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Q96HN2

- SAHH3_HUMAN

UniProt

Q96HN2 - SAHH3_HUMAN

Protein

Putative adenosylhomocysteinase 3

Gene

AHCYL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 NAD per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei236 – 2361SubstrateBy similarity
    Binding sitei310 – 3101SubstrateBy similarity
    Binding sitei335 – 3351SubstrateBy similarity
    Binding sitei365 – 3651SubstrateBy similarity
    Binding sitei369 – 3691SubstrateBy similarity
    Binding sitei370 – 3701NADBy similarity
    Binding sitei422 – 4221NAD1 Publication
    Binding sitei457 – 4571NAD1 Publication
    Binding sitei525 – 5251NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi336 – 3383NADBy similarity
    Nucleotide bindingi401 – 4066NAD1 Publication
    Nucleotide bindingi478 – 4792NAD1 Publication

    GO - Molecular functioni

    1. adenosylhomocysteinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. one-carbon metabolic process Source: UniProtKB-KW

    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 3 (EC:3.3.1.1)
    Short name:
    AdoHcyase 3
    Alternative name(s):
    S-adenosyl-L-homocysteine hydrolase 3
    S-adenosylhomocysteine hydrolase-like protein 2
    Gene namesi
    Name:AHCYL2
    Synonyms:KIAA0828
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:22204. AHCYL2.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162376046.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 611610Putative adenosylhomocysteinase 3PRO_0000116909Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei107 – 1071Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96HN2.
    PaxDbiQ96HN2.
    PRIDEiQ96HN2.

    PTM databases

    PhosphoSiteiQ96HN2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96HN2.
    BgeeiQ96HN2.
    CleanExiHS_AHCYL2.
    GenevestigatoriQ96HN2.

    Organism-specific databases

    HPAiHPA053128.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi116958. 7 interactions.
    IntActiQ96HN2. 7 interactions.
    MINTiMINT-5005542.
    STRINGi9606.ENSP00000315931.

    Structurei

    Secondary structure

    1
    611
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi191 – 1933
    Helixi194 – 20613
    Helixi209 – 21810
    Turni223 – 2264
    Beta strandi228 – 2336
    Helixi237 – 24812
    Beta strandi252 – 26110
    Helixi265 – 27410
    Helixi286 – 29712
    Beta strandi305 – 3128
    Helixi313 – 3219
    Helixi323 – 3275
    Beta strandi331 – 3344
    Helixi337 – 3437
    Beta strandi356 – 3583
    Helixi363 – 3697
    Helixi371 – 38616
    Beta strandi394 – 3985
    Helixi402 – 41312
    Beta strandi417 – 4215
    Helixi425 – 4339
    Helixi441 – 4444
    Turni445 – 4473
    Beta strandi449 – 4535
    Helixi463 – 4686
    Beta strandi473 – 4775
    Turni481 – 4844
    Helixi487 – 4904
    Beta strandi496 – 5016
    Beta strandi504 – 5085
    Beta strandi514 – 5185
    Helixi519 – 5213
    Helixi524 – 5285
    Helixi533 – 55220
    Turni555 – 5573
    Beta strandi560 – 5645
    Helixi567 – 57711
    Helixi578 – 5814
    Helixi590 – 5967

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GVPX-ray2.25A/B/C/D175-607[»]
    ProteinModelPortaliQ96HN2.
    SMRiQ96HN2. Positions 176-607.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96HN2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the adenosylhomocysteinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0499.
    HOGENOMiHOG000227986.
    HOVERGENiHBG005041.
    InParanoidiQ96HN2.
    KOiK01251.
    OMAiAENWQPN.
    OrthoDBiEOG76739S.
    PhylomeDBiQ96HN2.
    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]
    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 (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96HN2-1) [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

    MSVQVVSAAA AAKVPEVELK DLSPSEAESQ LGLSTAAVGA MAPPAGGGDP    50
    EAPAPAAERP PVPGPGSGPA AALSPAAGKV PQASAMKRSD PHHQHQRHRD 100
    GGEALVSPDG TVTEAPRTVK KQIQFADQKQ EFNKRPTKIG RRSLSRSISQ 150
    SSTDSYSSAA SYTDSSDDET SPRDKQQKNS KGSSDFCVKN IKQAEFGRRE 200
    IEIAEQEMPA LMALRKRAQG EKPLAGAKIV GCTHITAQTA VLMETLGALG 250
    AQCRWAACNI YSTLNEVAAA LAESGFPVFA WKGESEDDFW WCIDRCVNVE 300
    GWQPNMILDD GGDLTHWIYK KYPNMFKKIK GIVEESVTGV HRLYQLSKAG 350
    KLCVPAMNVN DSVTKQKFDN LYCCRESILD GLKRTTDMMF GGKQVVVCGY 400
    GEVGKGCCAA LKAMGSIVYV TEIDPICALQ ACMDGFRLVK LNEVIRQVDI 450
    VITCTGNKNV VTREHLDRMK NSCIVCNMGH SNTEIDVASL RTPELTWERV 500
    RSQVDHVIWP DGKRIVLLAE GRLLNLSCST VPTFVLSITA TTQALALIEL 550
    YNAPEGRYKQ DVYLLPKKMD EYVASLHLPT FDAHLTELTD EQAKYLGLNK 600
    NGPFKPNYYR Y 611
    Length:611
    Mass (Da):66,721
    Last modified:December 1, 2001 - v1
    Checksum:iA76B1275FC0D891D
    GO
    Isoform 2 (identifier: Q96HN2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         122-122: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:610
    Mass (Da):66,593
    Checksum:iD54ED0745D3A286B
    GO
    Isoform 3 (identifier: Q96HN2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MSVQVVSAAAAAKVPEVE → MLGSKKKYIVNGNSGIKA
         19-121: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:508
    Mass (Da):56,697
    Checksum:i1198694128CB2301
    GO
    Isoform 4 (identifier: Q96HN2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: MSVQVVSAAAAAKVPEVEL → MEKWDGNEGTSAFHMPEWM
         20-122: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:508
    Mass (Da):56,944
    Checksum:i197CA80AF2940465
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1919MSVQV…PEVEL → MEKWDGNEGTSAFHMPEWM in isoform 4. 1 PublicationVSP_046278Add
    BLAST
    Alternative sequencei1 – 1818MSVQV…VPEVE → MLGSKKKYIVNGNSGIKA in isoform 3. 1 PublicationVSP_043185Add
    BLAST
    Alternative sequencei19 – 121103Missing in isoform 3. 1 PublicationVSP_043186Add
    BLAST
    Alternative sequencei20 – 122103Missing in isoform 4. 1 PublicationVSP_046279Add
    BLAST
    Alternative sequencei122 – 1221Missing in isoform 2. 1 PublicationVSP_040095

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020635 mRNA. Translation: BAA74851.1. Different initiation.
    AK025372 mRNA. No translation available.
    AK295851 mRNA. Translation: BAG58657.1.
    AK316073 mRNA. Translation: BAH14444.1.
    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.
    CCDSiCCDS47706.1. [Q96HN2-2]
    CCDS47707.2. [Q96HN2-3]
    CCDS47708.1. [Q96HN2-4]
    CCDS5812.1. [Q96HN2-1]
    RefSeqiNP_001124192.1. NM_001130720.2. [Q96HN2-2]
    NP_001124194.2. NM_001130722.2. [Q96HN2-3]
    NP_001124195.1. NM_001130723.2. [Q96HN2-4]
    NP_056143.1. NM_015328.3. [Q96HN2-1]
    UniGeneiHs.600789.

