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P17542

- TAL1_HUMAN

UniProt

P17542 - TAL1_HUMAN

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Protein
T-cell acute lymphocytic leukemia protein 1
Gene
TAL1, BHLHA17, SCL, TCL5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation By similarity.1 Publication

GO - Molecular functioni

  1. E-box binding Source: BHF-UCL
  2. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  3. RNA polymerase II transcription factor binding Source: BHF-UCL
  4. chromatin binding Source: MGI
  5. enzyme binding Source: BHF-UCL
  6. histone deacetylase binding Source: BHF-UCL
  7. protein binding Source: UniProtKB
  8. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: Ensembl
  9. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  10. transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. astrocyte fate commitment Source: Ensembl
  3. basophil differentiation Source: BHF-UCL
  4. cell fate commitment Source: BHF-UCL
  5. definitive hemopoiesis Source: Ensembl
  6. embryonic hemopoiesis Source: UniProtKB
  7. erythrocyte differentiation Source: BHF-UCL
  8. erythrocyte maturation Source: Ensembl
  9. hemangioblast cell differentiation Source: Ensembl
  10. hematopoietic stem cell differentiation Source: Ensembl
  11. hemopoiesis Source: BHF-UCL
  12. locomotory behavior Source: Ensembl
  13. megakaryocyte development Source: Ensembl
  14. megakaryocyte differentiation Source: BHF-UCL
  15. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  16. platelet formation Source: Ensembl
  17. positive regulation of cell division Source: BHF-UCL
  18. positive regulation of chromatin assembly or disassembly Source: BHF-UCL
  19. positive regulation of erythrocyte differentiation Source: UniProtKB
  20. positive regulation of mitotic cell cycle Source: BHF-UCL
  21. positive regulation of protein complex assembly Source: BHF-UCL
  22. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  23. positive regulation of transcription, DNA-templated Source: UniProtKB
  24. regulation of cell proliferation Source: Ensembl
  25. regulation of mast cell differentiation Source: Ensembl
  26. regulation of stem cell maintenance Source: Ensembl
  27. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  28. spinal cord association neuron differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiP17542.

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell acute lymphocytic leukemia protein 1
Short name:
TAL-1
Alternative name(s):
Class A basic helix-loop-helix protein 17
Short name:
bHLHa17
Stem cell protein
T-cell leukemia/lymphoma protein 5
Gene namesi
Name:TAL1
Synonyms:BHLHA17, SCL, TCL5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:11556. TAL1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nuclear chromatin Source: BHF-UCL
  2. nucleus Source: BHF-UCL
  3. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TAL1 may be a cause of some T-cell acute lymphoblastic leukemias (T-ALL). Translocation t(1;14)(p32;q11) with T-cell receptor alpha chain (TCRA) genes.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA36326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331T-cell acute lymphocytic leukemia protein 1
PRO_0000127454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei122 – 1221Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine residues. Phosphorylation of Ser-122 is strongly stimulated by hypoxia By similarity.1 Publication
Ubiquitinated; subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system. This process may be characteristic for microvascular endothelial cells, since it could not be observed in large vessel endothelial cells By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP17542.
PaxDbiP17542.
PRIDEiP17542.

PTM databases

PhosphoSiteiP17542.

Miscellaneous databases

PMAP-CutDBP17542.

Expressioni

Tissue specificityi

Leukemic stem cell.

Gene expression databases

ArrayExpressiP17542.
BgeeiP17542.
CleanExiHS_TAL1.
GenevestigatoriP17542.

Organism-specific databases

HPAiCAB017805.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Forms heterodimers with TCF3. Binds to the LIM domain containing protein LMO2 and to DRG1. Can assemble in a complex with LDB1 and LMO2. Component of a TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3 By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
ETS1P149212EBI-1753878,EBI-913209
Lmo2P258015EBI-1753878,EBI-3903256From a different organism.
RUNX1Q011962EBI-1753878,EBI-925904
TCF3P159235EBI-1753878,EBI-769630

Protein-protein interaction databases

BioGridi112749. 50 interactions.
DIPiDIP-40640N.
IntActiP17542. 15 interactions.
MINTiMINT-2801392.
STRINGi9606.ENSP00000294339.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi184 – 21128
Helixi225 – 24521

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YPAX-ray2.80A180-253[»]
2YPBX-ray2.87A180-253[»]
ProteinModelPortaliP17542.
SMRiP17542. Positions 182-248.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini187 – 23953bHLH
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi89 – 13244Pro-rich
Add
BLAST
Compositional biasi263 – 27412Poly-Gly
Add
BLAST

Domaini

The helix-loop-helix domain is necessary and sufficient for the interaction with DRG1.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG307510.
HOGENOMiHOG000113414.
HOVERGENiHBG005018.
KOiK09068.
OrthoDBiEOG7SN8DF.
PhylomeDBiP17542.
TreeFamiTF315153.

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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: The splicing pattern is cell-lineage dependent.

Isoform PP42-TAL1 (identifier: P17542-1) [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

MTERPPSEAA RSDPQLEGRD AAEASMAPPH LVLLNGVAKE TSRAAAAEPP    50
VIELGARGGP GGGPAGGGGA ARDLKGRDAA TAEARHRVPT TELCRPPGPA 100
PAPAPASVTA ELPGDGRMVQ LSPPALAAPA APGRALLYSL SQPLASLGSG 150
FFGEPDAFPM FTTNNRVKRR PSPYEMEITD GPHTKVVRRI FTNSRERWRQ 200
QNVNGAFAEL RKLIPTHPPD KKLSKNEILR LAMKYINFLA KLLNDQEEEG 250
TQRAKTGKDP VVGAGGGGGG GGGGAPPDDL LQDVLSPNSS CGSSLDGAAS 300
PDSYTEEPAP KHTARSLHPA MLPAADGAGP R 331
Length:331
Mass (Da):34,271
Last modified:November 1, 1991 - v2
Checksum:i33BBE31589DBB7C7
GO
Isoform PP39-TAL1 (identifier: P17542-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.

Show »
Length:306
Mass (Da):31,617
Checksum:i4457C743678771FE
GO
Isoform PP22-TAL1 (identifier: P17542-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-175: Missing.

Show »
Length:156
Mass (Da):16,548
Checksum:i5BC0D5F12E261CDE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 175175Missing in isoform PP22-TAL1.
VSP_002154Add
BLAST
Alternative sequencei1 – 2525Missing in isoform PP39-TAL1.
VSP_002153Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M61108 mRNA. Translation: AAA36600.1.
M61103 Genomic DNA. No translation available.
M61104 Genomic DNA. No translation available.
M61105 Genomic DNA. No translation available.
M63572 Genomic DNA. No translation available.
M63589, M63576, M63584 Genomic DNA. Translation: AAA36599.1.
AL135960 Genomic DNA. Translation: CAB72103.1.
CH471059 Genomic DNA. Translation: EAX06875.1.
CH471059 Genomic DNA. Translation: EAX06876.1.
CH471059 Genomic DNA. Translation: EAX06877.1.
X58621 Genomic DNA. Translation: CAA41476.1. Sequence problems.
X58622 Genomic DNA. Translation: CAA41477.1.
M29038 mRNA. Translation: AAA36598.1.
X51990 mRNA. Translation: CAA36246.1.
CCDSiCCDS547.1. [P17542-1]
PIRiA36358.
I38253.
RefSeqiNP_001274276.1. NM_001287347.2. [P17542-1]
NP_001277332.1. NM_001290403.1. [P17542-1]
NP_001277333.1. NM_001290404.1. [P17542-1]
NP_001277334.1. NM_001290405.1. [P17542-1]
NP_001277335.1. NM_001290406.1.
NP_003180.1. NM_003189.5. [P17542-1]
XP_005271216.1. XM_005271159.2. [P17542-1]
XP_005271217.1. XM_005271160.2. [P17542-1]
XP_006710925.1. XM_006710862.1. [P17542-1]
UniGeneiHs.705618.
Hs.737706.

Genome annotation databases

EnsembliENST00000294339; ENSP00000294339; ENSG00000162367. [P17542-1]
ENST00000371884; ENSP00000360951; ENSG00000162367. [P17542-1]
GeneIDi6886.
KEGGihsa:6886.
UCSCiuc001cqx.2. human. [P17542-1]

Polymorphism databases

DMDMi134305.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M61108 mRNA. Translation: AAA36600.1 .
M61103 Genomic DNA. No translation available.
M61104 Genomic DNA. No translation available.
M61105 Genomic DNA. No translation available.
M63572 Genomic DNA. No translation available.
M63589 , M63576 , M63584 Genomic DNA. Translation: AAA36599.1 .
AL135960 Genomic DNA. Translation: CAB72103.1 .
CH471059 Genomic DNA. Translation: EAX06875.1 .
CH471059 Genomic DNA. Translation: EAX06876.1 .
CH471059 Genomic DNA. Translation: EAX06877.1 .
X58621 Genomic DNA. Translation: CAA41476.1 . Sequence problems.
X58622 Genomic DNA. Translation: CAA41477.1 .
M29038 mRNA. Translation: AAA36598.1 .
X51990 mRNA. Translation: CAA36246.1 .
CCDSi CCDS547.1. [P17542-1 ]
PIRi A36358.
I38253.
RefSeqi NP_001274276.1. NM_001287347.2. [P17542-1 ]
NP_001277332.1. NM_001290403.1. [P17542-1 ]
NP_001277333.1. NM_001290404.1. [P17542-1 ]
NP_001277334.1. NM_001290405.1. [P17542-1 ]
NP_001277335.1. NM_001290406.1.
NP_003180.1. NM_003189.5. [P17542-1 ]
XP_005271216.1. XM_005271159.2. [P17542-1 ]
XP_005271217.1. XM_005271160.2. [P17542-1 ]
XP_006710925.1. XM_006710862.1. [P17542-1 ]
UniGenei Hs.705618.
Hs.737706.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YPA X-ray 2.80 A 180-253 [» ]
2YPB X-ray 2.87 A 180-253 [» ]
ProteinModelPortali P17542.
SMRi P17542. Positions 182-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112749. 50 interactions.
DIPi DIP-40640N.
IntActi P17542. 15 interactions.
MINTi MINT-2801392.
STRINGi 9606.ENSP00000294339.

PTM databases

PhosphoSitei P17542.

Polymorphism databases

DMDMi 134305.

Proteomic databases

MaxQBi P17542.
PaxDbi P17542.
PRIDEi P17542.

Protocols and materials databases

DNASUi 6886.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000294339 ; ENSP00000294339 ; ENSG00000162367 . [P17542-1 ]
ENST00000371884 ; ENSP00000360951 ; ENSG00000162367 . [P17542-1 ]
GeneIDi 6886.
KEGGi hsa:6886.
UCSCi uc001cqx.2. human. [P17542-1 ]

Organism-specific databases

CTDi 6886.
GeneCardsi GC01M047681.
H-InvDB HIX0029300.
HGNCi HGNC:11556. TAL1.
HPAi CAB017805.
MIMi 187040. gene.
neXtProti NX_P17542.
Orphaneti 99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBi PA36326.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307510.
HOGENOMi HOG000113414.
HOVERGENi HBG005018.
KOi K09068.
OrthoDBi EOG7SN8DF.
PhylomeDBi P17542.
TreeFami TF315153.

Enzyme and pathway databases

SignaLinki P17542.

Miscellaneous databases

GeneWikii TAL1.
GenomeRNAii 6886.
NextBioi 26909.
PMAP-CutDB P17542.
PROi P17542.
SOURCEi Search...

Gene expression databases

ArrayExpressi P17542.
Bgeei P17542.
CleanExi HS_TAL1.
Genevestigatori P17542.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
[Graphical view ]
SMARTi SM00353. HLH. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The SCL gene is formed from a transcriptionally complex locus."
    Aplan P.D., Begley C.G., Bertness V., Nussmeier M., Ezquerra A., Coligan J., Kirsch I.R.
    Mol. Cell. Biol. 10:6426-6435(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Coding sequences of the tal-1 gene are disrupted by chromosome translocation in human T cell leukemia."
    Chen Q., Yang C.Y.C., Tsan J.T., Xia Y., Ragab A.H., Peiper S.C., Carroll A., Baer R.
    J. Exp. Med. 172:1403-1408(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-148.
  5. "The gene SCL is expressed during early hematopoiesis and encodes a differentiation-related DNA-binding motif."
    Begley C.G., Aplan P.D., Denning S.M., Haynes B.F., Waldmann T.A., Kirsch I.R.
    Proc. Natl. Acad. Sci. U.S.A. 86:10128-10132(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 118-331.
    Tissue: Bone marrow.
  6. "The tal gene undergoes chromosome translocation in T cell leukemia and potentially encodes a helix-loop-helix protein."
    Chen Q., Cheng J.-T., Tsai L.H., Schneider N., Buchanan G., Carroll A., Crist W., Ozanne B., Siciliano M.J., Baer R.
    EMBO J. 9:415-424(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 181-331.
  7. "The SCL gene product: a positive regulator of erythroid differentiation."
    Aplan P.D., Nakahara K., Orkin S.H., Kirsch I.R.
    EMBO J. 11:4073-4081(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Products of the TAL1 oncogene: basic helix-loop-helix proteins phosphorylated at serine residues."
    Cheng J.-T., Hsu H.-L., Hwang L.-Y., Baer R.
    Oncogene 8:677-683(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiTAL1_HUMAN
AccessioniPrimary (citable) accession number: P17542
Secondary accession number(s): D3DQ24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1991
Last modified: July 9, 2014
This is version 154 of the entry and version 2 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi