O43865 (SAHH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative adenosylhomocysteinase 2
Short name=AdoHcyase 2
EC=3.3.1.1

Alternative name(s):
DC-expressed AHCY-like molecule
S-adenosyl-L-homocysteine hydrolase 2
S-adenosylhomocysteine hydrolase-like protein 1

Gene names

Name:	AHCYL1
Synonyms:	DCAL, XPVKONA

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	530 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)

Catalytic activity	S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.
Cofactor	Binds 1 NAD per subunit. Ref.14
Pathway	Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.
Subunit structure	Interacts with ITPR1. Competes with IP3 for interaction with ITPR1 and attenuates IP3-induced Ca2+ release through the ITPR1 from the non-mitochondrial intracellular stores By similarity.
Subcellular location	Endoplasmic reticulum By similarity.
Tissue specificity	Expressed in dendritic cells. Ref.1
Developmental stage	Expression increases markedly during activation of blood and skin DC (Langerhans cells), but is diminished in terminally differentiated tonsil DC. Ref.1
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 AAC01960.1 differs from that shown. Reason: Erroneous initiation. The sequence BI460083 differs from that shown. Reason: Frameshift at several positions. The sequence CAB43223.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Ligand	NAD
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA polyadenylation Inferred from electronic annotation. Source: Compara one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of sodium ion transport Inferred from electronic annotation. Source: Compara protein export from nucleus Inferred from electronic annotation. Source: Compara regulation of anion transport Inferred from electronic annotation. Source: Compara regulation of ion transmembrane transporter activity Inferred from electronic annotation. Source: Compara regulation of mRNA 3'-end processing Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	adenosylhomocysteinase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
tat	P04608	5	EBI-2371423,EBI-6164389	From a different organism.

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.

Note: Derived from EST data.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.13

Chain

2 – 530

529

Putative adenosylhomocysteinase 2

PRO_0000116908

Regions

Nucleotide binding

318 – 322

5

NAD

Nucleotide binding

397 – 399

3

NAD

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

Binding site

341

1

NAD

Binding site

376

1

NAD

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.13

Modified residue

2

1

Phosphoserine Ref.13

Modified residue

82

1

Phosphothreonine By similarity

Modified residue

84

1

Phosphoserine By similarity

Modified residue

85

1

Phosphoserine By similarity

Modified residue

391

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 47

47

Missing in isoform 2.

VSP_021751

Experimental info

Sequence conflict

94

1

K → M in T19009. Ref.9

Sequence conflict

99

1

S → F in T19009. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

530

Helix Strand Turn

Details...

Helix

113 – 124

12

Helix

128 – 137

10

Turn

142 – 145

4

Beta strand

147 – 152

6

Helix

156 – 167

12

Beta strand

171 – 175

5

Beta strand

177 – 180

4

Helix

184 – 193

10

Beta strand

196 – 198

3

Helix

205 – 216

12

Beta strand

224 – 231

8

Helix

232 – 240

9

Helix

242 – 245

4

Beta strand

249 – 253

5

Helix

256 – 265

10

Turn

266 – 269

4

Beta strand

275 – 277

3

Helix

282 – 293

12

Helix

299 – 305

7

Beta strand

313 – 317

5

Helix

321 – 333

13

Beta strand

336 – 340

5

Helix

344 – 352

9

Helix

360 – 362

3

Turn

363 – 366

4

Beta strand

368 – 372

5

Helix

382 – 387

6

Beta strand

392 – 396

5

Turn

400 – 403

4

Helix

406 – 409

4

Beta strand

415 – 420

6

Beta strand

423 – 427

5

Beta strand

433 – 437

5

Helix

438 – 440

3

Helix

444 – 446

3

Helix

452 – 471

20

Beta strand

479 – 482

4

Helix

486 – 496

11

Helix

497 – 500

4

Helix

509 – 514

6

Beta strand

519 – 521

3

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	FASTA	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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"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] (ISOFORM 2). Tissue: Kidney and Thalamus.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton 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 (JUL-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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-251 (ISOFORM 2). Tissue: Brain, Colon, Eye, Placenta, PNS and Testis.
[7]	"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.
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-164 (ISOFORM 2). Tissue: Chondrocyte.
[9]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-105 (ISOFORM 2). Tissue: Testis.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION (ISOFORM 2).
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[14]	"Crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein." Structural genomics consortium (SGC) Submitted (MAY-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 89-530 IN COMPLEX WITH NAD, COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF315687 mRNA. Translation: AAL26869.1.
AL036027 mRNA. No translation available.
AK303690 mRNA. Translation: BAG64680.1.
AK316110 mRNA. Translation: BAH14481.1.
AL049954 mRNA. Translation: CAB43223.2. Different initiation.
AL772411 Genomic DNA. Translation: CAH70965.1.
AL772411 Genomic DNA. Translation: CAH70966.1.
CH471122 Genomic DNA. Translation: EAW56426.1.
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.

IPI

IPI00182938.
IPI00479201.

PIR

T08681.

RefSeq

NP_001229602.1. NM_001242673.1.
NP_001229603.1. NM_001242674.1.
NP_001229604.1. NM_001242675.1.
NP_001229605.1. NM_001242676.1.
NP_006612.2. NM_006621.5.

UniGene

Hs.741170.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MTG	X-ray	2.64	A/B	89-530	[»]

ProteinModelPortal

O43865.

ModBase

Search...

Protein-protein interaction databases

IntAct

O43865. 7 interactions.

STRING

9606.ENSP00000358814.

PTM databases

PhosphoSite

O43865.

Proteomic databases

PaxDb

O43865.

PeptideAtlas

O43865.

PRIDE

O43865.

Protocols and materials databases

DNASU

10768.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359172; ENSP00000352092; ENSG00000168710.
ENST00000369799; ENSP00000358814; ENSG00000168710.
ENST00000393614; ENSP00000377238; ENSG00000168710.

GeneID

10768.

KEGG

hsa:10768.

UCSC

uc001dyx.3. human.

Organism-specific databases

CTD

10768.

GeneCards

GC01P110529.

HGNC

HGNC:344. AHCYL1.

HPA

HPA042589.

MIM

607826. gene.

neXtProt

NX_O43865.

PharmGKB

PA24637.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0499.

HOGENOM

HOG000227986.

HOVERGEN

HBG005041.

KO

K01251.

OMA

KQIQFVE.

OrthoDB

EOG4GMTWR.

PhylomeDB

O43865.

Enzyme and pathway databases

UniPathway

UPA00314; UER00076.

Gene expression databases

ArrayExpress

O43865.

Bgee

O43865.

CleanEx

HS_AHCYL1.

Genevestigator

O43865.

GermOnline

ENSG00000168710. 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

ChiTaRS

AHCYL1. human.

EvolutionaryTrace

O43865.

GenomeRNAi

10768.

NextBio

40889.

PMAP-CutDB

O43865.

SOURCE

Search...

Entry information

Entry name

SAHH2_HUMAN

Accession

Primary (citable) accession number: O43865
Secondary accession number(s): B4E168 , Q2TAJ6, Q502W8, Q5VSM0, Q6P171, Q96PK4, Q9UG84

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	April 4, 2006
Last modified:	May 1, 2013
This is version 125 of the entry and version 2 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.