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Protein

Transcription initiation factor TFIID subunit 3

Gene

Taf3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri867 – 91751PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • p53 binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

  • maintenance of protein location in nucleus Source: MGI
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-73776. RNA Polymerase II Promoter Escape.
R-MMU-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-MMU-75953. RNA Polymerase II Transcription Initiation.
R-MMU-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 3
Alternative name(s):
140 kDa TATA box-binding protein-associated factor
TBP-associated factor 3
Transcription initiation factor TFIID 140 kDa subunit
Short name:
TAF(II)140
Short name:
TAF140
Short name:
TAFII-140
Short name:
TAFII140
Gene namesi
Name:Taf3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2388097. Taf3.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: MGI
  • transcription factor TFIID complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 932932Transcription initiation factor TFIID subunit 3PRO_0000245529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831PhosphoserineCombined sources
Modified residuei229 – 2291PhosphoserineBy similarity
Modified residuei243 – 2431PhosphoserineBy similarity
Modified residuei266 – 2661N6-acetyllysineCombined sources
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei297 – 2971PhosphoserineBy similarity
Modified residuei301 – 3011PhosphoserineBy similarity
Modified residuei502 – 5021PhosphothreonineBy similarity
Cross-linki749 – 749Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei779 – 7791N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5HZG4.
MaxQBiQ5HZG4.
PaxDbiQ5HZG4.
PRIDEiQ5HZG4.

PTM databases

iPTMnetiQ5HZG4.
PhosphoSiteiQ5HZG4.

Expressioni

Gene expression databases

BgeeiQ5HZG4.
ExpressionAtlasiQ5HZG4. baseline and differential.
GenevisibleiQ5HZG4. MM.

Interactioni

Subunit structurei

Belongs to the TFIID complex which is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). Interacts with TAF10 via histone fold. Interacts with TAF13, TBP, SAP130 and GCN5L2 (By similarity). Interacts with TBPL2.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Tbpl2Q6SJ953EBI-1561080,EBI-1571412

GO - Molecular functioni

  • p53 binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi229072. 2 interactions.
IntActiQ5HZG4. 10 interactions.
MINTiMINT-4123417.
STRINGi10090.ENSMUSP00000026888.

Structurei

Secondary structure

1
932
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi857 – 8604Combined sources
Beta strandi862 – 8643Combined sources
Beta strandi866 – 8683Combined sources
Turni871 – 8733Combined sources
Beta strandi882 – 8843Combined sources
Beta strandi886 – 8938Combined sources
Helixi894 – 8974Combined sources
Beta strandi905 – 9073Combined sources
Turni912 – 9143Combined sources
Helixi915 – 9184Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K16NMR-A857-924[»]
2K17NMR-A857-924[»]
ProteinModelPortaliQ5HZG4.
SMRiQ5HZG4. Positions 7-83, 857-924.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5HZG4.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi136 – 1416Poly-Glu
Compositional biasi163 – 1686Poly-Glu
Compositional biasi221 – 367147Pro-richAdd
BLAST
Compositional biasi508 – 749242Lys-richAdd
BLAST
Compositional biasi782 – 83453Pro-richAdd
BLAST

Domaini

The PHD-type zinc finger mediates binding to histone H3 methyllysine at position 4 (H3K4me3).

Sequence similaritiesi

Belongs to the TAF3 family.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri867 – 91751PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
KOG2389. Eukaryota.
ENOG410ZS4D. LUCA.
GeneTreeiENSGT00710000106806.
HOGENOMiHOG000231905.
HOVERGENiHBG083188.
InParanoidiQ5HZG4.
KOiK14650.
OMAiMPPNFPY.
OrthoDBiEOG7X0VK0.
PhylomeDBiQ5HZG4.
TreeFamiTF316513.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR006565. BTP.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF07524. Bromo_TP. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00576. BTP. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5HZG4-1) [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

        10         20         30         40         50
MCESYSRSLL RVSVAQICQA LGWDSVQLSA CHLLTDVLQR YLQQLGRGCH
60 70 80 90 100
RYSELYGRTD PILDDVGEAF QLMGVNLHEL EDYIHNIEPV TFPHQIPSFP
110 120 130 140 150
VSKNNVLQFP QPGSKDAEER KDYIPDYLPP IVSSQEEEEE EQVPTDGGTS
160 170 180 190 200
AEAMQVPLEE DDEMEEEEVI NDENFLGKRP LDSPEVEEMP SMKRPRLLST
210 220 230 240 250
KGDSLDVVLL EAREPLSSIN PQKTPPVLSP VRVQDRADLA PPSPQPPMLA
260 270 280 290 300
PFAKSQLPIA KPLETKSFTP KTKTKASSPG QKTKSPKAAL SPARLGSPIR
310 320 330 340 350
SPKTIPKEKK SPGRSKSPKS PKSPKIVAHV PQTPVRPETP NRTPSAMVVE
360 370 380 390 400
KTVKETIPVM KPTQTPPEVV KLNIEMQPKK PVVTDKTIDD SIDAVIARAC
410 420 430 440 450
AEREPDPFEF SSGSESEGDT FTSPKRISGS ECATPKASTS SNNFTKSLAT
460 470 480 490 500
PLPLSSGTSS SDNSWTMDAS IDEVVRKAKL GAPSNMPPTF PYISSPSISP
510 520 530 540 550
PTPEPLHKGY EEKAKLPSSV DVKKKLKKEL KTKLKKKEKQ RDRERERERN
560 570 580 590 600
KERSKEKDKM REREKEKEAG KELKYPWREL MKDEDSDPYK FKIKEFEDID
610 620 630 640 650
AAKVRLKDGI VRREREKHKD KKKDRERSKR EKDKRERERL KEKNREDKIK
660 670 680 690 700
APPTQLVLPP KEMALPLFSP SAVRVPAMLP AFSPMLPEKL FEEKEKPKEK
710 720 730 740 750
ERKKDKKEKK KKKEKEKEKE KKEREREKER REREKREKEK EKHKHEKIKV
760 770 780 790 800
EPVIPAPSPV IPRLTLRVGA GQDKIVISKV VPAPEAKPAP SLNRPKTPPP
810 820 830 840 850
APVPIPVRVS PTPLQPPLLT QAAVCPALMP SPAPALSGIG SAKAPVRSVV
860 870 880 890 900
TETVSTYVIR DEWGNQIWIC PGCNKPDDGS PMIGCDDCDD WYHWPCVGIM
910 920 930
AAPPEEMQWF CPKCANKIKK DKKHKKRKHR AH
Length:932
Mass (Da):105,115
Last modified:July 11, 2006 - v2
Checksum:i8061D8E599A650EE
GO
Isoform 2 (identifier: Q5HZG4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-741: Missing.
     742-747: KHKHEK → MYKFPQ

Note: No experimental confirmation available.
Show »
Length:191
Mass (Da):20,794
Checksum:i55D0EC92119F1C03
GO

Sequence cautioni

The sequence AAH89030.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti545 – 5451R → G in BAE32543 (PubMed:16141072).Curated
Sequence conflicti721 – 7211K → E in BAE22792 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 741741Missing in isoform 2. 1 PublicationVSP_019736Add
BLAST
Alternative sequencei742 – 7476KHKHEK → MYKFPQ in isoform 2. 1 PublicationVSP_019737

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ292189 mRNA. Translation: CAC34476.1.
AK084574 mRNA. Translation: BAC39218.1.
AK136045 mRNA. Translation: BAE22792.1.
AK154372 mRNA. Translation: BAE32543.1.
BC089030 mRNA. Translation: AAH89030.1. Different initiation.
CCDSiCCDS15675.1. [Q5HZG4-1]
RefSeqiNP_082024.2. NM_027748.3. [Q5HZG4-1]
UniGeneiMm.86343.

Genome annotation databases

EnsembliENSMUST00000026888; ENSMUSP00000026888; ENSMUSG00000025782. [Q5HZG4-1]
GeneIDi209361.
KEGGimmu:209361.
UCSCiuc008ihk.2. mouse. [Q5HZG4-2]
uc008ihl.2. mouse. [Q5HZG4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ292189 mRNA. Translation: CAC34476.1.
AK084574 mRNA. Translation: BAC39218.1.
AK136045 mRNA. Translation: BAE22792.1.
AK154372 mRNA. Translation: BAE32543.1.
BC089030 mRNA. Translation: AAH89030.1. Different initiation.
CCDSiCCDS15675.1. [Q5HZG4-1]
RefSeqiNP_082024.2. NM_027748.3. [Q5HZG4-1]
UniGeneiMm.86343.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K16NMR-A857-924[»]
2K17NMR-A857-924[»]
ProteinModelPortaliQ5HZG4.
SMRiQ5HZG4. Positions 7-83, 857-924.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229072. 2 interactions.
IntActiQ5HZG4. 10 interactions.
MINTiMINT-4123417.
STRINGi10090.ENSMUSP00000026888.

PTM databases

iPTMnetiQ5HZG4.
PhosphoSiteiQ5HZG4.

Proteomic databases

EPDiQ5HZG4.
MaxQBiQ5HZG4.
PaxDbiQ5HZG4.
PRIDEiQ5HZG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026888; ENSMUSP00000026888; ENSMUSG00000025782. [Q5HZG4-1]
GeneIDi209361.
KEGGimmu:209361.
UCSCiuc008ihk.2. mouse. [Q5HZG4-2]
uc008ihl.2. mouse. [Q5HZG4-1]

Organism-specific databases

CTDi83860.
MGIiMGI:2388097. Taf3.

Phylogenomic databases

eggNOGiKOG1973. Eukaryota.
KOG2389. Eukaryota.
ENOG410ZS4D. LUCA.
GeneTreeiENSGT00710000106806.
HOGENOMiHOG000231905.
HOVERGENiHBG083188.
InParanoidiQ5HZG4.
KOiK14650.
OMAiMPPNFPY.
OrthoDBiEOG7X0VK0.
PhylomeDBiQ5HZG4.
TreeFamiTF316513.

Enzyme and pathway databases

ReactomeiR-MMU-674695. RNA Polymerase II Pre-transcription Events.
R-MMU-73776. RNA Polymerase II Promoter Escape.
R-MMU-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-MMU-75953. RNA Polymerase II Transcription Initiation.
R-MMU-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

ChiTaRSiTaf3. mouse.
EvolutionaryTraceiQ5HZG4.
NextBioi372647.
PROiQ5HZG4.
SOURCEiSearch...

Gene expression databases

BgeeiQ5HZG4.
ExpressionAtlasiQ5HZG4. baseline and differential.
GenevisibleiQ5HZG4. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR006565. BTP.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF07524. Bromo_TP. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00576. BTP. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger."
    Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.
    Mol. Cell. Biol. 21:5109-5121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TAF10.
    Tissue: Embryonic carcinoma.
  2. "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.
    , 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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Dendritic cell, Egg and Heart.
  3. "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).
    Strain: C57BL/6J.
    Tissue: Head.
  4. "Switching of the core transcription machinery during myogenesis."
    Deato M.D.E., Tjian R.
    Genes Dev. 21:2137-2149(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TBPL2.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Lung, Pancreas, Spleen and Testis.
  6. "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-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. "Structural insight into the recognition of the H3K4me3 mark by the TFIID subunit TAF3."
    van Ingen H., van Schaik F.M., Wienk H., Ballering J., Rehmann H., Dechesne A.C., Kruijzer J.A., Liskamp R.M., Timmers H.T., Boelens R.
    Structure 16:1245-1256(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 857-924 IN COMPLEX WITH H3K4ME3 PEPTIDE.

Entry informationi

Entry nameiTAF3_MOUSE
AccessioniPrimary (citable) accession number: Q5HZG4
Secondary accession number(s): Q3U490
, Q3UWX2, Q8BIU8, Q99JH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: March 16, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.