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P49756

- RBM25_HUMAN

UniProt

P49756 - RBM25_HUMAN

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Protein

RNA-binding protein 25

Gene

RBM25

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

Functioni

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 S to antiapoptotic BCL2L1 isoform L mRNA expression. When overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice site (5'-ss) selection, whereas its depletion caused the accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1 isoform S 5'-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.2 Publications

GO - Molecular functioni

  1. mRNA binding Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  3. regulation of apoptotic process Source: UniProtKB
  4. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RBM25
Synonyms:RNPC7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:23244. RBM25.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nuclear speck Source: UniProtKB
  3. nucleus Source: HPA
  4. spliceosomal complex Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi734 – 7363KRK → AAA: Reduced DNA/RNA binding. 1 Publication
Mutagenesisi777 – 7782KK → AA: Reduced DNA/RNA binding. 1 Publication
Mutagenesisi825 – 8251K → A: Reduced DNA/RNA binding; when associated with A-828. 1 Publication
Mutagenesisi828 – 8281R → A: Reduced DNA/RNA binding; when associated with A-825. 1 Publication

Organism-specific databases

PharmGKBiPA134912024.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 843843RNA-binding protein 25PRO_0000081784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei135 – 1351N6-acetyllysineBy similarity
Cross-linki477 – 477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei583 – 5831Phosphoserine2 Publications
Modified residuei677 – 6771Phosphoserine5 Publications
Modified residuei683 – 6831Phosphoserine3 Publications
Modified residuei703 – 7031Phosphoserine3 Publications

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP49756.
PaxDbiP49756.
PRIDEiP49756.

PTM databases

PhosphoSiteiP49756.

Expressioni

Gene expression databases

BgeeiP49756.
CleanExiHS_RBM25.
ExpressionAtlasiP49756. baseline and differential.
GenevestigatoriP49756.

Organism-specific databases

HPAiHPA003025.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi121843. 48 interactions.
IntActiP49756. 12 interactions.
MINTiMINT-4545359.

Structurei

Secondary structure

1
843
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi739 – 7446Combined sources
Helixi749 – 7546Combined sources
Turni759 – 7613Combined sources
Helixi764 – 7696Combined sources
Helixi771 – 78212Combined sources
Helixi789 – 79911Combined sources
Helixi804 – 81512Combined sources
Helixi818 – 83922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V53X-ray2.90A/B/C/D/E734-843[»]
ProteinModelPortaliP49756.
SMRiP49756. Positions 84-161, 734-841.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 16478RRMPROSITE-ProRule annotationAdd
BLAST
Domaini750 – 84394PWIPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni285 – 644360Necessary for nuclear speckle localizationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi292 – 608317Glu-richAdd
BLAST
Compositional biasi309 – 549241Arg-richAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 PWI domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG250187.
GeneTreeiENSGT00730000111019.
HOVERGENiHBG068941.
InParanoidiP49756.
KOiK12822.
OMAiDSTLMER.
OrthoDBiEOG7D2FDZ.
PhylomeDBiP49756.
TreeFamiTF320185.

Family and domain databases

Gene3Di1.20.1390.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR002483. PWI_dom.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF01480. PWI. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00311. PWI. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF101233. SSF101233. 1 hit.
PROSITEiPS51025. PWI. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49756-1) [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

        10         20         30         40         50
MSFPPHLNRP PMGIPALPPG IPPPQFPGFP PPVPPGTPMI PVPMSIMAPA
60 70 80 90 100
PTVLVPTVSM VGKHLGARKD HPGLKAKEND ENCGPTTTVF VGNISEKASD
110 120 130 140 150
MLIRQLLAKC GLVLSWKRVQ GASGKLQAFG FCEYKEPEST LRALRLLHDL
160 170 180 190 200
QIGEKKLLVK VDAKTKAQLD EWKAKKKASN GNARPETVTN DDEEALDEET
210 220 230 240 250
KRRDQMIKGA IEVLIREYSS ELNAPSQESD SHPRKKKKEK KEDIFRRFPV
260 270 280 290 300
APLIPYPLIT KEDINAIEME EDKRDLISRE ISKFRDTHKK LEEEKGKKEK
310 320 330 340 350
ERQEIEKERR ERERERERER ERRERERERE REREREKEKE RERERERDRD
360 370 380 390 400
RDRTKERDRD RDRERDRDRD RERSSDRNKD RSRSREKSRD RERERERERE
410 420 430 440 450
RERERERERE RERERERERE REREREKDKK RDREEDEEDA YERRKLERKL
460 470 480 490 500
REKEAAYQER LKNWEIRERK KTREYEKEAE REEERRREMA KEAKRLKEFL
510 520 530 540 550
EDYDDDRDDP KYYRGSALQK RLRDREKEME ADERDRKREK EELEEIRQRL
560 570 580 590 600
LAEGHPDPDA ELQRMEQEAE RRRQPQIKQE PESEEEEEEK QEKEEKREEP
610 620 630 640 650
MEEEEEPEQK PCLKPTLRPI SSAPSVSSAS GNATPNTPGD ESPCGIIIPH
660 670 680 690 700
ENSPDQQQPE EHRPKIGLSL KLGASNSPGQ PNSVKRKKLP VDSVFNKFED
710 720 730 740 750
EDSDDVPRKR KLVPLDYGED DKNATKGTVN TEEKRKHIKS LIEKIPTAKP
760 770 780 790 800
ELFAYPLDWS IVDSILMERR IRPWINKKII EYIGEEEATL VDFVCSKVMA
810 820 830 840
HSSPQSILDD VAMVLDEEAE VFIVKMWRLL IYETEAKKIG LVK
Length:843
Mass (Da):100,185
Last modified:April 14, 2009 - v3
Checksum:i80534590147A342A
GO
Isoform 2 (identifier: P49756-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     290-294: KLEEE → RSYGD
     295-843: Missing.

