P82094 (TMF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1093 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Componement 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Golgi apparatus Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	DNA-binding
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Traceable author statement Ref.2. Source: ProtInc transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW transcription cofactor activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NR3C1	P04150	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1093	1093	TATA element modulatory factor		PRO_0000072589
Regions
	Region	333 – 342	10	Interaction with Elongin BC complex
	Coiled coil	439 – 922	484	Potential
	Coiled coil	984 – 1092	109	Potential
Amino acid modifications
	Modified residue	72	1	Phosphoserine Ref.11
	Modified residue	77	1	Phosphoserine Ref.11 Ref.12
	Modified residue	112	1	Phosphoserine Ref.11
	Modified residue	217	1	Phosphoserine Ref.13
	Modified residue	328	1	Phosphoserine Ref.11 Ref.12
	Modified residue	338	1	Phosphoserine Ref.11
	Modified residue	344	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15
	Modified residue	415	1	Phosphothreonine By similarity
	Modified residue	925	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	449	1	K → KVTL in isoform 2.		VSP_037411
	Natural variant	430	1	Q → E. Corresponds to variant rs35447207 [ dbSNP | Ensembl ].		VAR_051439
	Natural variant	448	1	C → Y. Corresponds to variant rs34428015 [ dbSNP | Ensembl ].		VAR_051440
	Natural variant	682	1	Q → R. Corresponds to variant rs3736422 [ dbSNP | Ensembl ].		VAR_051441
	Natural variant	798	1	D → H. Corresponds to variant rs1532918 [ dbSNP | Ensembl ].		VAR_024284
Experimental info
	Mutagenesis	333 – 335	3	SLD → AAA: Strongly reduced the ubiquitination directing activity of the protein. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 566BBE3EC36EF11C	FASTA	1,093	122,842
	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
	Isoform 2 [UniParc]. Checksum: A539A619EE47842D	FASTA	1,096	123,155
	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 LSEKEDVCKV TLTVEFLNEK LEKREAQLLS LSKEKALLEE 490 500 510 520 530 540 AFDNLKDEMF RVKEESSSIS SLKDEFTQRI AEAEKKVQLA CKERDAAKKE IKNIKEELAT 550 560 570 580 590 600 RLNSSETADL LKEKDEQIRG LMEEGEKLSK QQLHNSNIIK KLRAKDKENE NMVAKLNKKV 610 620 630 640 650 660 KELEEELQHL KQVLDGKEEV EKQHRENIKK LNSMVERQEK DLGRLQVDMD ELEEKNRSIQ 670 680 690 700 710 720 AALDSAYKEL TDLHKANAAK DSEAQEAALS REMKAKEELS AALEKAQEEA RQQQETLAIQ 730 740 750 760 770 780 VGDLRLALQR TEQAAARKED YLRHEIGELQ QRLQEAENRN QELSQSVSST TRPLLRQIEN 790 800 810 820 830 840 LQATLGSQTS SWEKLEKNLS DRLGESQTLL AAAVERERAA TEELLANKIQ MSSMESQNSL 850 860 870 880 890 900 LRQENSRFQA QLESEKNRLC KLEDENNRYQ VELENLKDEY VRTLEETRKE KTLLNSQLEM 910 920 930 940 950 960 ERMKVEQERK KAIFTQETIK EKERKPFSVS STPTMSRSSS ISGVDMAGLQ TSFLSQDESH 970 980 990 1000 1010 1020 DHSFGPMPIS ANGSNLYDAV RMGAGSSIIE NLQSQLKLRE GEITHLQLEI GNLEKTRSIM 1030 1040 1050 1060 1070 1080 AEELVKLTNQ NDELEEKVKE IPKLRTQLRD LDQRYNTILQ MYGEKAEEAE ELRLDLEDVK 1090 NMYKTQIDEL LRQSLS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00010586. IPI00930399.
PIR	A47212.
RefSeq	NP_009045.2. NM_007114.2.
UniGene	Hs.267632.
3D structure databases
ProteinModelPortal	P82094.
SMR	P82094. Positions 446-491.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5933N.
IntAct	P82094. 5 interactions.
MINT	MINT-2863632.
STRING	9606.ENSP00000381567.
PTM databases
PhosphoSite	P82094.
Polymorphism databases
DMDM	218511858.
Proteomic databases
PaxDb	P82094.
PRIDE	P82094.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000398559; ENSP00000381567; ENSG00000144747. ENST00000543976; ENSP00000438706; ENSG00000144747.
GeneID	7110.
KEGG	hsa:7110.
UCSC	uc003dnn.3. human. uc011bfx.2. human.
Organism-specific databases
CTD	7110.
GeneCards	GC03M069068.
HGNC	HGNC:11870. TMF1.
HPA	HPA008729.
MIM	601126. gene.
neXtProt	NX_P82094.
PharmGKB	PA36571.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG127593.
HOGENOM	HOG000154639.
HOVERGEN	HBG016599.
OMA	EKNRSIQ.
OrthoDB	EOG47M1X4.
Enzyme and pathway databases
Pathway_Interaction_DB	ar_pathway. Coregulation of Androgen receptor activity.
Gene expression databases
ArrayExpress	P82094.
Bgee	P82094.
CleanEx	HS_TMF1.
Genevestigator	P82094.
GermOnline	ENSG00000144747. Homo sapiens.
Family and domain databases
InterPro	IPR022092. TMF_DNA-bd. IPR022091. TMF_TATA-bd. [Graphical view]
Pfam	PF12329. TMF_DNA_bd. 1 hit. PF12325. TMF_TATA_bd. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TMF1. human.
GenomeRNAi	7110.
NextBio	27831.
SOURCE	Search...

Entry information

Entry name

TMF1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 98 of the entry and version 2 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.