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Q15572 (TAF1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TATA box-binding protein-associated factor RNA polymerase I subunit C
Alternative name(s):
RNA polymerase I-specific TBP-associated factor 110 kDa
Short name=TAFI110
TATA box-binding protein-associated factor 1C
Short name=TBP-associated factor 1C
Transcription initiation factor SL1/TIF-IB subunit C
Gene names
Name:TAF1C
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length869 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits. Recruits RNA polymerase I to the rRNA gene promoter via interaction with RRN3. Ref.8 Ref.9

Subunit structure

Component of the transcription factor SL1/TIF-IB complex, composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the complex interacts directly with TBP, TAF1A and TAF1B. Interaction of the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the transcription factor IID (TFIID) subunits. Interacts with MYC and RRN3. Interacts with p53/TP53; the interaction prevents the association of SL1/TIF-IB with UBTF and represses RNA polymerase I transcription. Ref.1 Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.12

Sequence caution

The sequence BAD92831.1 differs from that shown. Reason: Probable cloning artifact.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15572-1)

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: Q15572-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.
     280-306: SKALIYTFLPHWLTCYLTPGPFHPSSA → T
     521-521: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q15572-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-332: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q15572-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-409: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q15572-6)

The sequence of this isoform differs from the canonical sequence as follows:
     280-306: SKALIYTFLPHWLTCYLTPGPFHPSSA → T
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 869869TATA box-binding protein-associated factor RNA polymerase I subunit C
PRO_0000118863

Amino acid modifications

Modified residue8341Phosphothreonine Ref.12
Modified residue8481Phosphoserine Ref.11
Modified residue8581Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 409409Missing in isoform 5.
VSP_038086
Alternative sequence1 – 332332Missing in isoform 4.
VSP_038087
Alternative sequence1 – 6767Missing in isoform 2.
VSP_015153
Alternative sequence280 – 30627SKALI…HPSSA → T in isoform 2 and isoform 6.
VSP_015154
Alternative sequence5211Missing in isoform 2.
VSP_015156
Natural variant911C → Y. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs4782591 [ dbSNP | Ensembl ].
VAR_058966
Natural variant3041S → F. Ref.4
Corresponds to variant rs4150145 [ dbSNP | Ensembl ].
VAR_023245
Natural variant3571R → H. Ref.4
Corresponds to variant rs4150147 [ dbSNP | Ensembl ].
VAR_023246
Natural variant3871S → L. Ref.4
Corresponds to variant rs4150151 [ dbSNP | Ensembl ].
VAR_023247
Natural variant5181H → Y. Ref.4
Corresponds to variant rs4150165 [ dbSNP | Ensembl ].
VAR_023248
Natural variant5231G → R.
Corresponds to variant rs4150167 [ dbSNP | Ensembl ].
VAR_057261
Natural variant5731P → L. Ref.4
Corresponds to variant rs4150170 [ dbSNP | Ensembl ].
VAR_023249
Natural variant5751L → M. Ref.2 Ref.4 Ref.6
Corresponds to variant rs2230129 [ dbSNP | Ensembl ].
VAR_023250
Natural variant5911A → G. Ref.4
Corresponds to variant rs4150172 [ dbSNP | Ensembl ].
VAR_023251
Natural variant6351G → S. Ref.4
Corresponds to variant rs4150173 [ dbSNP | Ensembl ].
VAR_023252
Natural variant7911T → M. Ref.4
Corresponds to variant rs4150175 [ dbSNP | Ensembl ].
VAR_023253
Natural variant7931P → L. Ref.2 Ref.4
Corresponds to variant rs2230131 [ dbSNP | Ensembl ].
VAR_023254
Natural variant8081P → S.
Corresponds to variant rs3743640 [ dbSNP | Ensembl ].
VAR_057262
Natural variant8161R → H. Ref.4
Corresponds to variant rs4150176 [ dbSNP | Ensembl ].
VAR_023255

Experimental info

Sequence conflict2441E → K in BAH13010. Ref.2
Sequence conflict4811N → S in BAH14353. Ref.2
Sequence conflict7771S → G in BAH14144. Ref.2

Sequences

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

Last modified November 30, 2010. Version 2.
Checksum: 6AAFAF296D98A5DB

FASTA86995,213
        10         20         30         40         50         60 
MDFPSSLRPA LFLTGPLGLS DVPDLSFMCS WRDALTLPEA QPQNSENGAL HVTKDLLWEP 

        70         80         90        100        110        120 
ATPGPLPMLP PLIDPWDPGL TARDLLFRGG CRYRKRPRVV LDVTEQISRF LLDHGDVAFA 

       130        140        150        160        170        180 
PLGKLMLENF KLEGAGSRTK KKTVVSVKKL LQDLGGHQPW GCPWAYLSNR QRRFSILGGP 

       190        200        210        220        230        240 
ILGTSVASHL AELLHEELVL RWEQLLLDEA CTGGALAWVP GRTPQFGQLV YPAGGAQDRL 

       250        260        270        280        290        300 
HFQEVVLTPG DNPQFLGKPG RIQLQGPVRQ VVTCTVQGES KALIYTFLPH WLTCYLTPGP 

       310        320        330        340        350        360 
FHPSSALLAV RSDYHCAVWK FGKQWQPTLL QAMQVEKGAT GISLSPHLPG ELAICSRSGA 

       370        380        390        400        410        420 
VCLWSPEDGL RQIYRDPETL VFRDSSSWRW ADFTAHPRVL TVGDRTGVKM LDTQGPPGCG 

       430        440        450        460        470        480 
LLLFRLGAEA SCQKGERVLL TQYLGHSSPK CLPPTLHLVC TQFSLYLVDE RLPLVPMLKW 

       490        500        510        520        530        540 
NHGLPSPLLL ARLLPPPRPS CVQPLLLGGQ GGQLQLLHLA GEGASVPRLA GPPQSLPSRI 

       550        560        570        580        590        600 
DSLPAFPLLE PKIQWRLQER LKAPTIGLAA VVPPLPSAPT PGLVLFQLSA AGDVFYQQLR 

       610        620        630        640        650        660 
PQVDSSLRRD AGPPGDTQPD CHAPTASWTS QDTAGCSQWL KALLKVPLAP PVWTAPTFTH 

       670        680        690        700        710        720 
RQMLGSTELR REEEEGQRLG VLRKAMARGQ LLLQRDLGSL PAAEPPPAPE SGLEDKLSER 

       730        740        750        760        770        780 
LGEAWAGRGA AWWERQQGRT SEPGRQTRRP KRRTQLSSSF SLSGHVDPSE DTSSPHSPEW 

       790        800        810        820        830        840 
PPADALPLPP TTPPSQELTP DACAQGVPSE QRQMLRDYMA KLPPQRDTPG CATTPPHSQA 

       850        860 
SSVRATRSQQ HTPVLSSSQP LRKKPRMGF 

« Hide

Isoform 2 [UniParc].

Checksum: 29B8C09D7F9228EF
Show »

FASTA77584,985
Isoform 4 [UniParc].

Checksum: 6C36809B5E6D2203
Show »

FASTA53758,441
Isoform 5 [UniParc].

Checksum: DBE3CAD1F8541D45
Show »

FASTA46049,946
Isoform 6 [UniParc].

Checksum: 75D245B40F7E9948
Show »

FASTA84392,284

References

« Hide 'large scale' references
[1]"Reconstitution of transcription factor SL1: exclusive binding of TBP by SL1 or TFIID subunits."
Comai L., Zomerdijk J.C.B.M., Beckmann H., Zhou S., Admon A., Tjian R.
Science 266:1966-1972(1994) [PubMed: 7801123] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 55-65; 96-112; 125-131; 324-337; 338-354; 553-561; 563-582 AND 646-659, INTERACTION WITH TBP; TAF1A AND TAF1B, IDENTIFICATION IN THE SL1 COMPLEX, VARIANT TYR-91.
[2]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6), VARIANTS TYR-91; MET-575 AND LEU-793.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Spleen.
[4]NIEHS SNPs program
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-91; PHE-304; HIS-357; LEU-387; TYR-518; LEU-573; MET-575; GLY-591; SER-635; MET-791; LEU-793 AND HIS-816.
[5]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed: 15616553] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS TYR-91 AND MET-575.
Tissue: Lung.
[7]"Repression of RNA polymerase I transcription by the tumor suppressor p53."
Zhai W., Comai L.
Mol. Cell. Biol. 20:5930-5938(2000) [PubMed: 10913176] [Abstract]
Cited for: INTERACTION WITH TP53.
[8]"hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to rRNA gene promoters."
Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I., Zomerdijk J.C.B.M.
EMBO J. 20:1373-1382(2001) [PubMed: 11250903] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RRN3.
[9]"TBP-TAF complex SL1 directs RNA polymerase I pre-initiation complex formation and stabilizes upstream binding factor at the rDNA promoter."
Friedrich J.K., Panov K.I., Cabart P., Russell J., Zomerdijk J.C.B.M.
J. Biol. Chem. 280:29551-29558(2005) [PubMed: 15970593] [Abstract]
Cited for: FUNCTION OF THE SL1 COMPLEX.
[10]"c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I."
Grandori C., Gomez-Roman N., Felton-Edkins Z.A., Ngouenet C., Galloway D.A., Eisenman R.N., White R.J.
Nat. Cell Biol. 7:311-318(2005) [PubMed: 15723054] [Abstract]
Cited for: INTERACTION WITH MYC.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-848 AND SER-858, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[12]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-834, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L39059 mRNA. Translation: AAA62861.1.
AK299060 mRNA. Translation: BAH12941.1.
AK299347 mRNA. Translation: BAH13010.1.
AK304261 mRNA. Translation: BAH14144.1.
AK315982 mRNA. Translation: BAH14353.1.
AB209594 mRNA. Translation: BAD92831.1. Sequence problems.
AY158985 Genomic DNA. Translation: AAN38818.1.
AC009123 Genomic DNA. No translation available.
BC028131 mRNA. Translation: AAH28131.1.
IPIIPI00246842.
IPI00328322.
IPI00944587.
IPI00944609.
IPI00944618.
PIRA55384.
RefSeqNP_001230085.1. NM_001243156.1.
NP_001230086.1. NM_001243157.1.
NP_001230087.1. NM_001243158.1.
NP_001230088.1. NM_001243159.1.
NP_005670.3. NM_005679.3.
NP_647610.2. NM_139353.2.
UniGeneHs.153022.

3D structure databases

ProteinModelPortalQ15572.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-269N.
IntActQ15572. 1 interaction.
MINTMINT-3031839.
STRINGQ15572.

PTM databases

PhosphoSiteQ15572.

Polymorphism databases

DMDM73621973.

Proteomic databases

PRIDEQ15572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341690; ENSP00000345305; ENSG00000103168.
ENST00000378541; ENSP00000367802; ENSG00000103168.
GeneID9013.
KEGGhsa:9013.
UCSCuc002fhm.1. human.
uc002fhn.1. human.
uc002fho.1. human.

Organism-specific databases

CTD9013.
GeneCardsGC16M084211.
H-InvDBHIX0013290.
HGNCHGNC:11534. TAF1C.
MIM604905. gene.
neXtProtNX_Q15572.
PharmGKBPA36309.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04639.
GeneTreeENSGT00390000010767.
HOGENOMHBG283428.
HOVERGENHBG079499.
InParanoidQ15572.
OMAKKPRMGF.
OrthoDBEOG4X97GS.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.

Gene expression databases

ArrayExpressQ15572.
BgeeQ15572.
CleanExHS_TAF1C.
GenevestigatorQ15572.
GermOnlineENSG00000103168. Homo sapiens.

Family and domain databases

InterProIPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KOK15214.
ProtoNetSearch...

Other

NextBio33765.
SOURCESearch...

Entry information

Entry nameTAF1C_HUMAN
AccessionPrimary (citable) accession number: Q15572
Secondary accession number(s): B7Z5K5 expand/collapse secondary AC list , B7Z5S4, B7Z908, B7Z9L7, Q59F67, Q8N6V3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 30, 2010
Last modified: January 25, 2012
This is version 88 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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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