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Q9UET6

- TRM7_HUMAN

UniProt

Q9UET6 - TRM7_HUMAN

Protein

Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase

Gene

FTSJ1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.UniRule annotation

    Catalytic activityi

    S-adenosyl-L-methionine + cytidine(32)/guanosine(34) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei55 – 551S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei75 – 751S-adenosyl-L-methionineUniRule annotation
    Binding sitei91 – 911S-adenosyl-L-methionineUniRule annotation
    Binding sitei116 – 1161S-adenosyl-L-methionineUniRule annotation
    Active sitei156 – 1561Proton acceptorUniRule annotation

    GO - Molecular functioni

    1. tRNA methyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cytoplasmic translation Source: UniProtKB-HAMAP
    2. tRNA nucleoside ribose methylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferaseUniRule annotation (EC:2.1.1.205UniRule annotation)
    Alternative name(s):
    2'-O-ribose RNA methyltransferase TRM7 homologUniRule annotation
    Protein ftsJ homolog 1UniRule annotation
    Gene namesi
    Name:FTSJ1UniRule annotation
    ORF Names:JM23
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13254. FTSJ1.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked 44 (MRX44) [MIM:309549]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi309549. phenotype.
    Orphaneti777. X-linked non-syndromic intellectual disability.
    PharmGKBiPA28417.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferasePRO_0000155575Add
    BLAST

    Proteomic databases

    MaxQBiQ9UET6.
    PaxDbiQ9UET6.
    PRIDEiQ9UET6.

    PTM databases

    PhosphoSiteiQ9UET6.

    Expressioni

    Tissue specificityi

    Found in fetal brain, lung, liver and kidney. In the adult brain, expressed in amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus.1 Publication

    Gene expression databases

    ArrayExpressiQ9UET6.
    BgeeiQ9UET6.
    CleanExiHS_FTSJ1.
    GenevestigatoriQ9UET6.

    Organism-specific databases

    HPAiHPA002718.

    Interactioni

    Protein-protein interaction databases

    BioGridi117291. 4 interactions.
    IntActiQ9UET6. 1 interaction.
    STRINGi9606.ENSP00000326948.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UET6.
    SMRiQ9UET6. Positions 20-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the methyltransferase superfamily. RlmE family. TRM7 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0293.
    HOGENOMiHOG000162368.
    HOVERGENiHBG017749.
    InParanoidiQ9UET6.
    KOiK14864.
    OMAiIIRHFEG.
    PhylomeDBiQ9UET6.
    TreeFamiTF314897.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    HAMAPiMF_01547. RNA_methyltr_E.
    MF_03162. RNA_methyltr_E_TRM7.
    InterProiIPR028590. RNA_methyltr_E_Trm7.
    IPR015507. rRNA-MeTfrase_E.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR10920. PTHR10920. 1 hit.
    PfamiPF01728. FtsJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UET6-1) [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

    MGRTSKDKRD VYYRLAKENG WRARSAFKLL QLDKEFQLFQ GVTRAVDLCA    50
    APGSWSQVLS QKIGGQGSGH VVAVDLQAMA PLPGVVQIQG DITQLSTAKE 100
    IIQHFKGCPA DLVVCDGAPD VTGLHDVDEY MQAQLLLAAL NIATHVLKPG 150
    GCFVAKIFRG RDVTLLYSQL QVFFSSVLCA KPRSSRNSSI EAFAVCQGYD 200
    PPEGFIPDLS KPLLDHSYDP DFNQLDGPTR IIVPFVTCGD LSSYDSDRSY 250
    PLDLEGGSEY KYTPPTQPPI SPPYQEACTL KRKGQLAKEI RPQDCPISRV 300
    DTFPQPLAAP QCHTLLAPEM EDNEMSCSP 329
    Length:329
    Mass (Da):36,079
    Last modified:December 1, 2000 - v2
    Checksum:i9A85D63A4FA80615
    GO
    Isoform 2 (identifier: Q9UET6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         219-220: Missing.

    Show »
    Length:327
    Mass (Da):35,867
    Checksum:i54417CCDEB515C55
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei219 – 2202Missing in isoform 2. 1 PublicationVSP_041419

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF063015 mRNA. Translation: AAC33734.1.
    AJ005892 mRNA. Translation: CAA06749.1.
    AK315138 mRNA. Translation: BAG37587.1.
    AF196972 Genomic DNA. No translation available.
    CH471224 Genomic DNA. Translation: EAW50782.1.
    BC023584 mRNA. Translation: AAH23584.1.
    CCDSiCCDS14294.1. [Q9UET6-1]
    CCDS14295.1. [Q9UET6-2]
    RefSeqiNP_001269086.1. NM_001282157.1.
    NP_036412.1. NM_012280.3. [Q9UET6-1]
    NP_803188.1. NM_177439.2. [Q9UET6-2]
    XP_005272652.1. XM_005272595.1. [Q9UET6-2]
    UniGeneiHs.23170.

