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P38159

- RBMX_HUMAN

UniProt

P38159 - RBMX_HUMAN

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Protein
RNA-binding motif protein, X chromosome
Gene
RBMX, HNRPG, RBMXP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Plays also a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment.7 Publications

GO - Molecular functioni

  1. RNA binding Source: UniProtKB
  2. chromatin binding Source: UniProtKB
  3. core promoter binding Source: UniProtKB
  4. mRNA binding Source: UniProtKB
  5. nucleotide binding Source: InterPro
  6. poly(A) RNA binding Source: UniProtKB
  7. protein binding Source: UniProtKB
  8. single-stranded RNA binding Source: Ensembl

GO - Biological processi

  1. RNA splicing Source: Reactome
  2. cellular response to interleukin-1 Source: UniProtKB
  3. gene expression Source: Reactome
  4. mRNA splice site selection Source: Ensembl
  5. mRNA splicing, via spliceosome Source: UniProtKB
  6. membrane protein ectodomain proteolysis Source: UniProtKB
  7. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  8. osteoblast differentiation Source: UniProt
  9. positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
  10. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  11. protein homooligomerization Source: UniProtKB
  12. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  13. transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding motif protein, X chromosome
Alternative name(s):
Glycoprotein p43
Heterogeneous nuclear ribonucleoprotein G
Short name:
hnRNP G
Cleaved into the following chain:
Gene namesi
Name:RBMX
Synonyms:HNRPG, RBMXP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:9910. RBMX.

Subcellular locationi

Nucleus
Note: Component of ribonucleosomes. Localizes in numerous small granules in the nucleus.2 Publications

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProt
  5. nuclear euchromatin Source: UniProtKB
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProtKB
  8. ribonucleoprotein complex Source: UniProtKB
  9. supraspliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221K → A: Promotes cell proliferation. Inhibits transcriptional up-regulation of the TXNIP promoter. 2 Publications

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA34277.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391RNA-binding motif protein, X chromosome
PRO_0000081854Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 391390RNA-binding motif protein, X chromosome, N-terminally processed
PRO_0000304582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein G; alternate1 Publication
Modified residuei2 – 21N-acetylvaline; in Heterogeneous nuclear ribonucleoprotein G, N-terminally processed1 Publication
Modified residuei30 – 301N6-acetyllysine1 Publication
Modified residuei88 – 881Phosphoserine5 Publications
Modified residuei329 – 3291Phosphoserine1 Publication
Modified residuei332 – 3321Phosphoserine2 Publications
Modified residuei352 – 3521Phosphoserine2 Publications

Post-translational modificationi

O-glycosylated.1 Publication
Arg-185 is dimethylated, probably to asymmetric dimethylarginine.
Cleavage of initiator Met is partial. If Met-1 is not removed, it is acetylated. If it is removed, Val-2 is acetylated.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP38159.
PaxDbiP38159.
PRIDEiP38159.

2D gel databases

SWISS-2DPAGEP38159.

PTM databases

PhosphoSiteiP38159.

Expressioni

Tissue specificityi

Expressed strongly in oral keratinocytes, but only weakly detected in oral squamous cell carcinomas (at protein level).1 Publication

Gene expression databases

ArrayExpressiP38159.
BgeeiP38159.
CleanExiHS_RBMX.
GenevestigatoriP38159.

Organism-specific databases

HPAiHPA057707.

Interactioni

Subunit structurei

Homomultimer. Interacts with SAFB/SAFB1 By similarity. Found in the supraspliceosome complex. Identified in the spliceosome C complex. Interacts with KHDRBS3. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with CLK2, KHDRBS2, SAFB, TRA2B and YTHDC1. Interacts with ERAP1; the interaction is RNA-independent.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HNRNPKP619783EBI-743526,EBI-304185
KHDRBS2Q5VWX12EBI-743526,EBI-742808
Srek1Q9JKL73EBI-743526,EBI-6452221From a different organism.

Protein-protein interaction databases

BioGridi118134. 93 interactions.
DIPiDIP-34447N.
IntActiP38159. 46 interactions.
MINTiMINT-5000999.
STRINGi9606.ENSP00000359645.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135
Helixi21 – 288
Turni29 – 313
Beta strandi34 – 396
Turni43 – 453
Beta strandi50 – 589
Helixi61 – 666
Beta strandi67 – 748
Beta strandi80 – 834

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MB0NMR-B1-95[»]
2MKSNMR-A1-90[»]
ProteinModelPortaliP38159.
SMRiP38159. Positions 1-90.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 8679RRM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 23651Necessary for the association to nascent RNAPII transcripts and nuclear localization
Add
BLAST
Regioni333 – 39159Necessary for RNA-binding
Add
BLAST

