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P82094 (TMF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TATA element modulatory factor

Short name=TMF
Alternative name(s):
Androgen receptor coactivator 160 kDa protein
Androgen receptor-associated protein of 160 kDa
Gene names
Name:TMF1
Synonyms:ARA160
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1093 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP). Ref.1 Ref.2 Ref.8 Ref.9

Subunit structure

Interacts with TRNP1; may regulate TRNP1 proteasomal degradation By similarity. Component of the SNF/SWI transcription factor complexes. Interacts with RAB6A. Interacts with STAT3 and FER. Interacts with TCEB1. Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm. Nucleus. Golgi apparatus membrane. Note: Concentrated at the budding structures localized at the tips of cisternae. Ref.7 Ref.9

Induction

Down-regulated in malignant brain tumors. Ref.8

Domain

The Elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV].

Post-translational modification

Phosphorylated by FER By similarity.

Sequence caution

The sequence AAD54608.1 differs from that shown. Reason: Frameshift at positions 969, 971, 975 and 985.

The sequence BAD92346.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandDNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig cell differentiation

Inferred from electronic annotation. Source: Ensembl

acrosome assembly

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

defense response to bacterium

Inferred from electronic annotation. Source: Ensembl

luteinizing hormone secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine production

Inferred from electronic annotation. Source: Ensembl

positive regulation of testosterone secretion

Inferred from electronic annotation. Source: Ensembl

regulation of proteasomal protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement Ref.2. Source: ProtInc

sperm motility

Inferred from electronic annotation. Source: Ensembl

spermatid nucleus differentiation

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 20195357. Source: IntAct

transcription cofactor activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NR3C1P041503EBI-949763,EBI-493507

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P82094-1)

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: P82094-2)

The sequence of this isoform differs from the canonical sequence as follows:
     449-449: K → KVTL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10931093TATA element modulatory factor
PRO_0000072589

Regions

Region333 – 34210Interaction with Elongin BC complex
Coiled coil439 – 922484 Potential
Coiled coil984 – 1092109 Potential

Amino acid modifications

Modified residue721Phosphoserine Ref.11
Modified residue771Phosphoserine Ref.11 Ref.13
Modified residue1121Phosphoserine Ref.11
Modified residue2171Phosphoserine Ref.14
Modified residue3281Phosphoserine Ref.11 Ref.13
Modified residue3381Phosphoserine Ref.11
Modified residue3441Phosphoserine Ref.11 Ref.13 Ref.14 Ref.16
Modified residue9251Phosphoserine Ref.11

Natural variations

Alternative sequence4491K → KVTL in isoform 2.
VSP_037411
Natural variant4301Q → E.
Corresponds to variant rs35447207 [ dbSNP | Ensembl ].
VAR_051439
Natural variant4481C → Y.
Corresponds to variant rs34428015 [ dbSNP | Ensembl ].
VAR_051440
Natural variant6821Q → R.
Corresponds to variant rs3736422 [ dbSNP | Ensembl ].
VAR_051441
Natural variant7981D → H.
Corresponds to variant rs1532918 [ dbSNP | Ensembl ].
VAR_024284

Experimental info

Mutagenesis333 – 3353SLD → AAA: Strongly reduced the ubiquitination directing activity of the protein. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 566BBE3EC36EF11C

FASTA1,093122,842
        10         20         30         40         50         60 
MSWFNASQLS SFAKQALSQA QKSIDRVLDI QEEEPSIWAE TIPYGEPGIS SPVSGGWDTS 

        70         80         90        100        110        120 
TWGLKSNTEP QSPPIASPKA ITKPVRRTVV DESENFFSAF LSPTDVQTIQ KSPVVSKPPA 

       130        140        150        160        170        180 
KSQRPEEEVK SSLHESLHIG QSRTPETTES QVKDSSLCVS GETLAAGTSS PKTEGKHEET 

       190        200        210        220        230        240 
VNKESDMKVP TVSLKVSESV IDVKTTMESI SNTSTQSLTA ETKDIALEPK EQKHEDRQSN 

       250        260        270        280        290        300 
TPSPPVSTFS SGTSTTSDIE VLDHESVISE SSASSRQETT DSKSSLHLMQ TSFQLLSASA 

       310        320        330        340        350        360 
CPEYNRLDDF QKLTESCCSS DAFERIDSFS VQSLDSRSVS EINSDDELSG KGYALVPIIV 

       370        380        390        400        410        420 
NSSTPKSKTV ESAEGKSEEV NETLVIPTEE AEMEESGRSA TPVNCEQPDI LVSSTPINEG 

       430        440        450        460        470        480 
QTVLDKVAEQ CEPAESQPEA LSEKEDVCKT VEFLNEKLEK REAQLLSLSK EKALLEEAFD 

       490        500        510        520        530        540 
NLKDEMFRVK EESSSISSLK DEFTQRIAEA EKKVQLACKE RDAAKKEIKN IKEELATRLN 

       550        560        570        580        590        600 
SSETADLLKE KDEQIRGLME EGEKLSKQQL HNSNIIKKLR AKDKENENMV AKLNKKVKEL 

       610        620        630        640        650        660 
EEELQHLKQV LDGKEEVEKQ HRENIKKLNS MVERQEKDLG RLQVDMDELE EKNRSIQAAL 

       670        680        690        700        710        720 
DSAYKELTDL HKANAAKDSE AQEAALSREM KAKEELSAAL EKAQEEARQQ QETLAIQVGD 

       730        740        750        760        770        780 
LRLALQRTEQ AAARKEDYLR HEIGELQQRL QEAENRNQEL SQSVSSTTRP LLRQIENLQA 

       790        800        810        820        830        840 
TLGSQTSSWE KLEKNLSDRL GESQTLLAAA VERERAATEE LLANKIQMSS MESQNSLLRQ 

       850        860        870        880        890        900 
ENSRFQAQLE SEKNRLCKLE DENNRYQVEL ENLKDEYVRT LEETRKEKTL LNSQLEMERM 

       910        920        930        940        950        960 
KVEQERKKAI FTQETIKEKE RKPFSVSSTP TMSRSSSISG VDMAGLQTSF LSQDESHDHS 

       970        980        990       1000       1010       1020 
FGPMPISANG SNLYDAVRMG AGSSIIENLQ SQLKLREGEI THLQLEIGNL EKTRSIMAEE 

      1030       1040       1050       1060       1070       1080 
LVKLTNQNDE LEEKVKEIPK LRTQLRDLDQ RYNTILQMYG EKAEEAEELR LDLEDVKNMY 

      1090 
KTQIDELLRQ SLS 

« Hide

Isoform 2 [UniParc].

Checksum: A539A619EE47842D
Show »

FASTA1,096123,155

References

« Hide 'large scale' references
[1]"Cloning and chromosomal mapping of a human immunodeficiency virus 1 'TATA' element modulatory factor."
Garcia J.A., Ou S.-H.I., Wu F., Lusis A.J., Sparkes R.S., Gaynor R.B.
Proc. Natl. Acad. Sci. U.S.A. 89:9372-9376(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
Tissue: Cervix carcinoma.
[2]"Isolation and characterization of ARA160 as the first androgen receptor N-terminal-associated coactivator in human prostate cells."
Hsiao P.W., Chang C.
J. Biol. Chem. 274:22373-22379(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[7]"A putative nuclear receptor coactivator (TMF/ARA160) associates with hbrm/hSNF2 alpha and BRG-1/hSNF2 beta and localizes in the Golgi apparatus."
Mori K., Kato H.
FEBS Lett. 520:127-132(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN SWI/SNF COMPLEXES.
[8]"TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3."
Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.
Oncogene 23:8908-8919(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 333-LEU--ASP-335, INTERACTION WITH TCEB1 AND STAT3, INDUCTION.
[9]"Functional involvement of TMF/ARA160 in Rab6-dependent retrograde membrane traffic."
Yamane J., Kubo A., Nakayama K., Yuba-Kubo A., Katsuno T., Tsukita S., Tsukita S.
Exp. Cell Res. 313:3472-3485(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB6A.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-77; SER-112; SER-328; SER-338; SER-344 AND SER-925, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-328 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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-217 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L01042 mRNA. Translation: AAD54608.1. Frameshift.
AB209109 mRNA. Translation: BAD92346.1. Different initiation.
AC109587 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65468.1.
BC117418 mRNA. Translation: AAI17419.1.
BC126123 mRNA. Translation: AAI26124.1.
BC143840 mRNA. Translation: AAI43841.1.
CCDSCCDS43105.1. [P82094-1]
PIRA47212.
RefSeqNP_009045.2. NM_007114.2. [P82094-1]
UniGeneHs.267632.

3D structure databases

ProteinModelPortalP82094.
SMRP82094. Positions 473-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112965. 9 interactions.
DIPDIP-5933N.
IntActP82094. 6 interactions.
MINTMINT-2863632.
STRING9606.ENSP00000381567.

PTM databases

PhosphoSiteP82094.

Polymorphism databases

DMDM218511858.

Proteomic databases

MaxQBP82094.
PaxDbP82094.
PRIDEP82094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398559; ENSP00000381567; ENSG00000144747. [P82094-1]
ENST00000543976; ENSP00000438706; ENSG00000144747. [P82094-2]
GeneID7110.
KEGGhsa:7110.
UCSCuc003dnn.3. human. [P82094-1]
uc011bfx.2. human. [P82094-2]

Organism-specific databases

CTD7110.
GeneCardsGC03M069068.
HGNCHGNC:11870. TMF1.
HPAHPA008729.
MIM601126. gene.
neXtProtNX_P82094.
PharmGKBPA36571.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG127593.
HOGENOMHOG000154639.
HOVERGENHBG016599.
OMASWFNASQ.
OrthoDBEOG7X0VHV.
PhylomeDBP82094.
TreeFamTF329420.

Gene expression databases

ArrayExpressP82094.
BgeeP82094.
CleanExHS_TMF1.
GenevestigatorP82094.

Family and domain databases

InterProIPR022092. TMF_DNA-bd.
IPR022091. TMF_TATA-bd.
[Graphical view]
PfamPF12329. TMF_DNA_bd. 1 hit.
PF12325. TMF_TATA_bd. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTMF1. human.
GeneWikiTMF1.
GenomeRNAi7110.
NextBio27831.
PROP82094.
SOURCESearch...

Entry information

Entry nameTMF1_HUMAN
AccessionPrimary (citable) accession number: P82094
Secondary accession number(s): B7ZLJ2, Q17R87, Q59GK0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM