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Q96HN2 (SAHH3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative adenosylhomocysteinase 3
Short name=AdoHcyase 3
EC=3.3.1.1
Alternative name(s):
S-adenosyl-L-homocysteine hydrolase 3
S-adenosylhomocysteine hydrolase-like protein 2
Gene names
Name:AHCYL2
Synonyms:KIAA0828
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

Cofactor

Binds 1 NAD per subunit.

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.

Subunit structure

Homotetramer Probable. Ref.5

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Sequence caution

The sequence BAA74851.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Coding sequence diversityAlternative splicing
   LigandNAD
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionadenosylhomocysteinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96HN2-1)

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: Q96HN2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     122-122: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Putative adenosylhomocysteinase 3
PRO_0000116909

Regions

Nucleotide binding336 – 3383NAD By similarity
Nucleotide binding401 – 4066NAD
Nucleotide binding478 – 4792NAD

Sites

Binding site2361Substrate By similarity
Binding site3101Substrate By similarity
Binding site3351Substrate By similarity
Binding site3651Substrate By similarity
Binding site3691Substrate By similarity
Binding site3701NAD By similarity
Binding site4221NAD
Binding site4571NAD
Binding site5251NAD

Amino acid modifications

Modified residue1071Phosphoserine Ref.4

Natural variations

Alternative sequence1221Missing in isoform 2.
VSP_040095

Secondary structure

1 ....................................................................... 611
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A76B1275FC0D891D

FASTA61166,721
        10         20         30         40         50         60 
MSVQVVSAAA AAKVPEVELK DLSPSEAESQ LGLSTAAVGA MAPPAGGGDP EAPAPAAERP 

        70         80         90        100        110        120 
PVPGPGSGPA AALSPAAGKV PQASAMKRSD PHHQHQRHRD GGEALVSPDG TVTEAPRTVK 

       130        140        150        160        170        180 
KQIQFADQKQ EFNKRPTKIG RRSLSRSISQ SSTDSYSSAA SYTDSSDDET SPRDKQQKNS 

       190        200        210        220        230        240 
KGSSDFCVKN IKQAEFGRRE IEIAEQEMPA LMALRKRAQG EKPLAGAKIV GCTHITAQTA 

       250        260        270        280        290        300 
VLMETLGALG AQCRWAACNI YSTLNEVAAA LAESGFPVFA WKGESEDDFW WCIDRCVNVE 

       310        320        330        340        350        360 
GWQPNMILDD GGDLTHWIYK KYPNMFKKIK GIVEESVTGV HRLYQLSKAG KLCVPAMNVN 

       370        380        390        400        410        420 
DSVTKQKFDN LYCCRESILD GLKRTTDMMF GGKQVVVCGY GEVGKGCCAA LKAMGSIVYV 

       430        440        450        460        470        480 
TEIDPICALQ ACMDGFRLVK LNEVIRQVDI VITCTGNKNV VTREHLDRMK NSCIVCNMGH 

       490        500        510        520        530        540 
SNTEIDVASL RTPELTWERV RSQVDHVIWP DGKRIVLLAE GRLLNLSCST VPTFVLSITA 

       550        560        570        580        590        600 
TTQALALIEL YNAPEGRYKQ DVYLLPKKMD EYVASLHLPT FDAHLTELTD EQAKYLGLNK 

       610 
NGPFKPNYYR Y

« Hide

Isoform 2 [UniParc].

Checksum: D54ED0745D3A286B
Show »

FASTA61066,593

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed: 10048485] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed: 12853948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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).
Tissue: Lung and Uterus.
[4]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]"Human S-adenosyl homocysteine hydrolase-like 2 protein crystal structure."
Structural genomics consortium (SGC)
Submitted (JUN-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 175-607 IN COMPLEX WITH NAD, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB020635 mRNA. Translation: BAA74851.1. Different initiation.
AC009244 Genomic DNA. No translation available.
AC011005 Genomic DNA. No translation available.
AC083866 Genomic DNA. No translation available.
AC093149 Genomic DNA. No translation available.
BC008349 mRNA. Translation: AAH08349.1.
BC024325 mRNA. Translation: AAH24325.1.
IPIIPI00101645.
IPI00908473.
RefSeqNP_001124192.1. NM_001130720.2.
NP_001124194.2. NM_001130722.2.
NP_001124195.1. NM_001130723.2.
NP_056143.1. NM_015328.3.
UniGeneHs.600789.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GVPX-ray2.25A/B/C/D175-607[»]
ProteinModelPortalQ96HN2.
SMRQ96HN2. Positions 176-607.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96HN2. 4 interactions.
STRINGQ96HN2.

PTM databases

PhosphoSiteQ96HN2.

Polymorphism databases

DMDM21759427.

Proteomic databases

PRIDEQ96HN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325006; ENSP00000315931; ENSG00000158467.
GeneID23382.
KEGGhsa:23382.
NMPDRfig|9606.3.peg.29423.
UCSCuc003vot.1. human.

Organism-specific databases

CTD23382.
GeneCardsGC07P128865.
HGNCHGNC:22204. AHCYL2.
neXtProtNX_Q96HN2.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG10864.
GeneTreeENSGT00390000003626.
HOGENOMHBG352029.
HOVERGENHBG005041.
InParanoidQ96HN2.
OMANTEIDVN.
OrthoDBEOG4GMTWR.
PhylomeDBQ96HN2.

Gene expression databases

ArrayExpressQ96HN2.
BgeeQ96HN2.
CleanExHS_AHCYL2.
GenevestigatorQ96HN2.

Family and domain databases

InterProIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
KOK01251.
PANTHERPTHR23420. Ad_hcy_hydrolase. 1 hit.
PfamPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
SMARTSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsTIGR00936. AhcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio45489.

Entry information

Entry nameSAHH3_HUMAN
AccessionPrimary (citable) accession number: Q96HN2
Secondary accession number(s): O94917
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents