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Protein

Vinculin

Gene

VCL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.1 Publication

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • alpha-catenin binding Source: UniProtKB
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • dystroglycan binding Source: UniProtKB
  • structural molecule activity Source: InterPro
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • adherens junction assembly Source: BHF-UCL
  • apical junction assembly Source: UniProtKB
  • axon extension Source: Ensembl
  • cell adhesion Source: UniProtKB
  • cell-matrix adhesion Source: BHF-UCL
  • epithelial cell-cell adhesion Source: BHF-UCL
  • lamellipodium assembly Source: UniProtKB
  • morphogenesis of an epithelium Source: BHF-UCL
  • muscle contraction Source: Reactome
  • negative regulation of cell migration Source: UniProtKB
  • neutrophil degranulation Source: Reactome
  • platelet aggregation Source: UniProtKB
  • platelet degranulation Source: Reactome
  • protein localization to cell surface Source: BHF-UCL

Keywordsi

Molecular functionActin-binding
Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-445355 Smooth Muscle Contraction
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-6798695 Neutrophil degranulation
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
SIGNORiP18206

Names & Taxonomyi

Protein namesi
Recommended name:
Vinculin
Alternative name(s):
Metavinculin
Short name:
MV
Gene namesi
Name:VCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000035403.16
HGNCiHGNC:12665 VCL
MIMi193065 gene
neXtProtiNX_P18206

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Cardiomyopathy, dilated 1W (CMD1W)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:611407
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035104954Missing in CMD1W. 1 Publication1
Natural variantiVAR_035105975R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. 2 PublicationsCorresponds to variant dbSNP:rs121917776Ensembl.1
Cardiomyopathy, familial hypertrophic 15 (CMH15)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
See also OMIM:613255
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035101277L → M in CMH15. 1 PublicationCorresponds to variant dbSNP:rs71579353Ensembl.1

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

DisGeNETi7414
GeneReviewsiVCL
MalaCardsiVCL
MIMi611407 phenotype
613255 phenotype
OpenTargetsiENSG00000035403
Orphaneti154 Familial isolated dilated cardiomyopathy
155 Familial isolated hypertrophic cardiomyopathy
PharmGKBiPA37288

Polymorphism and mutation databases

BioMutaiVCL
DMDMi21903479

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000642521 – 1134VinculinAdd BLAST1134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei97PhosphoserineBy similarity1
Modified residuei173N6-acetyllysineCombined sources1
Modified residuei260PhosphoserineCombined sources1
Modified residuei272PhosphoserineBy similarity1
Modified residuei275PhosphoserineCombined sources1
Modified residuei288PhosphoserineCombined sources1
Modified residuei290PhosphoserineCombined sources1
Modified residuei346PhosphoserineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei496N6-acetyllysineCombined sources1
Modified residuei537PhosphotyrosineCurated1
Modified residuei574PhosphoserineBy similarity1
Modified residuei579PhosphoserineCombined sources1
Modified residuei600PhosphoserineCombined sources1
Modified residuei604PhosphothreonineCombined sources1
Modified residuei672PhosphothreonineCombined sources1
Modified residuei721PhosphoserineCombined sources1
Modified residuei795PhosphoserineCombined sources1
Modified residuei809PhosphoserineCombined sources1
Modified residuei822PhosphotyrosineCombined sources1
Modified residuei1133Phosphotyrosine; by SRC-type Tyr-kinases1 Publication1

Post-translational modificationi

Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1133 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques (By similarity).By similarity
Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP18206
PaxDbiP18206
PeptideAtlasiP18206
PRIDEiP18206

2D gel databases

DOSAC-COBS-2DPAGEiP18206
OGPiP18206
REPRODUCTION-2DPAGEiIPI00291175
SWISS-2DPAGEiP18206
UCD-2DPAGEiP18206

PTM databases

iPTMnetiP18206
PhosphoSitePlusiP18206
SwissPalmiP18206

Expressioni

Tissue specificityi

Metavinculin is muscle-specific.

Gene expression databases

BgeeiENSG00000035403
CleanExiHS_VCL
ExpressionAtlasiP18206 baseline and differential
GenevisibleiP18206 HS

Organism-specific databases

HPAiCAB002453
HPA002131
HPA063777

Interactioni

Subunit structurei

Exhibits self-association properties. Interacts with APBB1IP and NRAP (By similarity). Interacts with 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 (By similarity). Interacts with SYNM. Interacts with SORBS1 (By similarity). Interacts with CTNNA1 (PubMed:26691986). Binds to ACTN4; this interaction triggers conformational changes (PubMed:15988023).By similarity5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • alpha-catenin binding Source: UniProtKB
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • dystroglycan binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi113257, 114 interactors
CORUMiP18206
DIPiDIP-35570N
ELMiP18206
IntActiP18206, 50 interactors
MINTiP18206
STRINGi9606.ENSP00000211998

Structurei

Secondary structure

11134
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi7 – 13Combined sources7
Helixi16 – 26Combined sources11
Beta strandi28 – 30Combined sources3
Beta strandi33 – 35Combined sources3
Helixi38 – 40Combined sources3
Helixi41 – 64Combined sources24
Helixi68 – 97Combined sources30
Helixi102 – 145Combined sources44
Helixi146 – 150Combined sources5
Helixi154 – 179Combined sources26
Helixi185 – 218Combined sources34
Beta strandi220 – 222Combined sources3
Helixi223 – 248Combined sources26
Helixi253 – 255Combined sources3
Helixi258 – 274Combined sources17
Helixi277 – 284Combined sources8
Helixi294 – 310Combined sources17
Helixi315 – 338Combined sources24
Turni339 – 342Combined sources4
Helixi343 – 345Combined sources3
Helixi347 – 351Combined sources5
Helixi353 – 393Combined sources41
Turni394 – 396Combined sources3
Helixi402 – 420Combined sources19
Helixi425 – 447Combined sources23
Turni448 – 450Combined sources3
Turni455 – 458Combined sources4
Helixi460 – 482Combined sources23
Helixi493 – 505Combined sources13
Helixi514 – 530Combined sources17
Helixi535 – 561Combined sources27
Helixi568 – 577Combined sources10
Helixi579 – 598Combined sources20
Helixi604 – 614Combined sources11
Turni620 – 624Combined sources5
Helixi625 – 650Combined sources26
Helixi655 – 681Combined sources27
Helixi690 – 714Combined sources25
Helixi719 – 743Combined sources25
Helixi746 – 772Combined sources27
Helixi777 – 792Combined sources16
Helixi794 – 806Combined sources13
Turni811 – 813Combined sources3
Helixi814 – 833Combined sources20
Helixi896 – 909Combined sources14
Helixi964 – 977Combined sources14
Helixi986 – 1005Combined sources20
Helixi1009 – 1011Combined sources3
Helixi1012 – 1037Combined sources26
Helixi1043 – 1053Combined sources11
Helixi1056 – 1072Combined sources17
Turni1073 – 1076Combined sources4
Beta strandi1077 – 1079Combined sources3
Helixi1081 – 1113Combined sources33
Beta strandi1114 – 1117Combined sources4
Turni1120 – 1122Combined sources3
Beta strandi1128 – 1130Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RKCX-ray2.70A1-258[»]
1RKEX-ray2.35A1-258[»]
B882-1134[»]
1SYQX-ray2.42A1-258[»]
1TR2X-ray2.90A/B1-1134[»]
1YDIX-ray1.80A1-258[»]
2GWWX-ray2.72A1-258[»]
2HSQX-ray3.97A1-258[»]
2IBFX-ray3.20A1-258[»]
3H2UX-ray2.75A/C879-1134[»]
3H2VX-ray2.90A/B/C/D879-1134[»]
3JBKelectron microscopy8.20M858-1129[»]
3MYIX-ray2.20A959-1130[»]
3RF3X-ray1.61A/B1-258[»]
3S90X-ray1.97A/B1-252[»]
3TJ5X-ray1.99A1-255[»]
3TJ6X-ray2.76A1-257[»]
3VF0X-ray2.54A856-1134[»]
4DJ9X-ray2.25A1-258[»]
4EHPX-ray2.66A1-252[»]
4LN2X-ray1.00B857-867[»]
4LNPX-ray1.41B870-879[»]
4PR9X-ray3.20A/B/C/D/E/F891-1134[»]
5L0CX-ray3.10A/B/C/D959-1134[»]
5L0DX-ray2.75A/B/C/D959-1130[»]
5L0FX-ray2.76A/B959-1134[»]
5L0GX-ray3.40A/B/C/D959-1134[»]
5L0HX-ray2.90A959-1134[»]
5L0IX-ray2.45A959-1134[»]
5L0JX-ray4.00A/B969-1134[»]
5O2QNMR-A854-870[»]
6FUYX-ray3.00A1-1134[»]
ProteinModelPortaliP18206
SMRiP18206
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18206

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati259 – 3691Sequence analysisAdd BLAST111
Repeati370 – 4792Sequence analysisAdd BLAST110
Repeati480 – 5893Sequence analysisAdd BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 835N-terminal globular head1 PublicationAdd BLAST835
Regioni168 – 208Talin-interactionBy similarityAdd BLAST41
Regioni259 – 5893 X 112 AA tandem repeatsSequence analysisAdd BLAST331
Regioni741 – 764Interaction with ACTN4Combined sources1 PublicationAdd BLAST24
Regioni836 – 878Linker (Pro-rich)1 PublicationAdd BLAST43
Regioni879 – 1134C-terminal tail1 PublicationAdd BLAST256
Regioni1003 – 1046Facilitates phospholipid membrane insertionBy similarityAdd BLAST44
Regioni1120 – 1134Facilitates phospholipid membrane insertionBy similarityAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi837 – 878Pro-richPROSITE-ProRule annotationAdd BLAST42

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.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. In isoform 2 (metavinculin) a 68 residue insertion in the tail domain promotes actin severing instead of bundling. 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.1 Publication

Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3681 Eukaryota
ENOG410XSRU LUCA
GeneTreeiENSGT00550000074411
HOGENOMiHOG000007828
HOVERGENiHBG079758
InParanoidiP18206
KOiK05700
OMAiTPGREQN
OrthoDBiEOG091G038S
PhylomeDBiP18206
TreeFamiTF313686

Family and domain databases

InterProiView protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR017997 Vinculin
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS
PANTHERiPTHR18914 PTHR18914, 3 hits
PTHR18914:SF1 PTHR18914:SF1, 3 hits
PfamiView protein in Pfam
PF01044 Vinculin, 3 hits
SUPFAMiSSF47220 SSF47220, 6 hits
PROSITEiView protein in PROSITE
PS00663 VINCULIN_1, 1 hit
PS00664 VINCULIN_2, 3 hits

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P18206-1) [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

        10         20         30         40         50
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA
60 70 80 90 100
VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY
110 120 130 140 150
SVPARDYLID GSRGILSGTS DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV
160 170 180 190 200
VETMEDLVTY TKNLGPGMTK MAKMIDERQQ ELTHQEHRVM LVNSMNTVKE
210 220 230 240 250
LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE INEIIRVLQL
260 270 280 290 300
TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPSAS PGDAGEQAIR
310 320 330 340 350
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGSSPVAM
360 370 380 390 400
QKAQQVSQGL DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG
410 420 430 440 450
GPEGEEQIRG ALAEARKIAE LCDDPKERDD ILRSLGEISA LTSKLADLRR
460 470 480 490 500
QGKGDSPEAR ALAKQVATAL QNLQTKTNRA VANSRPAKAA VHLEGKIEQA
510 520 530 540 550
QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD LLAKCDRVDQ
560 570 580 590 600
LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKARMQEA MTQEVSDVFS
610 620 630 640 650
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGKL GATAEKAAAV
660 670 680 690 700
GTANKSTVEG IQASVKTARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN
710 720 730 740 750
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANIQPQMLV
760 770 780 790 800
AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD
810 820 830 840 850
AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE
860 870 880 890 900
QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM
910 920 930 940 950
AARQLHDEAR KWSSKPGIPA AEVGIGVVAE ADAADAAGFP VPPDMEDDYE
960 970 980 990 1000
PELLLMPSNQ PVNQPILAAA QSLHREATKW SSKGNDIIAA AKRMALLMAE
1010 1020 1030 1040 1050
MSRLVRGGSG TKRALIQCAK DIAKASDEVT RLAKEVAKQC TDKRIRTNLL
1060 1070 1080 1090 1100
QVCERIPTIS TQLKILSTVK ATMLGRTNIS DEESEQATEM LVHNAQNLMQ
1110 1120 1130
SVKETVREAE AASIKIRTDA GFTLRWVRKT PWYQ
Length:1,134
Mass (Da):123,799
Last modified:January 23, 2007 - v4
Checksum:iBFBD687DA836B0FA
GO
Isoform 1 (identifier: P18206-2) [UniParc]FASTAAdd to basket
Also known as: Vinculin

The sequence of this isoform differs from the canonical sequence as follows:
     916-983: Missing.

Show »
Length:1,066
Mass (Da):116,722
Checksum:iC9B67AA072009EBD
GO
Isoform 3 (identifier: P18206-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
     262-295: DTEAMKRALASIDSKLNQAKGWLRDPSASPGDAG → VRVLSGEISKIPNSPWLGVLIGTCLILYLVIFVA
     296-1134: Missing.

Note: No experimental confirmation available.
Show »
Length:222
Mass (Da):24,904
Checksum:iCBC9C4E86C7B5002
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037667234V → L1 PublicationCorresponds to variant dbSNP:rs17853882Ensembl.1
Natural variantiVAR_035101277L → M in CMH15. 1 PublicationCorresponds to variant dbSNP:rs71579353Ensembl.1
Natural variantiVAR_035102934A → V1 PublicationCorresponds to variant dbSNP:rs16931179Ensembl.1
Natural variantiVAR_035103943P → A1 PublicationCorresponds to variant dbSNP:rs71579375Ensembl.1
Natural variantiVAR_035104954Missing in CMD1W. 1 Publication1
Natural variantiVAR_035105975R → W in CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments. 2 PublicationsCorresponds to variant dbSNP:rs121917776Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0118571 – 73Missing in isoform 3. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_011858262 – 295DTEAM…PGDAG → VRVLSGEISKIPNSPWLGVL IGTCLILYLVIFVA in isoform 3. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_011859296 – 1134Missing in isoform 3. 1 PublicationAdd BLAST839
Alternative sequenceiVSP_006731916 – 983Missing in isoform 1. 2 PublicationsAdd BLAST68

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33308 mRNA Translation: AAA61283.1
BX537994 mRNA Translation: CAD97952.1
AL596247, AL731576 Genomic DNA Translation: CAI13972.1
AL731576, AL596247 Genomic DNA Translation: CAI39673.1
BC039174 mRNA Translation: AAH39174.1
L04933 Genomic DNA Translation: AAA61271.1
S87180, S87175, S87178 Genomic DNA Translation: AAB21656.1
S87223, S87218 Genomic DNA Translation: AAB21657.1
CCDSiCCDS7340.1 [P18206-2]
CCDS7341.1 [P18206-1]
PIRiA35955
RefSeqiNP_003364.1, NM_003373.3 [P18206-2]
NP_054706.1, NM_014000.2 [P18206-1]
UniGeneiHs.643896

Genome annotation databases

EnsembliENST00000211998; ENSP00000211998; ENSG00000035403 [P18206-1]
ENST00000372755; ENSP00000361841; ENSG00000035403 [P18206-2]
GeneIDi7414
KEGGihsa:7414
UCSCiuc001jwe.4 human [P18206-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiVINC_HUMAN
AccessioniPrimary (citable) accession number: P18206
Secondary accession number(s): Q16450
, Q5SWX2, Q7Z3B8, Q8IXU7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 204 of the entry and version 4 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health