Reviewed, UniProtKB/Swiss-Prot P62995 (TRA2B_HUMAN)

Names and origin

Protein names

Recommended name:
Transformer-2 protein homolog beta
Short name=TRA-2 beta
Short name=TRA2-beta
Short name=hTRA2-beta

Alternative name(s):
Transformer-2 protein homolog B
Splicing factor, arginine/serine-rich 10

Gene names

Name:	TRA2B
Synonyms:	SFRS10

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	288 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Ref.8
Subunit structure	Interacts with SAFB/SAFB1 By similarity. Found in a pre-mRNA exonic splicing enhancer (ESE) complex with TRA2B/SFRS10, SNRNP70, SNRPA1 and SRRM1. Binds to A3 enhancer proteins SFRS4, SFRS5, SFRS6 and SFRS9. Interacts with CPSF6, RBMY1A1, RNPS1 and phosphorylated SFRS13A. Ref.10 Ref.11 Ref.12 Ref.14
Subcellular location	Nucleus Ref.8 Ref.1.
Tissue specificity	Highest expression in heart, skeletal muscle and pancreas. Less abundant in kidney, placenta and brain. Lowest expression in kidney and liver. Ref.2
Post-translational modification	Phosphorylated in the RS domains. Ref.8 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Dimethylation at Arg-241 is probably asymmetric.
Sequence similarities	Belongs to the splicing factor SR family. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Ref.8 Inferred from direct assay. Source: UniProtKB
Cellular component	nucleus Ref.8 Inferred from direct assay. Source: UniProtKB
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Ref.11 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RNPS1	Q15287	1	EBI-725485,EBI-395959
YWHAZ	P63104	1	EBI-725485,EBI-347088

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P62995-1)

Also known as: HTRA2-beta1;

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: P62995-2)

Also known as: HTRA2-beta2;

The sequence of this isoform differs from the canonical sequence as follows:
     13-38: ESRSASRSGSAHGSGKSARHTPARSR → VNVEEGKCGSRHLTSFINEYLKLRNK
     39-288: Missing.

Isoform 3 (identifier: P62995-3)

Also known as: HTRA2-beta3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 288

288

Transformer-2 protein homolog beta

PRO_0000081983

Regions

Domain

118 – 196

79

RRM

Region

193 – 230

38

Linker

Compositional bias

31 – 113

83

Arg/Ser-rich (RS1 domain)

Compositional bias

231 – 287

57

Arg/Ser-rich (RS2 domain)

Amino acid modifications

Modified residue

2

1

Phosphoserine Ref.16 Ref.21 Ref.24

Modified residue

4

1

Phosphoserine By similarity

Modified residue

14

1

Phosphoserine Ref.20 Ref.21 Ref.24

Modified residue

29

1

Phosphoserine Ref.16

Modified residue

33

1

Phosphothreonine Ref.16

Modified residue

37

1

Phosphoserine Ref.16

Modified residue

39

1

Phosphoserine Ref.16

Modified residue

50

1

Phosphoserine By similarity

Modified residue

52

1

Phosphoserine By similarity

Modified residue

54

1

Phosphoserine By similarity

Modified residue

56

1

Phosphoserine By similarity

Modified residue

69

1

Phosphothreonine Ref.16

Modified residue

71

1

Phosphoserine Ref.16

Modified residue

83

1

Phosphoserine Ref.22

Modified residue

85

1

Phosphoserine Ref.22

Modified residue

87

1

Phosphoserine Ref.22

Modified residue

95

1

Phosphoserine Ref.16

Modified residue

97

1

Phosphoserine Ref.16

Modified residue

99

1

Phosphoserine Ref.16

Modified residue

201

1

Phosphothreonine Ref.19 Ref.22

Modified residue

207

1

Phosphotyrosine Ref.19

Modified residue

212

1

Phosphothreonine Ref.22

Modified residue

215

1

Phosphoserine Ref.19

Modified residue

216

1

Phosphoserine Ref.19

Modified residue

241

1

Dimethylated arginine Ref.7 Ref.13

Modified residue

264

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.21

Modified residue

266

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.21

Modified residue

268

1

Phosphotyrosine Ref.18

Modified residue

269

1

Phosphotyrosine Ref.18

Modified residue

276

1

Phosphoserine Ref.16

Modified residue

280

1

Phosphoserine By similarity

Modified residue

282

1

Phosphoserine By similarity

Modified residue

284

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 100

100

Missing in isoform 3.

VSP_005896

Alternative sequence

13 – 38

26

ESRSA…PARSR → VNVEEGKCGSRHLTSFINEY LKLRNK in isoform 2.

VSP_005898

Alternative sequence

39 – 288

250

Missing in isoform 2.

VSP_005899

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

288

Helix Strand Turn

Details...

Helix

116 – 118

3

Beta strand

120 – 124

5

Helix

131 – 139

9

Beta strand

144 – 151

8

Beta strand

153 – 168

16

Helix

169 – 179

11

Beta strand

182 – 184

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (HTRA2-beta1) [UniParc]. Last modified August 31, 2004. Version 1. Checksum: 60B310C8BA443E28	FASTA	288	33,666
	10 20 30 40 50 60 MSDSGEQNYG ERESRSASRS GSAHGSGKSA RHTPARSRSK EDSRRSRSKS RSRSESRSRS 70 80 90 100 110 120 RRSSRRHYTR SRSRSRSHRR SRSRSYSRDY RRRHSHSHSP MSTRRRHVGN RANPDPNCCL 130 140 150 160 170 180 GVFGLSLYTT ERDLREVFSK YGPIADVSIV YDQQSRRSRG FAFVYFENVD DAKEAKERAN 190 200 210 220 230 240 GMELDGRRIR VDFSITKRPH TPTPGIYMGR PTYGSSRRRD YYDRGYDRGY DDRDYYSRSY 250 260 270 280 RGGGGGGGGW RAAQDRDQIY RRRSPSPYYS RGGYRSRSRS RSYSPRRY
	Isoform 2 (HTRA2-beta2) [UniParc] [UniParc]. Checksum: 9E1E02297010CF61	FASTA	38	4,390
	10 20 30 MSDSGEQNYG ERVNVEEGKC GSRHLTSFIN EYLKLRNK
	Isoform 3 (HTRA2-beta3) [UniParc] [UniParc]. Checksum: AC9D4171E481BAF7	FASTA	188	21,935
	10 20 30 40 50 60 MSTRRRHVGN RANPDPNCCL GVFGLSLYTT ERDLREVFSK YGPIADVSIV YDQQSRRSRG 70 80 90 100 110 120 FAFVYFENVD DAKEAKERAN GMELDGRRIR VDFSITKRPH TPTPGIYMGR PTYGSSRRRD 130 140 150 160 170 180 YYDRGYDRGY DDRDYYSRSY RGGGGGGGGW RAAQDRDQIY RRRSPSPYYS RGGYRSRSRS RSYSPRRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of htra2-beta-1 and htra2-beta-2, two human homologs of tra-2 generated by alternative splicing." Beil B., Screaton G., Stamm S. DNA Cell Biol. 16:679-690(1997) [PubMed: 9212162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[2]	"Human transformer-2-beta gene (SFRS10): complete nucleotide sequence, chromosomal localization, and generation of a tissue-specific isoform." Nayler O., Cap C., Stamm S. Genomics 53:191-202(1998) [PubMed: 9790768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), TISSUE SPECIFICITY.
[3]	"The human transformer-2 beta gene is a functional homologue of the D. melanogaster sex determination factor transformer-2." Dauwalder B., Manzanares F.A., Mattox W. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[4]	"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] (ISOFORM 3). Tissue: Spleen.
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung, Placenta and Skin.
[7]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 141-156; 160-173; 179-187; 189-210 AND 229-251, METHYLATION AT ARG-241, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[8]	"Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing." Tacke R., Tohyama M., Ogawa S., Manley J.L. Cell 93:139-148(1998) [PubMed: 9546399] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION. Tissue: Cervix carcinoma.
[9]	"The SRm160/300 splicing coactivator is required for exon-enhancer function." Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J. Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999) [PubMed: 10339552] [Abstract] Cited for: IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH SNRNP70; SNRPA1 AND SRRM1.
[10]	"RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2beta and affect splicing." Venables J.P., Elliott D.J., Makarova O.V., Makarov E.M., Cooke H.J., Eperon E.C. Hum. Mol. Genet. 9:685-694(2000) [PubMed: 10749975] [Abstract] Cited for: INTERACTION WITH RBMY1A1.
[11]	"Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization." Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M. J. Biol. Chem. 279:35788-35797(2004) [PubMed: 15169763] [Abstract] Cited for: INTERACTION WITH CPSF6.
[12]	"Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo." Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A. Mol. Cell. Biol. 24:1174-1187(2004) [PubMed: 14729963] [Abstract] Cited for: INTERACTION WITH RNPS1.
[13]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-241, MASS SPECTROMETRY.
[14]	"Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock." Shin C., Feng Y., Manley J.L. Nature 427:553-558(2004) [PubMed: 14765198] [Abstract] Cited for: INTERACTION WITH SFRS13A.
[15]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-266, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"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-2; SER-29; THR-33; SER-37; SER-39; THR-69; SER-71; SER-95; SER-97; SER-99; SER-264; SER-266 AND SER-276, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-266, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-268 AND TYR-269, MASS SPECTROMETRY.
[19]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; TYR-207; SER-215 AND SER-216, MASS SPECTROMETRY.
[20]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY.
[21]	"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-2; SER-14; SER-264 AND SER-266, MASS SPECTROMETRY.
[22]	"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-83; SER-85; SER-87; THR-201 AND THR-212, MASS SPECTROMETRY.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-14, MASS SPECTROMETRY.
[25]	"Solution structure of the RNA recognition motif in arginine/serine-rich splicing factor 10." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 109-191.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U61267 mRNA. Translation: AAC28242.1.
U87836 mRNA. Translation: AAB69763.1.
AF057159 Genomic DNA. Translation: AAD19277.1.
AF057159 Genomic DNA. Translation: AAD19278.1.
AF057159 Genomic DNA. Translation: AAD19279.1.
U68063 mRNA. Translation: AAB08701.1.
AK301118 mRNA. Translation: BAG62714.1.
CH471052 Genomic DNA. Translation: EAW78204.1.
BC000160 mRNA. Translation: AAH00160.1.
BC000451 mRNA. Translation: AAH00451.1.
BC005898 mRNA. Translation: AAH05898.1.

IPI

IPI00220938.
IPI00301503.
IPI00927500.

RefSeq

NP_004584.1.

UniGene

Hs.533122

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CQC	NMR	-	A	110-191	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P62995. 5 interactions.

STRING

P62995.

PTM databases

PhosphoSite

P62995.

Proteomic databases

PRIDE

P62995.

Genome annotation databases

Ensembl

ENST00000453386; ENSP00000416959; ENSG00000136527; Homo sapiens. [Genome view]

GeneID

6434.

KEGG

hsa:6434.

UCSC

uc003fpv.1. human.

Organism-specific databases

CTD

6434.

GeneCards

GC03M187117.

HGNC

HGNC:10781. TRA2B.

HPA

CAB011692.

MIM

602719. gene.

PharmGKB

PA35697.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20143.

HOVERGEN

HBG104971.

InParanoid

P62995.

PhylomeDB

P62995.

Gene expression databases

ArrayExpress

P62995.

Bgee

P62995.

CleanEx

HS_SFRS10.

Genevestigator

P62995.

GermOnline

ENSG00000136527. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

24991.

SOURCE

Search...

Entry information

Entry name

TRA2B_HUMAN

Accession

Primary (citable) accession number: P62995
Secondary accession number(s): B4DVK2 , O15449, Q15815, Q64283

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 31, 2004
Last modified:	March 2, 2010
This is version 67 of the entry and version 1 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.