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D3ZKB9 (TSH3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Teashirt homolog 3
Alternative name(s):
Zinc finger protein 537
Gene names
Name:Tshz3
Synonyms:Zfp537
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1072 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator involved in developmental processes. Function in association with APBB1, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. TSHZ3-mediated transcription repression involves the recruitment of histone deacetylases HDAC1 and HDAC2. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Regulates the development of neurons involved in both respiratory rhythm and airflow control. Promotes maintenance of nucleus ambiguus (nA) motoneurons, which govern upper airway function, and establishes a respiratory rhythm generator (RRG) activity compatible with survival at birth. Involved in the differentiation of the proximal uretic smooth muscle cells during developmental processes. Involved in the up-regulation of myocardin, that directs the expression of smooth muscle cells in the proximal ureter By similarity.

Subunit structure

Interacts (via N-terminus) with HDAC1 and HDAC2; the interaction is direct. Found in a trimeric complex with APBB1 and HDAC1; the interaction between HDAC1 and APBB1 is mediated by TSHZ3 By similarity. Interacts (via homeobox domain) with APBB1 (via PID domain 1). Ref.2

Subcellular location

Nucleus. Cell projectiongrowth cone. Note: Colocalizes with APBB1 in the nucleus By similarity. Colocalizes with APBB1 in axonal growth cone. Ref.2

Tissue specificity

Expressed in cortical neurons. Ref.2

Sequence similarities

Belongs to the teashirt C2H2-type zinc-finger protein family.

Contains 5 C2H2-type zinc fingers.

Contains 1 homeobox DNA-binding domain.

Sequence caution

The sequence EDM07600.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell projection
Nucleus
   DomainHomeobox
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processin utero embryonic development

Inferred from electronic annotation. Source: Ensembl

kidney morphogenesis

Inferred from electronic annotation. Source: Ensembl

kidney smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

metanephros development

Inferred from electronic annotation. Source: Ensembl

musculoskeletal movement

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of respiratory gaseous exchange by neurological system process

Inferred from sequence or structural similarity. Source: UniProtKB

sensory perception of touch

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ureter smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

ureteric peristalsis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentgrowth cone

Inferred from direct assay Ref.2. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10721072Teashirt homolog 3
PRO_0000399476

Regions

Zinc finger204 – 22825C2H2-type 1
Zinc finger265 – 28925C2H2-type 2
Zinc finger376 – 40025C2H2-type 3; atypical
DNA binding882 – 95271Homeobox; atypical
Zinc finger967 – 98923C2H2-type 4
Zinc finger1032 – 105524C2H2-type 5
Compositional bias131 – 15424Ser-rich

Amino acid modifications

Modified residue6721Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
D3ZKB9 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 9CB7824517771F35

FASTA1,072117,463
        10         20         30         40         50         60 
MAAYVSDELK AAALVEDDIE PEEQVADGEP SAKYMCPEKE LSKACPSYQN SPAAEFSSHE 

        70         80         90        100        110        120 
MDSESHISET SDRMADFESS SIKNEEETKE VQVPLEDTTV SDSLEQMKAV YNNFLSNSYW 

       130        140        150        160        170        180 
SNLNLNLHQP SSENNGGGSS SSSSSSSSSC GSGSFDWHQS AMAKTLQQVS QNRMLPEPSL 

       190        200        210        220        230        240 
FSTVQLYRQS SKLYGSIFTG ASKFRCKDCS AAYDTLVELT VHMNETGHYR DDNHETDNNN 

       250        260        270        280        290        300 
PKRWSKPRKR SLLEMEGKED AQKVLKCMYC GHSFESLQDL SVHMIKTKHY QKVPLKEPVT 

       310        320        330        340        350        360 
PVAAKIIPAA RKKPSLELEL PSSPDSTGGT PKATLSDASD ALQKNSNPYI TPNNRYGHQN 

       370        380        390        400        410        420 
GASYAWHFEA RKSQILKCME CGSSHDTLQE LTAHMMVTGH FIKVTNSAMK KGKPIMETPV 

       430        440        450        460        470        480 
TPTITTLLDE KVQSVPLAAT TFTSPSNTPA SVSPKLTVEI KKEVDKEKAV LDEKPKEKEK 

       490        500        510        520        530        540 
ASEEEEKYDI SSKYHYLTEN DLEESPKGGL DILKSLENTV TSAINKAQNG TPSWGGYPSI 

       550        560        570        580        590        600 
HAAYQLPNMM KLSLGSSGKS TPLKPMFGNS EIVSPTKTQT LVSPPSSQTS PMPKTNFHAM 

       610        620        630        640        650        660 
EELVKKVTEK VAKVEEKMKE PDSKLSPPKR ATPSPCSSEQ SEPIKMEASS GSGFKSQENS 

       670        680        690        700        710        720 
PSPPRDVCKE ASPSAEPVEN GKELVKPLSG GSLSGSTAII TDHPPEQPFV NPLSALQSVM 

       730        740        750        760        770        780 
NIHLGKAAKP SLPALDPMSM LFKMSNSLAE KAAVATPPPL QAKKAEHLDR YFYHVNNDQP 

       790        800        810        820        830        840 
IDLTKGKSDK GCSLGSGLLS PTSTSPATSS STVTTAKTSA VVSFMSNSPL RENALSDISD 

       850        860        870        880        890        900 
MLKNLTESHT SKSSTPSSIS EKSDIDGATL EEAEESTPAQ KRKGRQSNWN PQHLLILQAQ 

       910        920        930        940        950        960 
FAASLRQTSE GKYIMSDLSP QERMHISRFT GLSMTTISHW LANVKYQLRR TGGTKFLKNL 

       970        980        990       1000       1010       1020 
DTGHPVFFCN DCASQIRTPS TYISHLESHL GFRLRDLSKL STEQINNQIA QTKSPSEKMV 

      1030       1040       1050       1060       1070 
TSSPEEDLGT TYQCKLCNRT FASKHAVKLH LSKTHGKSPE DHLLFVSELE KQ 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4."
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.
PLoS ONE 4:E5071-E5071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APBB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Web resources

Protein Spotlight

Life's first breath - Issue 122 of October 2010

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH473979 Genomic DNA. Translation: EDM07600.1. Different initiation.
RefSeqNP_001100976.1. NM_001107506.1.
XP_006228956.1. XM_006228894.1.
XP_006228957.1. XM_006228895.1.
UniGeneRn.9411.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID308523.
KEGGrno:308523.
UCSCRGD:1306322. rat.

Organism-specific databases

CTD57616.
RGD1306322. Tshz3.

Phylogenomic databases

KOK09236.
OrthoDBEOG7NPFSF.
PhylomeDBD3ZKB9.
TreeFamTF328447.

Family and domain databases

InterProIPR001356. Homeobox_dom.
IPR027008. Teashirt_fam.
IPR026810. Tshz3.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERPTHR12487. PTHR12487. 1 hit.
PTHR12487:SF5. PTHR12487:SF5. 1 hit.
SMARTSM00389. HOX. 1 hit.
SM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEPS50071. HOMEOBOX_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio659069.
PROD3ZKB9.

Entry information

Entry nameTSH3_RAT
AccessionPrimary (citable) accession number: D3ZKB9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 35 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries