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Protein

Transcription factor 4

Gene

TCF4

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

Functioni

Transcription factor that binds to the immunoglobulin enchancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'.By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. E-box binding Source: UniProtKB
  3. protein C-terminus binding Source: UniProtKB
  4. protein heterodimerization activity Source: UniProtKB
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
  7. sequence-specific DNA binding RNA polymerase recruiting transcription factor activity Source: BHF-UCL
  8. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  9. TFIIB-class binding transcription factor activity Source: BHF-UCL
  10. TFIIB-class transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. DNA-templated transcription, initiation Source: BHF-UCL
  2. positive regulation of neuron differentiation Source: UniProtKB
  3. positive regulation of transcription, DNA-templated Source: UniProtKB
  4. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  5. protein-DNA complex assembly Source: BHF-UCL
  6. transcription initiation from RNA polymerase II promoter Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_21402. CDO in myogenesis.
SignaLinkiP15884.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor 4
Short name:
TCF-4
Alternative name(s):
Class B basic helix-loop-helix protein 19
Short name:
bHLHb19
Immunoglobulin transcription factor 2
Short name:
ITF-2
SL3-3 enhancer factor 2
Short name:
SEF-2
Gene namesi
Name:TCF4
Synonyms:BHLHB19, ITF2, SEF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:11634. TCF4.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Pitt-Hopkins syndrome6 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA syndrome characterized by mental retardation, wide mouth and distinctive facial features, and intermittent hyperventilation followed by apnea. Features include intellectual disability with severe speech impairment, normal growth parameters at birth, postnatal microcephaly, breathing anomalies, severe motor developmental delay, motor incoordination, ocular anomalies, constipation, seizures, typical behavior and subtle brain abnormalities.

See also OMIM:610954
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti358 – 3581G → V in PTHS; also expressed in the nucleus with a pattern indistinguishable from the wild-type; does not have a major impact on homodimer formation; affects transcriptional activity in a context-dependent manner. 2 Publications
VAR_066839
Natural varianti535 – 5351D → G in PTHS; loss of function; also expressed in the nucleus with a pattern indistinguishable from the wild-type; does not have a major impact on homodimer formation; affects transcriptional activity in a context-dependent manner. 2 Publications
VAR_058632
Natural varianti565 – 5651R → W in PTHS. 1 Publication
VAR_066970
Natural varianti572 – 5721R → G in PTHS; loss of function. 2 Publications
VAR_058633
Natural varianti572 – 5721R → Q in PTHS. 1 Publication
VAR_066971
Natural varianti574 – 5741R → H in PTHS. 1 Publication
VAR_066972
Natural varianti574 – 5741R → P in PTHS; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner. 3 Publications
VAR_066840
Natural varianti576 – 5761R → Q in PTHS; loss of function. 3 Publications
VAR_034704
Natural varianti576 – 5761R → W in PTHS; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner. 4 Publications
VAR_034705
Natural varianti578 – 5781R → H in PTHS. 1 Publication
VAR_066841
Natural varianti578 – 5781R → P in PTHS. 2 Publications
VAR_066973
Natural varianti583 – 5831A → P in PTHS. 1 Publication
VAR_066974
Natural varianti610 – 6101A → V in PTHS; loss of function; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner. 3 Publications
VAR_058634

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation, Primary microcephaly

Organism-specific databases

MIMi610954. phenotype.
Orphaneti178469. Autosomal dominant non-syndromic intellectual disability.
98974. Fuchs endothelial corneal dystrophy.
2896. Pitt-Hopkins syndrome.
171. Primary sclerosing cholangitis.
3140. Schizophrenia.
PharmGKBiPA164742621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 667667Transcription factor 4PRO_0000127256Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661PhosphoserineBy similarity
Modified residuei297 – 2971PhosphothreonineBy similarity
Modified residuei318 – 3181PhosphoserineBy similarity
Modified residuei515 – 5151Phosphoserine1 Publication
Modified residuei546 – 5461PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15884.
PaxDbiP15884.
PRIDEiP15884.

PTM databases

PhosphoSiteiP15884.

Expressioni

Tissue specificityi

Expressed in adult heart, brain, placenta, skeletal muscle and to a lesser extent in the lung. In developing embryonic tissues, expression mostly occurs in the brain.

Gene expression databases

BgeeiP15884.
CleanExiHS_TCF4.
ExpressionAtlasiP15884. baseline and differential.
GenevestigatoriP15884.

Organism-specific databases

HPAiCAB020722.
HPA025958.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Forms homo- or heterooligomers with myogenin. Interacts with HIVEP2. Interacts with NEUROD2 (By similarity). Interacts with AGBL1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ASCL1P505537EBI-533224,EBI-957042
CTNNB1P3522219EBI-533224,EBI-491549
ctnnb1P262332EBI-533224,EBI-7373758From a different organism.
FERMT2Q96AC16EBI-533224,EBI-4399465
Sox17Q614735EBI-533224,EBI-9106822From a different organism.
Sox4Q068312EBI-533224,EBI-6262177From a different organism.

Protein-protein interaction databases

BioGridi112787. 181 interactions.
DIPiDIP-163N.
IntActiP15884. 21 interactions.
MINTiMINT-4508073.
STRINGi9606.ENSP00000346440.

Structurei

Secondary structure

1
667
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KWFNMR-B11-27[»]
DisProtiDP00224.
ProteinModelPortaliP15884.
SMRiP15884. Positions 565-624.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15884.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini564 – 61754bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8383Essential for MYOD1 inhibitionBy similarityAdd
BLAST
Regioni379 – 40022Leucine-zipperAdd
BLAST
Regioni619 – 64224Class A specific domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi18 – 2699aaTAD

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi228 – 2314Poly-Ser

Domaini

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG282899.
GeneTreeiENSGT00510000046438.
HOVERGENiHBG003854.
InParanoidiP15884.
KOiK15603.
OrthoDBiEOG72G16Q.
PhylomeDBiP15884.
TreeFamiTF321672.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequences (16)i

Sequence statusi: Complete.

This entry describes 16 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform SEF2-1B (identifier: P15884-1) [UniParc]FASTAAdd to basket

Also known as: B-

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
MHHQQRMAAL GTDKELSDLL DFSAMFSPPV SSGKNGPTSL ASGHFTGSNV
60 70 80 90 100
EDRSSSGSWG NGGHPSPSRN YGDGTPYDHM TSRDLGSHDN LSPPFVNSRI
110 120 130 140 150
QSKTERGSYS SYGRESNLQG CHQQSLLGGD MDMGNPGTLS PTKPGSQYYQ
160 170 180 190 200
YSSNNPRRRP LHSSAMEVQT KKVRKVPPGL PSSVYAPSAS TADYNRDSPG
210 220 230 240 250
YPSSKPATST FPSSFFMQDG HHSSDPWSSS SGMNQPGYAG MLGNSSHIPQ
260 270 280 290 300
SSSYCSLHPH ERLSYPSHSS ADINSSLPPM STFHRSGTNH YSTSSCTPPA
310 320 330 340 350
NGTDSIMANR GSGAAGSSQT GDALGKALAS IYSPDHTNNS FSSNPSTPVG
360 370 380 390 400
SPPSLSAGTA VWSRNGGQAS SSPNYEGPLH SLQSRIEDRL ERLDDAIHVL
410 420 430 440 450
RNHAVGPSTA MPGGHGDMHG IIGPSHNGAM GGLGSGYGTG LLSANRHSLM
460 470 480 490 500
VGTHREDGVA LRGSHSLLPN QVPVPQLPVQ SATSPDLNPP QDPYRGMPPG
510 520 530 540 550
LQGQSVSSGS SEIKSDDEGD ENLQDTKSSE DKKLDDDKKD IKSITSNNDD
560 570 580 590 600
EDLTPEQKAE REKERRMANN ARERLRVRDI NEAFKELGRM VQLHLKSDKP
610 620 630 640 650
QTKLLILHQA VAVILSLEQQ VRERNLNPKA ACLKRREEEK VSSEPPPLSL
660
AGPHPGMGDA SNHMGQM
Length:667
Mass (Da):71,308
Last modified:December 15, 1998 - v3
Checksum:i53459FC7989D9487
GO
Isoform SEF2-1A (identifier: P15884-2) [UniParc]FASTAAdd to basket

Also known as: A+

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     161-183: LHSSAMEVQTKKVRKVPPGLPSS → MYCAYTIPGMGGNSLMYYYNGKA
     545-545: T → TRSRS

Show »
Length:511
Mass (Da):54,621
Checksum:i53BE8B2756C9C26B
GO
Isoform SEF2-1D (identifier: P15884-3) [UniParc]FASTAAdd to basket

Also known as: B+

The sequence of this isoform differs from the canonical sequence as follows:
     545-545: T → TRSRS

Show »
Length:671
Mass (Da):71,795
Checksum:i2A3AE4C1E87B81E4
GO
Isoform B+delta (identifier: P15884-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-183: Missing.
     545-545: T → TRSRS

Show »
Length:611
Mass (Da):65,282
Checksum:iC9C6986AA5563828
GO
Isoform B-delta (identifier: P15884-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-183: Missing.

