helixi15 – 2612
    Helixi30 – 3910
    Turni40 – 423
    Turni44 – 474
    Beta strandi49 – 546
    Helixi58 – 6912
    Beta strandi73 – 775
    Beta strandi79 – 824
    Helixi86 – 949
    Beta strandi99 – 1013
    Helixi107 – 1159
    Beta strandi118 – 1203
    Beta strandi126 – 1338
    Helixi134 – 1429
    Helixi144 – 1496
    Beta strandi152 – 1554
    Helixi158 – 16912
    Beta strandi175 – 1795
    Helixi184 – 1874
    Helixi190 – 20718
    Beta strandi215 – 2195
    Helixi223 – 23412
    Beta strandi238 – 2425
    Helixi246 – 2549
    Helixi262 – 2654
    Turni266 – 2683
    Beta strandi270 – 2745
    Beta strandi277 – 2793
    Helixi284 – 2874
    Beta strandi294 – 2985
    Beta strandi300 – 3023
    Helixi308 – 3147
    Beta strandi316 – 3227
    Beta strandi325 – 3295
    Beta strandi335 – 3395
    Helixi340 – 3423
    Helixi345 – 3484
    Helixi355 – 37420
    Helixi376 – 3783
    Beta strandi381 – 3844
    Helixi388 – 39912
    Turni400 – 4034
    Helixi411 – 4177
    Beta strandi421 – 4233

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A7AX-ray2.80A/B1-432[»]
    1LI4X-ray2.01A1-432[»]
    3NJ4X-ray2.50A/B/C/D1-432[»]
    ProteinModelPortaliP23526.
    SMRiP23526. Positions 3-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23526.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the adenosylhomocysteinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0499.
    HOGENOMiHOG000227987.
    HOVERGENiHBG005041.
    InParanoidiP23526.
    KOiK01251.
    OMAiMGVEIDS.
    OrthoDBiEOG76739S.
    PhylomeDBiP23526.
    TreeFamiTF300415.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00563. AdoHcyase.
    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. Align

    Isoform 1 (identifier: P23526-1) [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

    MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMRERYS ASKPLKGARI    50
    AGCLHMTVET AVLIETLVTL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY 100
    AWKGETDEEY LWCIEQTLYF KDGPLNMILD DGGDLTNLIH TKYPQLLPGI 150
    RGISEETTTG VHNLYKMMAN GILKVPAINV NDSVTKSKFD NLYGCRESLI 200
    DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI ITEIDPINAL 250
    QAAMEGYEVT TMDEACQEGN IFVTTTGCID IILGRHFEQM KDDAIVCNIG 300
    HFDVEIDVKW LNENAVEKVN IKPQVDRYRL KNGRRIILLA EGRLVNLGCA 350
    MGHPSFVMSN SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG 400
    KLNVKLTKLT EKQAQYLGMS CDGPFKPDHY RY 432
    Length:432
    Mass (Da):47,716
    Last modified:January 23, 2007 - v4
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti249 – 2491A → V in BAG53495. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → W.1 Publication
    Corresponds to variant rs13043752 [ dbSNP | Ensembl ].
    VAR_052286
    Natural varianti49 – 491R → C in HMAHCHD. 2 Publications
    VAR_058588
    Natural varianti86 – 861D → G in HMAHCHD. 2 Publications
    VAR_058589
    Natural varianti86 – 861D → N.1 Publication
    VAR_006934
    Natural varianti89 – 891A → V in HMAHCHD. 1 Publication
    VAR_058590
    Natural varianti143 – 1431Y → C in HMAHCHD. 2 Publications
    VAR_058591

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform 2. 1 PublicationVSP_045404Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAC09528.1.
    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_000687.2. [P23526-1]
    NP_001155238.1. NM_001161766.1. [P23526-2]
    XP_005260373.1. XM_005260316.2. [P23526-2]
    XP_005260374.1. XM_005260317.1. [P23526-2]
    UniGeneiHs.388004.

    Genome annotation databases

    EnsembliENST00000217426; ENSP00000217426; ENSG00000101444. [P23526-1]
    ENST00000538132; ENSP00000442820; ENSG00000101444. [P23526-2]
    GeneIDi191.
    KEGGihsa:191.
    UCSCiuc002xai.3. human. [P23526-1]

    Polymorphism databases

    DMDMi20141702.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAC09528.1 .
    CH471077 Genomic DNA. Translation: EAW76279.1 .
    CH471077 Genomic DNA. Translation: EAW76280.1 .
    BC010018 mRNA. Translation: AAH10018.1 .
    BC011606 mRNA. Translation: AAH11606.1 .
    CCDSi CCDS13233.1. [P23526-1 ]
    CCDS54457.1. [P23526-2 ]
    PIRi A43629.
    RefSeqi NP_000678.1. NM_000687.2. [P23526-1 ]
    NP_001155238.1. NM_001161766.1. [P23526-2 ]
    XP_005260373.1. XM_005260316.2. [P23526-2 ]
    XP_005260374.1. XM_005260317.1. [P23526-2 ]
    UniGenei Hs.388004.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A7A X-ray 2.80 A/B 1-432 [» ]
    1LI4 X-ray 2.01 A 1-432 [» ]
    3NJ4 X-ray 2.50 A/B/C/D 1-432 [» ]
    ProteinModelPortali P23526.
    SMRi P23526. Positions 3-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106696. 50 interactions.
    IntActi P23526. 13 interactions.
    MINTi MINT-5000523.
    STRINGi 9606.ENSP00000217426.

    Chemistry

    BindingDBi P23526.
    ChEMBLi CHEMBL2664.
    GuidetoPHARMACOLOGYi 1233.

    PTM databases

    PhosphoSitei P23526.

    Polymorphism databases

    DMDMi 20141702.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00012007.

    Proteomic databases

    MaxQBi P23526.
    PaxDbi P23526.
    PeptideAtlasi P23526.
    PRIDEi P23526.

    Protocols and materials databases

    DNASUi 191.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217426 ; ENSP00000217426 ; ENSG00000101444 . [P23526-1 ]
    ENST00000538132 ; ENSP00000442820 ; ENSG00000101444 . [P23526-2 ]
    GeneIDi 191.
    KEGGi hsa:191.
    UCSCi uc002xai.3. human. [P23526-1 ]

    Organism-specific databases

    CTDi 191.
    GeneCardsi GC20M032868.
    HGNCi HGNC:343. AHCY.
    HPAi HPA041225.
    HPA044675.
    MIMi 180960. gene.
    613752. phenotype.
    neXtProti NX_P23526.
    Orphaneti 88618. Psychomotor retardation due to S-adenosylhomocysteine hydrolase deficiency.
    PharmGKBi PA24636.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0499.
    HOGENOMi HOG000227987.
    HOVERGENi HBG005041.
    InParanoidi P23526.
    KOi K01251.
    OMAi MGVEIDS.
    OrthoDBi EOG76739S.
    PhylomeDBi P23526.
    TreeFami TF300415.

    Enzyme and pathway databases

    UniPathwayi UPA00314 ; UER00076 .
    Reactomei REACT_115639. Sulfur amino acid metabolism.
    REACT_6946. Methylation.
    SABIO-RK P23526.

    Miscellaneous databases

    ChiTaRSi AHCY. human.
    EvolutionaryTracei P23526.
    GenomeRNAii 191.
    NextBioi 780.
    PROi P23526.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23526.
    Bgeei P23526.
    CleanExi HS_AHCY.
    Genevestigatori P23526.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00563. AdoHcyase.
    InterProi IPR000043. Adenosylhomocysteinase.
    IPR015878. Ado_hCys_hydrolase_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    IPR020082. S-Ado-L-homoCys_hydrolase_CS.
    [Graphical view ]
    PANTHERi PTHR23420. PTHR23420. 1 hit.
    Pfami PF05221. AdoHcyase. 1 hit.
    PF00670. AdoHcyase_NAD. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001109. Ad_hcy_hydrolase. 1 hit.
    SMARTi SM00996. AdoHcyase. 1 hit.
    SM00997. AdoHcyase_NAD. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00936. ahcY. 1 hit.
    PROSITEi PS00738. ADOHCYASE_1. 1 hit.
    PS00739. ADOHCYASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of full length cDNA for human S-adenosylhomocysteine hydrolase."
      Coulter-Karis D.E., Hershfield M.S.
      Ann. Hum. Genet. 53:169-175(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-86.
      Tissue: Placenta.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Testis and Umbilical cord blood.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [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).
      Tissue: Placenta and Skin.
    7. "Limited proteolysis of S-adenosylhomocysteine hydrolase: implications for the three-dimensional structure."
      Gupta R.A., Yuan C.-S., Ault-Riche D.B., Borchardt R.T.
      Arch. Biochem. Biophys. 319:365-371(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6; 104-108 AND 198-202.
    8. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-34; 95-103; 143-186; 215-226; 336-343 AND 389-405, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    9. "Isozyme and DNA analysis of human S-adenosyl-L-homocysteine hydrolase (AHCY)."
      Arredondo-Vega F.X., Charlton J.A., Edwards Y.H., Hopkinson D.A., Whitehouse D.B.
      Ann. Hum. Genet. 53:157-167(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-432 (ISOFORM 1).
      Tissue: Placenta.
    10. "Photoaffinity labeling of human placental S-adenosylhomocysteine hydrolase with [2-3H]8-azido-adenosine."
      Yuan C.S., Borchardt R.T.
      J. Biol. Chem. 270:16140-16146(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 175-186 AND 319-327.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength."
      Turner M.A., Yuan C.S., Borchardt R.T., Hershfield M.S., Smith G.D., Howell P.L.
      Nat. Struct. Biol. 5:369-376(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD AND ADENOSINE ANALOG, SUBUNIT, COFACTOR.
      Tissue: Placenta.
    14. "Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions."
      Yang X., Hu Y., Yin D.H., Turner M.A., Wang M., Borchardt R.T., Howell P.L., Kuczera K., Schowen R.L.
      Biochemistry 42:1900-1909(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH NAD AND NEPLANOCIN A, FUNCTION, COFACTOR.
    15. "Effect of genetic variation in the human S-adenosylhomocysteine hydrolase gene on total homocysteine concentrations and risk of recurrent venous thrombosis."
      Gellekink H., den Heijer M., Kluijtmans L.A., Blom H.J.
      Eur. J. Hum. Genet. 12:942-948(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TRP-38.
    16. Cited for: VARIANT HMAHCHD CYS-143.
    17. Cited for: VARIANTS HMAHCHD VAL-89 AND CYS-143.
    18. "S-adenosylhomocysteine hydrolase (AHCY) deficiency: two novel mutations with lethal outcome."
      Vugrek O., Beluzic R., Nakic N., Mudd S.H.
      Hum. Mutat. 30:E555-E565(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HMAHCHD CYS-49 AND GLY-86.
    19. "S-adenosylhomocysteine hydrolase deficiency: two siblings with fetal hydrops and fatal outcomes."
      Grubbs R., Vugrek O., Deisch J., Wagner C., Stabler S., Allen R., Baric I., Rados M., Mudd S.H.
      J. Inherit. Metab. Dis. 33:705-713(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HMAHCHD CYS-49 AND GLY-86.

    Entry informationi

    Entry nameiSAHH_HUMAN
    AccessioniPrimary (citable) accession number: P23526
    Secondary accession number(s): A8K307
    , B3KUN3, E1P5P2, F5H737, Q96A36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 160 of the entry and version 4 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

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3