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P18621

- RL17_HUMAN

UniProt

P18621 - RL17_HUMAN

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Protein

60S ribosomal protein L17

Gene
RPL17
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L17
Alternative name(s):
60S ribosomal protein L23
PD-1
Gene namesi
Name:RPL17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:10307. RPL17.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
  3. nucleus Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34676.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 18418360S ribosomal protein L17UniRule annotationPRO_0000125331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP18621.
PaxDbiP18621.
PRIDEiP18621.

PTM databases

PhosphoSiteiP18621.

Expressioni

Tissue specificityi

Expressed in pancreas, lung, colon, cystic duct, gall bladder, kidney and liver. Expressed at high levels in the well differentiated pancreatic tumor cell lines HPAF, COLO 357 and Capan-1, the moderately differentiated pancreatic tumor cell lines T3M-4, AsPc-1 and BxPc-3, the poorly differentiated pancreatic tumor cell line MIA PaCa-2, and the pancreatic tumor cell lines of undefined differentiation status such as SW979. Expressed at lower levels in the poorly differentiated pancreatic tumor cell lines HCG-25 and PANC-1.1 Publication

Gene expression databases

BgeeiP18621.
CleanExiHS_RPL17.
GenevestigatoriP18621.

Organism-specific databases

HPAiHPA043724.
HPA046385.

Interactioni

Protein-protein interaction databases

BioGridi112059. 101 interactions.
IntActiP18621. 30 interactions.
MINTiMINT-1393841.
STRINGi9606.ENSP00000389465.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00P1-184[»]
ProteinModelPortaliP18621.
SMRiP18621. Positions 2-179.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0091.
HOGENOMiHOG000205045.
HOVERGENiHBG000955.
InParanoidiP18621.
KOiK02880.
OMAiYSREPTN.
OrthoDBiEOG70GMHF.
PhylomeDBiP18621.
TreeFamiTF300042.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
HAMAPiMF_01331_A. Ribosomal_L22_A.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005721. Ribosomal_L22/L17_euk/arc.
[Graphical view]
PANTHERiPTHR11593. PTHR11593. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01038. L22_arch. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P18621-1) [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

MVRYSLDPEN PTKSCKSRGS NLRVHFKNTR ETAQAIKGMH IRKATKYLKD    50
VTLQKQCVPF RRYNGGVGRC AQAKQWGWTQ GRWPKKSAEF LLHMLKNAES 100
NAELKGLDVD SLVIEHIQVN KAPKMRRRTY RAHGRINPYM SSPCHIEMIL 150
TEKEQIVPKP EEEVAQKKKI SQKKLKKQKL MARE 184
Length:184
Mass (Da):21,397
Last modified:January 23, 2007 - v3
Checksum:i2FC595DD74ED1CA0
GO
Isoform 2 (identifier: P18621-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Show »
Length:146
Mass (Da):17,094
Checksum:iF29AFEFE03D5CA59
GO
Isoform 3 (identifier: P18621-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-184: ISQKKLKKQKLMARE → LRSSSLGKWCAFLVSSFQFCSGSTKNSWSHIYTLWFPPSLVVYGLRKQYKNPMIQTKAK

Show »
Length:228
Mass (Da):26,373
Checksum:iDF45454F21504C77
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform 2. VSP_045445Add
BLAST
Alternative sequencei170 – 18415ISQKK…LMARE → LRSSSLGKWCAFLVSSFQFC SGSTKNSWSHIYTLWFPPSL VVYGLRKQYKNPMIQTKAK in isoform 3. VSP_046965Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331H → R in AAH66324. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53777 mRNA. Translation: CAA37793.1.
AB061824 Genomic DNA. Translation: BAB79462.1.
AC100778 Genomic DNA. No translation available.
AK304659 mRNA. Translation: BAG65434.1.
AK311828 mRNA. Translation: BAG34770.1.
BX393840 mRNA. No translation available.
CH471096 Genomic DNA. Translation: EAW62940.1.
BC000502 mRNA. Translation: AAH00502.1.
BC017831 mRNA. Translation: AAH17831.1.
BC066323 mRNA. Translation: AAH66323.1.
BC066324 mRNA. Translation: AAH66324.1.
BC106031 mRNA. Translation: AAI06032.1.
AB007174 Genomic DNA. Translation: BAA25834.1.
CCDSiCCDS45865.1. [P18621-1]
CCDS56070.1. [P18621-2]
PIRiA61192.
S11218. R5HU22.
RefSeqiNP_000976.1. NM_000985.4. [P18621-1]
NP_001030178.1. NM_001035006.2. [P18621-1]
NP_001186269.1. NM_001199340.1. [P18621-1]
NP_001186270.1. NM_001199341.1. [P18621-1]
NP_001186271.1. NM_001199342.1. [P18621-1]
NP_001186272.1. NM_001199343.1. [P18621-1]
NP_001186273.1. NM_001199344.1. [P18621-1]
NP_001186274.1. NM_001199345.1. [P18621-2]
NP_001186284.1. NM_001199355.1. [P18621-3]
UniGeneiHs.293653.
Hs.374588.
Hs.485081.
Hs.603040.