Show »
Length:607
Mass (Da):64,796
Checksum:iAE68260B30C1B9E6
GO
Isoform A- (identifier: P15884-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MHHQQRMAALGTDKELSDLLDFS → MYCAYTIPGMGGNSLMYYYNGKA
     24-123: Missing.
     124-183: Missing.

Show »
Length:507
Mass (Da):54,135
Checksum:i2DF7DC48C2D3EE83
GO
Isoform G- (identifier: P15884-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MHHQQRMAALGTDKELSDLLDFSAMFSPPVSS → MKDIFFQFIIARVRKCYSLSCLHTLPVVPTLR
     33-102: Missing.
     123-123: Missing.

Show »
Length:596
Mass (Da):64,116
Checksum:i5912C40D16E30908
GO
Isoform H- (identifier: P15884-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MHHQQRMAALGTDKELSDLLDFS → MKFKQCRCSDTGLCCLDHEGKAE
     24-183: Missing.

Show »
Length:507
Mass (Da):54,169
Checksum:iF88FFDCB9733FB31
GO
Isoform D- (identifier: P15884-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.

Show »
Length:537
Mass (Da):57,425
Checksum:i7F77B2E736AC27E4
GO
Isoform F- (identifier: P15884-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSN → MEEDSRD

Show »
Length:625
Mass (Da):67,027
Checksum:i36CF6C747000814D
GO
Isoform 11 (identifier: P15884-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: MHHQQRMAAL...PPFVNSRIQS → MKDIFFQFIIARVRKCYSLSCLHTLPVVPTLR
     123-123: Missing.
     545-545: T → TRSRS

Show »
Length:600
Mass (Da):64,602
Checksum:iFA530DE0722CDA2E
GO
Isoform E- (identifier: P15884-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MHHQQRMAALGTDKELSDLLDFSA → MQRAKTELFRLQIVTDDLRKNE
     357-357: Missing.

Show »
Length:664
Mass (Da):71,227
Checksum:i064EA9F64B55C741
GO
Isoform 13 (identifier: P15884-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     545-545: T → TRSRS

Show »
Length:647
Mass (Da):69,098
Checksum:i1ED8C14A73F678C1
GO
Isoform C- (identifier: P15884-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.

Show »
Length:643
Mass (Da):68,611
Checksum:i68C866E2BBBAB621
GO
Isoform C-delta (identifier: P15884-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     124-183: Missing.

Show »
Length:583
Mass (Da):62,099
Checksum:i6B694DB9DDCB93B6
GO
Isoform I- (identifier: P15884-16) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-216: Missing.

Show »
Length:451
Mass (Da):48,098
Checksum:iFD0EE9CD3312CFB4
GO

Sequence cautioni

The sequence AAA60310.1 differs from that shown.Incomplete and probable erroneous sequence.Curated
The sequence AAA60312.1 differs from that shown.Incomplete and probable erroneous sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 494TGSN → EFGG in CAA36298 (PubMed:2308860).Curated
Sequence conflicti205 – 2051Missing in AV761952 (Ref. 7) Curated
Sequence conflicti334 – 3341P → S in CAA36298 (PubMed:2308860).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti358 – 3581G → V in PTHS; also expressed in the nucleus with a pattern indistinguishable from the wild-type; does not have a major impact on homodimer formation; affects transcriptional activity in a context-dependent manner. 2 Publications
VAR_066839
Natural varianti450 – 4501M → I.
Corresponds to variant rs11660217 [ dbSNP | Ensembl ].
VAR_049545
Natural varianti535 – 5351D → G in PTHS; loss of function; also expressed in the nucleus with a pattern indistinguishable from the wild-type; does not have a major impact on homodimer formation; affects transcriptional activity in a context-dependent manner. 2 Publications
VAR_058632
Natural varianti565 – 5651R → W in PTHS. 1 Publication
VAR_066970
Natural varianti572 – 5721R → G in PTHS; loss of function. 2 Publications
VAR_058633
Natural varianti572 – 5721R → Q in PTHS. 1 Publication
VAR_066971
Natural varianti574 – 5741R → H in PTHS. 1 Publication
VAR_066972
Natural varianti574 – 5741R → P in PTHS; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner. 3 Publications
VAR_066840
Natural varianti576 – 5761R → Q in PTHS; loss of function. 3 Publications
VAR_034704
Natural varianti576 – 5761R → W in PTHS; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner. 4 Publications
VAR_034705
Natural varianti578 – 5781R → H in PTHS. 1 Publication
VAR_066841
Natural varianti578 – 5781R → P in PTHS. 2 Publications
VAR_066973
Natural varianti583 – 5831A → P in PTHS. 1 Publication
VAR_066974
Natural varianti610 – 6101A → V in PTHS; loss of function; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner. 3 Publications
VAR_058634

