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Protein

Testin

Gene

TES

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

Functioni

Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth.3 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • negative regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Testin
Alternative name(s):
TESS
Gene namesi
Name:TES
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:14620. TES.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • cytoplasm Source: HPA
  • focal adhesion Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi328 – 3281C → A: Abolishes interaction with ACTL7A. 1 Publication
Mutagenesisi391 – 3911C → A: Abolishes localization at focal adhesions. 1 Publication

Organism-specific databases

PharmGKBiPA37906.

Polymorphism and mutation databases

BioMutaiTES.
DMDMi17380320.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421TestinPRO_0000075906Add
BLAST

Proteomic databases

MaxQBiQ9UGI8.
PaxDbiQ9UGI8.
PeptideAtlasiQ9UGI8.
PRIDEiQ9UGI8.

PTM databases

PhosphoSiteiQ9UGI8.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9UGI8.
CleanExiHS_TES.
ExpressionAtlasiQ9UGI8. baseline and differential.
GenevisibleiQ9UGI8. HS.

Organism-specific databases

HPAiCAB003690.
HPA015269.
HPA018123.

Interactioni

Subunit structurei

Interacts via LIM domain 1 with ZYX. Interacts (via LIM domain 3) with ENAH and VASP. Interacts with ALKBH4, talin, actin, alpha-actinin, GRIP1 and PXN. Interacts (via LIM domain 2) with ACTL7A (via N-terminus). Heterodimer with ACTL7A; the heterodimer interacts with ENAH to form a heterotrimer.5 Publications

Protein-protein interaction databases

BioGridi117572. 33 interactions.
IntActiQ9UGI8. 18 interactions.
MINTiMINT-2821159.
STRINGi9606.ENSP00000350937.

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni302 – 3043Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi313 – 3164Combined sources
Beta strandi319 – 3213Combined sources
Helixi323 – 3253Combined sources
Turni329 – 3313Combined sources
Beta strandi338 – 3436Combined sources
Beta strandi346 – 3494Combined sources
Helixi350 – 3567Combined sources
Turni362 – 3643Combined sources
Beta strandi365 – 3684Combined sources
Beta strandi374 – 3774Combined sources
Beta strandi380 – 3834Combined sources
Turni384 – 3874Combined sources
Turni392 – 3943Combined sources
Beta strandi404 – 4063Combined sources
Beta strandi409 – 4135Combined sources
Helixi414 – 4185Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IYBX-ray2.35E/F/G/H357-421[»]
2XQNX-ray2.62T296-421[»]
ProteinModelPortaliQ9UGI8.
SMRiQ9UGI8. Positions 258-421.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UGI8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 199108PETPROSITE-ProRule annotationAdd
BLAST
Domaini234 – 29764LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini299 – 35961LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini362 – 42160LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 4625Cys-richAdd
BLAST

Domaini

The N-terminal and the C-terminal halves of the protein can associate with each other, thereby hindering interactions with ZYX.1 Publication

Sequence similaritiesi

Belongs to the prickle / espinas / testin family.Curated
Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation
Contains 1 PET domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG272178.
GeneTreeiENSGT00550000074438.
HOGENOMiHOG000231628.
HOVERGENiHBG001038.
InParanoidiQ9UGI8.
OMAiNNFNWHA.
OrthoDBiEOG7P8P7M.
PhylomeDBiQ9UGI8.
TreeFamiTF313265.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR010442. PET_domain.
IPR027683. Testin.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24211:SF1. PTHR24211:SF1. 1 hit.
PfamiPF00412. LIM. 2 hits.
PF06297. PET. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS51303. PET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UGI8-1) [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
MDLENKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE
60 70 80 90 100
HDVLLSNEED RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA
110 120 130 140 150
KKNVSINTVT YEWAPPVQNQ ALARQYMQML PKEKQPVAGS EGAQYRKKQL
160 170 180 190 200
AKQLPAHDQD PSKCHELSPR EVKEMEQFVK KYKSEALGVG DVKLPCEMDA
210 220 230 240 250
QGPKQMNIPG GDRSTPAAVG AMEDKSAEHK RTQYSCYCCK LSMKEGDPAI
260 270 280 290 300
YAERAGYDKL WHPACFVCST CHELLVDMIY FWKNEKLYCG RHYCDSEKPR
310 320 330 340 350
CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDSILAGEIY VMVNDKPVCK
360 370 380 390 400
PCYVKNHAVV CQGCHNAIDP EVQRVTYNNF SWHASTECFL CSCCSKCLIG
410 420
QKFMPVEGMV FCSVECKKRM S
Length:421
Mass (Da):47,996
Last modified:May 1, 2000 - v1
Checksum:iAB9FF6669C50D492
GO
Isoform 2 (identifier: Q9UGI8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.

Show »
Length:412
Mass (Da):46,910
Checksum:iC97A6D97364B3569
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321K → E in BAB13846 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211A → V.
Corresponds to variant rs2272193 [ dbSNP | Ensembl ].
VAR_050170

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99Missing in isoform 2. 2 PublicationsVSP_003122

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF260225 Genomic DNA. Translation: AAG17635.1.
AF260225 Genomic DNA. Translation: AAG17636.1.
AF245356 mRNA. Translation: AAG17612.1.
AF245357 mRNA. Translation: AAG17613.1.
AJ250865 mRNA. Translation: CAB65119.1.
AK021575 mRNA. Translation: BAB13846.1.
AK291802 mRNA. Translation: BAF84491.1.
AC073130 Genomic DNA. Translation: AAQ93367.1.
CH236947 Genomic DNA. Translation: EAL24365.1.
BC001451 mRNA. Translation: AAH01451.1.
CCDSiCCDS5763.1. [Q9UGI8-1]
CCDS5764.1. [Q9UGI8-2]
RefSeqiNP_056456.1. NM_015641.3. [Q9UGI8-1]
NP_690042.1. NM_152829.2. [Q9UGI8-2]
UniGeneiHs.592286.
Hs.664957.

Genome annotation databases

EnsembliENST00000358204; ENSP00000350937; ENSG00000135269.
ENST00000393481; ENSP00000377121; ENSG00000135269. [Q9UGI8-2]
GeneIDi26136.
KEGGihsa:26136.
UCSCiuc003vho.3. human. [Q9UGI8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF260225 Genomic DNA. Translation: AAG17635.1.
AF260225 Genomic DNA. Translation: AAG17636.1.
AF245356 mRNA. Translation: AAG17612.1.
AF245357 mRNA. Translation: AAG17613.1.
AJ250865 mRNA. Translation: CAB65119.1.
AK021575 mRNA. Translation: BAB13846.1.
AK291802 mRNA. Translation: BAF84491.1.
AC073130 Genomic DNA. Translation: AAQ93367.1.
CH236947 Genomic DNA. Translation: EAL24365.1.
BC001451 mRNA. Translation: AAH01451.1.
CCDSiCCDS5763.1. [Q9UGI8-1]
CCDS5764.1. [Q9UGI8-2]
RefSeqiNP_056456.1. NM_015641.3. [Q9UGI8-1]
NP_690042.1. NM_152829.2. [Q9UGI8-2]
UniGeneiHs.592286.
Hs.664957.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IYBX-ray2.35E/F/G/H357-421[»]
2XQNX-ray2.62T296-421[»]
ProteinModelPortaliQ9UGI8.
SMRiQ9UGI8. Positions 258-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117572. 33 interactions.
IntActiQ9UGI8. 18 interactions.
MINTiMINT-2821159.
STRINGi9606.ENSP00000350937.

PTM databases

PhosphoSiteiQ9UGI8.

Polymorphism and mutation databases

BioMutaiTES.
DMDMi17380320.

Proteomic databases

MaxQBiQ9UGI8.
PaxDbiQ9UGI8.
PeptideAtlasiQ9UGI8.
PRIDEiQ9UGI8.

Protocols and materials databases

DNASUi26136.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358204; ENSP00000350937; ENSG00000135269.
ENST00000393481; ENSP00000377121; ENSG00000135269. [Q9UGI8-2]
GeneIDi26136.
KEGGihsa:26136.
UCSCiuc003vho.3. human. [Q9UGI8-1]

Organism-specific databases

CTDi26136.
GeneCardsiGC07P115850.
HGNCiHGNC:14620. TES.
HPAiCAB003690.
HPA015269.
HPA018123.
MIMi606085. gene.
neXtProtiNX_Q9UGI8.
PharmGKBiPA37906.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG272178.
GeneTreeiENSGT00550000074438.
HOGENOMiHOG000231628.
HOVERGENiHBG001038.
InParanoidiQ9UGI8.
OMAiNNFNWHA.
OrthoDBiEOG7P8P7M.
PhylomeDBiQ9UGI8.
TreeFamiTF313265.

Miscellaneous databases

ChiTaRSiTES. human.
EvolutionaryTraceiQ9UGI8.
GeneWikiiTestin.
GenomeRNAii26136.
NextBioi48175.
PROiQ9UGI8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UGI8.
CleanExiHS_TES.
ExpressionAtlasiQ9UGI8. baseline and differential.
GenevisibleiQ9UGI8. HS.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR010442. PET_domain.
IPR027683. Testin.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24211:SF1. PTHR24211:SF1. 1 hit.
PfamiPF00412. LIM. 2 hits.
PF06297. PET. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS51303. PET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the human TESTIN gene localized in the FRA7G region at 7q31.2."
    Tatarelli C., Linnenbach A., Mimori K., Croce C.M.
    Genomics 68:1-12(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
  2. "The TES gene at 7q31.1 is methylated in tumours and encodes a novel growth-suppressing LIM domain protein."
    Tobias E.S., Hurlstone A.F.L., MacKenzie E., McFarlane R., Black D.M.
    Oncogene 20:2844-2853(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Embryo and Prostate.
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  7. "The conformational state of Tes regulates its zyxin-dependent recruitment to focal adhesions."
    Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N., Koecher T., Piddini E., Griffiths G., Way M.
    J. Cell Biol. 161:33-39(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-391, INTERACTION WITH ENAH; ZYX; VASP; ACTIN FIBERS; ALPHA-ACTININ AND PXN.
  8. "TES is a novel focal adhesion protein with a role in cell spreading."
    Coutts A.S., MacKenzie E., Griffith E., Black D.M.
    J. Cell Sci. 116:897-906(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZYX; GRIP1; ENAH AND TALIN, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Human ALKBH4 interacts with proteins associated with transcription."
    Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
    PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALKBH4.
  11. "Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding."
    Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J., McDonald N.Q., Way M.
    Mol. Cell 28:1071-1082(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 357-421 IN COMPLEX WITH ZINC IONS AND ENAH.
  12. "Molecular recognition of the Tes LIM2-3 domains by the actin-related protein Arp7A."
    Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E., Garvalov B.K., McDonald N.Q., Way M.
    J. Biol. Chem. 286:11543-11554(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 296-421 IN COMPLEX WITH ZINC IONS; ENAH AND ACTL7A, MUTAGENESIS OF CYS-328, SUBUNIT.

Entry informationi

Entry nameiTES_HUMAN
AccessioniPrimary (citable) accession number: Q9UGI8
Secondary accession number(s): A4D0U6, Q9GZQ1, Q9HAJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 136 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.