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O95671

- ASML_HUMAN

UniProt

O95671 - ASML_HUMAN

Protein

N-acetylserotonin O-methyltransferase-like protein

Gene

ASMTL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    Unknown. The presence of the putative catalytic domain of S-adenosyl-L-methionine binding argues for a methyltransferase activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei44 – 441Sequence Analysis
    Binding sitei482 – 4821S-adenosyl-L-methionineBy similarity
    Binding sitei525 – 5251S-adenosyl-L-methionineBy similarity

    GO - Molecular functioni

    1. O-methyltransferase activity Source: InterPro

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylserotonin O-methyltransferase-like protein (EC:2.1.1.-)
    Short name:
    ASMTL
    Gene namesi
    Name:ASMTL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:751. ASMTL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25050.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 621621N-acetylserotonin O-methyltransferase-like proteinPRO_0000064702Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei239 – 2391Phosphoserine7 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95671.
    PaxDbiO95671.
    PRIDEiO95671.

    PTM databases

    PhosphoSiteiO95671.

    Expressioni

    Tissue specificityi

    Widely expressed. In adult, highly expressed in pancreas, placenta, fibroblast, thymus, prostate, testis, ovary and colon. Expressed at lower levels in spleen, small intestine and leukocytes. In fetus, expressed at high levels in the lung and kidney and at lower level in brain and liver.

    Gene expression databases

    ArrayExpressiO95671.
    BgeeiO95671.
    CleanExiHS_ASMTL.
    GenevestigatoriO95671.

    Organism-specific databases

    HPAiHPA003630.
    HPA021865.

    Interactioni

    Protein-protein interaction databases

    BioGridi114178. 8 interactions.
    IntActiO95671. 2 interactions.
    STRINGi9606.ENSP00000370718.

    Structurei

    Secondary structure

    1
    621
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 173
    Helixi22 – 309
    Helixi48 – 503
    Beta strandi51 – 533
    Helixi54 – 7724
    Beta strandi82 – 9312
    Beta strandi96 – 983
    Helixi104 – 11411
    Beta strandi117 – 13317
    Beta strandi136 – 15217
    Helixi157 – 16610
    Helixi168 – 1714
    Helixi173 – 1753
    Beta strandi178 – 1803
    Helixi181 – 1844
    Beta strandi186 – 1916
    Helixi193 – 1975
    Helixi201 – 21212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P5XX-ray2.00A/B10-239[»]
    ProteinModelPortaliO95671.
    SMRiO95671. Positions 10-213, 287-618.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95671.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 223213MAF-likeAdd
    BLAST
    Regioni277 – 621345ASMT-likeAdd
    BLAST
    Regioni508 – 5103S-adenosyl-L-methionine bindingBy similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the maf family.Curated

    Phylogenomic databases

    eggNOGiCOG0500.
    HOGENOMiHOG000034104.
    HOVERGENiHBG036737.
    InParanoidiO95671.
    OMAiWEYINSG.
    OrthoDBiEOG7W1557.
    PhylomeDBiO95671.
    TreeFamiTF314574.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.40.50.150. 1 hit.
    3.90.950.10. 1 hit.
    HAMAPiMF_00528. Maf.
    InterProiIPR025772. ASMT-like.
    IPR029001. ITPase-like_fam.
    IPR003697. Maf.
    IPR001077. O_MeTrfase_2.
    IPR029063. SAM-dependent_MTases-like.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF02545. Maf. 1 hit.
    PF00891. Methyltransf_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52972. SSF52972. 1 hit.
    SSF53335. SSF53335. 1 hit.
    TIGRFAMsiTIGR00172. maf. 1 hit.
    PROSITEiPS51683. SAM_OMT_II. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95671-1) [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