Note: No experimental confirmation available.

Show »
Length:294
Mass (Da):32,822
Checksum:i184FE9019A3E3D95
GO
Isoform 3 (identifier: P49756-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     290-300: KLEEEKGKKEK → VVFLSFHLIPI
     301-843: Missing.

Show »
Length:300
Mass (Da):33,510
Checksum:i81D1498626DDD750
GO
Isoform 4 (identifier: P49756-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:164
Mass (Da):17,953
Checksum:i5D5562C8AAD78BAE
GO

Sequence cautioni

The sequence AAH62440.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH62440.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH83496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti428 – 4281D → K in BAB15362. (PubMed:14702039)Curated
Sequence conflicti571 – 5744RRRQ → EAQE in AAC41999. (PubMed:7596406)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei109 – 16456KCGLV…KVDAK → PSDSVSTRSQNLPSVHSDYY MTCKLERKSYSLKLMQRQRH SWMNGKQRRKLLMGLG in isoform 4. 1 PublicationVSP_039881Add
BLAST
Alternative sequencei165 – 843679Missing in isoform 4. 1 PublicationVSP_039882Add
BLAST
Alternative sequencei290 – 30011KLEEEKGKKEK → VVFLSFHLIPI in isoform 3. 1 PublicationVSP_036791Add
BLAST
Alternative sequencei290 – 2945KLEEE → RSYGD in isoform 2. 1 PublicationVSP_036792
Alternative sequencei295 – 843549Missing in isoform 2. 1 PublicationVSP_036793Add
BLAST
Alternative sequencei301 – 843543Missing in isoform 3. 1 PublicationVSP_036794Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32113.1. [P49756-1]
RefSeqiNP_067062.1. NM_021239.2. [P49756-1]
UniGeneiHs.531106.

Genome annotation databases

EnsembliENST00000261973; ENSP00000261973; ENSG00000119707. [P49756-1]
ENST00000525321; ENSP00000436868; ENSG00000119707. [P49756-3]
ENST00000526754; ENSP00000436225; ENSG00000119707. [P49756-2]
ENST00000527432; ENSP00000431150; ENSG00000119707. [P49756-1]
ENST00000528081; ENSP00000434444; ENSG00000119707. [P49756-4]
GeneIDi58517.
KEGGihsa:58517.
UCSCiuc001xnn.4. human. [P49756-2]
uc001xno.3. human. [P49756-1]

Polymorphism databases

DMDMi226693631.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS32113.1. [P49756-1 ]
RefSeqi NP_067062.1. NM_021239.2. [P49756-1 ]
UniGenei Hs.531106.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3V53 X-ray 2.90 A/B/C/D/E 734-843 [» ]
ProteinModelPortali P49756.
SMRi P49756. Positions 84-161, 734-841.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121843. 48 interactions.
IntActi P49756. 12 interactions.
MINTi MINT-4545359.

PTM databases

PhosphoSitei P49756.

Polymorphism databases

DMDMi 226693631.

Proteomic databases

MaxQBi P49756.
PaxDbi P49756.
PRIDEi P49756.

Protocols and materials databases

DNASUi 58517.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261973 ; ENSP00000261973 ; ENSG00000119707 . [P49756-1 ]
ENST00000525321 ; ENSP00000436868 ; ENSG00000119707 . [P49756-3 ]
ENST00000526754 ; ENSP00000436225 ; ENSG00000119707 . [P49756-2 ]
ENST00000527432 ; ENSP00000431150 ; ENSG00000119707 . [P49756-1 ]
ENST00000528081 ; ENSP00000434444 ; ENSG00000119707 . [P49756-4 ]
GeneIDi 58517.
KEGGi hsa:58517.
UCSCi uc001xnn.4. human. [P49756-2 ]
uc001xno.3. human. [P49756-1 ]

Organism-specific databases

CTDi 58517.
GeneCardsi GC14P073525.
HGNCi HGNC:23244. RBM25.
HPAi HPA003025.
MIMi 612427. gene.
neXtProti NX_P49756.
PharmGKBi PA134912024.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250187.
GeneTreei ENSGT00730000111019.
HOVERGENi HBG068941.
InParanoidi P49756.
KOi K12822.
OMAi DSTLMER.
OrthoDBi EOG7D2FDZ.
PhylomeDBi P49756.
TreeFami TF320185.

Miscellaneous databases

ChiTaRSi RBM25. human.
GeneWikii RBM25.
GenomeRNAii 58517.
NextBioi 65066.
PROi P49756.
SOURCEi Search...

Gene expression databases

Bgeei P49756.
CleanExi HS_RBM25.
ExpressionAtlasi P49756. baseline and differential.
Genevestigatori P49756.

Family and domain databases

Gene3Di 1.20.1390.10. 1 hit.
3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR002483. PWI_dom.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF01480. PWI. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00311. PWI. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view ]
SUPFAMi SSF101233. SSF101233. 1 hit.
PROSITEi PS51025. PWI. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. 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.

Entry informationi

Entry nameiRBM25_HUMAN
AccessioniPrimary (citable) accession number: P49756
Secondary accession number(s): A0PJL9
, B2RNA8, B3KT03, Q2TA72, Q5XJ17, Q6P665, Q9H6A1, Q9UEQ5, Q9UIE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 14, 2009
Last modified: November 26, 2014
This is version 117 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 14
    Human chromosome 14: 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