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UniProtKB/Swiss-Prot entry P23526


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SAHH_HUMAN
Primary accession number P23526
Secondary accession number Q96A36
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 95)
Name and origin of the protein
Protein name Adenosylhomocysteinase
Synonyms AdoHcyase
EC 3.3.1.1
S-adenosyl-L-homocysteine hydrolase
Gene name
Name: AHCY
Synonyms: SAHH
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-86.
TISSUE=Placenta;
PubMed=2596825 [NCBI, ExPASy, EBI, Israel, Japan]
Coulter-Karis D.E., Hershfield M.S.;
"Sequence of full length cDNA for human S-adenosylhomocysteine hydrolase.";
Ann. Hum. Genet. 53:169-175(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-6; 104-108 AND 198-202.
DOI=10.1006/abbi.1995.1306; PubMed=7786017 [NCBI, ExPASy, EBI, Israel, Japan]
Gupta R.A., Yuan C.-S., Ault-Riche D.B., Borchardt R.T.;
"Limited proteolysis of S-adenosylhomocysteine hydrolase: implications for the three-dimensional structure.";
Arch. Biochem. Biophys. 319:365-371(1995).
[6]
PROTEIN SEQUENCE OF 2-34; 95-103; 143-186; 215-226; 336-343 AND 389-405, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 122-432.
TISSUE=Placenta;
PubMed=2574561 [NCBI, ExPASy, EBI, Israel, Japan]
Arredondo-Vega F.X., Charlton J.A., Edwards Y.H., Hopkinson D.A., Whitehouse D.B.;
"Isozyme and DNA analysis of human S-adenosyl-L-homocysteine hydrolase (AHCY).";
Ann. Hum. Genet. 53:157-167(1989).
[8]
PROTEIN SEQUENCE OF 175-186 AND 319-327.
DOI=10.1074/jbc.270.27.16140; PubMed=7608178 [NCBI, ExPASy, EBI, Israel, Japan]
Yuan C.S., Borchardt R.T.;
"Photoaffinity labeling of human placental S-adenosylhomocysteine hydrolase with [2-3H]8-azido-adenosine.";
J. Biol. Chem. 270:16140-16146(1995).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[10]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
TISSUE=Placenta;
DOI=10.1038/nsb0598-369; PubMed=9586999 [NCBI, ExPASy, EBI, Israel, Japan]
Turner M.A., Yuan C.S., Borchardt R.T., Hershfield M.S., Smith G.D., Howell P.L.;
"Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength.";
Nat. Struct. Biol. 5:369-376(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M61831; AAA51681.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M61832; AAA51682.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006697; AAP35343.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356299; CAC09528.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010018; AAH10018.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011606; AAH11606.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A43629; A43629.
RefSeq NP_000678.1; -.
UniGene Hs.388004
3D structure databases
PDB
1A7A; X-ray; 2.80 A; A/B=1-432.[ExPASy / RCSB / EBI]
1LI4; X-ray; 2.01 A; A=1-432.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A7A; -.
1LI4; -.
ModBase P23526.
Protein-protein interaction databases
IntAct P23526; -.
PTM databases
PhosphoSite P23526; -.
Enzyme and pathway databases
Reactome REACT_2063; Metabolism of xenobiotics.
2D gel databases
REPRODUCTION-2DPAGE IPI00012007; -.
Organism-specific databases
H-InvDB HIX0015744; -.
HGNC HGNC:343; AHCY.
GenAtlas AHCY.
MIM 180960; gene+phenotype. [NCBI / EBI]
Orphanet 88618; Psychomotor retardation due to S-adenosylhomocysteine hydrolase deficiency.
PharmGKB PA24636; -.
GeneCards P23526.
Gene expression databases
ArrayExpress P23526; -.
CleanEx HS_AHCY; -.
GermOnline ENSG00000101444; Homo sapiens.
Ontologies
GO
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004013; Molecular function: adenosylhomocysteinase activity (traceable author statement from UniProtKB).
GO:0006730; Biological process: one-carbon compound metabolic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000043; Ad_hcy_hydrolase.
IPR015878; Ado_hCys_hydrolase_NAD-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.1480; Ad_hcy_hydrolase; 1.
PANTHER PTHR23420; Ad_hcy_hydrolase; 1.
Pfam PF05221; AdoHcyase; 1.
PF00670; AdoHcyase_NAD; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001109; Ad_hcy_hydrolase; 1.
TIGRFAMs TIGR00936; ahcY; 1.
PROSITE PS00738; ADOHCYASE_1; 1.
PS00739; ADOHCYASE_2; 1.
ProtoNet P23526.
Proteomic databases
PeptideAtlas P23526; -.
Genome annotation databases
Ensembl ENSG00000101444; Homo sapiens. [Contig view]
GeneID 191; -.
KEGG hsa:191; -.
Phylogenomic databases
HOGENOM P23526; -.
HOVERGEN P23526; -.
Other
LinkHub P23526; -.
NextBio 780; -.
SOURCE AHCY; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; NAD; One-carbon metabolism; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   432  431     Adenosylhomocysteinase. PRO_0000116902
REGION   183   350  168     NAD binding (By similarity). 
BINDING   57    57        Substrate (By similarity). 
BINDING   131   131        Substrate (By similarity). 
BINDING   156   156        Substrate (By similarity). 
BINDING   186   186        Substrate (By similarity). 
BINDING   190   190        Substrate (By similarity). 
MOD_RES   2     2        N-acetylserine. 
VARIANT   86    86  1     D -> N. VAR_006934 
STRAND   8    10  3      
HELIX   12    14  3      
HELIX   15    26  12      
HELIX   30    39  10      
TURN   40    42  3      
TURN   44    47  4      
STRAND   49    54  6      
HELIX   58    69  12      
STRAND   73    77  5      
HELIX   86    94  9      
STRAND   99   101  3      
HELIX   107   115  9      
STRAND   118   120  3      
STRAND   126   133  8      
HELIX   134   142  9      
HELIX   144   149  6      
STRAND   152   155  4      
HELIX   158   169  12      
STRAND   175   179  5      
HELIX   184   187  4      
HELIX   190   207  18      
STRAND   215   219  5      
HELIX   223   234  12      
STRAND   238   242  5      
HELIX   246   254  9      
HELIX   262   265  4      
TURN   266   268  3      
STRAND   270   274  5      
HELIX   284   287  4      
STRAND   294   298  5      
STRAND   300   302  3      
HELIX   308   314  7      
STRAND   316   322  7      
STRAND   325   329  5      
STRAND   335   339  5      
HELIX   340   342  3      
HELIX   345   348  4      
HELIX   355   374  20      
HELIX   376   378  3      
STRAND   381   384  4      
HELIX   388   399  12      
TURN   400   403  4      
HELIX   411   417  7      
Sequence information
Length: 432 AA [This is the length of the unprocessed precursor] Molecular weight: 47716 Da [This is the MW of the unprocessed precursor] CRC64: 2833C025F969553E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMRERYS ASKPLKGARI AGCLHMTVET 

        70         80         90        100        110        120 
AVLIETLVTL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY AWKGETDEEY LWCIEQTLYF 

       130        140        150        160        170        180 
KDGPLNMILD DGGDLTNLIH TKYPQLLPGI RGISEETTTG VHNLYKMMAN GILKVPAINV 

       190        200        210        220        230        240 
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI 

       250        260        270        280        290        300 
ITEIDPINAL QAAMEGYEVT TMDEACQEGN IFVTTTGCID IILGRHFEQM KDDAIVCNIG 

       310        320        330        340        350        360 
HFDVEIDVKW LNENAVEKVN IKPQVDRYRL KNGRRIILLA EGRLVNLGCA MGHPSFVMSN 

       370        380        390        400        410        420 
SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMS 

       430 
CDGPFKPDHY RY 

P23526 in FASTA format

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