Reviewed, UniProtKB/Swiss-Prot O43865 (SAHH2_HUMAN)

Names and origin

Protein names

Recommended name:
    Putative adenosylhomocysteinase 2
      Short name=AdoHcyase 2
    EC=3.3.1.1
Alternative name(s):
    S-adenosyl-L-homocysteine hydrolase 2
    S-adenosylhomocysteine hydrolase-like protein 1
    DC-expressed AHCY-like molecule

Gene names

Name:	AHCYL1
Synonyms:	DCAL, XPVKONA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine.
Cofactor	Binds 1 NAD per subunit By similarity.
Pathway	Amino-acid biosynthesis; homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1. Context: Activated methyl cycle.
Subunit structure	Interacts with ITPR1. Competes with IP3 for interaction with ITPR1 and attenuates IP3-induced Ca(2+) release through the ITPR1 from the non-mitochondrial intracellular stores By similarity.
Subcellular location	Endoplasmic reticulumBy similarity.
Tissue specificity	Expressed in dendritic cells.
Developmental stage	Expression increases markedly during activation of blood and skin DC (Langerhans cells), but is diminished in terminally differentiated tonsil DC.
Domain	The PEST region is essential for the interaction with ITPR1. The PDZ-binding region is required for maximal interaction with ITPR1 and is also responsible for the IP3-insensitive interaction with ITPR1 By similarity.
Sequence similarities	Belongs to the adenosylhomocysteinase family.
Sequence caution	The sequence BI460083 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Ligand	NAD
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
None. [Check GOA]

Alternative products

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

Isoform 1 (identifier: O43865-1)

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: O43865-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Notes: Derived from EST data.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 530	530	Putative adenosylhomocysteinase 2
Regions
	Region	65 – 92	28	PEST By similarity
	Region	281 – 448	168	NAD binding By similarity
	Region	520 – 530	11	PDZ-binding By similarity
Sites
	Binding site	155	1	Substrate By similarity
	Binding site	229	1	Substrate By similarity
	Binding site	254	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
Amino acid modifications
	Modified residue	28	1	Phosphotyrosine
	Modified residue	82	1	Phosphothreonine By similarity
	Modified residue	84	1	Phosphoserine By similarity
	Modified residue	85	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 47	47	Missing in isoform 2.
Experimental info
	Sequence conflict	94	1	K → M in T19009. Ref.7
	Sequence conflict	99	1	S → F in T19009. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 4, 2006. Version 2. Checksum: 974D23361A245D04	FASTA	530	58,951
	10 20 30 40 50 60 MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE FTKFPTKTGR 70 80 90 100 110 120 RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK GSSNFCVKNI KQAEFGRREI 130 140 150 160 170 180 EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV LIETLCALGA QCRWSACNIY 190 200 210 220 230 240 STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK 250 260 270 280 290 300 YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG 310 320 330 340 350 360 LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA CMDGFRVVKL 370 380 390 400 410 420 NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS NTEIDVTSLR TPELTWERVR 430 440 450 460 470 480 SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV PTFVLSITAT TQALALIELY NAPEGRYKQD 490 500 510 520 530 VYLLPKKMDE YVASLHLPSF DAHLTELTDD QAKYLGLNKN GPFKPNYYRY
	Isoform 2 [UniParc]. Checksum: 18DFC7E74697E1D4		483	53,753
	10 20 30 40 50 60 MQEFTKFPTK TGRRSLSRSI SQSSTDSYSS AASYTDSSDD EVSPREKQQT NSKGSSNFCV 70 80 90 100 110 120 KNIKQAEFGR REIEIAEQDM SALISLRKRA QGEKPLAGAK IVGCTHITAQ TAVLIETLCA 130 140 150 160 170 180 LGAQCRWSAC NIYSTQNEVA AALAEAGVAV FAWKGESEDD FWWCIDRCVN MDGWQANMIL 190 200 210 220 230 240 DDGGDLTHWV YKKYPNVFKK IRGIVEESVT GVHRLYQLSK AGKLCVPAMN VNDSVTKQKF 250 260 270 280 290 300 DNLYCCRESI LDGLKRTTDV MFGGKQVVVC GYGEVGKGCC AALKALGAIV YITEIDPICA 310 320 330 340 350 360 LQACMDGFRV VKLNEVIRQV DVVITCTGNK NVVTREHLDR MKNSCIVCNM GHSNTEIDVT 370 380 390 400 410 420 SLRTPELTWE RVRSQVDHVI WPDGKRVVLL AEGRLLNLSC STVPTFVLSI TATTQALALI 430 440 450 460 470 480 ELYNAPEGRY KQDVYLLPKK MDEYVASLHL PSFDAHLTEL TDDQAKYLGL NKNGPFKPNY YRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11904675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	The German cDNA consortium Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-251 (ISOFORM 2). Tissue: Brain, Colon, Eye, Placenta, PNS and Testis.
[5]	"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.
[6]	"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: 12878157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-164 (ISOFORM 2). Tissue: Chondrocyte.
[7]	"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: 7782076] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-105 (ISOFORM 2). Tissue: Testis.
[8]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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: 16754674] [Abstract] Cited for: IDENTIFICATION (ISOFORM 2).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF315687 mRNA. Translation: AAL26869.1. AL036027 mRNA. No translation available. AL049954 mRNA. Translation: CAB43223.2. Different initiation. AL772411 Genomic DNA. Translation: CAH70965.1. AL772411 Genomic DNA. Translation: CAH70966.1. 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.
PIR	T08681.
RefSeq	NP_006612.2.
UniGene	Hs.705418
3D structure databases
HSSP	HSSP built from PDB template 1B3R based on UniProtKB P10760.
ModBase	Search...
PTM databases
PhosphoSite	O43865.
Proteomic databases
PeptideAtlas	O43865.
Genome annotation databases
Ensembl	ENSG00000168710. Homo sapiens. [Contig view]
GeneID	10768.
KEGG	hsa:10768.
Organism-specific databases
HGNC	HGNC:344. AHCYL1.
MIM	607826. gene.
PharmGKB	PA24637.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	O43865.
Gene expression databases
ArrayExpress	O43865.
CleanEx	HS_AHCYL1.
GermOnline	ENSG00000168710. Homo sapiens.
Family and domain databases
InterPro	IPR000043. Ad_hcy_hydrolase. IPR015878. Ado_hCys_hydrolase_NAD-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.1480. Ad_hcy_hydrolase. 1 hit.
PANTHER	PTHR23420. Ad_hcy_hydrolase. 1 hit.
Pfam	PF05221. AdoHcyase. 1 hit. PF00670. AdoHcyase_NAD. 1 hit. [Graphical view]
PIRSF	PIRSF001109. Ad_hcy_hydrolase. 1 hit.
TIGRFAMs	TIGR00936. ahcY. 1 hit.
PROSITE	PS00738. ADOHCYASE_1. 1 hit. PS00739. ADOHCYASE_2. 1 hit. [Graphical view]
ProDom	O43865. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

SAHH2_HUMAN

Accession

Primary (citable) accession number: O43865
Secondary accession number(s): Q2TAJ6 , Q502W8, Q5VSM0, Q6P171, Q96PK4, Q9UG84

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	April 4, 2006
Last modified:	July 22, 2008
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)