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
Submitted name:

RNA-binding protein 34

Gene

RBM34

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. nucleotide binding Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
RNA-binding protein 34Imported
Gene namesi
Name:RBM34Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28965. RBM34.

Subcellular locationi

GO - Cellular componenti

  1. nucleolus Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiA2A2V2.

Expressioni

Gene expression databases

BgeeiA2A2V2.
ExpressionAtlasiA2A2V2. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliA2A2V2.
SMRiA2A2V2. Positions 180-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00390000011249.
HOGENOMiHOG000060230.
HOVERGENiHBG052167.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

A2A2V2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LEGMSKRKRK RSVQEGENPD DGVRGSPPED YRLGQVASSL FRGEHHSRGG
60 70 80 90 100
TGRLASLFSS LEPQIQPVYV PVPKQTIKKT KRNEEEESTS QIERPLSQEP
110 120 130 140 150
AKKVKAKKKH TNAEKKLADR ESALASADLE EEIHQKQGQK RKNSQPGVKV
160 170 180 190 200
ADRKILDDTE DTVVSQRKKI QINQEEERLK NERTVFVGNL PVTCNKKIPA
210 220 230 240 250
EGTLSKKLAA IKRKIHPDQK NINAYVVFKE ESAATQALKR NGAQIADGFR
260 270 280 290 300
IRVDLASETS SRDKRSVFVG NLPYKVEESA IEKHFLDCGS IMAVRIVRDK
310 320 330 340 350
MTGIGKGFGY VLFENTDSVH LALKLNNSEL MGRKLRVMRS VNKEKFKQQN
360 370 380 390 400
SNPRLKNVSK PKQGLNFTSK TAEGHPKSLF IGEKAVLLKT KKKGQKKSGR

PKKQRKQK
Length:408
Mass (Da):45,918
Last modified:February 20, 2007 - v1
Checksum:iEB5746244A814CBF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL133418 Genomic DNA. No translation available.
AL732292 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000447801; ENSP00000400000; ENSG00000188739.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL133418 Genomic DNA. No translation available.
AL732292 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliA2A2V2.
SMRiA2A2V2. Positions 180-341.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA2A2V2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000447801; ENSP00000400000; ENSG00000188739.

Organism-specific databases

HGNCiHGNC:28965. RBM34.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000011249.
HOGENOMiHOG000060230.
HOVERGENiHBG052167.

Miscellaneous databases

ChiTaRSiRBM34. human.
NextBioi35460743.

Gene expression databases

BgeeiA2A2V2.
ExpressionAtlasiA2A2V2. baseline and differential.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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].
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiA2A2V2_HUMAN
AccessioniPrimary (citable) accession number: A2A2V2
Entry historyi
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: April 29, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.