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Q80UV9 (TAF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription initiation factor TFIID subunit 1

EC=2.3.1.48
EC=2.7.11.1
Alternative name(s):
Cell cycle gene 1 protein
TBP-associated factor 250 kDa
Short name=p250
Transcription initiation factor TFIID 250 kDa subunit
Short name=TAF(II)250
Short name=TAFII-250
Short name=TAFII250
Gene names
Name:Taf1
Synonyms:Ccg1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1891 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Largest component and core scaffold of the TFIID basal transcription factor complex. Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Exhibits histone acetyltransferase activity towards histones H3 and H4 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Cofactor

Magnesium By similarity.

Enzyme regulation

Autophosphorylates on Ser residues. Inhibited by retinoblastoma tumor suppressor protein, RB1. Binding to TAF1 or CIITA inhibits the histone acetyltransferase activity By similarity.

Subunit structure

TAF1 is the largest component of transcription factor TFIID that is composed of TBP and a variety of TBP-associated factors. TAF1, when part of the TFIID complex, interacts with C-terminus of TP53. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. RB1 interacts with the N-terminal domain of TAF1. Interacts with ASF1A and ASF1B. Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro) By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the TAF1 family.

Contains 2 bromo domains.

Contains 1 HMG box DNA-binding domain.

Contains 2 protein kinase domains.

Sequence caution

The sequence BAC34383.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainBromodomain
Repeat
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionAcyltransferase
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-templated transcription, initiation

Inferred from electronic annotation. Source: InterPro

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

histone acetylation

Inferred from direct assay PubMed 11592977. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 22323595. Source: MGI

pronucleus

Inferred from direct assay PubMed 16822332. Source: MGI

transcription factor TFIID complex

Inferred from sequence orthology PubMed 14580349. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from direct assay PubMed 18722179. Source: MGI

histone acetyltransferase activity

Inferred from direct assay PubMed 11592977. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11592977. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80UV9-1)

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: Q80UV9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-962: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q80UV9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     178-198: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18911891Transcription initiation factor TFIID subunit 1
PRO_0000278524

Regions

Domain1 – 435435Protein kinase 1
Domain1418 – 148871Bromo 1
Domain1446 – 1891446Protein kinase 2
Domain1541 – 161171Bromo 2
DNA binding1216 – 129479HMG box By similarity
Region538 – 997460Histone acetyltransferase (HAT) By similarity
Region1363 – 1650288Interaction with ASF1A and ASF1B By similarity
Motif1372 – 13798Nuclear localization signal Potential
Compositional bias157 – 1659Poly-Pro
Compositional bias204 – 2118Poly-Ser
Compositional bias1848 – 18558Poly-Glu

Amino acid modifications

Modified residue3281Phosphoserine; by autocatalysis By similarity
Modified residue5651N6-acetyllysine Ref.7
Modified residue18471Phosphoserine By similarity
Disulfide bond1385 ↔ 1640 By similarity

Natural variations

Alternative sequence1 – 962962Missing in isoform 2.
VSP_023320
Alternative sequence178 – 19821Missing in isoform 3.
VSP_023321

Experimental info

Sequence conflict2171D → E in AAD23348. Ref.4
Sequence conflict2211S → A in AAD23348. Ref.4
Sequence conflict2611R → H in AAD23348. Ref.4
Sequence conflict2891E → K in AAD23348. Ref.4
Sequence conflict867 – 8682LK → EG in AAC62118. Ref.5
Sequence conflict8761T → Q in AAD23349. Ref.4
Sequence conflict1302 – 13065LYYQT → AFVAS in AAC62118. Ref.5
Sequence conflict13581R → P in AAD23350. Ref.4
Sequence conflict13881L → F in AAD23350. Ref.4
Sequence conflict14501T → E in AAD23350. Ref.4
Sequence conflict1469 – 14702HL → QM in AAD23350. Ref.4
Sequence conflict17361D → N in AAH94568. Ref.2

Sequences

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

Last modified March 6, 2007. Version 2.
Checksum: 9A4EA0475BB3E885

FASTA1,891214,419
        10         20         30         40         50         60 
MGPGWAGLLQ DKGGGSPSVV MSDTDSDEES AGGGPFSLTG FLFGNINGAG QLEGESVLDD 

        70         80         90        100        110        120 
ECKKHLAGLG ALGLGSLITE LTANEELSGS DGALVNDEGW IRSREDAVDY SDINEVAEDE 

       130        140        150        160        170        180 
SRRYQQTMGS LQPLCHTDYD EDDYDADCED IDCKLMPPPP PPPGPLKKEK DQDDITGVSE 

       190        200        210        220        230        240 
DGEGIILPSI IAPSSLASEK VDFSSSSDSE SEMGPQDAAQ SESKDGQLTL PLAGIMQHDA 

       250        260        270        280        290        300 
TKLLPSVTEL FPEFRPGKVL RFLRLFGPGK NVPSVWRSAR RKRKKKHREL IQEGQVQEEE 

       310        320        330        340        350        360 
CSVELEVNQK SLWNYDYAPP PLPDQCLSDD EITMMAPVES KFSQSTGDTD KVMDTKPRVA 

       370        380        390        400        410        420 
EWRYGPARLW YDMLGVPEDG SGFDYGFKMK KTEHESTIKC NIMKKLRKLE ENSGVDLLAD 

       430        440        450        460        470        480 
ENFLMVTQLH WEDDIIWDGE DVKHKGTKPQ RASLAGWLPS SMTRNAMAYN VQQGFTATLD 

       490        500        510        520        530        540 
DDKPWYSIFP IDNEDLVYGR WEDNIIWDAQ NMPRILEPPV LTLDPNDENL ILEIPDEKEE 

       550        560        570        580        590        600 
ATSNSPSKEN KKESSLKKSR ILLGKTGVIK EEPQQNMSQP EVKDPWNLSN DEYYYPKQQG 

       610        620        630        640        650        660 
LRGTFGGNII QHSIPAVELR QPFFPTHMGP IKLRQFHRPP LKKYSFGALS QPGPHSVQPL 

       670        680        690        700        710        720 
LKHIKKKAKM REQERQASGG GEMFFMRTPQ DLTGKDGDLI LAEYSEENGP LMMQVGMATK 

       730        740        750        760        770        780 
IKNYYKRKPG KDPGAPDCKY GETVYCHTSP FLGSLHPGQL LQAFENNLFR APIYLHKMPE 

       790        800        810        820        830        840 
SDFLIIRTRQ GYFIRELVDI FVVGQQCPLF EVPGPNSKRA NTHIRDFLQV FIYRLFWKSK 

       850        860        870        880        890        900 
DRPRRIRMED IKKAFPSHSE SSIRKRLKLC ADFKRTGMDS NWWVLKSDFR LPTEEEIRAM 

       910        920        930        940        950        960 
VSPEQCCAYY SMIAAEQRLK DAGYGEKSFF APEEENEEDF QMKIDDEVRT APWNTTRAFI 

       970        980        990       1000       1010       1020 
AAMKGKCLLE VTGVADPTGC GEGFSYVKIP NKPTQQKDDK EPQPVKKTVT GTDADLRRLS 

      1030       1040       1050       1060       1070       1080 
LKNAKQLLRK FGVPEEEIKK LSRWEVIDVV RTMSTEQARS GEGPMSKFAR GSRFSVAEHQ 

      1090       1100       1110       1120       1130       1140 
ERYKEECQRI FDLQNKVLSS TEVLSTDTDS SSAEDSDFEE MGKNIENMLQ NKKTSSQLSR 

      1150       1160       1170       1180       1190       1200 
EREEQERKEL QRMLLAAGSA AAGNNHRDDD TASVTSLNSS ATGRCLKIYR TFRDEEGKEY 

      1210       1220       1230       1240       1250       1260 
VRCETVRKAT VIDAYVRIRT TKDEEFIRKF ALFDEQHREE MRKERRRIQE QLRRLKRNQE 

      1270       1280       1290       1300       1310       1320 
KEKLKGPPEK KPKKMKERPD LKLKCGACGA IGHMRTNKFC PLYYQTNAPP SNPVAMTEEQ 

      1330       1340       1350       1360       1370       1380 
EEELEKTVIH NDNEELIKVE GTKIVLGKQL IESADEVRRK SLVLKFPKQQ LPPKKKRRVG 

      1390       1400       1410       1420       1430       1440 
TTVHCDYLNR PHKSIHRRRT DPMVTLSSIL ESIINDMRDL PNTYPFHTPV NAKVVKDYYK 

      1450       1460       1470       1480       1490       1500 
IITRPMDLQT LRENVRKRLY PSREEFREHL ELIVKNSATY NGPKHSLTQI SQSMLDLCDE 

      1510       1520       1530       1540       1550       1560 
KLKEKEDKLA RLEKAINPLL DDDDQVAFSF ILDNIVTQKM MAVPDSWPFH HPVNKKFVPD 

      1570       1580       1590       1600       1610       1620 
YYKVIVSPMD LETIRKNISK HKYQSRESFL DDVNLILANS VKYNGPESQY TKTAQEIVNV 

      1630       1640       1650       1660       1670       1680 
CHQTLTEYDE HLTQLEKDIC TAKEAALEEA ELESLDPMTP GPYTPQPPDL YDNNTSLSVS 

      1690       1700       1710       1720       1730       1740 
RDASVYQDES NLSVLDIPSA TSEKQLTQEG GDGDGDLADE EEGTVQQPQA SVLYEDLLMS 

      1750       1760       1770       1780       1790       1800 
EGEDDEEDAG SDEEGDNPFF AIQLSESGSD SDVESGSLRP KQPRVLQENT RMGMENEESM 

      1810       1820       1830       1840       1850       1860 
MSYEGDGGDA SRGLEDSNIS YGSYEEPDPK SNTQDTSFSS IGGYEVSEEE EDEEEQRSGP 

      1870       1880       1890 
SVLSQVHLSE DEEDSEDFHS IAGDTDLDSD E 

« Hide

Isoform 2 [UniParc].

Checksum: A92987089CF8811D
Show »

FASTA929105,780
Isoform 3 [UniParc].

Checksum: C7C3C29E868C630F
Show »

FASTA1,870212,382

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-1891.
Strain: C57BL/6 and Czech II.
Tissue: Brain and Mammary tumor.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-280 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 849-1237 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-401 AND 1143-1891.
Strain: C57BL/6J.
Tissue: Adipose tissue, Corpora quadrigemina, Head, Hippocampus and Spleen.
[4]"TAFII250, Egr-1, and D-type cyclin expression in mice and neonatal rat cardiomyocytes treated with doxorubicin."
Saadane N., Alpert L., Chalifour L.E.
Am. J. Physiol. 276:H803-H814(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 217-370; 841-876 AND 1199-1488.
Strain: CD-1.
Tissue: Heart.
[5]"HIV-1 tat binds TAFII250 and represses TAFII250-dependent transcription of major histocompatibility class I genes."
Weissman J.D., Brown J.A., Howcroft T.K., Hwang J., Chawla A., Roche P.A., Schiltz L., Nakatani Y., Singer D.S.
Proc. Natl. Acad. Sci. U.S.A. 95:11601-11606(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 867-1306.
Tissue: Spleen.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL831722, AL806534 Genomic DNA. Translation: CAM20496.1.
AL831722, AL806534 Genomic DNA. Translation: CAM20497.1.
AL806534, AL831722 Genomic DNA. Translation: CAM21283.1.
AL806534, AL831722 Genomic DNA. Translation: CAM21284.1.
BC047418 mRNA. Translation: AAH47418.1.
BC094568 mRNA. Translation: AAH94568.1.
AK045586 mRNA. Translation: BAC32425.1.
AK046668 mRNA. Translation: BAC32828.1.
AK049826 mRNA. Translation: BAC33938.1.
AK050691 mRNA. Translation: BAC34383.1. Different initiation.
AK132088 mRNA. Translation: BAE20976.1.
AK143571 mRNA. Translation: BAE25442.1.
AF081115 mRNA. Translation: AAD23349.1.
AF081116 mRNA. Translation: AAD23348.1.
AF081117 mRNA. Translation: AAD23350.1.
AF022178 mRNA. Translation: AAC62118.1.
RefSeqNP_001277658.1. NM_001290729.1.
XP_006528113.1. XM_006528050.1. [Q80UV9-1]
XP_006528115.1. XM_006528052.1. [Q80UV9-3]
UniGeneMm.261750.

3D structure databases

ProteinModelPortalQ80UV9.
SMRQ80UV9. Positions 1380-1646.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ80UV9.

Proteomic databases

PaxDbQ80UV9.
PRIDEQ80UV9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000118878; ENSMUSP00000112772; ENSMUSG00000031314. [Q80UV9-3]
GeneID270627.
KEGGmmu:270627.
UCSCuc009txv.2. mouse. [Q80UV9-1]
uc009txy.1. mouse. [Q80UV9-2]

Organism-specific databases

CTD6872.
MGIMGI:1336878. Taf1.

Phylogenomic databases

eggNOGCOG5076.
GeneTreeENSGT00390000012659.
HOVERGENHBG050223.
KOK03125.
OrthoDBEOG7QNVK2.

Gene expression databases

BgeeQ80UV9.
GenevestigatorQ80UV9.

Family and domain databases

Gene3D1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.
InterProIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR011177. TAF1_animal.
IPR009067. TAF_II_230-bd.
IPR022591. TFIID_sub1_DUF3591.
[Graphical view]
PfamPF00439. Bromodomain. 2 hits.
PF12157. DUF3591. 1 hit.
PF09247. TBP-binding. 1 hit.
[Graphical view]
PIRSFPIRSF003047. TAF1_animal. 1 hit.
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMSSF47055. SSF47055. 1 hit.
SSF47370. SSF47370. 2 hits.
PROSITEPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

PROQ80UV9.
SOURCESearch...

Entry information

Entry nameTAF1_MOUSE
AccessionPrimary (citable) accession number: Q80UV9
Secondary accession number(s): A2AM32 expand/collapse secondary AC list , A2AM33, O35361, Q3UPF3, Q3V223, Q505F9, Q8BQH8, Q8BQQ7, Q8BR59, Q8C7N8, Q9WTW9, Q9WTX0, Q9WTX1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 84 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot