P23526 (SAHH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenosylhomocysteinase
Short name=AdoHcyase
EC=3.3.1.1

Alternative name(s):
S-adenosyl-L-homocysteine hydrolase

Gene names

Name:	AHCY
Synonyms:	SAHH

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.14
Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.
Cofactor	Binds 1 NAD per subunit. Ref.13 Ref.14
Pathway	Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subunit structure	Homotetramer. Ref.13
Subcellular location	Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.11
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.18 Ref.19
Sequence similarities	Belongs to the adenosylhomocysteinase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	NAD
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome methylation Traceable author statement. Source: Reactome one-carbon metabolic process Non-traceable author statement. Source: UniProtKB sulfur amino acid metabolic process Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	adenosylhomocysteinase activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P23526-1)

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.

Isoform 2 (identifier: P23526-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

Chain

2 – 432

431

Adenosylhomocysteinase

PRO_0000116902

Regions

Nucleotide binding

157 – 159

3

NAD

Nucleotide binding

222 – 227

6

NAD

Nucleotide binding

299 – 301

3

NAD

Sites

Binding site

57

1

Substrate By similarity

Binding site

131

1

Substrate By similarity

Binding site

156

1

Substrate By similarity

Binding site

186

1

Substrate By similarity

Binding site

190

1

Substrate By similarity

Binding site

243

1

NAD

Binding site

248

1

NAD

Binding site

346

1

NAD

Binding site

353

1

NAD

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.8

Natural variations

Alternative sequence

1 – 28

28

Missing in isoform 2.

VSP_045404

Natural variant

38

1

R → W. Ref.15
Corresponds to variant rs13043752 [ dbSNP | Ensembl ].

VAR_052286

Natural variant

49

1

R → C in HMAHCHD. Ref.18 Ref.19

VAR_058588

Natural variant

86

1

D → G in HMAHCHD. Ref.18 Ref.19

VAR_058589

Natural variant

86

1

D → N. Ref.1

VAR_006934

Natural variant

89

1

A → V in HMAHCHD. Ref.17

VAR_058590

Natural variant

143

1

Y → C in HMAHCHD. Ref.16 Ref.17

VAR_058591

Experimental info

Sequence conflict

249

1

A → V in BAG53495. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

432

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Helix

12 – 14

3

Helix

15 – 26

12

Helix

30 – 39

10

Turn

40 – 42

3

Turn

44 – 47

4

Beta strand

49 – 54

6

Helix

58 – 69

12

Beta strand

73 – 77

5

Beta strand

79 – 82

4

Helix

86 – 94

9

Beta strand

99 – 101

3

Helix

107 – 115

9

Beta strand

118 – 120

3

Beta strand

126 – 133

8

Helix

134 – 142

9

Helix

144 – 149

6

Beta strand

152 – 155

4

Helix

158 – 169

12

Beta strand

175 – 179

5

Helix

184 – 187

4

Helix

190 – 207

18

Beta strand

215 – 219

5

Helix

223 – 234

12

Beta strand

238 – 242

5

Helix

246 – 254

9

Helix

262 – 265

4

Turn

266 – 268

3

Beta strand

270 – 274

5

Beta strand

277 – 279

3

Helix

284 – 287

4

Beta strand

294 – 298

5

Beta strand

300 – 302

3

Helix

308 – 314

7

Beta strand

316 – 322

7

Beta strand

325 – 329

5

Beta strand

335 – 339

5

Helix

340 – 342

3

Helix

345 – 348

4

Helix

355 – 374

20

Helix

376 – 378

3

Beta strand

381 – 384

4

Helix

388 – 399

12

Turn

400 – 403

4

Helix

411 – 417

7

Beta strand

421 – 423

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 2833C025F969553E	FASTA	432	47,716
	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
	Isoform 2 [UniParc]. Checksum: 4AF904249AD2F35F	FASTA	404	44,659
	10 20 30 40 50 60 MPGLMRMRER YSASKPLKGA RIAGCLHMTV ETAVLIETLV TLGAEVQWSS CNIFSTQDHA 70 80 90 100 110 120 AAAIAKAGIP VYAWKGETDE EYLWCIEQTL YFKDGPLNMI LDDGGDLTNL IHTKYPQLLP 130 140 150 160 170 180 GIRGISEETT TGVHNLYKMM ANGILKVPAI NVNDSVTKSK FDNLYGCRES LIDGIKRATD 190 200 210 220 230 240 VMIAGKVAVV AGYGDVGKGC AQALRGFGAR VIITEIDPIN ALQAAMEGYE VTTMDEACQE 250 260 270 280 290 300 GNIFVTTTGC IDIILGRHFE QMKDDAIVCN IGHFDVEIDV KWLNENAVEK VNIKPQVDRY 310 320 330 340 350 360 RLKNGRRIIL LAEGRLVNLG CAMGHPSFVM SNSFTNQVMA QIELWTHPDK YPVGVHFLPK 370 380 390 400 KLDEAVAEAH LGKLNVKLTK LTEKQAQYLG MSCDGPFKPD HYRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, 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]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." 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. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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]	"S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism." Baric I., Fumic K., Glenn B., Cuk M., Schulze A., Finkelstein J.D., James S.J., Mejaski-Bosnjak V., Pazanin L., Pogribny I.P., Rados M., Sarnavka V., Scukanec-Spoljar M., Allen R.H., Stabler S., Uzelac L., Vugrek O., Wagner C., Zeisel S., Mudd S.H. Proc. Natl. Acad. Sci. U.S.A. 101:4234-4239(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HMAHCHD CYS-143.
[17]	"S-adenosylhomocysteine hydrolase deficiency in a 26-year-old man." Buist N.R., Glenn B., Vugrek O., Wagner C., Stabler S., Allen R.H., Pogribny I., Schulze A., Zeisel S.H., Baric I., Mudd S.H. J. Inherit. Metab. Dis. 29:538-545(2006) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00012007.
IPI00935818.

PIR

A43629.

RefSeq

NP_000678.1. NM_000687.2.
NP_001155238.1. NM_001161766.1.

UniGene

Hs.388004.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P23526.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23526. 12 interactions.

MINT

MINT-5000523.

STRING

9606.ENSP00000217426.

PTM databases

PhosphoSite

P23526.

Polymorphism databases

DMDM

20141702.

2D gel databases

REPRODUCTION-2DPAGE

IPI00012007.

Proteomic databases

PaxDb

P23526.

PeptideAtlas

P23526.

PRIDE

P23526.

Protocols and materials databases

DNASU

191.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000217426; ENSP00000217426; ENSG00000101444.
ENST00000538132; ENSP00000442820; ENSG00000101444.

GeneID

191.

KEGG

hsa:191.

UCSC

uc002xai.3. human.

Organism-specific databases

CTD

191.

GeneCards

GC20M032868.

HGNC

HGNC:343. AHCY.

HPA

HPA041225.
HPA044675.

MIM

180960. gene.
613752. phenotype.

neXtProt

NX_P23526.

Orphanet

88618. Psychomotor retardation due to S-adenosylhomocysteine hydrolase deficiency.

PharmGKB

PA24636.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0499.

HOGENOM

HOG000227987.

HOVERGEN

HBG005041.

InParanoid

P23526.

KO

K01251.

OMA

TIGMALH.

OrthoDB

EOG4MW862.

PhylomeDB

P23526.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P23526.

UniPathway

UPA00314; UER00076.

Gene expression databases

ArrayExpress

P23526.

Bgee

P23526.

CleanEx

HS_AHCY.

Genevestigator

P23526.

GermOnline

ENSG00000101444. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]

PANTHER

PTHR23420. PTHR23420. 1 hit.

Pfam

PF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]

PIRSF

PIRSF001109. Ad_hcy_hydrolase. 1 hit.

SMART

SM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00936. ahcY. 1 hit.

PROSITE

PS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P23526.

ChEMBL

CHEMBL2664.

ChiTaRS

AHCY. human.

EvolutionaryTrace

P23526.

GenomeRNAi

191.

NextBio

780.

SOURCE

Search...

Entry information

Entry name

SAHH_HUMAN

Accession

Primary (citable) accession number: P23526
Secondary accession number(s): A8K307 , B3KUN3, E1P5P2, F5H737, Q96A36

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 146 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.