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P49756 (RBM25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein 25
Alternative name(s):
Arg/Glu/Asp-rich protein of 120 kDa
Short name=RED120
Protein S164
RNA-binding motif protein 25
RNA-binding region-containing protein 7
Gene names
Name:RBM25
Synonyms:RNPC7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. Involved in apoptotic cell death through the regulation of the apoptotic factor BCL2L1 isoform expression Modulates the ratio of proapoptotic BCL2L1 isoform Sto antiapoptotic BCL2L1 isoform LmRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L Promotes BCL2L1 isoform S5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the BCL2L1 pre-mRNA. Also involved in the generation of an abnormal and truncated splice form of SCN5A in heart failure. Ref.14 Ref.20

Subunit structure

Interacts with LUC7L3 and SRRM1. Specifically associates with functional splicing complexes, including Sm proteins and U1, U2, U4, U5 and U6 snRNAs. Associates with exon junction complex (EJC) proteins, including APEX1, BAT1, NCBP1, RBM8A and RNPS1. Interaction with NCBP1 is RNA-dependent. Ref.7 Ref.14

Subcellular location

Nucleus speckle. Cytoplasm. Note: Colocalizes predominantly, with SFRS2 and LUC7L3 splicing factors, in nuclear speckles. Cytoplasmic localization is faint. Ref.7 Ref.14

Domain

The PWI domain binds nucleic acids with significant help from its N-terminal flanking basic region. It has an equal preference for binding to single- or double-stranded species, and it contributes to RBM25 role in modulation of alternative splicing, maybe by mediating RNA-dependent association with LUC7L3. Ref.22

Post-translational modification

Sumoylated. Ref.9

Sequence similarities

Contains 1 PWI domain.

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence AAH62440.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH62440.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH83496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAG52915.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49756-1)

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.
Isoform 2 (identifier: P49756-2)

The sequence of this isoform differs from the canonical sequence as follows:
     290-294: KLEEE → RSYGD
     295-843: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P49756-3)

The sequence of this isoform differs from the canonical sequence as follows:
     290-300: KLEEEKGKKEK → VVFLSFHLIPI
     301-843: Missing.
Isoform 4 (identifier: P49756-4)

The sequence of this isoform differs from the canonical sequence as follows:
     109-164: KCGLVLSWKR...KKLLVKVDAK → PSDSVSTRSQ...QRRKLLMGLG
     165-843: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 843843RNA-binding protein 25
PRO_0000081784

Regions

Domain87 – 16478RRM
Domain750 – 84394PWI
Region285 – 644360Necessary for nuclear speckle localization
Compositional bias292 – 608317Glu-rich
Compositional bias309 – 549241Arg-rich

Amino acid modifications

Modified residue1351N6-acetyllysine By similarity
Modified residue5831Phosphoserine Ref.18 Ref.21
Modified residue6771Phosphoserine Ref.6 Ref.11 Ref.17 Ref.18 Ref.21
Modified residue6831Phosphoserine Ref.11 Ref.18 Ref.21
Modified residue7031Phosphoserine Ref.15 Ref.18 Ref.21
Cross-link477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12

Natural variations

Alternative sequence109 – 16456KCGLV…KVDAK → PSDSVSTRSQNLPSVHSDYY MTCKLERKSYSLKLMQRQRH SWMNGKQRRKLLMGLG in isoform 4.
VSP_039881
Alternative sequence165 – 843679Missing in isoform 4.
VSP_039882
Alternative sequence290 – 30011KLEEEKGKKEK → VVFLSFHLIPI in isoform 3.
VSP_036791
Alternative sequence290 – 2945KLEEE → RSYGD in isoform 2.
VSP_036792
Alternative sequence295 – 843549Missing in isoform 2.
VSP_036793
Alternative sequence301 – 843543Missing in isoform 3.
VSP_036794

Experimental info

Mutagenesis734 – 7363KRK → AAA: Reduced DNA/RNA binding. Ref.22
Mutagenesis777 – 7782KK → AA: Reduced DNA/RNA binding.
Mutagenesis8251K → A: Reduced DNA/RNA binding; when associated with A-828. Ref.22
Mutagenesis8281R → A: Reduced DNA/RNA binding; when associated with A-825. Ref.22
Sequence conflict4281D → K in BAB15362. Ref.1
Sequence conflict571 – 5744RRRQ → EAQE in AAC41999. Ref.8

Secondary structure

................. 843
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 14, 2009. Version 3.
Checksum: 80534590147A342A

FASTA843100,185
        10         20         30         40         50         60 
MSFPPHLNRP PMGIPALPPG IPPPQFPGFP PPVPPGTPMI PVPMSIMAPA PTVLVPTVSM 

        70         80         90        100        110        120 
VGKHLGARKD HPGLKAKEND ENCGPTTTVF VGNISEKASD MLIRQLLAKC GLVLSWKRVQ 

       130        140        150        160        170        180 
GASGKLQAFG FCEYKEPEST LRALRLLHDL QIGEKKLLVK VDAKTKAQLD EWKAKKKASN 

       190        200        210        220        230        240 
GNARPETVTN DDEEALDEET KRRDQMIKGA IEVLIREYSS ELNAPSQESD SHPRKKKKEK 

       250        260        270        280        290        300 
KEDIFRRFPV APLIPYPLIT KEDINAIEME EDKRDLISRE ISKFRDTHKK LEEEKGKKEK 

       310        320        330        340        350        360 
ERQEIEKERR ERERERERER ERRERERERE REREREKEKE RERERERDRD RDRTKERDRD 

       370        380        390        400        410        420 
RDRERDRDRD RERSSDRNKD RSRSREKSRD RERERERERE RERERERERE RERERERERE 

       430        440        450        460        470        480 
REREREKDKK RDREEDEEDA YERRKLERKL REKEAAYQER LKNWEIRERK KTREYEKEAE 

       490        500        510        520        530        540 
REEERRREMA KEAKRLKEFL EDYDDDRDDP KYYRGSALQK RLRDREKEME ADERDRKREK 

       550        560        570        580        590        600 
EELEEIRQRL LAEGHPDPDA ELQRMEQEAE RRRQPQIKQE PESEEEEEEK QEKEEKREEP 

       610        620        630        640        650        660 
MEEEEEPEQK PCLKPTLRPI SSAPSVSSAS GNATPNTPGD ESPCGIIIPH ENSPDQQQPE 

       670        680        690        700        710        720 
EHRPKIGLSL KLGASNSPGQ PNSVKRKKLP VDSVFNKFED EDSDDVPRKR KLVPLDYGED 

       730        740        750        760        770        780 
DKNATKGTVN TEEKRKHIKS LIEKIPTAKP ELFAYPLDWS IVDSILMERR IRPWINKKII 

       790        800        810        820        830        840 
EYIGEEEATL VDFVCSKVMA HSSPQSILDD VAMVLDEEAE VFIVKMWRLL IYETEAKKIG 


LVK 

« Hide

Isoform 2 [UniParc].

Checksum: 184FE9019A3E3D95
Show »

FASTA29432,822
Isoform 3 [UniParc].

Checksum: 81D1498626DDD750
Show »

FASTA30033,510
Isoform 4 [UniParc].

Checksum: 5D5562C8AAD78BAE
Show »

FASTA16417,953

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-430 (ISOFORM 1).
Tissue: Amygdala and Kidney epithelium.
[2]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1; 2 AND 3).
Tissue: Cerebellum, Fetal brain, Prostate and Uterus.
[5]"Complete sequence of the gene for presenilin 1."
Rowen L., Madan A., Qin S., Abbasi N., Dors M., Ratcliffe A., Madan A., Dickhoff R., Shaffer T., James R., Lasky S., Hood L.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-843.
[6]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 146-155; 209-216 AND 672-685, PHOSPHORYLATION AT SER-677, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[7]"Identification and characterization of RED120: a conserved PWI domain protein with links to splicing and 3'-end formation."
Fortes P., Longman D., McCracken S., Ip J.Y., Poot R., Mattaj I.W., Caceres J.F., Blencowe B.J.
FEBS Lett. 581:3087-3097(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 146-155 AND 247-261, SUBCELLULAR LOCATION, INTERACTION WITH APEX1; BAT1; NCBP1; RBM8; RNPS1 AND SRRM1.
[8]"Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease."
Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L. expand/collapse author list , Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., Rommens J.M., St George-Hyslop P.H.
Nature 375:754-760(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 571-843.
Tissue: Brain.
[9]"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
Gocke C.B., Yu H., Kang J.
J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[10]"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].
Tissue: Cervix carcinoma.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-683, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-477.
Tissue: Mammary cancer.
[13]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[14]"Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site selection."
Zhou A., Ou A.C., Cho A., Benz E.J. Jr., Huang S.C.
Mol. Cell. Biol. 28:5924-5936(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LUC7L3, SUBCELLULAR LOCATION.
[15]"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-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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-677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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-583; SER-677; SER-683 AND SER-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"Role of RBM25/LUC7L3 in abnormal cardiac sodium channel splicing regulation in human heart failure."
Gao G., Xie A., Huang S.C., Zhou A., Zhang J., Herman A.M., Ghassemzadeh S., Jeong E.M., Kasturirangan S., Raicu M., Sobieski M.A. II, Bhat G., Tatooles A., Benz E.J. Jr., Kamp T.J., Dudley S.C. Jr.
Circulation 124:1124-1131(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"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-583; SER-677; SER-683 AND SER-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Crystal structure and functional characterization of the human RBM25 PWI domain and its flanking basic region."
Gong D., Yang F., Li F., Qian D., Wu M., Shao Z., Wu M., Wu J., Shi Y.
Biochem. J. 450:85-94(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 734-843, PWI DOMAIN, MUTAGENESIS OF 734-LYS--LYS-736; 777-LYS-LYS-778; LYS-825 AND ARG-828.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK026107 mRNA. Translation: BAB15362.1.
AK094697 mRNA. Translation: BAG52915.1. Sequence problems.
AL442663 Genomic DNA. No translation available.
AC004858 Genomic DNA. Translation: AAF19255.1.
CH471061 Genomic DNA. Translation: EAW81087.1.
BC062440 mRNA. Translation: AAH62440.1. Sequence problems.
BC083496 mRNA. Translation: AAH83496.1. Different initiation.
BC111066 mRNA. Translation: AAI11067.1.
BC113389 mRNA. Translation: AAI13390.1.
BC113391 mRNA. Translation: AAI13392.1.
BC136775 mRNA. Translation: AAI36776.1.
BC136776 mRNA. Translation: AAI36777.1.
BC144407 mRNA. Translation: AAI44408.1.
AF109907 Genomic DNA. Translation: AAC97961.1.
L40392 mRNA. Translation: AAC41999.1.
CCDSCCDS32113.1. [P49756-1]
RefSeqNP_067062.1. NM_021239.2. [P49756-1]
UniGeneHs.531106.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3V53X-ray2.90A/B/C/D/E734-843[»]
ProteinModelPortalP49756.
SMRP49756. Positions 85-163, 734-841.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121843. 44 interactions.
IntActP49756. 11 interactions.
MINTMINT-4545359.

PTM databases

PhosphoSiteP49756.

Polymorphism databases

DMDM226693631.

Proteomic databases

MaxQBP49756.
PaxDbP49756.
PRIDEP49756.

Protocols and materials databases

DNASU58517.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261973; ENSP00000261973; ENSG00000119707. [P49756-1]
ENST00000525321; ENSP00000436868; ENSG00000119707. [P49756-3]
ENST00000526754; ENSP00000436225; ENSG00000119707. [P49756-2]
ENST00000527432; ENSP00000431150; ENSG00000119707. [P49756-1]
ENST00000528081; ENSP00000434444; ENSG00000119707. [P49756-4]
ENST00000540173; ENSP00000437934; ENSG00000119707. [P49756-2]
GeneID58517.
KEGGhsa:58517.
UCSCuc001xnn.4. human. [P49756-2]
uc001xno.3. human. [P49756-1]

Organism-specific databases

CTD58517.
GeneCardsGC14P073525.
HGNCHGNC:23244. RBM25.
HPAHPA003025.
MIM612427. gene.
neXtProtNX_P49756.
PharmGKBPA134912024.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250187.
HOVERGENHBG068941.
InParanoidP49756.
KOK12822.
OMADSTLMER.
OrthoDBEOG7D2FDZ.
PhylomeDBP49756.
TreeFamTF320185.

Gene expression databases

ArrayExpressP49756.
BgeeP49756.
CleanExHS_RBM25.
GenevestigatorP49756.

Family and domain databases

Gene3D1.20.1390.10. 1 hit.
3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR002483. PWI_dom.
IPR000504. RRM_dom.
[Graphical view]
PfamPF01480. PWI. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00311. PWI. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
SUPFAMSSF101233. SSF101233. 1 hit.
PROSITEPS51025. PWI. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM25. human.
GeneWikiRBM25.
GenomeRNAi58517.
NextBio65066.
PROP49756.
SOURCESearch...

Entry information

Entry nameRBM25_HUMAN
AccessionPrimary (citable) accession number: P49756
Secondary accession number(s): A0PJL9 expand/collapse secondary AC list , B2RNA8, B3KT03, Q2TA72, Q5XJ17, Q6P665, Q9H6A1, Q9UEQ5, Q9UIE9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 14, 2009
Last modified: July 9, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM