Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribosomal L1 domain-containing protein 1

Gene

RSL1D1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage.2 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • osteoblast differentiation Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of cellular senescence Source: UniProtKB
  • 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 protein1 Publication
Protein PBK1
Gene namesi
Name:RSL1D1
Synonyms:CATX11, CSIG1 Publication, PBK1
ORF Names:L12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:24534. RSL1D1.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670966.

Polymorphism and mutation databases

BioMutaiRSL1D1.

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

Expressed at high intensities in the heart, skeletal muscle, and placenta.2 Publications

Inductioni

Down-regulated during cellular senescence.1 Publication

Gene expression databases

BgeeiO76021.
CleanExiHS_RSL1D1.
ExpressionAtlasiO76021. baseline and differential.
GenevisibleiO76021. HS.

Organism-specific databases

HPAiHPA043483.

Interactioni

Subunit structurei

Interacts with ING1 (isoform 2).1 Publication

Protein-protein interaction databases

BioGridi117587. 70 interactions.
IntActiO76021. 25 interactions.
MINTiMINT-1139726.
STRINGi9606.ENSP00000460871.

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.
GeneTreeiENSGT00440000038603.
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. AlignAdd to basket

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

        10         20         30         40         50
MEDSASASLS SAAATGTSTS TPAAPTARKQ LDKEQVRKAV DALLTHCKSR
60 70 80 90 100
KNNYGLLLNE NESLFLMVVL WKIPSKELRV RLTLPHSIRS DSEDICLFTK
110 120 130 140 150
DEPNSTPEKT EQFYRKLLNK HGIKTVSQII SLQTLKKEYK SYEAKLRLLS
160 170 180 190 200
SFDFFLTDAR IRRLLPSLIG RHFYQRKKVP VSVNLLSKNL SREINDCIGG
210 220 230 240 250
TVLNISKSGS CSAIRIGHVG MQIEHIIENI VAVTKGLSEK LPEKWESVKL
260 270 280 290 300
LFVKTEKSAA LPIFSSFVSN WDEATKRSLL NKKKKEARRK RRERNFEKQK
310 320 330 340 350
ERKKKRQQAR KTASVLSKDD VAPESGDTTV KKPESKKEQT PEHGKKKRGR
360 370 380 390 400
GKAQVKATNE SEDEIPQLVP IGKKTPANEK VEIQKHATGK KSPAKSPNPS
410 420 430 440 450
TPRGKKRKAL PASETPKAAE SETPGKSPEK KPKIKEEAVK EKSPSLGKKD
460 470 480 490
ARQTPKKPEA KFFTTPSKSV RKASHTPKKW PKKPKVPQST
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. Curated
The sequence AAH19069.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA07491.1 differs from that shown. Reason: Frameshift at position 486. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501R → G in AAN46298 (Ref. 3) Curated
Sequence conflicti189 – 1891N → D in CAB43231 (PubMed:17974005).Curated
Sequence conflicti294 – 2941R → G in AAN46298 (Ref. 3) Curated

Alternative sequence

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [O76021-1]
PIRiT08693.
RefSeqiNP_056474.2. NM_015659.2. [O76021-1]
UniGeneiHs.401842.

Genome annotation databases

EnsembliENST00000571133; ENSP00000460871; ENSG00000171490.
GeneIDi26156.
KEGGihsa:26156.
UCSCiuc002dbp.1. human. [O76021-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [O76021-1]
PIRiT08693.
RefSeqiNP_056474.2. NM_015659.2. [O76021-1]
UniGeneiHs.401842.

3D structure databases

ProteinModelPortaliO76021.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117587. 70 interactions.
IntActiO76021. 25 interactions.
MINTiMINT-1139726.
STRINGi9606.ENSP00000460871.

Chemistry

ChEMBLiCHEMBL1075139.

PTM databases

PhosphoSiteiO76021.

Polymorphism and mutation databases

BioMutaiRSL1D1.

2D gel databases

SWISS-2DPAGEO76021.

Proteomic databases

MaxQBiO76021.
PaxDbiO76021.
PRIDEiO76021.

Protocols and materials databases

DNASUi26156.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000571133; ENSP00000460871; ENSG00000171490.
GeneIDi26156.
KEGGihsa:26156.
UCSCiuc002dbp.1. human. [O76021-1]

Organism-specific databases

CTDi26156.
GeneCardsiGC16M011934.
HGNCiHGNC:24534. RSL1D1.
HPAiHPA043483.
MIMi615874. gene.
neXtProtiNX_O76021.
PharmGKBiPA142670966.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG247516.
GeneTreeiENSGT00440000038603.
HOVERGENiHBG054786.
InParanoidiO76021.
KOiK14775.
OMAiPSHLGRH.
OrthoDBiEOG7RV9GH.
PhylomeDBiO76021.
TreeFamiTF354254.

Miscellaneous databases

ChiTaRSiRSL1D1. human.
GeneWikiiRSL1D1.
GenomeRNAii26156.
NextBioi35472443.
PROiO76021.
SOURCEiSearch...

Gene expression databases

BgeeiO76021.
CleanExiHS_RSL1D1.
ExpressionAtlasiO76021. baseline and differential.
GenevisibleiO76021. HS.

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.
ProtoNetiSearch...

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] (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. "CSIG inhibits PTEN translation in replicative senescence."
    Ma L., Chang N., Guo S., Li Q., Zhang Z., Wang W., Tong T.
    Mol. Cell. Biol. 28:6290-6301(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
  18. 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.
  19. "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].
  20. "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.
  21. "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].
  22. "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.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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].
  25. "Nucleolar protein CSIG is required for p33ING1 function in UV-induced apoptosis."
    Li N., Zhao G., Chen T., Xue L., Ma L., Niu J., Tong T.
    Cell Death Dis. 3:E283-E283(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ING1.
  26. "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].
  27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: July 22, 2015
This is version 135 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.