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O43865

- SAHH2_HUMAN

UniProt

O43865 - SAHH2_HUMAN

Protein

Putative adenosylhomocysteinase 2

Gene

AHCYL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 NAD per subunit.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei155 – 1551SubstrateBy similarity
    Binding sitei229 – 2291SubstrateBy similarity
    Binding sitei254 – 2541SubstrateBy similarity
    Binding sitei284 – 2841SubstrateBy similarity
    Binding sitei288 – 2881SubstrateBy similarity
    Binding sitei341 – 3411NAD1 Publication
    Binding sitei376 – 3761NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi318 – 3225NAD1 Publication
    Nucleotide bindingi397 – 3993NAD1 Publication

    GO - Molecular functioni

    1. adenosylhomocysteinase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct

    GO - Biological processi

    1. mRNA polyadenylation Source: Ensembl
    2. one-carbon metabolic process Source: UniProtKB-KW
    3. positive regulation of sodium ion transport Source: Ensembl
    4. protein export from nucleus Source: Ensembl
    5. regulation of anion transport Source: Ensembl
    6. regulation of ion transmembrane transporter activity Source: Ensembl
    7. regulation of mRNA 3'-end processing Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00314; UER00076.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative adenosylhomocysteinase 2 (EC:3.3.1.1)
    Short name:
    AdoHcyase 2
    Alternative name(s):
    DC-expressed AHCY-like molecule
    S-adenosyl-L-homocysteine hydrolase 2
    S-adenosylhomocysteine hydrolase-like protein 1
    Gene namesi
    Name:AHCYL1
    Synonyms:DCAL, XPVKONA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:344. AHCYL1.

    Subcellular locationi

    Endoplasmic reticulum By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24637.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 530529Putative adenosylhomocysteinase 2PRO_0000116908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei40 – 401N6-acetyllysineBy similarity
    Modified residuei391 – 3911Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO43865.
    PaxDbiO43865.
    PeptideAtlasiO43865.
    PRIDEiO43865.

    PTM databases

    PhosphoSiteiO43865.

    Miscellaneous databases

    PMAP-CutDBO43865.

    Expressioni

    Tissue specificityi

    Expressed in dendritic cells.1 Publication

    Developmental stagei

    Expression increases markedly during activation of blood and skin DC (Langerhans cells), but is diminished in terminally differentiated tonsil DC.1 Publication

    Gene expression databases

    ArrayExpressiO43865.
    BgeeiO43865.
    CleanExiHS_AHCYL1.
    GenevestigatoriO43865.

    Organism-specific databases

    HPAiHPA042589.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    tatP046085EBI-2371423,EBI-6164389From a different organism.

    Protein-protein interaction databases

    BioGridi115987. 101 interactions.
    IntActiO43865. 9 interactions.
    STRINGi9606.ENSP00000358814.

    Structurei

    Secondary structure

    1
    530
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi113 – 12412
    Helixi128 – 13710
    Turni142 – 1454
    Beta strandi147 – 1526
    Helixi156 – 16712
    Beta strandi171 – 1755
    Beta strandi177 – 1804
    Helixi184 – 19310
    Beta strandi196 – 1983
    Helixi205 – 21612
    Beta strandi224 – 2318
    Helixi232 – 2409
    Helixi242 – 2454
    Beta strandi249 – 2535
    Helixi256 – 26510
    Turni266 – 2694
    Beta strandi275 – 2773
    Helixi282 – 29312
    Helixi299 – 3057
    Beta strandi313 – 3175
    Helixi321 – 33313
    Beta strandi336 – 3405
    Helixi344 – 3529
    Helixi360 – 3623
    Turni363 – 3664
    Beta strandi368 – 3725
    Helixi382 – 3876
    Beta strandi392 – 3965
    Turni400 – 4034
    Helixi406 – 4094
    Beta strandi415 – 4206
    Beta strandi423 – 4275
    Beta strandi433 – 4375
    Helixi438 – 4403
    Helixi444 – 4463
    Helixi452 – 47120
    Beta strandi479 – 4824
    Helixi486 – 49611
    Helixi497 – 5004
    Helixi509 – 5146
    Beta strandi519 – 5213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MTGX-ray2.64A/B89-530[»]
    ProteinModelPortaliO43865.
    SMRiO43865. Positions 101-530.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43865.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 9228PESTBy similarityAdd
    BLAST
    Regioni281 – 448168NAD bindingBy similarityAdd
    BLAST
    Regioni520 – 53011PDZ-bindingBy similarityAdd
    BLAST

    Domaini

    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.By similarity

    Sequence similaritiesi

    Belongs to the adenosylhomocysteinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0499.
    HOGENOMiHOG000227986.
    HOVERGENiHBG005041.
    KOiK01251.
    OMAiKQIQFVE.
    OrthoDBiEOG76739S.
    PhylomeDBiO43865.
    TreeFamiTF300415.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    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: O43865-1) [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

    MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE    50
    FTKFPTKTGR RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK 100
    GSSNFCVKNI KQAEFGRREI EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG 150
    CTHITAQTAV LIETLCALGA QCRWSACNIY STQNEVAAAL AEAGVAVFAW 200
    KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK YPNVFKKIRG 250
    IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG 300
    LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA 350
    CMDGFRVVKL NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS 400
    NTEIDVTSLR TPELTWERVR SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV 450
    PTFVLSITAT TQALALIELY NAPEGRYKQD VYLLPKKMDE YVASLHLPSF 500
    DAHLTELTDD QAKYLGLNKN GPFKPNYYRY 530
    Length:530
    Mass (Da):58,951
    Last modified:April 4, 2006 - v2
    Checksum:i974D23361A245D04
    GO
    Isoform 2 (identifier: O43865-2) [UniParc]FASTAAdd to Basket

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

    Note: Derived from EST data.

    Show »
    Length:483
    Mass (Da):53,753
    Checksum:i18DFC7E74697E1D4
    GO

    Sequence cautioni

    The sequence BI460083 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAC01960.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAB43223.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941K → M in T19009. (PubMed:7782076)Curated
    Sequence conflicti99 – 991S → F in T19009. (PubMed:7782076)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4747Missing in isoform 2. 5 PublicationsVSP_021751Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS55620.1. [O43865-2]
    CCDS818.1. [O43865-1]
    PIRiT08681.
    RefSeqiNP_001229602.1. NM_001242673.1. [O43865-2]
    NP_001229603.1. NM_001242674.1. [O43865-2]
    NP_001229604.1. NM_001242675.1. [O43865-2]
    NP_001229605.1. NM_001242676.1. [O43865-2]
    NP_006612.2. NM_006621.5. [O43865-1]
    UniGeneiHs.743973.

    Genome annotation databases

    EnsembliENST00000359172; ENSP00000352092; ENSG00000168710. [O43865-2]
    ENST00000369799; ENSP00000358814; ENSG00000168710. [O43865-1]
    ENST00000393614; ENSP00000377238; ENSG00000168710. [O43865-2]
    GeneIDi10768.
    KEGGihsa:10768.
    UCSCiuc001dyx.3. human. [O43865-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS55620.1. [O43865-2 ]
    CCDS818.1. [O43865-1 ]
    PIRi T08681.
    RefSeqi NP_001229602.1. NM_001242673.1. [O43865-2 ]
    NP_001229603.1. NM_001242674.1. [O43865-2 ]
    NP_001229604.1. NM_001242675.1. [O43865-2 ]
    NP_001229605.1. NM_001242676.1. [O43865-2 ]
    NP_006612.2. NM_006621.5. [O43865-1 ]
    UniGenei Hs.743973.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MTG X-ray 2.64 A/B 89-530 [» ]
    ProteinModelPortali O43865.
    SMRi O43865. Positions 101-530.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115987. 101 interactions.
    IntActi O43865. 9 interactions.
    STRINGi 9606.ENSP00000358814.

    PTM databases

    PhosphoSitei O43865.

    Proteomic databases

    MaxQBi O43865.
    PaxDbi O43865.
    PeptideAtlasi O43865.
    PRIDEi O43865.

    Protocols and materials databases

    DNASUi 10768.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359172 ; ENSP00000352092 ; ENSG00000168710 . [O43865-2 ]
    ENST00000369799 ; ENSP00000358814 ; ENSG00000168710 . [O43865-1 ]
    ENST00000393614 ; ENSP00000377238 ; ENSG00000168710 . [O43865-2 ]
    GeneIDi 10768.
    KEGGi hsa:10768.
    UCSCi uc001dyx.3. human. [O43865-1 ]

    Organism-specific databases

    CTDi 10768.
    GeneCardsi GC01P110529.
    HGNCi HGNC:344. AHCYL1.
    HPAi HPA042589.
    MIMi 607826. gene.
    neXtProti NX_O43865.
    PharmGKBi PA24637.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0499.
    HOGENOMi HOG000227986.
    HOVERGENi HBG005041.
    KOi K01251.
    OMAi KQIQFVE.
    OrthoDBi EOG76739S.
    PhylomeDBi O43865.
    TreeFami TF300415.

    Enzyme and pathway databases

    UniPathwayi UPA00314 ; UER00076 .

    Miscellaneous databases

    ChiTaRSi AHCYL1. human.
    EvolutionaryTracei O43865.
    GeneWikii AHCYL1.
    GenomeRNAii 10768.
    NextBioi 40889.
    PMAP-CutDB O43865.
    PROi O43865.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43865.
    Bgeei O43865.
    CleanExi HS_AHCYL1.
    Genevestigatori O43865.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    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

    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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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.

    Entry informationi

    Entry nameiSAHH2_HUMAN
    AccessioniPrimary (citable) accession number: O43865
    Secondary accession number(s): B4E168
    , Q2TAJ6, Q502W8, Q5VSM0, Q6P171, Q96PK4, Q9UG84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3