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 216216Missing in isoform I-. 1 PublicationVSP_054279Add
BLAST
Alternative sequencei1 – 160160Missing in isoform SEF2-1A. 4 PublicationsVSP_030819Add
BLAST
Alternative sequencei1 – 130130Missing in isoform D-. 2 PublicationsVSP_045149Add
BLAST
Alternative sequencei1 – 102102MHHQQ…SRIQS → MKDIFFQFIIARVRKCYSLS CLHTLPVVPTLR in isoform 11. 1 PublicationVSP_045150Add
BLAST
Alternative sequencei1 – 4949MHHQQ…FTGSN → MEEDSRD in isoform F-. 2 PublicationsVSP_045151Add
BLAST
Alternative sequencei1 – 3232MHHQQ…PPVSS → MKDIFFQFIIARVRKCYSLS CLHTLPVVPTLR in isoform G-. 1 PublicationVSP_044334Add
BLAST
Alternative sequencei1 – 2424Missing in isoform 13, isoform C- and isoform C-delta. 2 PublicationsVSP_047081Add
BLAST
Alternative sequencei1 – 2424MHHQQ…LDFSA → MQRAKTELFRLQIVTDDLRK NE in isoform E-. 1 PublicationVSP_047082Add
BLAST
Alternative sequencei1 – 2323MHHQQ…LLDFS → MYCAYTIPGMGGNSLMYYYN GKA in isoform A-. 1 PublicationVSP_044336Add
BLAST
Alternative sequencei1 – 2323MHHQQ…LLDFS → MKFKQCRCSDTGLCCLDHEG KAE in isoform H-. 1 PublicationVSP_044335Add
BLAST
Alternative sequencei24 – 183160Missing in isoform H-. 1 PublicationVSP_057364Add
BLAST
Alternative sequencei24 – 123100Missing in isoform A-. 1 PublicationVSP_044337Add
BLAST
Alternative sequencei33 – 10270Missing in isoform G-. 1 PublicationVSP_044338Add
BLAST
Alternative sequencei123 – 1231Missing in isoform G- and isoform 11. 2 PublicationsVSP_044339
Alternative sequencei124 – 18360Missing in isoform A-, isoform B-delta, isoform B+delta and isoform C-delta. 1 PublicationVSP_044340Add
BLAST
Alternative sequencei161 – 18323LHSSA…GLPSS → MYCAYTIPGMGGNSLMYYYN GKA in isoform SEF2-1A. 4 PublicationsVSP_002111Add
BLAST
Alternative sequencei357 – 3571Missing in isoform E-. 1 PublicationVSP_047083
Alternative sequencei545 – 5451T → TRSRS in isoform B+delta, isoform SEF2-1A, isoform SEF2-1D, isoform 11 and isoform 13. 5 PublicationsVSP_002112

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74718 mRNA. Translation: AAA60310.1. Sequence problems.
M74719 mRNA. Translation: AAA60311.1.
M74720 mRNA. Translation: AAA60312.1. Sequence problems.
FR748210 mRNA. Translation: CBY80189.1.
FR748211 mRNA. Translation: CBY80190.1.
FR748212 mRNA. Translation: CBY80191.1.
FR748213 mRNA. Translation: CBY80192.1.
FR748214 mRNA. Translation: CBY80193.1.
FR748215 mRNA. Translation: CBY80194.1.
FR748216 mRNA. Translation: CBY80195.1.
FR748217 mRNA. Translation: CBY80196.1.
FR748218 mRNA. Translation: CBY80197.1.
FR748219 mRNA. Translation: CBY80198.1.
FR748220 mRNA. Translation: CBY80199.1.
FR748221 mRNA. Translation: CBY80200.1.
FR748222 mRNA. Translation: CBY80201.1.
FR748223 mRNA. Translation: CBY80202.1.
AK095041 mRNA. Translation: BAG52974.1.
AK096862 mRNA. Translation: BAG53382.1.
AK299169 mRNA. Translation: BAH12962.1.
AK300636 mRNA. Translation: BAG62325.1.
AK300038 mRNA. Translation: BAG61849.1.
AK301144 mRNA. Translation: BAH13417.1.
AK300612 mRNA. Translation: BAH13314.1.
AK316165 mRNA. Translation: BAH14536.1.
AC013587 Genomic DNA. No translation available.
AC018994 Genomic DNA. No translation available.
AC090383 Genomic DNA. No translation available.
AC090684 Genomic DNA. No translation available.
AC091103 Genomic DNA. No translation available.
CH471096 Genomic DNA. Translation: EAW63017.1.
CH471096 Genomic DNA. Translation: EAW63018.1.
BC125084 mRNA. Translation: AAI25085.1.
BC125085 mRNA. Translation: AAI25086.1.
AV761952 mRNA. No translation available.
U75701 Genomic DNA. Translation: AAC51824.1.
X52079 mRNA. Translation: CAA36298.1.
CCDSiCCDS11960.1. [P15884-1]
CCDS42438.1. [P15884-3]
CCDS58624.1. [P15884-2]
CCDS58625.1. [P15884-6]
CCDS58626.1. [P15884-9]
CCDS58627.1. [P15884-11]
CCDS58628.1. [P15884-10]
CCDS58629.1. [P15884-13]
CCDS59321.1. [P15884-12]
PIRiA41311.
RefSeqiNP_001077431.1. NM_001083962.1. [P15884-3]
NP_001230155.2. NM_001243226.2.
NP_001230156.1. NM_001243227.1. [P15884-13]
NP_001230157.1. NM_001243228.1.
NP_001230159.1. NM_001243230.1. [P15884-12]
NP_001230160.1. NM_001243231.1. [P15884-10]
NP_001230161.1. NM_001243232.1. [P15884-11]
NP_001230162.1. NM_001243233.1. [P15884-9]
NP_001230163.1. NM_001243234.1. [P15884-2]
NP_001230164.1. NM_001243235.1. [P15884-6]
NP_001230165.1. NM_001243236.1.
NP_003190.1. NM_003199.2. [P15884-1]
XP_005266800.1. XM_005266743.2. [P15884-13]
XP_005266801.1. XM_005266744.2. [P15884-13]
XP_005266803.1. XM_005266746.2. [P15884-14]
XP_005266807.1. XM_005266750.2. [P15884-7]
XP_006722599.1. XM_006722536.1. [P15884-3]
XP_006722600.1. XM_006722537.1. [P15884-3]
XP_006722603.1. XM_006722540.1. [P15884-9]
UniGeneiHs.605153.
Hs.742885.

Genome annotation databases

EnsembliENST00000354452; ENSP00000346440; ENSG00000196628. [P15884-3]
ENST00000356073; ENSP00000348374; ENSG00000196628. [P15884-1]
ENST00000457482; ENSP00000409447; ENSG00000196628. [P15884-2]
ENST00000537578; ENSP00000440731; ENSG00000196628. [P15884-13]
ENST00000537856; ENSP00000439827; ENSG00000196628. [P15884-9]
ENST00000540999; ENSP00000445202; ENSG00000196628. [P15884-14]
ENST00000543082; ENSP00000439656; ENSG00000196628. [P15884-10]
ENST00000544241; ENSP00000441562; ENSG00000196628. [P15884-11]
ENST00000561831; ENSP00000457765; ENSG00000196628. [P15884-8]
ENST00000561992; ENSP00000455179; ENSG00000196628. [P15884-9]
ENST00000564228; ENSP00000455261; ENSG00000196628. [P15884-7]
ENST00000564999; ENSP00000457649; ENSG00000196628. [P15884-1]
ENST00000565018; ENSP00000455984; ENSG00000196628. [P15884-3]
ENST00000566279; ENSP00000456125; ENSG00000196628. [P15884-4]
ENST00000566286; ENSP00000455418; ENSG00000196628. [P15884-12]
ENST00000567880; ENSP00000454366; ENSG00000196628. [P15884-5]
ENST00000568673; ENSP00000455135; ENSG00000196628. [P15884-13]
ENST00000570177; ENSP00000454647; ENSG00000196628. [P15884-9]
ENST00000570287; ENSP00000455763; ENSG00000196628. [P15884-6]
ENST00000616053; ENSP00000478549; ENSG00000196628. [P15884-15]
GeneIDi6925.
KEGGihsa:6925.
UCSCiuc002lfw.4. human. [P15884-2]
uc002lfx.2. human.
uc002lfy.2. human.
uc002lfz.2. human. [P15884-1]
uc010dph.1. human. [P15884-3]
uc021ukh.1. human. [P15884-6]
uc021uki.1. human. [P15884-7]
uc021ukj.1. human. [P15884-5]
uc021ukk.1. human. [P15884-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74718 mRNA. Translation: AAA60310.1. Sequence problems.
M74719 mRNA. Translation: AAA60311.1.
M74720 mRNA. Translation: AAA60312.1. Sequence problems.
FR748210 mRNA. Translation: CBY80189.1.
FR748211 mRNA. Translation: CBY80190.1.
FR748212 mRNA. Translation: CBY80191.1.
FR748213 mRNA. Translation: CBY80192.1.
FR748214 mRNA. Translation: CBY80193.1.
FR748215 mRNA. Translation: CBY80194.1.
FR748216 mRNA. Translation: CBY80195.1.
FR748217 mRNA. Translation: CBY80196.1.
FR748218 mRNA. Translation: CBY80197.1.
FR748219 mRNA. Translation: CBY80198.1.
FR748220 mRNA. Translation: CBY80199.1.
FR748221 mRNA. Translation: CBY80200.1.
FR748222 mRNA. Translation: CBY80201.1.
FR748223 mRNA. Translation: CBY80202.1.
AK095041 mRNA. Translation: BAG52974.1.
AK096862 mRNA. Translation: BAG53382.1.
AK299169 mRNA. Translation: BAH12962.1.
AK300636 mRNA. Translation: BAG62325.1.
AK300038 mRNA. Translation: BAG61849.1.
AK301144 mRNA. Translation: BAH13417.1.
AK300612 mRNA. Translation: BAH13314.1.
AK316165 mRNA. Translation: BAH14536.1.
AC013587 Genomic DNA. No translation available.
AC018994 Genomic DNA. No translation available.
AC090383 Genomic DNA. No translation available.
AC090684 Genomic DNA. No translation available.
AC091103 Genomic DNA. No translation available.
CH471096 Genomic DNA. Translation: EAW63017.1.
CH471096 Genomic DNA. Translation: EAW63018.1.
BC125084 mRNA. Translation: AAI25085.1.
BC125085 mRNA. Translation: AAI25086.1.
AV761952 mRNA. No translation available.
U75701 Genomic DNA. Translation: AAC51824.1.
X52079 mRNA. Translation: CAA36298.1.
CCDSiCCDS11960.1. [P15884-1]
CCDS42438.1. [P15884-3]
CCDS58624.1. [P15884-2]
CCDS58625.1. [P15884-6]
CCDS58626.1. [P15884-9]
CCDS58627.1. [P15884-11]
CCDS58628.1. [P15884-10]
CCDS58629.1. [P15884-13]
CCDS59321.1. [P15884-12]
PIRiA41311.
RefSeqiNP_001077431.1. NM_001083962.1. [P15884-3]
NP_001230155.2. NM_001243226.2.
NP_001230156.1. NM_001243227.1. [P15884-13]
NP_001230157.1. NM_001243228.1.
NP_001230159.1. NM_001243230.1. [P15884-12]
NP_001230160.1. NM_001243231.1. [P15884-10]
NP_001230161.1. NM_001243232.1. [P15884-11]
NP_001230162.1. NM_001243233.1. [P15884-9]
NP_001230163.1. NM_001243234.1. [P15884-2]
NP_001230164.1. NM_001243235.1. [P15884-6]
NP_001230165.1. NM_001243236.1.
NP_003190.1. NM_003199.2. [P15884-1]
XP_005266800.1. XM_005266743.2. [P15884-13]
XP_005266801.1. XM_005266744.2. [P15884-13]
XP_005266803.1. XM_005266746.2. [P15884-14]
XP_005266807.1. XM_005266750.2. [P15884-7]
XP_006722599.1. XM_006722536.1. [P15884-3]
XP_006722600.1. XM_006722537.1. [P15884-3]
XP_006722603.1. XM_006722540.1. [P15884-9]
UniGeneiHs.605153.
Hs.742885.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KWFNMR-B11-27[»]
DisProtiDP00224.
ProteinModelPortaliP15884.
SMRiP15884. Positions 565-624.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112787. 181 interactions.
DIPiDIP-163N.
IntActiP15884. 21 interactions.
MINTiMINT-4508073.
STRINGi9606.ENSP00000346440.

PTM databases

PhosphoSiteiP15884.

Proteomic databases

MaxQBiP15884.
PaxDbiP15884.
PRIDEiP15884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354452; ENSP00000346440; ENSG00000196628. [P15884-3]
ENST00000356073; ENSP00000348374; ENSG00000196628. [P15884-1]
ENST00000457482; ENSP00000409447; ENSG00000196628. [P15884-2]
ENST00000537578; ENSP00000440731; ENSG00000196628. [P15884-13]
ENST00000537856; ENSP00000439827; ENSG00000196628. [P15884-9]
ENST00000540999; ENSP00000445202; ENSG00000196628. [P15884-14]
ENST00000543082; ENSP00000439656; ENSG00000196628. [P15884-10]
ENST00000544241; ENSP00000441562; ENSG00000196628. [P15884-11]
ENST00000561831; ENSP00000457765; ENSG00000196628. [P15884-8]
ENST00000561992; ENSP00000455179; ENSG00000196628. [P15884-9]
ENST00000564228; ENSP00000455261; ENSG00000196628. [P15884-7]
ENST00000564999; ENSP00000457649; ENSG00000196628. [P15884-1]
ENST00000565018; ENSP00000455984; ENSG00000196628. [P15884-3]
ENST00000566279; ENSP00000456125; ENSG00000196628. [P15884-4]
ENST00000566286; ENSP00000455418; ENSG00000196628. [P15884-12]
ENST00000567880; ENSP00000454366; ENSG00000196628. [P15884-5]
ENST00000568673; ENSP00000455135; ENSG00000196628. [P15884-13]
ENST00000570177; ENSP00000454647; ENSG00000196628. [P15884-9]
ENST00000570287; ENSP00000455763; ENSG00000196628. [P15884-6]
ENST00000616053; ENSP00000478549; ENSG00000196628. [P15884-15]
GeneIDi6925.
KEGGihsa:6925.
UCSCiuc002lfw.4. human. [P15884-2]
uc002lfx.2. human.
uc002lfy.2. human.
uc002lfz.2. human. [P15884-1]
uc010dph.1. human. [P15884-3]
uc021ukh.1. human. [P15884-6]
uc021uki.1. human. [P15884-7]
uc021ukj.1. human. [P15884-5]
uc021ukk.1. human. [P15884-4]

Organism-specific databases

CTDi6925.
GeneCardsiGC18M052889.
GeneReviewsiTCF4.
HGNCiHGNC:11634. TCF4.
HPAiCAB020722.
HPA025958.
MIMi602272. gene.
610954. phenotype.
neXtProtiNX_P15884.
Orphaneti178469. Autosomal dominant non-syndromic intellectual disability.
98974. Fuchs endothelial corneal dystrophy.
2896. Pitt-Hopkins syndrome.
171. Primary sclerosing cholangitis.
3140. Schizophrenia.
PharmGKBiPA164742621.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282899.
GeneTreeiENSGT00510000046438.
HOVERGENiHBG003854.
InParanoidiP15884.
KOiK15603.
OrthoDBiEOG72G16Q.
PhylomeDBiP15884.
TreeFamiTF321672.

Enzyme and pathway databases

ReactomeiREACT_21402. CDO in myogenesis.
SignaLinkiP15884.

Miscellaneous databases

ChiTaRSiTCF4. human.
EvolutionaryTraceiP15884.
GeneWikiiTCF4.
GenomeRNAii6925.
NextBioi27093.
PROiP15884.
SOURCEiSearch...

Gene expression databases

BgeeiP15884.
CleanExiHS_TCF4.
ExpressionAtlasiP15884. baseline and differential.
GenevestigatoriP15884.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Helix-loop-helix transcriptional activators bind to a sequence in glucocorticoid response elements of retrovirus enhancers."
    Corneliussen B., Thornell A., Hallberg B., Grundstroem T.
    J. Virol. 65:6084-6093(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SEF2-1A; SEF2-1B AND SEF2-1D), ALTERNATIVE SPLICING (ISOFORM SEF2-1C).
    Tissue: Thymocyte and Thymus.
  2. "Functional diversity of human basic helix-loop-helix transcription factor TCF4 isoforms generated by alternative 5' exon usage and splicing."
    Sepp M., Kannike K., Eesmaa A., Urb M., Timmusk T.
    PLoS ONE 6:E22138-E22138(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A-; B-DELTA; B+DELTA; C-; C-DELTA; D-; E-; F-; G-; H-; I-; SEF2-1A; SEF2-1B AND SEF2-1D), ALTERNATIVE SPLICING.
  3. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SEF2-1A; C-; D-; F-; 11 AND 13).
    Tissue: Brain, Hippocampus, Spleen and Teratocarcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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 SEF2-1B AND SEF2-1D).
  7. "MDSDCE06_MDS Homo sapiens cDNA clone MDSDCE06 5',mRNA sequence."
    Gu J., Zhao M., Huang Q., Xu X., Li Y., Peng Y., Song H., Xiao H., Gu Y., Li N., Qian B., Liu F., Qu J., Gao X., Cheng Z., Xu Z., Zeng L., Xu S.
    , Gu W., Tu Y., Jia J., Fu G., Ren S., Zhong M., Lu G., Yang Y., Gao G., Zhang Q., Chen S., Han Z., Chen Z.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-278 (ISOFORM SEF2-1A).
  8. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-48.
    Tissue: Skin fibroblast.
  9. "Sequence of the cDNA encoding ITF-2, a positive-acting transcription factor."
    Henthorn P., McCarrick-Walmsley R., Kadesch T.
    Nucleic Acids Res. 18:678-678(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-667 (ISOFORM SEF2-1B).
  10. "Two distinct transcription factors that bind the immunoglobulin enhancer microE5/kappa 2 motif."
    Henthorn P., Kiledjian M., Kadesch T.
    Science 247:467-470(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.
  11. "Nine-amino-acid transactivation domain: establishment and prediction utilities."
    Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
    Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  12. "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-515, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Functional analysis of TCF4 missense mutations that cause Pitt-Hopkins syndrome."
    Forrest M., Chapman R.M., Doyle A.M., Tinsley C.L., Waite A., Blake D.J.
    Hum. Mutat. 33:1676-1686(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS PTHS VAL-358; GLY-535; PRO-574; TRP-576 AND VAL-610.
  14. "Mutations in AGBL1 cause dominant late-onset Fuchs corneal dystrophy and alter protein-protein interaction with TCF4."
    Riazuddin S.A., Vasanth S., Katsanis N., Gottsch J.D.
    Am. J. Hum. Genet. 93:758-764(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGBL1.
  15. "Mutations in TCF4, encoding a class I basic helix-loop-helix transcription factor, are responsible for Pitt-Hopkins syndrome, a severe epileptic encephalopathy associated with autonomic dysfunction."
    Amiel J., Rio M., de Pontual L., Redon R., Malan V., Boddaert N., Plouin P., Carter N.P., Lyonnet S., Munnich A., Colleaux L.
    Am. J. Hum. Genet. 80:988-993(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PTHS TRP-576 AND GLN-576.
  16. Cited for: VARIANT PTHS TRP-576.
  17. Cited for: VARIANTS PTHS VAL-358; PRO-574 AND HIS-578.
  18. Cited for: VARIANTS PTHS GLY-535; GLY-572; GLN-576 AND VAL-610, CHARACTERIZATION OF VARIANTS PTHS GLY-535; GLY-572; GLN-576 AND VAL-610.
  19. "Two percent of patients suspected of having Angelman syndrome have TCF4 mutations."
    Takano K., Lyons M., Moyes C., Jones J., Schwartz C.E.
    Clin. Genet. 78:282-288(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PTHS PRO-578.
  20. Cited for: VARIANTS PTHS TRP-565; GLY-572; GLN-572; HIS-574; PRO-574; TRP-576; GLN-576; PRO-578; PRO-583 AND VAL-610.

Entry informationi

Entry nameiITF2_HUMAN
AccessioniPrimary (citable) accession number: P15884
Secondary accession number(s): B3KT62
, B3KUC0, B4DT37, B4DUG3, B7Z5M6, B7Z6Y1, G0LNT9, G0LNU0, G0LNU1, G0LNU2, G0LNU4, G0LNU5, G0LNU8, G0LNU9, G0LNV0, G0LNV1, G0LNV2, H3BPQ1, Q08AP2, Q08AP3, Q15439, Q15440, Q15441
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 15, 1998
Last modified: March 4, 2015
This is version 163 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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.