Reviewed, UniProtKB/Swiss-Prot P52756 (RBM5_HUMAN)

Names and origin

Protein names

Recommended name:
    RNA-binding protein 5
Alternative name(s):
    RNA-binding motif protein 5
    Putative tumor suppressor LUCA15
    Protein G15
    Renal carcinoma antigen NY-REN-9

Gene names

Name:	RBM5
ORF Names:	H37, LUCA15

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	815 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate aopotosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes exclusion of exon 9 thereby producing a catalytically active form of CASP2/Caspase-2 that induces apoptosis. Ref.5 Ref.10 Ref.11 Ref.12 Ref.13 Ref.18 Ref.20
Subunit structure	Component of the spliceosome A complex (also known as the prespliceosome). Appears to dissociate from the spliceosome upon formation of the spliceosome B complex (also known as the precatalytic spliceosome), in which the heterotrimeric U4/U6.U5 snRNPs are bound. Interacts with U2AF2; this interaction is direct. Also interacts with ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200; these interactions may be indirect. Ref.18
Subcellular location	Nucleus. Ref.18
Tissue specificity	Isoform 5 is widely expressed in normal tissues and is expressed at increased levels in T-leukaemic cell lines.
Sequence similarities	Belongs to the RBM5/RBM10 family. Contains 1 C2H2-type zinc finger. Contains 1 G-patch domain. Contains 1 RanBP2-type zinc finger. Contains 2 RRM (RNA recognition motif) domains.
Sequence caution	The sequence BAG59728.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS. The sequence BAG59871.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS. The sequence BAG63975.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Keywords
Biological process	Apoptosis mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell proliferation Traceable author statement. Source: UniProtKB positive regulation of apoptosis Ref.20 Inferred from direct assay. Source: UniProtKB regulation of alternative nuclear mRNA splicing, via spliceosome Ref.20 Inferred from direct assay. Source: UniProtKB spliceosome assembly Inferred from direct assay. Source: UniProtKB
Cellular component	spliceosomal complex Traceable author statement. Source: UniProtKB
Molecular function	DNA binding Traceable author statement. Source: ProtInc mRNA binding Ref.20 Inferred from direct assay. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P52756-1)

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: P52756-2)

The sequence of this isoform differs from the canonical sequence as follows:
     138-143: VSRGFA → ESLLSS
     144-815: Missing.

Isoform 3 (identifier: P52756-3)

The sequence of this isoform differs from the canonical sequence as follows:
     65-126: ERRNSDRSED...MMESFEGPQP → YSRNDGVLRR...DSRKAHCNAL
     127-815: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: P52756-4)

The sequence of this isoform differs from the canonical sequence as follows:
     142-815: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: P52756-5)

Also known as: delta-6;

The sequence of this isoform differs from the canonical sequence as follows:
     137-150: GVSRGFAFVEFYHL → EKVGDSRKAHCNAL
     151-815: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 815	815	RNA-binding protein 5		PRO_0000081759
Regions
	Domain	98 – 178	81	RRM 1
	Domain	231 – 315	85	RRM 2
	Domain	743 – 789	47	G-patch
	Zinc finger	181 – 210	30	RanBP2-type
	Zinc finger	647 – 677	31	C2H2-type; atypical
	Region	321 – 809	489	Required for interaction with U2AF2
	Region	452 – 535	84	Sufficient for interaction with ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200
Amino acid modifications
	Modified residue	59	1	Phosphoserine Ref.14
	Modified residue	69	1	Phosphoserine By similarity
	Modified residue	78	1	Phosphoserine By similarity
	Modified residue	542	1	N6-acetyllysine Ref.22
	Modified residue	621	1	Phosphoserine Ref.17 Ref.19
	Modified residue	624	1	Phosphoserine Ref.14 Ref.17 Ref.19 Ref.16
	Modified residue	712	1	Phosphotyrosine Ref.17
Natural variations
	Alternative sequence	65 – 126	62	ERRNS…EGPQP → YSRNDGVLRRPSACGCEADE EENRCKPWFRLRGVLSLARC YQLDGSQSEKVGDSRKAHCN AL in isoform 3.		VSP_037429
	Alternative sequence	127 – 815	689	Missing in isoform 3.		VSP_037430
	Alternative sequence	137 – 150	14	GVSRG…EFYHL → EKVGDSRKAHCNAL in isoform 5.		VSP_037431
	Alternative sequence	138 – 143	6	VSRGFA → ESLLSS in isoform 2.		VSP_037432
	Alternative sequence	142 – 815	674	Missing in isoform 4.		VSP_037433
	Alternative sequence	144 – 815	672	Missing in isoform 2.		VSP_037434
	Alternative sequence	151 – 815	665	Missing in isoform 5.		VSP_037435
Experimental info
	Sequence conflict	53 – 54	2	DY → GS in AAA99715. Ref.1
	Sequence conflict	354	1	G → V in AAA99715. Ref.1
	Sequence conflict	455	1	Missing in AAB42216. Ref.8
	Sequence conflict	788	1	G → A in AAB42216. Ref.8
	Sequence conflict	812	1	T → I in AAA99715. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: AA79962D13405479	FASTA	815	92,154
	10 20 30 40 50 60 MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP 70 80 90 100 110 120 ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES 130 140 150 160 170 180 FEGPQPADVR LMKRKTGVSR GFAFVEFYHL QDATSWMEAN QKKLVIQGKH IAMHYSNPRP 190 200 210 220 230 240 KFEDWLCNKC CLNNFRKRLK CFRCGADKFD SEQEVPPGTT ESVQSVDYYC DTIILRNIAP 250 260 270 280 290 300 HTVVDSIMTA LSPYASLAVN NIRLIKDKQT QQNRGFAFVQ LSSAMDASQL LQILQSLHPP 310 320 330 340 350 360 LKIDGKTIGV DFAKSARKDL VLSDGNRVSA FSVASTAIAA AQWSSTQSQS GEGGSVDYSY 370 380 390 400 410 420 LQPGQDGYAQ YAQYSQDYQQ FYQQQAGGLE SDASSASGTA VTTTSAAVVS QSPQLYNQTS 430 440 450 460 470 480 NPPGSPTEEA QPSTSTSTQA PAASPTGVVP GTKYAVPDTS TYQYDESSGY YYDPTTGLYY 490 500 510 520 530 540 DPNSQYYYNS LTQQYLYWDG EKETYVPAAE SSSHQQSGLP PAKEGKEKKE KPKSKTAQQI 550 560 570 580 590 600 AKDMERWAKS LNKQKENFKN SFQPVNSLRE EERRESAAAD AGFALFEKKG ALAERQQLIP 610 620 630 640 650 660 ELVRNGDEEN PLKRGLVAAY SGDSDNEEEL VERLESEEEK LADWKKMACL LCRRQFPNKD 670 680 690 700 710 720 ALVRHQQLSD LHKQNMDIYR RSRLSEQELE ALELREREMK YRDRAAERRE KYGIPEPPEP 730 740 750 760 770 780 KRKKQFDAGT VNYEQPTKDG IDHSNIGNKM LQAMGWREGS GLGRKCQGIT APIEAQVRLK 790 800 810 GAGLGAKGSA YGLSGADSYK DAVRKAMFAR FTEME
	Isoform 2. Checksum: 9D5FC205E7B15147	FASTA	143	17,055
	10 20 30 40 50 60 MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP 70 80 90 100 110 120 ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES 130 140 FEGPQPADVR LMKRKTGESL LSS
	Isoform 3. Checksum: DCF25D0B05DD2BF6	FASTA	126	14,897
	10 20 30 40 50 60 MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP 70 80 90 100 110 120 ERERYSRNDG VLRRPSACGC EADEEENRCK PWFRLRGVLS LARCYQLDGS QSEKVGDSRK AHCNAL
	Isoform 4. Checksum: 2D46C7A88147A429	FASTA	141	16,838
	10 20 30 40 50 60 MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP 70 80 90 100 110 120 ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES 130 140 FEGPQPADVR LMKRKTGVSR G
