Q9H7E2 (TDRD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tudor domain-containing protein 3

Gene names

Name:

TDRD3

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

General annotation (Comments)

Function	Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In cytoplasm, may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. Ref.1 Ref.7 Ref.11
Subunit structure	Component of mRNA stress granules. Interacts with FMR1, FXR1, FXR2, EWSR1, FUS, SERBP1, EEF1A1 and DDX3X or DDX3Y, and with the small nuclear ribonucleoprotein-associated proteins SNRPB and SNRPN. Interacts with 'Lys-48'-linked tetra-ubiquitin, but not with monoubiquitin or 'Lys-63'-linked ubiquitin chains. Ref.1 Ref.7 Ref.9
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly cytoplasmic. Associated with actively translating polyribosomes and with mRNA stress granules. Ref.1 Ref.9 Ref.11
Tissue specificity	Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.9
Domain	The Tudor domain specifically recognizes and binds asymmetric dimethylation of histone H3 'Arg-17' (H3R17me2a) and histones H4 'Arg-3', 2 tags for epigenetic transcriptional activation. Ref.11
Sequence similarities	Contains 1 Tudor domain. Contains 1 UBA domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Chromatin regulator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.11. Source: UniProtKB
Molecular function	chromatin binding Inferred from direct assay Ref.11. Source: UniProtKB methylated histone residue binding Inferred from direct assay Ref.11. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9H7E2-1)

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: Q9H7E2-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     97-97: Missing.

Isoform 3 (identifier: Q9H7E2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAQVAGAALS...NEESQAAPRM

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 651

651

Tudor domain-containing protein 3

PRO_0000183163

Regions

Domain

193 – 233

41

UBA

Domain

555 – 615

61

Tudor

Amino acid modifications

Modified residue

256

1

Phosphoserine Ref.8 Ref.10

Natural variations

Alternative sequence

1

1

M → MAQVAGAALSQAGWYLSDEG IEACTSSPDKVNVNDIILIA LNTDLRTIGKKFLPSDINSG KVEKLEGPCVLQIQKIRNVA APKDNEESQAAPRM in isoform 3.

VSP_037052

Alternative sequence

97

1

Missing in isoform 2.

VSP_037053

Experimental info

Mutagenesis

598

1

E → K: Abolishes interaction with dimethylarginine-containing protein motifs and reduces association with mRNA stress granules. Ref.1

Sequence conflict

101

1

H → R in AAH60876. Ref.6

Sequence conflict

509

1

P → H in AAH60876. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

651

Helix Strand Turn

Details...

Helix

196 – 203

8

Turn

204 – 206

3

Helix

209 – 218

10

Helix

223 – 233

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 1D82F323F6EF4B05	FASTA	651	73,185
	10 20 30 40 50 60 MLRLQMTDGH ISCTAVEFSY MSKISLNTPP GTKVKLSGIV DIKNGFLLLN DSNTTVLGGE 70 80 90 100 110 120 VEHLIEKWEL QRSLSKHNRS NIGTEGGPPP FVPFGQKCVS HVQVDSRELD RRKTLQVTMP 130 140 150 160 170 180 VKPTNDNDEF EKQRTAAIAE VAKSKETKTF GGGGGGARSN LNMNAAGNRN REVLQKEKST 190 200 210 220 230 240 KSEGKHEGVY RELVDEKALK HITEMGFSKE ASRQALMDNG NNLEAALNVL LTSNKQKPVM 250 260 270 280 290 300 GPPLRGRGKG RGRIRSEDEE DLGNARPSAP STLFDFLESK MGTLNVEEPK SQPQQLHQGQ 310 320 330 340 350 360 YRSSNTEQNG VKDNNHLRHP PRNDTRQPRN EKPPRFQRDS QNSKSVLEGS GLPRNRGSER 370 380 390 400 410 420 PSTSSVSEVW AEDRIKCDRP YSRYDRTKDT SYPLGSQHSD GAFKKRDNSM QSRSGKGPSF 430 440 450 460 470 480 AEAKENPLPQ GSVDYNNQKR GKRESQTSIP DYFYDRKSQT INNEAFSGIK IEKHFNVNTD 490 500 510 520 530 540 YQNPVRSNSF IGVPNGEVEM PLKGRRIGPI KPAGPVTAVP CDDKIFYNSG PKRRSGPIKP 550 560 570 580 590 600 EKILESSIPM EYAKMWKPGD ECFALYWEDN KFYRAEVEAL HSSGMTAVVK FIDYGNYEEV 610 620 630 640 650 LLSNIKPIQT EAWEEEGTYD QTLEFRRGGD GQPRRSTRPT QQFYQPPRAR N
	Isoform 2 (Long) [UniParc]. Checksum: 997FB4382F678469	FASTA	650	73,057
	10 20 30 40 50 60 MLRLQMTDGH ISCTAVEFSY MSKISLNTPP GTKVKLSGIV DIKNGFLLLN DSNTTVLGGE 70 80 90 100 110 120 VEHLIEKWEL QRSLSKHNRS NIGTEGGPPP FVPFGQCVSH VQVDSRELDR RKTLQVTMPV 130 140 150 160 170 180 KPTNDNDEFE KQRTAAIAEV AKSKETKTFG GGGGGARSNL NMNAAGNRNR EVLQKEKSTK 190 200 210 220 230 240 SEGKHEGVYR ELVDEKALKH ITEMGFSKEA SRQALMDNGN NLEAALNVLL TSNKQKPVMG 250 260 270 280 290 300 PPLRGRGKGR GRIRSEDEED LGNARPSAPS TLFDFLESKM GTLNVEEPKS QPQQLHQGQY 310 320 330 340 350 360 RSSNTEQNGV KDNNHLRHPP RNDTRQPRNE KPPRFQRDSQ NSKSVLEGSG LPRNRGSERP 370 380 390 400 410 420 STSSVSEVWA EDRIKCDRPY SRYDRTKDTS YPLGSQHSDG AFKKRDNSMQ SRSGKGPSFA 430 440 450 460 470 480 EAKENPLPQG SVDYNNQKRG KRESQTSIPD YFYDRKSQTI NNEAFSGIKI EKHFNVNTDY 490 500 510 520 530 540 QNPVRSNSFI GVPNGEVEMP LKGRRIGPIK PAGPVTAVPC DDKIFYNSGP KRRSGPIKPE 550 560 570 580 590 600 KILESSIPME YAKMWKPGDE CFALYWEDNK FYRAEVEALH SSGMTAVVKF IDYGNYEEVL 610 620 630 640 650 LSNIKPIQTE AWEEEGTYDQ TLEFRRGGDG QPRRSTRPTQ QFYQPPRARN
	Isoform 3 [UniParc]. Checksum: CF27720025EFBD81	FASTA	744	83,103
	10 20 30 40 50 60 MAQVAGAALS QAGWYLSDEG IEACTSSPDK VNVNDIILIA LNTDLRTIGK KFLPSDINSG 70 80 90 100 110 120 KVEKLEGPCV LQIQKIRNVA APKDNEESQA APRMLRLQMT DGHISCTAVE FSYMSKISLN 130 140 150 160 170 180 TPPGTKVKLS GIVDIKNGFL LLNDSNTTVL GGEVEHLIEK WELQRSLSKH NRSNIGTEGG 190 200 210 220 230 240 PPPFVPFGQK CVSHVQVDSR ELDRRKTLQV TMPVKPTNDN DEFEKQRTAA IAEVAKSKET 250 260 270 280 290 300 KTFGGGGGGA RSNLNMNAAG NRNREVLQKE KSTKSEGKHE GVYRELVDEK ALKHITEMGF 310 320 330 340 350 360 SKEASRQALM DNGNNLEAAL NVLLTSNKQK PVMGPPLRGR GKGRGRIRSE DEEDLGNARP 370 380 390 400 410 420 SAPSTLFDFL ESKMGTLNVE EPKSQPQQLH QGQYRSSNTE QNGVKDNNHL RHPPRNDTRQ 430 440 450 460 470 480 PRNEKPPRFQ RDSQNSKSVL EGSGLPRNRG SERPSTSSVS EVWAEDRIKC DRPYSRYDRT 490 500 510 520 530 540 KDTSYPLGSQ HSDGAFKKRD NSMQSRSGKG PSFAEAKENP LPQGSVDYNN QKRGKRESQT 550 560 570 580 590 600 SIPDYFYDRK SQTINNEAFS GIKIEKHFNV NTDYQNPVRS NSFIGVPNGE VEMPLKGRRI 610 620 630 640 650 660 GPIKPAGPVT AVPCDDKIFY NSGPKRRSGP IKPEKILESS IPMEYAKMWK PGDECFALYW 670 680 690 700 710 720 EDNKFYRAEV EALHSSGMTA VVKFIDYGNY EEVLLSNIKP IQTEAWEEEG TYDQTLEFRR 730 740 GGDGQPRRST RPTQQFYQPP RARN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules." Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J. Hum. Mol. Genet. 17:3055-3074(2008) [PubMed: 18632687] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-598, INTERACTION WITH EWSR1; FMR1; FUS; SERBP1; EEF1A1 AND DDX3X OR DDX3Y.
[2]	"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 1).
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Fetal kidney.
[4]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (JUL-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] (ISOFORMS 1 AND 2). Tissue: Placenta and Testis.
[7]	"Tudor domains bind symmetrical dimethylated arginines." Cote J., Richard S. J. Biol. Chem. 280:28476-28483(2005) [PubMed: 15955813] [Abstract] Cited for: FUNCTION, INTERACTION WITH SNRPB AND SNRPN.
[8]	"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-256, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP." Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B., Meister G., Keidel E., Fischer U. Hum. Mol. Genet. 17:3236-3246(2008) [PubMed: 18664458] [Abstract] Cited for: INTERACTION WITH LYS-48-LINKED TETRA-UBIQUITIN; FMR1; FXR1 AND FXR2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]	"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-256, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"TDRD3 is an effector molecule for arginine-methylated histone marks." Yang Y., Lu Y., Espejo A., Wu J., Xu W., Liang S., Bedford M.T. Mol. Cell 40:1016-1023(2010) [PubMed: 21172665] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN TUDOR.
[12]	"Solution structure of the UBA domain of human Tudor domain containing protein 3." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 194-243.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

EU643838 mRNA. Translation: ACC94142.1.
AK024660 mRNA. Translation: BAB14950.1.
BX537910 mRNA. Translation: CAD97894.1.
AL354764, AL512666 Genomic DNA. Translation: CAH72281.1.
AL512666, AL354764 Genomic DNA. Translation: CAH74000.1.
CH471124 Genomic DNA. Translation: EAW52079.1.
BC030514 mRNA. Translation: AAH30514.1.
BC060876 mRNA. Translation: AAH60876.1.

IPI

IPI00006571.
IPI00924692.
IPI00929228.

RefSeq

NP_001139542.1. NM_001146070.1.
NP_001139543.1. NM_001146071.1.
NP_110421.1. NM_030794.2.

UniGene

Hs.525061.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WJI	NMR	-	A	194-243	[»]
3PMT	X-ray	1.80	A	553-611	[»]
3PNW	X-ray	2.05	C/F/I/L/O/R/U/X	540-615	[»]

ProteinModelPortal

Q9H7E2.

SMR

Q9H7E2. Positions 1-70, 194-243, 548-608.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H7E2. 1 interaction.

STRING

Q9H7E2.

PTM databases

PhosphoSite

Q9H7E2.

Polymorphism databases

DMDM

29337133.

Proteomic databases

PRIDE

Q9H7E2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000196169; ENSP00000196169; ENSG00000083544.
ENST00000377881; ENSP00000367113; ENSG00000083544.
ENST00000377894; ENSP00000367126; ENSG00000083544.
ENST00000411610; ENSP00000401740; ENSG00000083544.

GeneID

81550.

KEGG

hsa:81550.

UCSC

uc001vhz.2. human.

Organism-specific databases

CTD

81550.

GeneCards

GC13P060970.

H-InvDB

HIX0011353.

HGNC

HGNC:20612. TDRD3.

HPA

CAB034925.

neXtProt

NX_Q9H7E2.

PharmGKB

PA134962690.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12146.

GeneTree

ENSGT00440000038925.

HOGENOM

HBG402882.

HOVERGEN

HBG059153.

InParanoid

Q9H7E2.

OrthoDB

EOG4WM4T9.

PhylomeDB

Q9H7E2.

Gene expression databases

ArrayExpress

Q9H7E2.

Bgee

Q9H7E2.

CleanEx

HS_TDRD3.

Genevestigator

Q9H7E2.

Family and domain databases

InterPro

IPR008191. Maternal_tudor.
IPR002999. Tudor.
IPR018351. Tudor_subgr.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
[Graphical view]

Pfam

PF00567. TUDOR. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]

SMART

SM00333. TUDOR. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS50304. TUDOR. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

71791.

Entry information

Entry name

TDRD3_HUMAN

Accession

Primary (citable) accession number: Q9H7E2
Secondary accession number(s): B2MWP9, Q53XA6, Q6P992

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 81 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.