    Genome annotation databases

    EnsembliENST00000325006; ENSP00000315931; ENSG00000158467. [Q96HN2-1]
    ENST00000446544; ENSP00000413639; ENSG00000158467. [Q96HN2-2]
    ENST00000474594; ENSP00000420459; ENSG00000158467. [Q96HN2-4]
    ENST00000490911; ENSP00000420801; ENSG00000158467. [Q96HN2-3]
    GeneIDi23382.
    KEGGihsa:23382.
    UCSCiuc003vot.3. human. [Q96HN2-2]
    uc011kov.2. human. [Q96HN2-1]
    uc011kox.2. human. [Q96HN2-3]

    Polymorphism databases

    DMDMi21759427.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020635 mRNA. Translation: BAA74851.1 . Different initiation.
    AK025372 mRNA. No translation available.
    AK295851 mRNA. Translation: BAG58657.1 .
    AK316073 mRNA. Translation: BAH14444.1 .
    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 .
    CCDSi CCDS47706.1. [Q96HN2-2 ]
    CCDS47707.2. [Q96HN2-3 ]
    CCDS47708.1. [Q96HN2-4 ]
    CCDS5812.1. [Q96HN2-1 ]
    RefSeqi NP_001124192.1. NM_001130720.2. [Q96HN2-2 ]
    NP_001124194.2. NM_001130722.2. [Q96HN2-3 ]
    NP_001124195.1. NM_001130723.2. [Q96HN2-4 ]
    NP_056143.1. NM_015328.3. [Q96HN2-1 ]
    UniGenei Hs.600789.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GVP X-ray 2.25 A/B/C/D 175-607 [» ]
    ProteinModelPortali Q96HN2.
    SMRi Q96HN2. Positions 176-607.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116958. 7 interactions.
    IntActi Q96HN2. 7 interactions.
    MINTi MINT-5005542.
    STRINGi 9606.ENSP00000315931.

    PTM databases

    PhosphoSitei Q96HN2.

    Polymorphism databases

    DMDMi 21759427.

    Proteomic databases

    MaxQBi Q96HN2.
    PaxDbi Q96HN2.
    PRIDEi Q96HN2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325006 ; ENSP00000315931 ; ENSG00000158467 . [Q96HN2-1 ]
    ENST00000446544 ; ENSP00000413639 ; ENSG00000158467 . [Q96HN2-2 ]
    ENST00000474594 ; ENSP00000420459 ; ENSG00000158467 . [Q96HN2-4 ]
    ENST00000490911 ; ENSP00000420801 ; ENSG00000158467 . [Q96HN2-3 ]
    GeneIDi 23382.
    KEGGi hsa:23382.
    UCSCi uc003vot.3. human. [Q96HN2-2 ]
    uc011kov.2. human. [Q96HN2-1 ]
    uc011kox.2. human. [Q96HN2-3 ]

    Organism-specific databases

    CTDi 23382.
    GeneCardsi GC07P128865.
    HGNCi HGNC:22204. AHCYL2.
    HPAi HPA053128.
    neXtProti NX_Q96HN2.
    PharmGKBi PA162376046.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0499.
    HOGENOMi HOG000227986.
    HOVERGENi HBG005041.
    InParanoidi Q96HN2.
    KOi K01251.
    OMAi AENWQPN.
    OrthoDBi EOG76739S.
    PhylomeDBi Q96HN2.
    TreeFami TF300415.

    Enzyme and pathway databases

    UniPathwayi UPA00314 ; UER00076 .

    Miscellaneous databases

    ChiTaRSi AHCYL2. human.
    EvolutionaryTracei Q96HN2.
    GenomeRNAii 23382.
    NextBioi 45489.
    PROi Q96HN2.

    Gene expression databases

    ArrayExpressi Q96HN2.
    Bgeei Q96HN2.
    CleanExi HS_AHCYL2.
    Genevestigatori Q96HN2.

    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 ]
    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. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    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] (ISOFORMS 3 AND 4).
      Tissue: Colon mucosa and Hippocampus.
    3. "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.
      , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung and Uterus.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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.

    Entry informationi

    Entry nameiSAHH3_HUMAN
    AccessioniPrimary (citable) accession number: Q96HN2
    Secondary accession number(s): B4DIZ5, D9N155, O94917
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 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 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3