Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P52756 (RBM5_HUMAN)

Last modified November 25, 2008. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    RNA-binding protein 5
Alternative name(s):
    RNA-binding motif protein 5
    Tumor suppressor LUCA15
    Protein G15
    Renal carcinoma antigen NY-REN-9
Gene names
Name: RBM5
ORF Names: H37, LUCA15
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length815 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Tumor suppressor protein that reduces cell proliferation and promotes apoptosis and cell cycle arrest.

Subcellular location

NucleusPotential.

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 G-patch domain.

Contains 1 RanBP2-type zinc finger.

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords

   Biological processCell cycle
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionAnti-oncogene
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processnegative regulation of cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear mRNA splicing, via spliceosome

Inferred from Experiment. Source: Reactome

   Cellular componentnucleus

Traceable author statement. Source: ProtInc

   Molecular functionDNA binding

Traceable author statement. Source: ProtInc

RNA binding

Traceable author statement. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 815815RNA-binding protein 5
PRO_0000081759

Regions

Domain98 – 17881RRM 1
Domain231 – 31585RRM 2
Domain743 – 78947G-patch
Zinc finger181 – 21030RanBP2-type
Zinc finger647 – 67731C2H2-type; atypical

Amino acid modifications

Modified residue591Phosphoserine
Modified residue691Phosphoserine By similarity
Modified residue6211Phosphoserine
Modified residue6241Phosphoserine

Experimental info

Sequence conflict53 – 542DY → GS in AAA99715. Ref.1
Sequence conflict3541G → V in AAA99715. Ref.1
Sequence conflict4551Missing in AAB42216. Ref.5
Sequence conflict7881G → A in AAB42216. Ref.5
Sequence conflict8121T → I in AAA99715. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P52756-1 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: AA79962D13405479

FASTA81592,154
        10         20         30         40         50         60 
MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP 

        70         80         90        100        110        120 
ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES 

       130        140        150        160        170        180 
FEGPQPADVR LMKRKTGVSR GFAFVEFYHL QDATSWMEAN QKKLVIQGKH IAMHYSNPRP 

       190        200        210        220        230        240 
KFEDWLCNKC CLNNFRKRLK CFRCGADKFD SEQEVPPGTT ESVQSVDYYC DTIILRNIAP 

       250        260        270        280        290        300 
HTVVDSIMTA LSPYASLAVN NIRLIKDKQT QQNRGFAFVQ LSSAMDASQL LQILQSLHPP 

       310        320        330        340        350        360 
LKIDGKTIGV DFAKSARKDL VLSDGNRVSA FSVASTAIAA AQWSSTQSQS GEGGSVDYSY 

       370        380        390        400        410        420 
LQPGQDGYAQ YAQYSQDYQQ FYQQQAGGLE SDASSASGTA VTTTSAAVVS QSPQLYNQTS 

       430        440        450        460        470        480 
NPPGSPTEEA QPSTSTSTQA PAASPTGVVP GTKYAVPDTS TYQYDESSGY YYDPTTGLYY 

       490        500        510        520        530        540 
DPNSQYYYNS LTQQYLYWDG EKETYVPAAE SSSHQQSGLP PAKEGKEKKE KPKSKTAQQI 

       550        560        570        580        590        600 
AKDMERWAKS LNKQKENFKN SFQPVNSLRE EERRESAAAD AGFALFEKKG ALAERQQLIP 

       610        620        630        640        650        660 
ELVRNGDEEN PLKRGLVAAY SGDSDNEEEL VERLESEEEK LADWKKMACL LCRRQFPNKD 

       670        680        690        700        710        720 
ALVRHQQLSD LHKQNMDIYR RSRLSEQELE ALELREREMK YRDRAAERRE KYGIPEPPEP 

       730        740        750        760        770        780 
KRKKQFDAGT VNYEQPTKDG IDHSNIGNKM LQAMGWREGS GLGRKCQGIT APIEAQVRLK 

       790        800        810 
GAGLGAKGSA YGLSGADSYK DAVRKAMFAR FTEME 

« Hide

References

« Hide 'large scale' references
[1]"A putative tumor suppressor gene LUCA15 on 3p21.3 encodes two RNA recognizing motifs and is related to the Drosophila tumor suppresorgene Sxl."
Bader S., Latif F., Duh F.-M., Wei M., Kashuba V., Sekido Y., Lee C., Koonin E., Zabarofsky E., Klein G., Minna J.D., Lerman M.I.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"An evolutionary rearrangement of the Xp11.3-11.23 region in 3p21.3, a region frequently deleted in a variety of cancers."
Timmer T., Terpstra P., van den Berg A., Veldhuis P.M.J.F., Ter Elst A., van der Veen A.Y., Kok K., Naylor S.L., Buys C.H.C.M.
Genomics 60:238-240(1999) [PubMed: 10486216] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Identification of differentially expressed genes associated with HER-2/neu overexpression in human breast cancer cells."
Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.
Nucleic Acids Res. 27:4008-4017(1999) [PubMed: 10497265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]Oh J.J., Wong S.G., Slamon D.J.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 61.
[5]Bentley D., Maggi L.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-815.
[6]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[7]"3p21.3 tumor suppressor gene H37/Luca15/RBM5 inhibits growth of human lung cancer cells through cell cycle arrest and apoptosis."
Oh J.J., Razfar A., Delgado I., Reed R.A., Malkina A., Boctor B., Slamon D.J.
Cancer Res. 66:3419-3427(2006) [PubMed: 16585163] [Abstract]
Cited for: FUNCTION.
[8]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-624, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, MASS SPECTROMETRY.
[10]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-624, MASS SPECTROMETRY.

Cross-references

Sequence databases

U23946 mRNA. Translation: AAA99715.1.
AF091263 mRNA. Translation: AAD04159.1.
AF103802 mRNA. Translation: AAF02422.2.
U73168 Genomic DNA. Translation: AAB42216.1.
RefSeqNP_005769.1.
UniGeneHs.439480

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP52756.

PTM databases

PhosphoSiteP52756.

Genome annotation databases

EnsemblENSG00000003756. Homo sapiens. [Contig view]
GeneID10181.
KEGGhsa:10181.

Organism-specific databases

HGNCHGNC:9902. RBM5.
HPAHPA017335.
HPA018011.
MIM606884. gene.
PharmGKBPA34267.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP52756.
HOVERGENP52756.

Enzyme and pathway databases

ReactomeREACT_1675. mRNA Processing.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP52756.
GermOnlineENSG00000003756. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR000467. G_patch.
IPR000504. RRM_RNP1.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR001876. Znf_RanBP2.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
PfamPF01585. G-patch. 1 hit.
PF00076. RRM_1. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTSM00443. G_patch. 1 hit.
SM00360. RRM. 2 hits.
SM00355. ZnF_C2H2. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEPS50174. G_PATCH. 1 hit.
PS50102. RRM. 2 hits.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. False negative.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio38542.
SOURCESearch...

Entry information

Entry nameRBM5_HUMAN
AccessionPrimary (citable) accession number: P52756
Secondary accession number(s): Q93021 expand/collapse secondary AC list , Q9BU14, Q9UKY8, Q9UL24
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 21, 2001
Last modified: November 25, 2008
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents