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Q10587

- TEF_HUMAN

UniProt

Q10587 - TEF_HUMAN

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Protein

Thyrotroph embryonic factor

Gene
TEF, KIAA1655
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcription factor that binds to and transactivates the TSHB promoter. Binds to a minimal DNA-binding sequence 5'-[TC][AG][AG]TTA[TC][AG]-3'.

GO - Molecular functioni

  1. double-stranded DNA binding Source: Ensembl
  2. sequence-specific DNA binding Source: Ensembl
  3. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  2. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  3. rhythmic process Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiQ10587.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyrotroph embryonic factor
Gene namesi
Name:TEF
Synonyms:KIAA1655
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:11722. TEF.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Thyrotroph embryonic factorPRO_0000076512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ10587.
PRIDEiQ10587.

PTM databases

PhosphoSiteiQ10587.

Expressioni

Inductioni

Accumulates according to a robust circadian rhythm By similarity.

Gene expression databases

ArrayExpressiQ10587.
BgeeiQ10587.
CleanExiHS_TEF.
GenevestigatoriQ10587.

Organism-specific databases

HPAiHPA028868.

Interactioni

Subunit structurei

Binds DNA as a homodimer or a heterodimer. Can form a heterodimer with DBP.

Protein-protein interaction databases

IntActiQ10587. 29 interactions.
STRINGi9606.ENSP00000266304.

Structurei

3D structure databases

ProteinModelPortaliQ10587.
SMRiQ10587. Positions 232-287.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini233 – 29664bZIPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 25521Basic motif By similarityAdd
BLAST
Regioni256 – 2638Leucine-zipper By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi166 – 21752Pro-rich (proline/acidic region (PAR))Add
BLAST

Sequence similaritiesi

Belongs to the bZIP family. PAR subfamily.

Phylogenomic databases

eggNOGiNOG323431.
HOVERGENiHBG004983.
InParanoidiQ10587.
KOiK09058.
OMAiCKNIVSK.
OrthoDBiEOG712TZJ.
PhylomeDBiQ10587.
TreeFamiTF315869.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q10587-1) [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

MSDAGGGKKP PVDPQAGPGP GPGRAAGERG LSGSFPLVLK KLMENPPREA    50
RLDKEKGKEK LEEDEAAAAS TMAVSASLMP PIWDKTIPYD GESFHLEYMD 100
LDEFLLENGI PASPTHLAHN LLLPVAELEG KESASSSTAS PPSSSTAIFQ 150
PSETVSSTES SLEKERETPS PIDPNCVEVD VNFNPDPADL VLSSVPGGEL 200
FNPRKHKFAE EDLKPQPMIK KAKKVFVPDE QKDEKYWTRR KKNNVAAKRS 250
RDARRLKENQ ITIRAAFLEK ENTALRTEVA ELRKEVGKCK TIVSKYETKY 300
GPL 303
Length:303
Mass (Da):33,248
Last modified:August 16, 2004 - v3
Checksum:i4A87B7BFA7248C6F
GO
Isoform 2 (identifier: Q10587-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: MSDAGGGKKPPVDPQAGPGPGPGRAAGERGLSGSFPLVLKKLMENPPREARL → MDMPEVLKSLLEHSLPWPEKRT

Note: No experimental confirmation available.

Show »
Length:273
Mass (Da):30,635
Checksum:iB1A956839CBC4AC4
GO

Sequence cautioni

The sequence AAA81373.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5252MSDAG…REARL → MDMPEVLKSLLEHSLPWPEK RT in isoform 2. VSP_041376Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541K → E in AAA81373. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U06935 mRNA. Translation: AAA81373.1. Different initiation.
U44059 mRNA. Translation: AAB06497.1.
CR456592 mRNA. Translation: CAG30478.1.
CR541827 mRNA. Translation: CAG46626.1.
AK091916 mRNA. Translation: BAG52441.1.
AK314906 mRNA. Translation: BAG37419.1.
AL035659 Genomic DNA. Translation: CAI23516.1.
AL035659 Genomic DNA. Translation: CAQ08872.1.
CH471095 Genomic DNA. Translation: EAW60430.1.
CH471095 Genomic DNA. Translation: EAW60431.1.
BC039258 mRNA. Translation: AAH39258.1.
BC042476 mRNA. Translation: AAH42476.1.
BX537848 mRNA. Translation: CAD97856.1.
CCDSiCCDS14014.1. [Q10587-1]
CCDS46716.1. [Q10587-2]
PIRiG02360.
RefSeqiNP_001138870.1. NM_001145398.2. [Q10587-2]
NP_003207.1. NM_003216.3. [Q10587-1]
UniGeneiHs.181159.

Genome annotation databases

EnsembliENST00000266304; ENSP00000266304; ENSG00000167074. [Q10587-1]
ENST00000406644; ENSP00000385256; ENSG00000167074. [Q10587-2]
GeneIDi7008.
KEGGihsa:7008.
UCSCiuc003azx.4. human. [Q10587-2]
uc003azy.4. human. [Q10587-1]

Polymorphism databases

DMDMi51338730.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U06935 mRNA. Translation: AAA81373.1 . Different initiation.
U44059 mRNA. Translation: AAB06497.1 .
CR456592 mRNA. Translation: CAG30478.1 .
CR541827 mRNA. Translation: CAG46626.1 .
AK091916 mRNA. Translation: BAG52441.1 .
AK314906 mRNA. Translation: BAG37419.1 .
AL035659 Genomic DNA. Translation: CAI23516.1 .
AL035659 Genomic DNA. Translation: CAQ08872.1 .
CH471095 Genomic DNA. Translation: EAW60430.1 .
CH471095 Genomic DNA. Translation: EAW60431.1 .
BC039258 mRNA. Translation: AAH39258.1 .
BC042476 mRNA. Translation: AAH42476.1 .
BX537848 mRNA. Translation: CAD97856.1 .
CCDSi CCDS14014.1. [Q10587-1 ]
CCDS46716.1. [Q10587-2 ]
PIRi G02360.
RefSeqi NP_001138870.1. NM_001145398.2. [Q10587-2 ]
NP_003207.1. NM_003216.3. [Q10587-1 ]
UniGenei Hs.181159.

3D structure databases

ProteinModelPortali Q10587.
SMRi Q10587. Positions 232-287.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q10587. 29 interactions.
STRINGi 9606.ENSP00000266304.

PTM databases

PhosphoSitei Q10587.

Polymorphism databases

DMDMi 51338730.

Proteomic databases

PaxDbi Q10587.
PRIDEi Q10587.

Protocols and materials databases

DNASUi 7008.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000266304 ; ENSP00000266304 ; ENSG00000167074 . [Q10587-1 ]
ENST00000406644 ; ENSP00000385256 ; ENSG00000167074 . [Q10587-2 ]
GeneIDi 7008.
KEGGi hsa:7008.
UCSCi uc003azx.4. human. [Q10587-2 ]
uc003azy.4. human. [Q10587-1 ]

Organism-specific databases

CTDi 7008.
GeneCardsi GC22P041763.
HGNCi HGNC:11722. TEF.
HPAi HPA028868.
MIMi 188595. gene.
neXtProti NX_Q10587.
PharmGKBi PA36439.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG323431.
HOVERGENi HBG004983.
InParanoidi Q10587.
KOi K09058.
OMAi CKNIVSK.
OrthoDBi EOG712TZJ.
PhylomeDBi Q10587.
TreeFami TF315869.

Enzyme and pathway databases

SignaLinki Q10587.

Miscellaneous databases

ChiTaRSi TEF. human.
GeneWikii TEF_(gene).
GenomeRNAii 7008.
NextBioi 27374.
PROi Q10587.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q10587.
Bgeei Q10587.
CleanExi HS_TEF.
Genevestigatori Q10587.

Family and domain databases

InterProi IPR004827. bZIP.
[Graphical view ]
Pfami PF07716. bZIP_2. 1 hit.
[Graphical view ]
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Chromosomal localization and cDNA cloning of the human DBP and TEF genes."
    Khatib Z.A., Inaba T., Valentine M., Look A.T.
    Genomics 23:344-351(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The proto-oncogene HLF and the related basic leucine zipper protein TEF display highly similar DNA-binding and transcriptional regulatory properties."
    Hunger S.P., Li S., Fall M.Z., Naumovski L., Cleary M.L.
    Blood 87:4607-4617(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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: Cerebellum and Kidney.
  6. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Brain.
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 164-303.
    Tissue: Retina.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiTEF_HUMAN
AccessioniPrimary (citable) accession number: Q10587
Secondary accession number(s): B0QYS8
, B2RC22, Q15729, Q7Z3J7, Q8IU94, Q96TG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 132 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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