Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O76021

- RL1D1_HUMAN

UniProt

O76021 - RL1D1_HUMAN

Protein

Ribosomal L1 domain-containing protein 1

Gene

RSL1D1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (26 Apr 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. osteoblast differentiation Source: UniProt
    2. regulation of protein localization Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosomal L1 domain-containing protein 1
    Alternative name(s):
    CATX-11
    Cellular senescence-inhibited gene protein
    Protein PBK1
    Gene namesi
    Name:RSL1D1
    Synonyms:CATX11, CSIG, PBK1
    ORF Names:L12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:24534. RSL1D1.

    Subcellular locationi

    Nucleusnucleolus 2 Publications

    GO - Cellular componenti

    1. membrane Source: UniProt
    2. nucleolus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142670966.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 490490Ribosomal L1 domain-containing protein 1PRO_0000125844Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei340 – 3401Phosphothreonine2 Publications
    Modified residuei358 – 3581Phosphothreonine2 Publications
    Modified residuei361 – 3611Phosphoserine4 Publications
    Modified residuei375 – 3751Phosphothreonine1 Publication
    Modified residuei392 – 3921Phosphoserine3 Publications
    Modified residuei396 – 3961Phosphoserine3 Publications
    Modified residuei415 – 4151Phosphothreonine1 Publication
    Modified residuei423 – 4231Phosphothreonine2 Publications
    Modified residuei427 – 4271Phosphoserine6 Publications
    Modified residuei443 – 4431Phosphoserine1 Publication
    Modified residuei465 – 4651Phosphothreonine1 Publication
    Modified residuei468 – 4681N6-acetyllysine1 Publication
    Modified residuei469 – 4691Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO76021.
    PaxDbiO76021.
    PRIDEiO76021.

    2D gel databases

    SWISS-2DPAGEO76021.

    PTM databases

    PhosphoSiteiO76021.

    Expressioni

    Tissue specificityi

    Placenta.1 Publication

    Gene expression databases

    ArrayExpressiO76021.
    BgeeiO76021.
    CleanExiHS_RSL1D1.
    GenevestigatoriO76021.

    Organism-specific databases

    HPAiHPA043483.

    Interactioni

    Protein-protein interaction databases

    BioGridi117587. 50 interactions.
    IntActiO76021. 22 interactions.
    MINTiMINT-1139726.
    STRINGi9606.ENSP00000379760.

    Structurei

    3D structure databases

    ProteinModelPortaliO76021.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili280 – 31334Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG247516.
    HOVERGENiHBG054786.
    InParanoidiO76021.
    KOiK14775.
    OMAiPSHLGRH.
    OrthoDBiEOG7RV9GH.
    PhylomeDBiO76021.
    TreeFamiTF354254.

    Family and domain databases

    Gene3Di3.30.190.20. 1 hit.
    InterProiIPR023674. Ribosomal_L1-like.
    IPR028364. Ribosomal_L1/biogenesis.
    IPR016094. Ribosomal_L1_2-a/b-sand.
    [Graphical view]
    PfamiPF00687. Ribosomal_L1. 1 hit.
    [Graphical view]
    SUPFAMiSSF56808. SSF56808. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O76021-1) [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

    MEDSASASLS SAAATGTSTS TPAAPTARKQ LDKEQVRKAV DALLTHCKSR    50
    KNNYGLLLNE NESLFLMVVL WKIPSKELRV RLTLPHSIRS DSEDICLFTK 100
    DEPNSTPEKT EQFYRKLLNK HGIKTVSQII SLQTLKKEYK SYEAKLRLLS 150
    SFDFFLTDAR IRRLLPSLIG RHFYQRKKVP VSVNLLSKNL SREINDCIGG 200
    TVLNISKSGS CSAIRIGHVG MQIEHIIENI VAVTKGLSEK LPEKWESVKL 250
    LFVKTEKSAA LPIFSSFVSN WDEATKRSLL NKKKKEARRK RRERNFEKQK 300
    ERKKKRQQAR KTASVLSKDD VAPESGDTTV KKPESKKEQT PEHGKKKRGR 350
    GKAQVKATNE SEDEIPQLVP IGKKTPANEK VEIQKHATGK KSPAKSPNPS 400
    TPRGKKRKAL PASETPKAAE SETPGKSPEK KPKIKEEAVK EKSPSLGKKD 450
    ARQTPKKPEA KFFTTPSKSV RKASHTPKKW PKKPKVPQST 490
    Length:490
    Mass (Da):54,973
    Last modified:April 26, 2005 - v3
    Checksum:i5E5CDB8AA8BC3709
    GO
    Isoform 2 (identifier: O76021-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-220: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:270
    Mass (Da):30,354
    Checksum:i83491FBC2D92689C
    GO

    Sequence cautioni

    The sequence AAF98239.1 differs from that shown. Reason: Frameshift at position 394.
    The sequence CAA07491.1 differs from that shown. Reason: Frameshift at position 486.
    The sequence AAH19069.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501R → G in AAN46298. 1 PublicationCurated
    Sequence conflicti189 – 1891N → D in CAB43231. (PubMed:17974005)Curated
    Sequence conflicti294 – 2941R → G in AAN46298. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 220220Missing in isoform 2. 1 PublicationVSP_056143Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007398 mRNA. Translation: CAA07491.1. Frameshift.
    AY598331 mRNA. Translation: AAT06742.1.
    AY154473 mRNA. Translation: AAN46298.1.
    AK295935 mRNA. Translation: BAG58720.1.
    AC010654 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85133.1.
    CH471112 Genomic DNA. Translation: EAW85135.1.
    BC019069 mRNA. Translation: AAH19069.2. Different initiation.
    BC112228 mRNA. Translation: AAI12229.1.
    BC113699 mRNA. Translation: AAI13700.1.
    AL049999 mRNA. Translation: CAB43231.2.
    AF083127 mRNA. Translation: AAF98239.1. Frameshift.
    CCDSiCCDS10551.1.
    PIRiT08693.
    RefSeqiNP_056474.2. NM_015659.2.
    UniGeneiHs.401842.

    Genome annotation databases

    EnsembliENST00000542106; ENSP00000442089; ENSG00000171490.
    ENST00000571133; ENSP00000460871; ENSG00000171490.
    GeneIDi26156.
    KEGGihsa:26156.
    UCSCiuc002dbp.1. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007398 mRNA. Translation: CAA07491.1 . Frameshift.
    AY598331 mRNA. Translation: AAT06742.1 .
    AY154473 mRNA. Translation: AAN46298.1 .
    AK295935 mRNA. Translation: BAG58720.1 .
    AC010654 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85133.1 .
    CH471112 Genomic DNA. Translation: EAW85135.1 .
    BC019069 mRNA. Translation: AAH19069.2 . Different initiation.
    BC112228 mRNA. Translation: AAI12229.1 .
    BC113699 mRNA. Translation: AAI13700.1 .
    AL049999 mRNA. Translation: CAB43231.2 .
    AF083127 mRNA. Translation: AAF98239.1 . Frameshift.
    CCDSi CCDS10551.1.
    PIRi T08693.
    RefSeqi NP_056474.2. NM_015659.2.
    UniGenei Hs.401842.

    3D structure databases

    ProteinModelPortali O76021.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117587. 50 interactions.
    IntActi O76021. 22 interactions.
    MINTi MINT-1139726.
    STRINGi 9606.ENSP00000379760.

    Chemistry

    ChEMBLi CHEMBL1075139.

    PTM databases

    PhosphoSitei O76021.

    2D gel databases

    SWISS-2DPAGE O76021.

    Proteomic databases

    MaxQBi O76021.
    PaxDbi O76021.
    PRIDEi O76021.

    Protocols and materials databases

    DNASUi 26156.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000542106 ; ENSP00000442089 ; ENSG00000171490 .
    ENST00000571133 ; ENSP00000460871 ; ENSG00000171490 .
    GeneIDi 26156.
    KEGGi hsa:26156.
    UCSCi uc002dbp.1. human.

    Organism-specific databases

    CTDi 26156.
    GeneCardsi GC16M011933.
    HGNCi HGNC:24534. RSL1D1.
    HPAi HPA043483.
    neXtProti NX_O76021.
    PharmGKBi PA142670966.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247516.
    HOVERGENi HBG054786.
    InParanoidi O76021.
    KOi K14775.
    OMAi PSHLGRH.
    OrthoDBi EOG7RV9GH.
    PhylomeDBi O76021.
    TreeFami TF354254.

    Miscellaneous databases

    GeneWikii RSL1D1.
    GenomeRNAii 26156.
    NextBioi 48251.
    PROi O76021.

    Gene expression databases

    ArrayExpressi O76021.
    Bgeei O76021.
    CleanExi HS_RSL1D1.
    Genevestigatori O76021.

    Family and domain databases

    Gene3Di 3.30.190.20. 1 hit.
    InterProi IPR023674. Ribosomal_L1-like.
    IPR028364. Ribosomal_L1/biogenesis.
    IPR016094. Ribosomal_L1_2-a/b-sand.
    [Graphical view ]
    Pfami PF00687. Ribosomal_L1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56808. SSF56808. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of differentially expressed genes in human trophoblast cells by DDRT-PCR."
      Huch G., Hohn H.-P., Denker H.-W.
      Placenta 19:557-567(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. "Suppression subtractive hybridization and expression profiling identifies a unique set of genes overexpressed in non-small-cell lung cancer."
      Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C., Cerveny C., Law C.-L., Wahl A., Carter P.
      Oncogene 23:7734-7745(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Identification of a new gene associated with cellular senescence in human diploid fibroblast."
      Guo S.-Z., Zhang Z.-Y., Tong T.-J.
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    4. "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: Substantia nigra.
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Brain and Lung.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-290 (ISOFORM 1).
      Tissue: Brain.
    9. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-28; 90-100; 125-136; 148-160; 164-171; 179-188; 193-207 AND 258-276, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    10. "Isolation of novel genes from human colonic epithelial cells."
      Kairo A., Wang L., Gao Z.Q., Gao Z.P., Boman B.M.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-401 (ISOFORM 1).
      Tissue: Colon.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    13. "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 THR-340 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-396; THR-423; SER-427 AND SER-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    16. "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-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358; SER-361; SER-392; SER-396; THR-415; THR-423; SER-427; SER-443; THR-465 AND SER-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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].
    19. "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-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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 THR-340; SER-361; THR-375; SER-392 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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 THR-358; SER-361; SER-396 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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].
    25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRL1D1_HUMAN
    AccessioniPrimary (citable) accession number: O76021
    Secondary accession number(s): B4DJ58
    , D3DUG7, Q2M1T7, Q6PL22, Q8IWS7, Q8WUZ1, Q9HDA9, Q9Y3Z9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 127 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3