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P23526

- SAHH_HUMAN

UniProt

P23526 - SAHH_HUMAN

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Protein

Adenosylhomocysteinase

Gene

AHCY

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

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
  2. adenyl nucleotide binding Source: Ensembl
  3. NAD binding Source: Ensembl

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. chronic inflammatory response to antigenic stimulus Source: Ensembl
  3. circadian sleep/wake cycle Source: Ensembl
  4. homocysteine biosynthetic process Source: Ensembl
  5. methylation Source: Reactome
  6. one-carbon metabolic process Source: UniProtKB-KW
  7. response to hypoxia Source: Ensembl
  8. response to nutrient Source: Ensembl
  9. S-adenosylhomocysteine catabolic process Source: Ensembl
  10. small molecule metabolic process Source: Reactome
  11. sulfur amino acid metabolic process Source: Reactome
  12. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

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: UniProtKB
  4. neuron projection Source: Ensembl
  5. nucleus Source: Ensembl
Complete GO annotation...

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

BgeeiP23526.
CleanExiHS_AHCY.
ExpressionAtlasiP23526. baseline and differential.
GenevestigatoriP23526.

Organism-specific databases

HPAiHPA041225.
HPA044675.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

BioGridi106696. 55 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.
GeneTreeiENSGT00390000003626.
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) [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
MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMRERYS ASKPLKGARI
60 70 80 90 100
AGCLHMTVET AVLIETLVTL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY
110 120 130 140 150
AWKGETDEEY LWCIEQTLYF KDGPLNMILD DGGDLTNLIH TKYPQLLPGI
160 170 180 190 200
RGISEETTTG VHNLYKMMAN GILKVPAINV NDSVTKSKFD NLYGCRESLI
210 220 230 240 250
DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI ITEIDPINAL
260 270 280 290 300
QAAMEGYEVT TMDEACQEGN IFVTTTGCID IILGRHFEQM KDDAIVCNIG
310 320 330 340 350
HFDVEIDVKW LNENAVEKVN IKPQVDRYRL KNGRRIILLA EGRLVNLGCA
360 370 380 390 400
MGHPSFVMSN SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG
410 420 430
KLNVKLTKLT EKQAQYLGMS CDGPFKPDHY RY
Length:432
Mass (Da):47,716
Last modified:January 23, 2007 - v4
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. 55 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.
GeneTreei ENSGT00390000003626.
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

Bgeei P23526.
CleanExi HS_AHCY.
ExpressionAtlasi P23526. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 161 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