P98179 (RBM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative RNA-binding protein 3

Alternative name(s):
RNA-binding motif protein 3
RNPL

Gene names

Name:	RBM3
Synonyms:	RNPL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation By similarity.
Subunit structure	Interacts with RPL4. Associates with the 60S ribosomal subunits in an RNA-independent manner. Associates with ribosomes By similarity.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Cell projection › dendrite By similarity. Note: Localizes in mRNA granules in dentrites By similarity.
Induction	Up-regulated by hypoxia. Ref.6
Post-translational modification	Arg-105 is dimethylated, probably to asymmetric dimethylarginine. Ref.4 Phosphorylated By similarity.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cell projection Cytoplasm Nucleus
Ligand	RNA-binding
PTM	Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	RNA processing Traceable author statement Ref.1. Source: ProtInc positive regulation of translation Inferred from sequence or structural similarity. Source: UniProtKB production of miRNAs involved in gene silencing by miRNA Inferred from electronic annotation. Source: Compara response to cold Inferred from electronic annotation. Source: Compara translation Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB dendrite Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro ribosomal large subunit binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 157	157	Putative RNA-binding protein 3		PRO_0000081752
Regions
	Domain	6 – 84	79	RRM
	Compositional bias	88 – 149	62	Gly-rich
Amino acid modifications
	Modified residue	105	1	Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.4
	Modified residue	105	1	Omega-N-methylated arginine Ref.4
	Modified residue	132	1	Phosphoserine By similarity
	Modified residue	147	1	Phosphoserine Ref.7
	Modified residue	155	1	Phosphotyrosine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P98179 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 91C12E2A3E32CFA4	FASTA	157	17,170
	10 20 30 40 50 60 MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG FITFTNPEHA 70 80 90 100 110 120 SVAMRAMNGE SLDGRQIRVD HAGKSARGTR GGGFGAHGRG RSYSRGGGDQ GYGSGRYYDS 130 140 150 RPGGYGYGYG RSRDYNGRNQ GGYDRYSGGN YRDNYDN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RBM3, a novel human gene in Xp11.23 with a putative RNA-binding domain." Derry J.M., Kerns J.A., Francke U. Hum. Mol. Genet. 4:2307-2311(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: Placenta.
[4]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 48-75 AND 102-131, METHYLATION AT ARG-105, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[5]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[6]	"Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a HIF-1-independent mechanism." Wellmann S., Buehrer C., Moderegger E., Zelmer A., Kirschner R., Koehne P., Fujita J., Seeger K. J. Cell Sci. 117:1785-1794(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY HYPOXIA.
[7]	"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 SER-147, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U28686 mRNA. Translation: AAB17212.1. AF196969 Genomic DNA. No translation available. BC006825 mRNA. Translation: AAH06825.1.
IPI	IPI00024320.
PIR	G01859.
RefSeq	NP_006734.1. NM_006743.4.
UniGene	Hs.301404.
3D structure databases
ProteinModelPortal	P98179.
ModBase	Search...
Protein-protein interaction databases
IntAct	P98179. 2 interactions.
MINT	MINT-5002714.
STRING	9606.ENSP00000365946.
PTM databases
PhosphoSite	P98179.
Polymorphism databases
DMDM	1710620.
Proteomic databases
PaxDb	P98179.
PeptideAtlas	P98179.
PRIDE	P98179.
Protocols and materials databases
DNASU	5935.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000376755; ENSP00000365946; ENSG00000102317. ENST00000376759; ENSP00000365950; ENSG00000102317. ENST00000598825; ENSP00000470199; ENSG00000268489. ENST00000600134; ENSP00000471507; ENSG00000268489.
GeneID	5935.
KEGG	hsa:5935.
UCSC	uc004dkf.2. human.
Organism-specific databases
CTD	5935.
GeneCards	GC0XP048432.
HGNC	HGNC:9900. RBM3.
HPA	HPA003624.
MIM	300027. gene.
neXtProt	NX_P98179.
PharmGKB	PA34265.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0724.
HOGENOM	HOG000276232.
HOVERGEN	HBG107480.
InParanoid	P98179.
KO	K13186.
OMA	SDAMRAM.
OrthoDB	EOG4HHP40.
PhylomeDB	P98179.
Gene expression databases
ArrayExpress	P98179.
Bgee	P98179.
CleanEx	HS_RBM3.
Genevestigator	P98179.
GermOnline	ENSG00000102317. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RBM3. human.
GenomeRNAi	5935.
NextBio	23136.
SOURCE	Search...

Entry information

Entry name

RBM3_HUMAN

Accession

Primary (citable) accession number: P98179

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.