SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P12003

- VINC_CHICK

UniProt

P12003 - VINC_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Vinculin

Gene
VCL, VINC1
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.3 Publications

GO - Molecular functioni

  1. alpha-catenin binding Source: BHF-UCL
  2. beta-catenin binding Source: BHF-UCL
  3. cadherin binding Source: BHF-UCL
  4. protein binding Source: IntAct
  5. structural molecule activity Source: InterPro

GO - Biological processi

  1. adherens junction assembly Source: BHF-UCL
  2. apical junction assembly Source: Ensembl
  3. epithelial cell-cell adhesion Source: BHF-UCL
  4. lamellipodium assembly Source: UniProtKB
  5. morphogenesis of an epithelium Source: BHF-UCL
  6. protein localization to cell surface Source: Ensembl
  7. regulation of cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Vinculin
Alternative name(s):
Metavinculin
Gene namesi
Name:VCL
Synonyms:VINC1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side
Note: Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions.2 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: InterPro
  2. adherens junction Source: UniProtKB
  3. cell-cell junction Source: UniProtKB
  4. costamere Source: UniProtKB
  5. fascia adherens Source: Ensembl
  6. focal adhesion Source: UniProtKB
  7. mitochondrial inner membrane Source: UniProtKB
  8. plasma membrane Source: UniProtKB-SubCell
  9. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001Y → F: Some reduction of phosphorylation levels in platelets. Little change in cell spreading. Complete loss of phosphorylation. No change in subcellular location nor on in vitro actin binding. 40% decrease in cell spreading; when associated with F-1134. 1 Publication
Mutagenesisi160 – 1601Y → F: No change of phosphorylation levels in platelets. 1 Publication
Mutagenesisi537 – 5371Y → F: No change of phosphorylation levels in platelets. 1 Publication
Mutagenesisi692 – 6921Y → F: No change of phosphorylation levels in platelets. 1 Publication
Mutagenesisi822 – 8221Y → F: No change of phosphorylation levels in platelets. 1 Publication
Mutagenesisi1134 – 11341Y → F: Greatly reduced phosphorylation levels in platelets. Little change in cell spreading. Complete loss of phosphorylation. No change in subcellular location nor on in vitro actin binding. 40% decrease in cell spreading; when associated with F-100. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 11351134VinculinPRO_0000064255Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001Phosphotyrosine1 Publication
Modified residuei537 – 5371Phosphotyrosine Reviewed prediction
Modified residuei822 – 8221Phosphotyrosine Reviewed prediction
Modified residuei1134 – 11341Phosphotyrosine; by SRC-type Tyr-kinases1 Publication

Post-translational modificationi

Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1134 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques.1 Publication
Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP12003.
PRIDEiP12003.

Expressioni

Tissue specificityi

Isoform Metavinculin is muscle-specific.

Interactioni

Subunit structurei

Exhibits self-association properties. Interacts with APBB1IP, NRAP and TLN1. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN1P05094-25EBI-1039563,EBI-6049246
PXNP490245EBI-1039563,EBI-2896280
Tln1P260393EBI-1039563,EBI-1039593From a different organism.
VASPP505522EBI-1039563,EBI-748201From a different organism.

Protein-protein interaction databases

BioGridi676671. 2 interactions.
DIPiDIP-35191N.
IntActiP12003. 12 interactions.
STRINGi9031.ENSGALP00000008131.

Structurei

Secondary structure

1
1135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2822
Turni29 – 324
Beta strandi33 – 353
Helixi41 – 6323
Helixi68 – 736
Helixi75 – 9723
Helixi102 – 14645
Helixi148 – 1503
Helixi154 – 18128
Helixi185 – 21531
Beta strandi218 – 2214
Helixi222 – 24928
Helixi253 – 2553
Helixi256 – 27520
Helixi277 – 2859
Turni292 – 2954
Helixi296 – 31116
Helixi318 – 33821
Turni339 – 3424
Helixi347 – 39549
Helixi405 – 42117
Helixi428 – 45124
Helixi457 – 48226
Helixi493 – 50513
Helixi516 – 53116
Helixi535 – 55622
Helixi567 – 59832
Helixi604 – 61411
Helixi622 – 65029
Helixi654 – 68128
Turni682 – 6843
Helixi689 – 71426
Helixi719 – 73921
Beta strandi742 – 7443
Turni746 – 7483
Helixi752 – 77221
Helixi777 – 80226
Beta strandi803 – 8064
Turni809 – 8135
Helixi814 – 8174
Turni818 – 8236
Helixi824 – 83512
Beta strandi887 – 8904
Helixi892 – 8954
Helixi897 – 90913
Helixi987 – 100519
Helixi1010 – 10123
Helixi1013 – 104028
Helixi1044 – 105411
Helixi1057 – 107418
Beta strandi1075 – 10773
Helixi1082 – 111332
Helixi1121 – 11233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QKRX-ray1.80A/B879-1135[»]
1ST6X-ray3.10A1-1135[»]
1T01X-ray2.06A1-254[»]
1U6HX-ray2.38A1-259[»]
1XWJX-ray2.60A2-259[»]
1ZVZX-ray1.80A2-259[»]
1ZW2X-ray2.10A2-259[»]
1ZW3X-ray3.30A2-259[»]
2GDCX-ray2.74A1-266[»]
3ZDLX-ray2.30A1-259[»]
4E17X-ray2.30A1-259[»]
4E18X-ray2.40A1-259[»]
DisProtiDP00556.
ProteinModelPortaliP12003.
SMRiP12003. Positions 1-254.

Miscellaneous databases

EvolutionaryTraceiP12003.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati259 – 3691111Add
BLAST
Repeati370 – 4791102Add
BLAST
Repeati480 – 5891103Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 835834N-terminal globular head By similarityAdd
BLAST
Regioni168 – 20841Talin-interactionAdd
BLAST
Regioni259 – 5893313 X 112 AA tandem repeatsAdd
BLAST
Regioni836 – 87843Linker (Pro-rich) By similarityAdd
BLAST
Regioni879 – 1135257C-terminal tail By similarityAdd
BLAST
Regioni1004 – 104744Facilitates phospholipid membrane insertion By similarityAdd
BLAST
Regioni1121 – 113515Facilitates phospholipid membrane insertion By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi837 – 87842Pro-richAdd
BLAST

Domaini

Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion By similarity.1 Publication
The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly By similarity.1 Publication

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG329927.
HOGENOMiHOG000007828.
HOVERGENiHBG079758.
InParanoidiP12003.
KOiK05700.
PhylomeDBiP12003.

Family and domain databases

InterProiIPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PfamiPF01044. Vinculin. 3 hits.
[Graphical view]
PRINTSiPR00806. VINCULIN.
SUPFAMiSSF47220. SSF47220. 8 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]

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 splicing. Align

Isoform 2 (identifier: P12003-2) [UniParc]FASTAAdd to Basket

Also known as: Metavinculin

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

MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA     50
VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY 100
SVPARDYLID GSRGILSGTS DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV 150
VETMEDLVTY TKNLGPGMTK MAKMIDERQQ ELTHQEHRVM LVNSMNTVKE 200
LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE INEIIRVLQL 250
TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR 300
QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM 350
QKAQQVSQGL DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG 400
GSEGEEHIRG IMSEARKVAE LCEEPKERDD ILRSLGEISA LTAKLSDLRR 450
HGKGDSPEAR ALAKQIATSL QNLQSKTNRA VANTRPVKAA VHLEGKIEQA 500
QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD LLAKCDRVDQ 550
LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS 600
DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV 650
GTANKTTVEG IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN 700
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANMQPQMLV 750
AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD 800
AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE 850
HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM 900
AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY 950
EPELLLMPTN QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA 1000
EMSRLVRGGS GNKRALIQCA KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL 1050
LQVCERIPTI STQLKILSTV KATMLGRTNI SDEESEQATE MLVHNAQNLM 1100
QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ 1135
Length:1,135
Mass (Da):124,560
Last modified:January 23, 2007 - v4
Checksum:i28CC2699C9511058
GO
Isoform 1 (identifier: P12003-1) [UniParc]FASTAAdd to Basket

Also known as: Vinculin

The sequence of this isoform differs from the canonical sequence as follows:
     916-984: Missing.

Show »
Length:1,066
Mass (Da):116,999
Checksum:i6F585201260BA47F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei916 – 98469Missing in isoform 1. VSP_010772Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti442 – 4476TAKLSD → QLSCQI1 Publication
Sequence conflicti442 – 4476TAKLSD → QLSCQI in CAA68412. 1 Publication
Sequence conflicti701 – 7011Q → H1 Publication
Sequence conflicti701 – 7011Q → H in CAA68412. 1 Publication
Sequence conflicti880 – 8801E → K in CAA68412. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04126 mRNA. Translation: AAA49136.1.
M87837 Genomic DNA. Translation: AAA49135.1.
Y00312 mRNA. Translation: CAA68412.1.
PIRiA31346. A29997.
RefSeqiNP_990772.1. NM_205441.1. [P12003-1]
UniGeneiGga.698.

Genome annotation databases

GeneIDi396422.
KEGGigga:396422.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04126 mRNA. Translation: AAA49136.1 .
M87837 Genomic DNA. Translation: AAA49135.1 .
Y00312 mRNA. Translation: CAA68412.1 .
PIRi A31346. A29997.
RefSeqi NP_990772.1. NM_205441.1. [P12003-1 ]
UniGenei Gga.698.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QKR X-ray 1.80 A/B 879-1135 [» ]
1ST6 X-ray 3.10 A 1-1135 [» ]
1T01 X-ray 2.06 A 1-254 [» ]
1U6H X-ray 2.38 A 1-259 [» ]
1XWJ X-ray 2.60 A 2-259 [» ]
1ZVZ X-ray 1.80 A 2-259 [» ]
1ZW2 X-ray 2.10 A 2-259 [» ]
1ZW3 X-ray 3.30 A 2-259 [» ]
2GDC X-ray 2.74 A 1-266 [» ]
3ZDL X-ray 2.30 A 1-259 [» ]
4E17 X-ray 2.30 A 1-259 [» ]
4E18 X-ray 2.40 A 1-259 [» ]
DisProti DP00556.
ProteinModelPortali P12003.
SMRi P12003. Positions 1-254.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 676671. 2 interactions.
DIPi DIP-35191N.
IntActi P12003. 12 interactions.
STRINGi 9031.ENSGALP00000008131.

Proteomic databases

PaxDbi P12003.
PRIDEi P12003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396422.
KEGGi gga:396422.

Organism-specific databases

CTDi 7414.

Phylogenomic databases

eggNOGi NOG329927.
HOGENOMi HOG000007828.
HOVERGENi HBG079758.
InParanoidi P12003.
KOi K05700.
PhylomeDBi P12003.

Miscellaneous databases

EvolutionaryTracei P12003.
NextBioi 20816463.
PROi P12003.

Family and domain databases

InterProi IPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view ]
PANTHERi PTHR18914. PTHR18914. 1 hit.
Pfami PF01044. Vinculin. 3 hits.
[Graphical view ]
PRINTSi PR00806. VINCULIN.
SUPFAMi SSF47220. SSF47220. 8 hits.
PROSITEi PS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "cDNA-derived sequence of chicken embryo vinculin."
    Coutu M.D., Craig S.W.
    Proc. Natl. Acad. Sci. U.S.A. 85:8535-8539(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Embryo.
  2. "Primary sequence and domain structure of chicken vinculin."
    Price G.J., Jones P., Davison M.D., Patel B., Bendori R., Geiger B., Critchley D.R.
    Biochem. J. 259:453-461(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Embryo.
  3. "Chicken vinculin and meta-vinculin are derived from a single gene by alternative splicing of a 207-base pair exon unique to meta-vinculin."
    Byrne B.J., Kaczorowski Y.J., Coutu M.D., Craig S.W.
    J. Biol. Chem. 267:12845-12850(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
  4. "Isolation and characterization of a vinculin cDNA from chick-embryo fibroblasts."
    Price G.J., Jones P., Davison M.D., Patel B., Eperon I.C., Critchley D.R.
    Biochem. J. 245:595-603(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-881.
    Tissue: Embryo.
  5. "The cytoskeletal protein vinculin is acylated by myristic acid."
    Kellie S., Wigglesworth N.M.
    FEBS Lett. 213:428-432(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION.
  6. "Identification of a talin binding site in the cytoskeletal protein vinculin."
    Jones P., Jackson P., Price G.J., Patel B., Ohanion V., Lear A.L., Critchley D.R.
    J. Cell Biol. 109:2917-2927(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: TALIN INTERACTION DOMAIN.
  7. "Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks."
    Luo G., Herrera A.H., Horowits R.
    Biochemistry 38:6135-6143(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRAP.
  8. "The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading."
    Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E., Haimovich B.
    Mol. Biol. Cell 15:4234-4247(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-100 AND TYR-1134, FUNCTION, MUTAGENESIS OF TYR-100; TYR-160; TYR-537; TYR-692; TYR-822 AND TYR-1134.
  9. "Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner."
    le Duc Q., Shi Q., Blonk I., Sonnenberg A., Wang N., Leckband D., de Rooij J.
    J. Cell Biol. 189:1107-1115(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin."
    Peng X., Cuff L.E., Lawton C.D., DeMali K.A.
    J. Cell Sci. 123:567-577(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1.
  11. "Crystal structure of the vinculin tail suggests a pathway for activation."
    Bakolitsa C., de Pereda J.M., Bagshaw C.R., Critchley D.R., Liddington R.C.
    Cell 99:603-613(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 881-1135 OF ISOFORM 1.
  12. "RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover."
    Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R., Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.
    J. Biol. Chem. 288:8238-8249(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-259 IN COMPLEX WITH APBB1IP, INTERACTION WITH TLN1 AND APBB1IP.

Entry informationi

Entry nameiVINC_CHICK
AccessioniPrimary (citable) accession number: P12003
Secondary accession number(s): Q91024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 137 of the entry and version 4 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi