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O76021

- RL1D1_HUMAN

UniProt

O76021 - RL1D1_HUMAN

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Protein
Ribosomal L1 domain-containing protein 1
Gene
RSL1D1, CATX11, CSIG, PBK1, L12
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 1
PRO_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.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili280 – 31334 Reviewed prediction
Add
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.

Sequencei

Sequence statusi: Complete.

O76021-1 [UniParc]FASTAAdd to Basket

« 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

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.

Sequence conflict

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

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.
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

EnsembliENST00000571133; ENSP00000460871; ENSG00000171490.
GeneIDi26156.
KEGGihsa:26156.
UCSCiuc002dbp.1. human.

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 .
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 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

« Hide 'large scale' publications
  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], 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].
  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].
    Tissue: Lung.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain and Lung.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-290.
    Tissue: Brain.
  7. 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.
  8. "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.
    Tissue: Colon.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. 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.
  16. "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].
  17. "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.
  18. "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].
  19. "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.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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].
  22. "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].
  23. 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): 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: September 3, 2014
This is version 126 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

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