Genome annotation databases

EnsembliENST00000418495; ENSP00000397798; ENSG00000265681. [P18621-1]
ENST00000579248; ENSP00000462023; ENSG00000265681. [P18621-1]
ENST00000579408; ENSP00000463842; ENSG00000265681. [P18621-1]
ENST00000580261; ENSP00000462385; ENSG00000265681. [P18621-1]
ENST00000581373; ENSP00000462944; ENSG00000265681. [P18621-2]
GeneIDi100526842.
6139.
KEGGihsa:100526842.
hsa:6139.
UCSCiuc002ldp.3. human. [P18621-1]

Polymorphism databases

DMDMi132799.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53777 mRNA. Translation: CAA37793.1 .
AB061824 Genomic DNA. Translation: BAB79462.1 .
AC100778 Genomic DNA. No translation available.
AK304659 mRNA. Translation: BAG65434.1 .
AK311828 mRNA. Translation: BAG34770.1 .
BX393840 mRNA. No translation available.
CH471096 Genomic DNA. Translation: EAW62940.1 .
BC000502 mRNA. Translation: AAH00502.1 .
BC017831 mRNA. Translation: AAH17831.1 .
BC066323 mRNA. Translation: AAH66323.1 .
BC066324 mRNA. Translation: AAH66324.1 .
BC106031 mRNA. Translation: AAI06032.1 .
AB007174 Genomic DNA. Translation: BAA25834.1 .
CCDSi CCDS45865.1. [P18621-1 ]
CCDS56070.1. [P18621-2 ]
PIRi A61192.
S11218. R5HU22.
RefSeqi NP_000976.1. NM_000985.4. [P18621-1 ]
NP_001030178.1. NM_001035006.2. [P18621-1 ]
NP_001186269.1. NM_001199340.1. [P18621-1 ]
NP_001186270.1. NM_001199341.1. [P18621-1 ]
NP_001186271.1. NM_001199342.1. [P18621-1 ]
NP_001186272.1. NM_001199343.1. [P18621-1 ]
NP_001186273.1. NM_001199344.1. [P18621-1 ]
NP_001186274.1. NM_001199345.1. [P18621-2 ]
NP_001186284.1. NM_001199355.1. [P18621-3 ]
UniGenei Hs.293653.
Hs.374588.
Hs.485081.
Hs.603040.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3B electron microscopy 5.00 P 1-184 [» ]
ProteinModelPortali P18621.
SMRi P18621. Positions 2-179.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112059. 101 interactions.
IntActi P18621. 30 interactions.
MINTi MINT-1393841.
STRINGi 9606.ENSP00000389465.

PTM databases

PhosphoSitei P18621.

Polymorphism databases

DMDMi 132799.

Proteomic databases

MaxQBi P18621.
PaxDbi P18621.
PRIDEi P18621.

Protocols and materials databases

DNASUi 6139.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000418495 ; ENSP00000397798 ; ENSG00000265681 . [P18621-1 ]
ENST00000579248 ; ENSP00000462023 ; ENSG00000265681 . [P18621-1 ]
ENST00000579408 ; ENSP00000463842 ; ENSG00000265681 . [P18621-1 ]
ENST00000580261 ; ENSP00000462385 ; ENSG00000265681 . [P18621-1 ]
ENST00000581373 ; ENSP00000462944 ; ENSG00000265681 . [P18621-2 ]
GeneIDi 100526842.
6139.
KEGGi hsa:100526842.
hsa:6139.
UCSCi uc002ldp.3. human. [P18621-1 ]

Organism-specific databases

CTDi 100526842.
6139.
GeneCardsi GC18M047009.
GC18M047014.
HGNCi HGNC:10307. RPL17.
HPAi HPA043724.
HPA046385.
MIMi 603661. gene.
neXtProti NX_P18621.
PharmGKBi PA34676.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0091.
HOGENOMi HOG000205045.
HOVERGENi HBG000955.
InParanoidi P18621.
KOi K02880.
OMAi YSREPTN.
OrthoDBi EOG70GMHF.
PhylomeDBi P18621.
TreeFami TF300042.

Enzyme and pathway databases

Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

GeneWikii RPL17.
NextBioi 23849.
PROi P18621.
SOURCEi Search...

Gene expression databases

Bgeei P18621.
CleanExi HS_RPL17.
Genevestigatori P18621.

Family and domain databases

Gene3Di 3.90.470.10. 1 hit.
HAMAPi MF_01331_A. Ribosomal_L22_A.
InterProi IPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005721. Ribosomal_L22/L17_euk/arc.
[Graphical view ]
PANTHERi PTHR11593. PTHR11593. 1 hit.
Pfami PF00237. Ribosomal_L22. 1 hit.
[Graphical view ]
SUPFAMi SSF54843. SSF54843. 1 hit.
TIGRFAMsi TIGR01038. L22_arch. 1 hit.
PROSITEi PS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human gene related to the ribosomal protein L23 gene of Halobacterium marismortui."
    Mager D.L., Freeman J.D.
    Nucleic Acids Res. 18:5301-5301(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Blood.
  2. "Isolation and characterization of a complementary DNA (PD-1) differentially expressed by human pancreatic ductal cell tumors."
    Batra S.K., Metzgar R.S., Hollingsworth M.A.
    Cell Growth Differ. 2:385-390(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Pancreatic tumor.
  3. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORMS 1 AND 2).
    Tissue: Uterus.
  5. Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Neuroblastoma.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Hypothalamus, Lung, Prostate and Testis.
  9. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
    Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
    J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, IDENTIFICATION BY MASS SPECTROMETRY.
  10. Bienvenut W.V., Calvo F., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 31-42; 47-55; 75-82; 86-96 AND 106-124, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  11. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 170-183.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL17_HUMAN
AccessioniPrimary (citable) accession number: P18621
Secondary accession number(s): B2R4H3
, B4E3C2, B5ME31, J3QL51, Q3KQW2, Q6NZ54, Q7M4M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 152 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi