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Protein

Transcription initiation factor IIA subunit 1

Gene

GTF2A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei274 – 2752Cleavage; by TASP1

GO - Molecular functioni

  • DNA binding Source: BHF-UCL
  • protein heterodimerization activity Source: BHF-UCL
  • TBP-class protein binding Source: BHF-UCL
  • transcription coactivator activity Source: ProtInc
  • transcription factor binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor IIA subunit 1
Alternative name(s):
General transcription factor IIA subunit 1
TFIIAL
Transcription initiation factor TFIIA 42 kDa subunit
Short name:
TFIIA-42
Cleaved into the following 2 chains:
Alternative name(s):
TFIIA p35 subunit
Alternative name(s):
TFIIA p19 subunit
Gene namesi
Name:GTF2A1
Synonyms:TF2A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:4646. GTF2A1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • transcription factor TFIIA complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi270 – 2701V → A: Slightly affects cleavage and yields elevated levels of the precursor. 1 Publication
Mutagenesisi272 – 2721Q → A: Abolishes cleavage. 1 Publication
Mutagenesisi273 – 2731V → A: Abolishes cleavage. 1 Publication
Mutagenesisi274 – 2741D → A: Abolishes cleavage. 1 Publication
Mutagenesisi275 – 2751G → A: Abolishes cleavage. 1 Publication
Mutagenesisi276 – 2761T → A: Does not affect cleavage. 1 Publication
Mutagenesisi277 – 2771G → A: Does not affect cleavage. 1 Publication
Mutagenesisi278 – 2781D → A: Significant reduction of cleavage. 1 Publication
Mutagenesisi280 – 2801S → A: Slightly affects cleavage, yields elevated levels of the precursor. Eliminates phosphorylation; when associated with A-281; A-316 and A-321. 2 Publications
Mutagenesisi281 – 2811S → A: Eliminates phosphorylation; when associated with A-280; A-316 and A-321. 1 Publication
Mutagenesisi282 – 2821E → A: Slightly affects cleavage and yields elevated levels of the precursor. 1 Publication
Mutagenesisi316 – 3161S → A: Strongly reduces phosphorylation; when associated with A-321. Eliminates phosphorylation; when associated with A-280; A-281 and A-321. 1 Publication
Mutagenesisi321 – 3211S → A: Strongly reduces phosphorylation; when associated with A-316. Eliminates phosphorylation; when associated with A-280; A-281 and A-316. 1 Publication

Organism-specific databases

PharmGKBiPA29033.

Polymorphism and mutation databases

BioMutaiGTF2A1.
DMDMi1711663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 376375Transcription initiation factor IIA subunit 1PRO_0000022481Add
BLAST
Chaini2 – 274273Transcription initiation factor IIA alpha chainPRO_0000042593Add
BLAST
Chaini275 – 376102Transcription initiation factor IIA beta chainPRO_0000042594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei280 – 2801Phosphoserine; by TAF11 Publication
Modified residuei281 – 2811Phosphoserine; by TAF11 Publication
Modified residuei316 – 3161Phosphoserine; by TAF12 Publications
Modified residuei321 – 3211Phosphoserine; by TAF12 Publications

Post-translational modificationi

The alpha and beta subunits are postranslationally produced from the precursor form by TASP1. The cleavage promotes proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52655.
PaxDbiP52655.
PRIDEiP52655.

PTM databases

PhosphoSiteiP52655.

Miscellaneous databases

PMAP-CutDBP52655.

Expressioni

Gene expression databases

BgeeiP52655.
ExpressionAtlasiP52655. baseline and differential.
GenevestigatoriP52655.

Organism-specific databases

HPAiHPA000869.

Interactioni

Subunit structurei

TFIIA is a heterodimer of the large unprocessed subunit 1 and a small subunit gamma. It was originally believed to be a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit (p12). TFIIA forms a complex with TBP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GTF2A2P526574EBI-389518,EBI-1045262
NFYAP235113EBI-389518,EBI-389739

Protein-protein interaction databases

BioGridi109212. 55 interactions.
IntActiP52655. 7 interactions.
STRINGi9606.ENSP00000298173.

Structurei

Secondary structure

1
376
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 3223Combined sources
Helixi36 – 5015Combined sources
Beta strandi334 – 34512Combined sources
Beta strandi348 – 36013Combined sources
Beta strandi363 – 37513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NVPX-ray2.10B2-58[»]
C303-376[»]
ProteinModelPortaliP52655.
SMRiP52655. Positions 9-51, 330-376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52655.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 8010Poly-Gln
Compositional biasi81 – 877Poly-His

Sequence similaritiesi

Belongs to the TFIIA subunit 1 family.Curated

Phylogenomic databases

eggNOGiCOG5149.
GeneTreeiENSGT00530000063152.
HOGENOMiHOG000015236.
HOVERGENiHBG052771.
InParanoidiP52655.
KOiK03122.
OMAiKAPRFAS.
OrthoDBiEOG7KWSJM.
PhylomeDBiP52655.
TreeFamiTF350445.

Family and domain databases

Gene3Di1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProiIPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]
PANTHERiPTHR12694. PTHR12694. 1 hit.
PfamiPF03153. TFIIA. 1 hit.
[Graphical view]
SUPFAMiSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 42 kDa (identifier: P52655-1) [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
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL
60 70 80 90 100
MQSRAVDGFH SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQA QPQQTVPQQA
110 120 130 140 150
QTQQVLIPAS QQATAPQVIV PDSKLIQHMN ASNMSAAATA ATLALPAGVT
160 170 180 190 200
PVQQILTNSG QLLQVVRAAN GAQYIFQPQQ SVVLQQQVIP QMQPGGVQAP
210 220 230 240 250
VIQQVLAPLP GGISPQTGVI IQPQQILFTG NKTQVIPTTV AAPTPAQAQI
260 270 280 290 300
TATGQQQPQA QPAQTQAPLV LQVDGTGDTS SEEDEDEEED YDDDEEEDKE
310 320 330 340 350
KDGAEDGQVE EEPLNSEDDV SDEEGQELFD TENVVVCQYD KIHRSKNKWK
360 370
FHLKDGIMNL NGRDYIFSKA IGDAEW
Length:376
Mass (Da):41,514
Last modified:October 1, 1996 - v1
Checksum:i4BAE1853E7E89218
GO
Isoform 37 kDa (identifier: P52655-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.

Show »
Length:337
Mass (Da):37,152
Checksum:i81D62BCC81399DE6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti30 – 301L → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035667
Natural varianti109 – 1091A → P.
Corresponds to variant rs17111579 [ dbSNP | Ensembl ].
VAR_054043

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939Missing in isoform 37 kDa. CuratedVSP_018798Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75383 mRNA. Translation: CAA53151.1.
X75383 mRNA. Translation: CAA53152.1.
X77225 mRNA. Translation: CAA54442.1.
D14887 mRNA. Translation: BAA03604.1.
D14886 mRNA. Translation: BAA03603.1.
AC010582 Genomic DNA. Translation: AAF26776.1.
BC107155 mRNA. Translation: AAI07156.1.
BC107156 mRNA. Translation: AAI07157.1.
CCDSiCCDS9873.1. [P52655-1]
CCDS9874.1. [P52655-2]
PIRiA49077.
RefSeqiNP_001265869.1. NM_001278940.1.
NP_056943.1. NM_015859.3. [P52655-1]
NP_963889.1. NM_201595.2. [P52655-2]
UniGeneiHs.592334.

Genome annotation databases

EnsembliENST00000434192; ENSP00000409492; ENSG00000165417. [P52655-2]
ENST00000553612; ENSP00000452454; ENSG00000165417. [P52655-1]
GeneIDi2957.
KEGGihsa:2957.
UCSCiuc001xve.2. human. [P52655-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75383 mRNA. Translation: CAA53151.1.
X75383 mRNA. Translation: CAA53152.1.
X77225 mRNA. Translation: CAA54442.1.
D14887 mRNA. Translation: BAA03604.1.
D14886 mRNA. Translation: BAA03603.1.
AC010582 Genomic DNA. Translation: AAF26776.1.
BC107155 mRNA. Translation: AAI07156.1.
BC107156 mRNA. Translation: AAI07157.1.
CCDSiCCDS9873.1. [P52655-1]
CCDS9874.1. [P52655-2]
PIRiA49077.
RefSeqiNP_001265869.1. NM_001278940.1.
NP_056943.1. NM_015859.3. [P52655-1]
NP_963889.1. NM_201595.2. [P52655-2]
UniGeneiHs.592334.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NVPX-ray2.10B2-58[»]
C303-376[»]
ProteinModelPortaliP52655.
SMRiP52655. Positions 9-51, 330-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109212. 55 interactions.
IntActiP52655. 7 interactions.
STRINGi9606.ENSP00000298173.

Chemistry

BindingDBiP52655.

PTM databases

PhosphoSiteiP52655.

Polymorphism and mutation databases

BioMutaiGTF2A1.
DMDMi1711663.

Proteomic databases

MaxQBiP52655.
PaxDbiP52655.
PRIDEiP52655.

Protocols and materials databases

DNASUi2957.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000434192; ENSP00000409492; ENSG00000165417. [P52655-2]
ENST00000553612; ENSP00000452454; ENSG00000165417. [P52655-1]
GeneIDi2957.
KEGGihsa:2957.
UCSCiuc001xve.2. human. [P52655-1]

Organism-specific databases

CTDi2957.
GeneCardsiGC14M081646.
HGNCiHGNC:4646. GTF2A1.
HPAiHPA000869.
MIMi600520. gene.
neXtProtiNX_P52655.
PharmGKBiPA29033.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5149.
GeneTreeiENSGT00530000063152.
HOGENOMiHOG000015236.
HOVERGENiHBG052771.
InParanoidiP52655.
KOiK03122.
OMAiKAPRFAS.
OrthoDBiEOG7KWSJM.
PhylomeDBiP52655.
TreeFamiTF350445.

Enzyme and pathway databases

ReactomeiREACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_6233. Transcription of the HIV genome.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6332. HIV Transcription Initiation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

ChiTaRSiGTF2A1. human.
EvolutionaryTraceiP52655.
GeneWikiiGTF2A1.
GenomeRNAii2957.
NextBioi11720.
PMAP-CutDBP52655.
PROiP52655.
SOURCEiSearch...

Gene expression databases

BgeeiP52655.
ExpressionAtlasiP52655. baseline and differential.
GenevestigatoriP52655.

Family and domain databases

Gene3Di1.10.287.100. 1 hit.
2.30.18.10. 1 hit.
InterProiIPR009083. TFIIA_a-hlx.
IPR004855. TFIIA_asu/bsu.
IPR013028. TFIIA_asu_N.
IPR009088. TFIIA_b-brl.
[Graphical view]
PANTHERiPTHR12694. PTHR12694. 1 hit.
PfamiPF03153. TFIIA. 1 hit.
[Graphical view]
SUPFAMiSSF47396. SSF47396. 1 hit.
SSF50784. SSF50784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a cDNA encoding the largest subunit of TFIIA reveals functions important for activated transcription."
    Ma D., Watanabe H., Mermelstein F., Admon A., Oguri K., Sun X., Wada T., Imai T., Shiroya T., Reinberg D., Handa H.
    Genes Dev. 7:2246-2257(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "A single cDNA, hTFIIA/alpha, encodes both the p35 and p19 subunits of human TFIIA."
    Dejong J., Roeder R.G.
    Genes Dev. 7:2220-2234(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  3. Watanabe H., Oguri K., Wada T., Imai T., Shiroya T., Handa H.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. "TAC, a TBP-sans-TAFs complex containing the unprocessed TFIIAalphabeta precursor and the TFIIAgamma subunit."
    Mitsiou D.J., Stunnenberg H.G.
    Mol. Cell 6:527-537(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH GTF2A2 AND TBP.
  7. "Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity."
    Solow S., Salunek M., Ryan R., Lieberman P.M.
    J. Biol. Chem. 276:15886-15892(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-280; SER-281; SER-316 AND SER-321, MUTAGENESIS OF SER-280; SER-281; SER-316 AND SER-321.
  8. "Cleavage and proteasome-mediated degradation of the basal transcription factor TFIIA."
    Hoiby T., Mitsiou D.J., Zhou H., Erdjument-Bromage H., Tempst P., Stunnenberg H.G.
    EMBO J. 23:3083-3091(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 278-289, MUTAGENESIS OF VAL-270; GLN-272; VAL-273; ASP-274; GLY-275; THR-276; GLY-277; ASP-278; SER-280 AND GLU-282.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: FUNCTION OF THE GTF2A1 PRECURSOR, CLEAVAGE BY TASP1.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-30.

Entry informationi

Entry nameiTF2AA_HUMAN
AccessioniPrimary (citable) accession number: P52655
Secondary accession number(s): Q3KNQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.