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O76021 (RL1D1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal L1 domain-containing protein 1
Alternative name(s):
CATX-11
Cellular senescence-inhibited gene protein
Protein PBK1
Gene names
Name:RSL1D1
Synonyms:CATX11, CSIG, PBK1
ORF Names:L12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Nucleusnucleolus Ref.9 Ref.10.

Tissue specificity

Placenta. Ref.1

Sequence similarities

Belongs to the ribosomal protein L1P family. Highly divergent.

Sequence caution

The sequence AAF98239.1 differs from that shown. Reason: Frameshift at position 394.

The sequence AAH19069.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAA07491.1 differs from that shown. Reason: Frameshift at position 486.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Ribosomal L1 domain-containing protein 1
PRO_0000125844

Regions

Coiled coil280 – 31334 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.16 Ref.22 Ref.23
Modified residue3401Phosphothreonine Ref.11 Ref.19
Modified residue3581Phosphothreonine Ref.15 Ref.21
Modified residue3611Phosphoserine Ref.15 Ref.17 Ref.19 Ref.21
Modified residue3751Phosphothreonine Ref.19
Modified residue3921Phosphoserine Ref.12 Ref.15 Ref.19
Modified residue3961Phosphoserine Ref.12 Ref.15 Ref.21
Modified residue4151Phosphothreonine Ref.15
Modified residue4231Phosphothreonine Ref.12 Ref.15
Modified residue4271Phosphoserine Ref.11 Ref.12 Ref.14 Ref.15 Ref.19 Ref.21
Modified residue4431Phosphoserine Ref.15
Modified residue4651Phosphothreonine Ref.15
Modified residue4681N6-acetyllysine Ref.18
Modified residue4691Phosphoserine Ref.12 Ref.15

Experimental info

Sequence conflict501R → G in AAN46298. Ref.3
Sequence conflict1891N → D in CAB43231. Ref.6
Sequence conflict2941R → G in AAN46298. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O76021 [UniParc].

Last modified April 26, 2005. Version 3.
Checksum: 5E5CDB8AA8BC3709

FASTA49054,973
        10         20         30         40         50         60 
MEDSASASLS SAAATGTSTS TPAAPTARKQ LDKEQVRKAV DALLTHCKSR KNNYGLLLNE 

        70         80         90        100        110        120 
NESLFLMVVL WKIPSKELRV RLTLPHSIRS DSEDICLFTK DEPNSTPEKT EQFYRKLLNK 

       130        140        150        160        170        180 
HGIKTVSQII SLQTLKKEYK SYEAKLRLLS SFDFFLTDAR IRRLLPSLIG RHFYQRKKVP 

       190        200        210        220        230        240 
VSVNLLSKNL SREINDCIGG TVLNISKSGS CSAIRIGHVG MQIEHIIENI VAVTKGLSEK 

       250        260        270        280        290        300 
LPEKWESVKL LFVKTEKSAA LPIFSSFVSN WDEATKRSLL NKKKKEARRK RRERNFEKQK 

       310        320        330        340        350        360 
ERKKKRQQAR KTASVLSKDD VAPESGDTTV KKPESKKEQT PEHGKKKRGR GKAQVKATNE 

       370        380        390        400        410        420 
SEDEIPQLVP IGKKTPANEK VEIQKHATGK KSPAKSPNPS TPRGKKRKAL PASETPKAAE 

       430        440        450        460        470        480 
SETPGKSPEK KPKIKEEAVK EKSPSLGKKD ARQTPKKPEA KFFTTPSKSV RKASHTPKKW 

       490 
PKKPKVPQST 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Directed proteomic analysis of the human nucleolus."
Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., Mann M., Lamond A.I.
Curr. Biol. 12:1-11(2002) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS10551.1.
PIRT08693.
RefSeqNP_056474.2. NM_015659.2.
UniGeneHs.401842.

3D structure databases

ProteinModelPortalO76021.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117587. 52 interactions.
IntActO76021. 22 interactions.
MINTMINT-1139726.
STRING9606.ENSP00000379760.

Chemistry

ChEMBLCHEMBL1075139.

PTM databases

PhosphoSiteO76021.

2D gel databases

SWISS-2DPAGEO76021.

Proteomic databases

MaxQBO76021.
PaxDbO76021.
PRIDEO76021.

Protocols and materials databases

DNASU26156.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000571133; ENSP00000460871; ENSG00000171490.
GeneID26156.
KEGGhsa:26156.
UCSCuc002dbp.1. human.

Organism-specific databases

CTD26156.
GeneCardsGC16M011933.
HGNCHGNC:24534. RSL1D1.
HPAHPA043483.
neXtProtNX_O76021.
PharmGKBPA142670966.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247516.
HOVERGENHBG054786.
InParanoidO76021.
KOK14775.
OMAPSHLGRH.
OrthoDBEOG7RV9GH.
PhylomeDBO76021.
TreeFamTF354254.

Gene expression databases

ArrayExpressO76021.
BgeeO76021.
CleanExHS_RSL1D1.
GenevestigatorO76021.

Family and domain databases

Gene3D3.30.190.20. 1 hit.
InterProIPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
[Graphical view]
PfamPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
SUPFAMSSF56808. SSF56808. 1 hit.
ProtoNetSearch...

Other

GeneWikiRSL1D1.
GenomeRNAi26156.
NextBio48251.
PROO76021.

Entry information

Entry nameRL1D1_HUMAN
AccessionPrimary (citable) accession number: O76021
Secondary accession number(s): D3DUG7 expand/collapse secondary AC list , Q2M1T7, Q6PL22, Q8IWS7, Q8WUZ1, Q9HDA9, Q9Y3Z9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: July 9, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM