P83876 (TXN4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin-like protein 4A

Alternative name(s):
DIM1 protein homolog
Spliceosomal U5 snRNP-specific 15 kDa protein
Thioredoxin-like U5 snRNP protein U5-15kD

Gene names

Name:	TXNL4A
Synonyms:	DIM1, TXNL4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential role in pre-mRNA splicing.
Subunit structure	Interacts with HNRPF, HNRPH2, NEDD9, ERBB4, and PQBP1. Ref.6 Ref.9
Subcellular location	Nucleus Ref.9.
Sequence similarities	Belongs to the DIM1 family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis mRNA processing mRNA splicing
Cellular component	Nucleus
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Non-traceable author statement. Source: UniProtKB spliceosome assembly Traceable author statement Ref.2. Source: UniProtKB
Cellular component	nucleoplasm Traceable author statement. Source: Reactome spliceosomal complex Traceable author statement Ref.2. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 142

142

Thioredoxin-like protein 4A

PRO_0000218287

Amino acid modifications

Modified residue

132

1

Phosphoserine Ref.7 Ref.8

Disulfide bond

38 ↔ 79

Experimental info

Mutagenesis

38

1

C → A: Viable when expressed in S.pombe. Ref.11

Secondary structure

1

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142

Helix Strand Turn

Details...

Helix

11 – 19

9

Beta strand

22 – 31

10

Helix

36 – 52

17

Turn

53 – 55

3

Beta strand

56 – 62

7

Turn

63 – 65

3

Turn

68 – 71

4

Beta strand

80 – 85

6

Beta strand

88 – 93

6

Helix

109 – 123

15

Turn

124 – 126

3

Beta strand

128 – 131

4

Sequences

	Sequence		Length	Mass (Da)
	P83876 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: EDDDAD7ADAEE87F3	FASTA	142	16,786
	10 20 30 40 50 60 MSYMLPHLHN GWQVDQAILS EEDRVVVIRF GHDWDPTCMK MDEVLYSIAE KVKNFAVIYL 70 80 90 100 110 120 VDITEVPDFN KMYELYDPCT VMFFFRNKHI MIDLGTGNNN KINWAMEDKQ EMVDIIETVY 130 140 RGARKGRGLV VSPKDYSTKY RY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human homologue of the S. pombe Dim1p gene." Larin D., Ross B.M., Gilliam T.C. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15kD protein." Reuter K., Nottrott S., Fabrizio P., Luehrmann R., Ficner R. J. Mol. Biol. 294:515-525(1999) [PubMed: 10610776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
[3]	"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]. Tissue: Cerebellum.
[4]	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].
[5]	"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]. Tissue: Lung.
[6]	"Evidence that Dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for Dim1 interactions with hnRNP F and Npw38/PQBP-1." Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A. Gene 257:33-43(2000) [PubMed: 11054566] [Abstract] Cited for: INTERACTION WITH HNRPF; HNRPH2; NEDD9 AND PQBP1, MUTAGENESIS.
[7]	"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-132, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways." Gilmore-Hebert M., Ramabhadran R., Stern D.F. Mol. Cancer Res. 8:1388-1398(2010) [PubMed: 20858735] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[10]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"The evolutionarily conserved Dim1 protein defines a novel branch of the thioredoxin fold superfamily." Zhang Y.-Z., Gould K.L., Dunbrack R.L. Jr., Cheng H., Roder H., Golemis E.A. Physiol. Genomics 1:109-118(1999) [PubMed: 11015569] [Abstract] Cited for: STRUCTURE BY NMR, 3D-STRUCTURE MODELING, MUTAGENESIS OF CYS-38.
[12]	"Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis." Zhang Y.Z., Cheng H., Gould K.L., Golemis E.A., Roder H. Biochemistry 42:9609-9618(2003) [PubMed: 12911302] [Abstract] Cited for: STRUCTURE BY NMR OF 1-128, CIRCULAR DICHROISM, MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF023611 mRNA. Translation: AAB81950.1.
AF146373 mRNA. Translation: AAF17332.1.
AK314901 mRNA. Translation: BAG37415.1.
CH471117 Genomic DNA. Translation: EAW66640.1.
BC001046 mRNA. Translation: AAH01046.1.
BC019272 mRNA. Translation: AAH19272.1.

IPI

IPI00216338.

RefSeq

NP_006692.1. NM_006701.2.

UniGene

Hs.465498.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PQN	NMR	-	A	2-128	[»]
1QGV	X-ray	1.40	A	1-142	[»]
1SYX	X-ray	2.35	A/C/E	1-142	[»]

ProteinModelPortal

P83876.

SMR

P83876. Positions 3-137.

ModBase

Search...

Protein-protein interaction databases

IntAct

P83876. 3 interactions.

MINT

MINT-1783239.

STRING

P83876.

PTM databases

PhosphoSite

P83876.

Polymorphism databases

DMDM

46577662.

Proteomic databases

PRIDE

P83876.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269601; ENSP00000269601; ENSG00000141759.

GeneID

10907.

KEGG

hsa:10907.

UCSC

uc002lnp.1. human.

Organism-specific databases

CTD

10907.

GeneCards

GC18M077732.

H-InvDB

HIX0014544.

HGNC

HGNC:30551. TXNL4A.

MIM

611595. gene.

neXtProt

NX_P83876.

PharmGKB

PA134937290.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000010779.

HOGENOM

HBG522501.

HOVERGEN

HBG053996.

InParanoid

P83876.

OMA

YRNKHIM.

OrthoDB

EOG4BG8X8.

PhylomeDB

P83876.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P83876.

Bgee

P83876.

CleanEx

HS_TXNL4A.

Genevestigator

P83876.

GermOnline

ENSG00000141759. Homo sapiens.

Family and domain databases

InterPro

IPR004123. mRNA_splic_U5.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

KO

K12859.

PANTHER

PTHR12052. mRNA_splic_U5. 1 hit.

Pfam

PF02966. DIM1. 1 hit.
[Graphical view]

PIRSF

PIRSF017199. mRNA_splic_U5. 1 hit.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

ProtoNet

Search...

Other

NextBio

41427.

SOURCE

Search...

Entry information

Entry name

TXN4A_HUMAN

Accession

Primary (citable) accession number: P83876
Secondary accession number(s): B2RC18, O14834

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.