	Isoform 5 (delta-6). Checksum: EC00925B099F81DC	FASTA	150	17,891
	10 20 30 40 50 60 MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP 70 80 90 100 110 120 ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES 130 140 150 FEGPQPADVR LMKRKTEKVG DSRKAHCNAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A putative tumor suppressor gene LUCA15 on 3p21.3 encodes two RNA recognizing motifs and is related to the Drosophila tumor suppresorgene Sxl." Bader S., Latif F., Duh F.-M., Wei M., Kashuba V., Sekido Y., Lee C., Koonin E., Zabarofsky E., Klein G., Minna J.D., Lerman M.I. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"An evolutionary rearrangement of the Xp11.3-11.23 region in 3p21.3, a region frequently deleted in a variety of cancers." Timmer T., Terpstra P., van den Berg A., Veldhuis P.M.J.F., Ter Elst A., van der Veen A.Y., Kok K., Naylor S.L., Buys C.H.C.M. Genomics 60:238-240(1999) [PubMed: 10486216] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Identification of differentially expressed genes associated with HER-2/neu overexpression in human breast cancer cells." Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J. Nucleic Acids Res. 27:4008-4017(1999) [PubMed: 10497265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[4]	Oh J.J., Wong S.G., Slamon D.J. Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 61. Tissue: Testis.
[5]	"LUCA-15-encoded sequence variants regulate CD95-mediated apoptosis." Sutherland L.C., Edwards S.E., Cable H.C., Poirier G.G., Miller B.A., Cooper C.S., Williams G.T. Oncogene 19:3774-3781(2000) [PubMed: 10949932] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, FUNCTION.
[6]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5). Tissue: Placenta.
[7]	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. , 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].
[8]	Bentley D., Maggi L. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-815.
[9]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[10]	"Candidate tumour suppressor LUCA-15 can regulate multiple apoptotic pathways." Mourtada-Maarabouni M., Sutherland L.C., Williams G.T. Apoptosis 7:421-432(2002) [PubMed: 12207175] [Abstract] Cited for: FUNCTION.
[11]	"Simultaneous acceleration of the cell cycle and suppression of apoptosis by splice variant delta-6 of the candidate tumour suppressor LUCA-15/RBM5." Mourtada-Maarabouni M., Sutherland L.C., Meredith J.M., Williams G.T. Genes Cells 8:109-119(2003) [PubMed: 12581154] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 5), FUNCTION.
[12]	"LUCA-15/RBM5, a putative tumour suppressor, enhances multiple receptor-initiated death signals." Rintala-Maki N.D., Sutherland L.C. Apoptosis 9:475-484(2004) [PubMed: 15192330] [Abstract] Cited for: FUNCTION.
[13]	"3p21.3 tumor suppressor gene H37/Luca15/RBM5 inhibits growth of human lung cancer cells through cell cycle arrest and apoptosis." Oh J.J., Razfar A., Delgado I., Reed R.A., Malkina A., Boctor B., Slamon D.J. Cancer Res. 66:3419-3427(2006) [PubMed: 16585163] [Abstract] Cited for: FUNCTION.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-624, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Composition and three-dimensional EM structure of double affinity-purified, human prespliceosomal A complexes." Behzadnia N., Golas M.M., Hartmuth K., Sander B., Kastner B., Deckert J., Dube P., Will C.L., Urlaub H., Stark H., Luehrmann R. EMBO J. 26:1737-1748(2007) [PubMed: 17332742] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL A COMPLEX.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, MASS SPECTROMETRY.
[17]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-624 AND TYR-712, MASS SPECTROMETRY.
[18]	"RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition." Bonnal S., Martinez C., Foerch P., Bachi A., Wilm M., Valcarcel J. Mol. Cell 32:81-95(2008) [PubMed: 18851835] [Abstract] Cited for: FUNCTION, INTERACTION WITH ACIN1; PRPF8; SFRS3; SNRPB; SNRPN; SNRNP70; SNRNP200 AND U2AF2, SUBCELLULAR LOCATION.
[19]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-624, MASS SPECTROMETRY.
[20]	"Up-regulation of the proapoptotic caspase 2 splicing isoform by a candidate tumor suppressor, RBM5." Fushimi K., Ray P., Kar A., Wang L., Sutherland L.C., Wu J.Y. Proc. Natl. Acad. Sci. U.S.A. 105:15708-15713(2008) [PubMed: 18840686] [Abstract] Cited for: FUNCTION, RNA-BINDING.
[21]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-542, MASS SPECTROMETRY.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	U23946 mRNA. Translation: AAA99715.1. AF091263 mRNA. Translation: AAD04159.1. AF103802 mRNA. Translation: AAF02422.2. AF107493 mRNA. Translation: AAF99551.1. AK297249 mRNA. Translation: BAG59728.1. Sequence problems. AK297445 mRNA. Translation: BAG59871.1. Sequence problems. AK302766 mRNA. Translation: BAG63975.1. Sequence problems. AK314032 mRNA. Translation: BAG36742.1. CH471055 Genomic DNA. Translation: EAW65040.1. CH471055 Genomic DNA. Translation: EAW65041.1. U73168 Genomic DNA. Translation: AAB42216.1.
IPI	IPI00005036. IPI00796867. IPI00927051. IPI00930333. IPI00930619.
RefSeq	NP_005769.1.
UniGene	Hs.439480
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P52756. 1 interaction.
STRING	P52756.
PTM databases
PhosphoSite	P52756.
Proteomic databases
PRIDE	P52756.
Genome annotation databases
Ensembl	ENST00000347869; ENSP00000343054; ENSG00000003756; Homo sapiens. [Genome view] ENST00000395174; ENSP00000378603; ENSG00000003756; Homo sapiens. [Genome view] ENST00000404526; ENSP00000384872; ENSG00000003756; Homo sapiens. [Genome view] ENST00000417905; ENSP00000406119; ENSG00000003756; Homo sapiens. [Genome view] ENST00000433556; ENSP00000396926; ENSG00000003756; Homo sapiens. [Genome view] ENST00000437500; ENSP00000394622; ENSG00000003756; Homo sapiens. [Genome view] ENST00000438369; ENSP00000414218; ENSG00000003756; Homo sapiens. [Genome view] ENST00000441305; ENSP00000390711; ENSG00000003756; Homo sapiens. [Genome view] ENST00000441812; ENSP00000398426; ENSG00000003756; Homo sapiens. [Genome view]
GeneID	10181.
KEGG	hsa:10181.
UCSC	uc003cyf.2. human. uc003cyg.1. human.
Organism-specific databases
CTD	10181.
GeneCards	GC03P050101.
HGNC	HGNC:9902. RBM5.
HPA	HPA017335. HPA018011.
MIM	606884. gene.
PharmGKB	PA34267.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P52756.
HOVERGEN	P52756.
OMA	SHQQAGL.
Enzyme and pathway databases
Reactome	REACT_125. Processing of Capped Intron-Containing Pre-mRNA. REACT_6167. Influenza Infection. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P52756.
Bgee	P52756.
Genevestigator	P52756.
GermOnline	ENSG00000003756. Homo sapiens.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR000467. G_patch. IPR000504. RRM_RNP1. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR001876. Znf_RanBP2. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
Pfam	PF01585. G-patch. 1 hit. PF00076. RRM_1. 1 hit. PF00641. zf-RanBP. 1 hit. [Graphical view]
SMART	SM00443. G_patch. 1 hit. SM00360. RRM. 2 hits. SM00355. ZnF_C2H2. 1 hit. SM00547. ZnF_RBZ. 1 hit. [Graphical view]
PROSITE	PS50174. G_PATCH. 1 hit. PS50102. RRM. 2 hits. PS01358. ZF_RANBP2_1. 1 hit. PS50199. ZF_RANBP2_2. 1 hit. PS00028. ZINC_FINGER_C2H2_1. False negative. PS50157. ZINC_FINGER_C2H2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	38542.
SOURCE	Search...

Entry information

Entry name

RBM5_HUMAN

Accession

Primary (citable) accession number: P52756
Secondary accession number(s): B2RA45 , B4DM16, B4DMF9, B4DZ63, Q93021, Q9BU14, Q9HDA6, Q9UKY8, Q9UL24

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	February 21, 2001
Last modified:	November 3, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.