    Genome annotation databases

    EnsembliENST00000019019; ENSP00000019019; ENSG00000068438. [Q9UET6-2]
    ENST00000348411; ENSP00000326948; ENSG00000068438. [Q9UET6-1]
    GeneIDi24140.
    KEGGihsa:24140.
    UCSCiuc004djn.1. human. [Q9UET6-2]
    uc004djo.1. human. [Q9UET6-1]

    Polymorphism databases

    DMDMi12643879.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF063015 mRNA. Translation: AAC33734.1 .
    AJ005892 mRNA. Translation: CAA06749.1 .
    AK315138 mRNA. Translation: BAG37587.1 .
    AF196972 Genomic DNA. No translation available.
    CH471224 Genomic DNA. Translation: EAW50782.1 .
    BC023584 mRNA. Translation: AAH23584.1 .
    CCDSi CCDS14294.1. [Q9UET6-1 ]
    CCDS14295.1. [Q9UET6-2 ]
    RefSeqi NP_001269086.1. NM_001282157.1.
    NP_036412.1. NM_012280.3. [Q9UET6-1 ]
    NP_803188.1. NM_177439.2. [Q9UET6-2 ]
    XP_005272652.1. XM_005272595.1. [Q9UET6-2 ]
    UniGenei Hs.23170.

    3D structure databases

    ProteinModelPortali Q9UET6.
    SMRi Q9UET6. Positions 20-201.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117291. 4 interactions.
    IntActi Q9UET6. 1 interaction.
    STRINGi 9606.ENSP00000326948.

    PTM databases

    PhosphoSitei Q9UET6.

    Polymorphism databases

    DMDMi 12643879.

    Proteomic databases

    MaxQBi Q9UET6.
    PaxDbi Q9UET6.
    PRIDEi Q9UET6.

    Protocols and materials databases

    DNASUi 24140.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000019019 ; ENSP00000019019 ; ENSG00000068438 . [Q9UET6-2 ]
    ENST00000348411 ; ENSP00000326948 ; ENSG00000068438 . [Q9UET6-1 ]
    GeneIDi 24140.
    KEGGi hsa:24140.
    UCSCi uc004djn.1. human. [Q9UET6-2 ]
    uc004djo.1. human. [Q9UET6-1 ]

    Organism-specific databases

    CTDi 24140.
    GeneCardsi GC0XP048334.
    HGNCi HGNC:13254. FTSJ1.
    HPAi HPA002718.
    MIMi 300499. gene.
    309549. phenotype.
    neXtProti NX_Q9UET6.
    Orphaneti 777. X-linked non-syndromic intellectual disability.
    PharmGKBi PA28417.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0293.
    HOGENOMi HOG000162368.
    HOVERGENi HBG017749.
    InParanoidi Q9UET6.
    KOi K14864.
    OMAi IIRHFEG.
    PhylomeDBi Q9UET6.
    TreeFami TF314897.

    Miscellaneous databases

    ChiTaRSi FTSJ1. human.
    GeneWikii FTSJ1.
    GenomeRNAii 24140.
    NextBioi 46813.
    PROi Q9UET6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UET6.
    Bgeei Q9UET6.
    CleanExi HS_FTSJ1.
    Genevestigatori Q9UET6.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    HAMAPi MF_01547. RNA_methyltr_E.
    MF_03162. RNA_methyltr_E_TRM7.
    InterProi IPR028590. RNA_methyltr_E_Trm7.
    IPR015507. rRNA-MeTfrase_E.
    IPR002877. rRNA_MeTrfase_FtsJ_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10920. PTHR10920. 1 hit.
    Pfami PF01728. FtsJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A human and yeast gene involved in cell division."
      Pengue G., Lutfiyya L.L., Mazzarella R.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Transcription map in Xp11.23."
      Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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 1).
    4. "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].
    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).
      Tissue: Lymph.
    7. "Mutations in the FTSJ1 gene coding for a novel S-adenosylmethionine-binding protein cause nonsyndromic X-linked mental retardation."
      Freude K., Hoffmann K., Jensen L.-R., Delatycki M.B., des Portes V., Moser B., Hamel B.C.J., van Bokhoven H., Moraine C., Fryns J.-P., Chelly J., Gecz J., Lenzner S., Kalscheuer V.M., Ropers H.-H.
      Am. J. Hum. Genet. 75:305-309(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MRX44, TISSUE SPECIFICITY.
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTRM7_HUMAN
    AccessioniPrimary (citable) accession number: Q9UET6
    Secondary accession number(s): B2RCJ0, O75670
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 127 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3