Domaini

The RRM domain is necessary for RNA-binding, but not for splice site selection, indicating that its splicing activity does not require direct binding to RNA By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000070250.
HOVERGENiHBG063314.
InParanoidiP38159.
KOiK12885.
OMAiGMARSRY.
OrthoDBiEOG780RPD.
PhylomeDBiP38159.
TreeFamiTF331833.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 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: P38159-1) [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

MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG    50
FAFVTFESPA DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP 100
RSRGPPRGLR GGRGGSGGTR GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK 150
RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR APVSRGRDSY GGPPRREPLP 200
SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD YTYRDYGHSS 250
SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP 300
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQERGLP 350
PSMERGYPPP RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y 391
Length:391
Mass (Da):42,332
Last modified:September 19, 2002 - v3
Checksum:i904FEB9BFC573546
GO
Isoform 2 (identifier: P38159-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-57: Missing.

Show »
Length:378
Mass (Da):40,846
Checksum:i032DD488FA08CE19
GO
Isoform 3 (identifier: P38159-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-196: SLDGKAIKVE...RDSYGGPPRR → LLYHVEEIVM...YGRGVLIDSQ
     197-391: Missing.

Note: No experimental confirmation available.

Show »
Length:196
Mass (Da):22,172
Checksum:i7FB2ABEE20A3D582
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei45 – 5713Missing in isoform 2.
VSP_042203Add
BLAST
Alternative sequencei73 – 196124SLDGK…GPPRR → LLYHVEEIVMEVHLEGNRCP LVEMFICPQEMMGILLKTAI QAEITQVLVILEIMHHHHEI ILTVIMVIPVHVMTIHQEDI AIEMDMVVIVTIQIIQVEVP TEIHMRVMVGDFAHYGRGVL IDSQ in isoform 3.
VSP_043650Add
BLAST
Alternative sequencei197 – 391195Missing in isoform 3.
VSP_043651Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591G → E in CAA80599. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z23064 mRNA. Translation: CAA80599.1.
AF266723
, AF266720, AF266721, AF266722 Genomic DNA. Translation: AAK58567.1.
AY464692 mRNA. Translation: AAR28036.1.
AK096015 mRNA. Translation: BAC04674.1.
AK304868 mRNA. Translation: BAG65606.1.
AL683813 Genomic DNA. Translation: CAI39448.1.
CH471150 Genomic DNA. Translation: EAW88453.1.
CH471150 Genomic DNA. Translation: EAW88454.1.
CH471150 Genomic DNA. Translation: EAW88455.1.
CH471150 Genomic DNA. Translation: EAW88457.1.
BC006550 mRNA. Translation: AAH06550.1.
BC007435 mRNA. Translation: AAH07435.1.
CCDSiCCDS14661.1. [P38159-1]
CCDS55510.1. [P38159-3]
RefSeqiNP_001158275.1. NM_001164803.1. [P38159-3]
NP_002130.2. NM_002139.3. [P38159-1]
UniGeneiHs.380118.
Hs.710162.

Genome annotation databases

EnsembliENST00000320676; ENSP00000359645; ENSG00000147274. [P38159-1]
ENST00000431446; ENSP00000411989; ENSG00000147274. [P38159-3]
GeneIDi27316.
KEGGihsa:27316.
UCSCiuc004fae.2. human. [P38159-1]
uc011mwf.1. human. [P38159-3]

Polymorphism databases

DMDMi23503093.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z23064 mRNA. Translation: CAA80599.1 .
AF266723
, AF266720 , AF266721 , AF266722 Genomic DNA. Translation: AAK58567.1 .
AY464692 mRNA. Translation: AAR28036.1 .
AK096015 mRNA. Translation: BAC04674.1 .
AK304868 mRNA. Translation: BAG65606.1 .
AL683813 Genomic DNA. Translation: CAI39448.1 .
CH471150 Genomic DNA. Translation: EAW88453.1 .
CH471150 Genomic DNA. Translation: EAW88454.1 .
CH471150 Genomic DNA. Translation: EAW88455.1 .
CH471150 Genomic DNA. Translation: EAW88457.1 .
BC006550 mRNA. Translation: AAH06550.1 .
BC007435 mRNA. Translation: AAH07435.1 .
CCDSi CCDS14661.1. [P38159-1 ]
CCDS55510.1. [P38159-3 ]
RefSeqi NP_001158275.1. NM_001164803.1. [P38159-3 ]
NP_002130.2. NM_002139.3. [P38159-1 ]
UniGenei Hs.380118.
Hs.710162.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MB0 NMR - B 1-95 [» ]
2MKS NMR - A 1-90 [» ]
ProteinModelPortali P38159.
SMRi P38159. Positions 1-90.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118134. 93 interactions.
DIPi DIP-34447N.
IntActi P38159. 46 interactions.
MINTi MINT-5000999.
STRINGi 9606.ENSP00000359645.

PTM databases

PhosphoSitei P38159.

Polymorphism databases

DMDMi 23503093.

2D gel databases

SWISS-2DPAGE P38159.

Proteomic databases

MaxQBi P38159.
PaxDbi P38159.
PRIDEi P38159.

Protocols and materials databases

DNASUi 27316.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320676 ; ENSP00000359645 ; ENSG00000147274 . [P38159-1 ]
ENST00000431446 ; ENSP00000411989 ; ENSG00000147274 . [P38159-3 ]
GeneIDi 27316.
KEGGi hsa:27316.
UCSCi uc004fae.2. human. [P38159-1 ]
uc011mwf.1. human. [P38159-3 ]

Organism-specific databases

CTDi 27316.
GeneCardsi GC0XM135951.
HGNCi HGNC:9910. RBMX.
HPAi HPA057707.
MIMi 300199. gene.
neXtProti NX_P38159.
PharmGKBi PA34277.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
HOGENOMi HOG000070250.
HOVERGENi HBG063314.
InParanoidi P38159.
KOi K12885.
OMAi GMARSRY.
OrthoDBi EOG780RPD.
PhylomeDBi P38159.
TreeFami TF331833.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi RBMX. human.
GeneWikii RBMX.
GenomeRNAii 27316.
NextBioi 50322.
PROi P38159.
SOURCEi Search...

Gene expression databases

ArrayExpressi P38159.
Bgeei P38159.
CleanExi HS_RBMX.
Genevestigatori P38159.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR012604. RBM1CTR.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF08081. RBM1CTR. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION.
    Tissue: Mammary gland.
  2. Venables J.P., Larsen C.-J.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  4. Lin T.-Y., Chiou S.-H.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "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 2 AND 3).
    Tissue: Kidney and Uterus.
  6. "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].
  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: Muscle.
  9. Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-30; 34-41; 50-63; 81-93; 126-144; 188-195; 204-210; 283-292; 299-317 AND 332-339, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Osteosarcoma.
  10. "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis."
    Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J., Cooke H.J., Artzt K., Eperon I.C.
    Hum. Mol. Genet. 8:959-969(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KHDRBS3.
    Tissue: Testis.
  11. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  12. "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta1."
    Hofmann Y., Wirth B.
    Hum. Mol. Genet. 11:2037-2049(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRA2B, RNA-BINDING.
  13. "HnRNP G and Tra2beta: opposite effects on splicing matched by antagonism in RNA binding."
    Nasim M.T., Chernova T.K., Chowdhury H.M., Yue B.G., Eperon I.C.
    Hum. Mol. Genet. 12:1337-1348(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  14. "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 SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive effect against oral squamous cell carcinoma cells."
    Shin K.H., Kang M.K., Kim R.H., Christensen R., Park N.H.
    Clin. Cancer Res. 12:3222-3228(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-22, TISSUE SPECIFICITY.
  16. "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
    Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
    Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; NCOA5 AND PPP1CA.
  17. "An association between RBMX, a heterogeneous nuclear ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release."
    Adamik B., Islam A., Rouhani F.N., Hawari F.I., Zhang J., Levine S.J.
    Biochem. Biophys. Res. Commun. 371:505-509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERAP1.
  18. "hnRNP G elicits tumor-suppressive activity in part by upregulating the expression of Txnip."
    Shin K.H., Kim R.H., Kim R.H., Kang M.K., Park N.H.
    Biochem. Biophys. Res. Commun. 372:880-885(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHROMATIN ASSOCIATION, MUTAGENESIS OF LYS-22.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-329 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA."
    Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R., Stamm S.
    J. Biol. Chem. 284:14303-14315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SUPRASPLICEOSOME COMPLEX, INTERACTION WITH CLK2; KHDRBS2; SAFB; TRA2B AND YTHDC1, SUBCELLULAR LOCATION.
  21. "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-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. "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-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Novel domains in the hnRNP G/RBMX protein with distinct roles in RNA binding and targeting nascent transcripts."
    Kanhoush R., Beenders B., Perrin C., Moreau J., Bellini M., Penrad-Mobayed M.
    Nucleus 1:109-122(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
  24. "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-88 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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 SER-88; SER-332 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "NMR structure of the first RRM domain of the protein RBM39 from Homo sapiens."
    Joint center for structural genomics (JCSG)
    Submitted (MAR-2014) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-90.

Entry informationi

Entry nameiRBMX_HUMAN
AccessioniPrimary (citable) accession number: P38159
Secondary accession number(s): B4E3U4
, D3DWH0, E9PG86, Q5JQ67, Q8N8Y7, Q969R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: September 19, 2002
Last modified: September 3, 2014
This is version 162 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 X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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