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Q9BXY0

- MAK16_HUMAN

UniProt

Q9BXY0 - MAK16_HUMAN

Protein

Protein MAK16 homolog

Gene

MAK16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein MAK16 homolog
    Alternative name(s):
    NNP78
    Protein RBM13
    Gene namesi
    Name:MAK16
    Synonyms:RBM13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:13703. MAK16.

    Subcellular locationi

    Nucleusnucleolus 2 Publications

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162394925.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 300300Protein MAK16 homologPRO_0000203794Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei197 – 1971Phosphoserine1 Publication
    Modified residuei199 – 1991PhosphoserineBy similarity
    Modified residuei200 – 2001Phosphoserine1 Publication
    Modified residuei229 – 2291Phosphoserine3 Publications
    Modified residuei232 – 2321Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BXY0.
    PaxDbiQ9BXY0.
    PRIDEiQ9BXY0.

    2D gel databases

    SWISS-2DPAGEQ9BXY0.

    PTM databases

    PhosphoSiteiQ9BXY0.

    Expressioni

    Gene expression databases

    BgeeiQ9BXY0.
    CleanExiHS_MAK16.
    GenevestigatoriQ9BXY0.

    Organism-specific databases

    HPAiHPA044417.
    HPA050574.

    Interactioni

    Protein-protein interaction databases

    BioGridi124134. 5 interactions.
    IntActiQ9BXY0. 1 interaction.
    MINTiMINT-3058483.
    STRINGi9606.ENSP00000353246.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BXY0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi198 – 24952Asp-richAdd
    BLAST
    Compositional biasi255 – 2595Poly-Glu

    Sequence similaritiesi

    Belongs to the MAK16 family.Curated

    Phylogenomic databases

    eggNOGiCOG5129.
    HOGENOMiHOG000201538.
    HOVERGENiHBG055328.
    InParanoidiQ9BXY0.
    KOiK14831.
    OMAiSPAHMWE.
    OrthoDBiEOG7TJ3KB.
    PhylomeDBiQ9BXY0.
    TreeFamiTF105759.

    Family and domain databases

    InterProiIPR029004. L28e/Mak16.
    IPR006958. Mak16.
    [Graphical view]
    PfamiPF04874. Mak16. 1 hit.
    PF01778. Ribosomal_L28e. 1 hit.
    [Graphical view]
    PIRSFiPIRSF003352. MAK16. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9BXY0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSDDVIWDT LGNKQFCSFK IRTKTQSFCR NEYSLTGLCN RSSCPLANSQ    50
    YATIKEEKGQ CYLYMKVIER AAFPRRLWER VRLSKNYEKA LEQIDENLIY 100
    WPRFIRHKCK QRFTKITQYL IRIRKLTLKR QRKLVPLSKK VERREKRREE 150
    KALIAAQLDN AIEKELLERL KQDTYGDIYN FPIHAFDKAL EQQEAESDSS 200
    DTEEKDDDDD DEEDVGKREF VEDGEVDESD ISDFEDMDKL DASSDEDQDG 250
    KSSSEEEEEK ALSAKHKGKM PLRGPLQRKR AYVEIEYEQE TEPVAKAKTT 300
    Length:300
    Mass (Da):35,369
    Last modified:July 19, 2005 - v2
    Checksum:i2A757589C4749760
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti200 – 2001S → L in BAB55134. (PubMed:14702039)Curated
    Sequence conflicti281 – 2811A → V in AAH39740. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti277 – 2771Q → R.2 Publications
    Corresponds to variant rs6468171 [ dbSNP | Ensembl ].
    VAR_023076

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF251062 mRNA. Translation: AAK34952.1.
    AK027469 mRNA. Translation: BAB55134.1.
    AK314491 mRNA. Translation: BAG37091.1.
    CH471080 Genomic DNA. Translation: EAW63400.1.
    BC028230 mRNA. Translation: AAH28230.1.
    BC039740 mRNA. Translation: AAH39740.1.
    BC050528 mRNA. Translation: AAH50528.1.
    CCDSiCCDS6089.1.
    RefSeqiNP_115898.2. NM_032509.3.
    UniGeneiHs.583805.

    Genome annotation databases

    EnsembliENST00000360128; ENSP00000353246; ENSG00000198042.
    GeneIDi84549.
    KEGGihsa:84549.
    UCSCiuc003xjj.3. human.

    Polymorphism databases

    DMDMi71152029.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF251062 mRNA. Translation: AAK34952.1 .
    AK027469 mRNA. Translation: BAB55134.1 .
    AK314491 mRNA. Translation: BAG37091.1 .
    CH471080 Genomic DNA. Translation: EAW63400.1 .
    BC028230 mRNA. Translation: AAH28230.1 .
    BC039740 mRNA. Translation: AAH39740.1 .
    BC050528 mRNA. Translation: AAH50528.1 .
    CCDSi CCDS6089.1.
    RefSeqi NP_115898.2. NM_032509.3.
    UniGenei Hs.583805.

    3D structure databases

    ProteinModelPortali Q9BXY0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124134. 5 interactions.
    IntActi Q9BXY0. 1 interaction.
    MINTi MINT-3058483.
    STRINGi 9606.ENSP00000353246.

    PTM databases

    PhosphoSitei Q9BXY0.

    Polymorphism databases

    DMDMi 71152029.

    2D gel databases

    SWISS-2DPAGE Q9BXY0.

    Proteomic databases

    MaxQBi Q9BXY0.
    PaxDbi Q9BXY0.
    PRIDEi Q9BXY0.

    Protocols and materials databases

    DNASUi 84549.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360128 ; ENSP00000353246 ; ENSG00000198042 .
    GeneIDi 84549.
    KEGGi hsa:84549.
    UCSCi uc003xjj.3. human.

    Organism-specific databases

    CTDi 84549.
    GeneCardsi GC08P033342.
    HGNCi HGNC:13703. MAK16.
    HPAi HPA044417.
    HPA050574.
    neXtProti NX_Q9BXY0.
    PharmGKBi PA162394925.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5129.
    HOGENOMi HOG000201538.
    HOVERGENi HBG055328.
    InParanoidi Q9BXY0.
    KOi K14831.
    OMAi SPAHMWE.
    OrthoDBi EOG7TJ3KB.
    PhylomeDBi Q9BXY0.
    TreeFami TF105759.

    Miscellaneous databases

    GeneWikii RBM13.
    GenomeRNAii 84549.
    NextBioi 74427.
    PROi Q9BXY0.

    Gene expression databases

    Bgeei Q9BXY0.
    CleanExi HS_MAK16.
    Genevestigatori Q9BXY0.

    Family and domain databases

    InterProi IPR029004. L28e/Mak16.
    IPR006958. Mak16.
    [Graphical view ]
    Pfami PF04874. Mak16. 1 hit.
    PF01778. Ribosomal_L28e. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003352. MAK16. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S., Tang R., Chen X., Wu C.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-277.
    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].
    3. 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], VARIANT ARG-277.
      Tissue: Brain, Testis and Uterus.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-229 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-229 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-197; SER-200; SER-229 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMAK16_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXY0
    Secondary accession number(s): B2RB44
    , Q5U5T1, Q86UC4, Q96SY6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 104 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 8
      Human chromosome 8: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3