    MVLCPVIGKL LHKRVVLASA SPRRQEILSN AGLRFEVVPS KFKEKLDKAS    50
    FATPYGYAME TAKQKALEVA NRLYQKDLRA PDVVIGADTI VTVGGLILEK 100
    PVDKQDAYRM LSRLSGREHS VFTGVAIVHC SSKDHQLDTR VSEFYEETKV 150
    KFSELSEELL WEYVHSGEPM DKAGGYGIQA LGGMLVESVH GDFLNVVGFP 200
    LNHFCKQLVK LYYPPRPEDL RRSVKHDSIP AADTFEDLSD VEGGGSEPTQ 250
    RDAGSRDEKA EAGEAGQATA EAECHRTRET LPPFPTRLLE LIEGFMLSKG 300
    LLTACKLKVF DLLKDEAPQK AADIASKVDA SACGMERLLD ICAAMGLLEK 350
    TEQGYSNTET ANVYLASDGE YSLHGFIMHN NDLTWNLFTY LEFAIREGTN 400
    QHHRALGKKA EDLFQDAYYQ SPETRLRFMR AMHGMTKLTA CQVATAFNLS 450
    RFSSACDVGG CTGALARELA REYPRMQVTV FDLPDIIELA AHFQPPGPQA 500
    VQIHFAAGDF FRDPLPSAEL YVLCRILHDW PDDKVHKLLS RVAESCKPGA 550
    GLLLVETLLD EEKRVAQRAL MQSLNMLVQT EGKERSLGEY QCLLELHGFH 600
    QVQVVHLGGV LDAILATKVA P 621
    Length:621
    Mass (Da):68,857
    Last modified:October 3, 2006 - v3
    Checksum:i564C2D538F4919EC
    GO
    Isoform 2 (identifier: O95671-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-91: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:605
    Mass (Da):67,193
    Checksum:i68D9C963275E9A36
    GO
    Isoform 3 (identifier: O95671-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-58: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:563
    Mass (Da):62,443
    Checksum:i5AC40CB68911EF40
    GO

    Sequence cautioni

    The sequence CAA75675.1 differs from that shown. Reason: Frameshift at position 616.
    The sequence CAA75676.1 differs from that shown. Reason: Frameshift at position 616.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti228 – 2281S → P in BAG63287. (PubMed:14702039)Curated
    Sequence conflicti364 – 3641Y → H in BAG63287. (PubMed:14702039)Curated
    Sequence conflicti434 – 4341G → S in BAG63287. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti458 – 4581V → M.1 Publication
    Corresponds to variant rs4503285 [ dbSNP | Ensembl ].
    VAR_054802
    Natural varianti541 – 5411R → K.2 Publications
    Corresponds to variant rs1127297 [ dbSNP | Ensembl ].
    VAR_054803

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5858Missing in isoform 3. 1 PublicationVSP_047412Add
    BLAST
    Alternative sequencei76 – 9116Missing in isoform 2. 1 PublicationVSP_007213Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15521 Genomic DNA. Translation: CAA75675.1. Frameshift.
    Y15521 Genomic DNA. Translation: CAA75676.1. Frameshift.
    AK090498 mRNA. Translation: BAC03468.1.
    AK301844 mRNA. Translation: BAG63287.1.
    AL683870 Genomic DNA. Translation: CAI39847.1.
    AL683870 Genomic DNA. Translation: CAI39848.1.
    BC002508 mRNA. Translation: AAH02508.1.
    BC010089 mRNA. Translation: AAH10089.1.
    CCDSiCCDS43917.1. [O95671-1]
    CCDS55362.1. [O95671-3]
    CCDS55363.1. [O95671-2]
    RefSeqiNP_001166944.1. NM_001173473.1. [O95671-3]
    NP_001166945.1. NM_001173474.1. [O95671-2]
    NP_004183.2. NM_004192.3. [O95671-1]
    XP_005274491.1. XM_005274434.1. [O95671-1]
    XP_005274840.1. XM_005274783.1. [O95671-1]
    UniGeneiHs.533514.

    Genome annotation databases

    EnsembliENST00000381317; ENSP00000370718; ENSG00000169093. [O95671-1]
    ENST00000381333; ENSP00000370734; ENSG00000169093. [O95671-2]
    ENST00000534940; ENSP00000446410; ENSG00000169093. [O95671-3]
    GeneIDi8623.
    KEGGihsa:8623.
    UCSCiuc004cpx.2. human. [O95671-1]
    uc004cpy.2. human. [O95671-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15521 Genomic DNA. Translation: CAA75675.1 . Frameshift.
    Y15521 Genomic DNA. Translation: CAA75676.1 . Frameshift.
    AK090498 mRNA. Translation: BAC03468.1 .
    AK301844 mRNA. Translation: BAG63287.1 .
    AL683870 Genomic DNA. Translation: CAI39847.1 .
    AL683870 Genomic DNA. Translation: CAI39848.1 .
    BC002508 mRNA. Translation: AAH02508.1 .
    BC010089 mRNA. Translation: AAH10089.1 .
    CCDSi CCDS43917.1. [O95671-1 ]
    CCDS55362.1. [O95671-3 ]
    CCDS55363.1. [O95671-2 ]
    RefSeqi NP_001166944.1. NM_001173473.1. [O95671-3 ]
    NP_001166945.1. NM_001173474.1. [O95671-2 ]
    NP_004183.2. NM_004192.3. [O95671-1 ]
    XP_005274491.1. XM_005274434.1. [O95671-1 ]
    XP_005274840.1. XM_005274783.1. [O95671-1 ]
    UniGenei Hs.533514.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P5X X-ray 2.00 A/B 10-239 [» ]
    ProteinModelPortali O95671.
    SMRi O95671. Positions 10-213, 287-618.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114178. 8 interactions.
    IntActi O95671. 2 interactions.
    STRINGi 9606.ENSP00000370718.

    PTM databases

    PhosphoSitei O95671.

    Proteomic databases

    MaxQBi O95671.
    PaxDbi O95671.
    PRIDEi O95671.

    Protocols and materials databases

    DNASUi 8623.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381317 ; ENSP00000370718 ; ENSG00000169093 . [O95671-1 ]
    ENST00000381333 ; ENSP00000370734 ; ENSG00000169093 . [O95671-2 ]
    ENST00000534940 ; ENSP00000446410 ; ENSG00000169093 . [O95671-3 ]
    GeneIDi 8623.
    KEGGi hsa:8623.
    UCSCi uc004cpx.2. human. [O95671-1 ]
    uc004cpy.2. human. [O95671-2 ]

    Organism-specific databases

    CTDi 8623.
    GeneCardsi GC0XM001522.
    H-InvDB HIX0176513.
    HIX0177590.
    HGNCi HGNC:751. ASMTL.
    HPAi HPA003630.
    HPA021865.
    MIMi 300162. gene.
    400011. gene.
    neXtProti NX_O95671.
    PharmGKBi PA25050.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0500.
    HOGENOMi HOG000034104.
    HOVERGENi HBG036737.
    InParanoidi O95671.
    OMAi WEYINSG.
    OrthoDBi EOG7W1557.
    PhylomeDBi O95671.
    TreeFami TF314574.

    Miscellaneous databases

    EvolutionaryTracei O95671.
    GeneWikii ASMTL.
    GenomeRNAii 8623.
    NextBioi 32321.
    PROi O95671.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95671.
    Bgeei O95671.
    CleanExi HS_ASMTL.
    Genevestigatori O95671.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.40.50.150. 1 hit.
    3.90.950.10. 1 hit.
    HAMAPi MF_00528. Maf.
    InterProi IPR025772. ASMT-like.
    IPR029001. ITPase-like_fam.
    IPR003697. Maf.
    IPR001077. O_MeTrfase_2.
    IPR029063. SAM-dependent_MTases-like.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF02545. Maf. 1 hit.
    PF00891. Methyltransf_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52972. SSF52972. 1 hit.
    SSF53335. SSF53335. 1 hit.
    TIGRFAMsi TIGR00172. maf. 1 hit.
    PROSITEi PS51683. SAM_OMT_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene duplications as a recurrent theme in the evolution of the human pseudoautosomal region 1: isolation of the gene ASMTL."
      Ried K., Rao E., Schiebel K., Rappold G.A.
      Hum. Mol. Genet. 7:1771-1778(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-541.
      Tissue: Bone marrow, Colon, Fetal brain, Pancreas and Placenta.
    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 2 AND 3).
      Tissue: Adrenal gland and Testis.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [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), VARIANTS MET-458 AND LYS-541.
      Tissue: Colon adenocarcinoma.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-239, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Crystal structure of maf domain of human N-acetylserotonin O-methyltransferase-like protein."
      Structural genomics consortium (SGC)
      Submitted (MAR-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 10-239.

    Entry informationi

    Entry nameiASML_HUMAN
    AccessioniPrimary (citable) accession number: O95671
    Secondary accession number(s): B4DX75
    , F5GXH4, J3JS33, Q5JQ53, Q8NBH5, Q96G02, Q9BUL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 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

    Miscellaneous

    The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes. It represents a unique fusion product of 2 different genes of different evolutionary origin and function. The N-terminus is homologous to the bacterial maf/orfE genes and the C-terminus is homologous to ASMT. Exon duplication, exon shuffling and gene fusion seem to be common characteristics of the PAR1 region.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3