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Protein

Vascular endothelial growth factor receptor 2

Gene

Kdr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol-1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC (By similarity).By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFC or VEGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. May be regulated by hydrogen sulfide (H2S) levels via a sensitive intracellular disulfide bond (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei864ATPPROSITE-ProRule annotation1
Active sitei1024Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi836 – 844ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • growth factor binding Source: RGD
  • vascular endothelial growth factor-activated receptor activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • angiogenesis Source: UniProtKB-KW
  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  • embryonic hemopoiesis Source: UniProtKB
  • endochondral bone growth Source: RGD
  • endothelium development Source: UniProtKB
  • hyaluronan metabolic process Source: RGD
  • male gonad development Source: RGD
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of endothelial cell apoptotic process Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: RGD
  • neuron projection morphogenesis Source: RGD
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of angiogenesis Source: RGD
  • positive regulation of calcium-mediated signaling Source: RGD
  • positive regulation of cell migration Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of cytosolic calcium ion concentration Source: RGD
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of long-term neuronal synaptic plasticity Source: RGD
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of neurogenesis Source: RGD
  • positive regulation of nitric-oxide synthase biosynthetic process Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: RGD
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of TOR signaling Source: RGD
  • positive regulation of vasculogenesis Source: UniProtKB
  • positive regulation of vasodilation Source: RGD
  • protein autophosphorylation Source: RGD
  • response to drug Source: RGD
  • response to hypoxia Source: RGD
  • response to oxygen levels Source: RGD
  • vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  • vasculogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor receptor 2 (EC:2.7.10.1)
Short name:
VEGFR-2
Alternative name(s):
Fetal liver kinase 1
Short name:
FLK-1
Protein-tyrosine kinase receptor flk-1
CD_antigen: CD309
Gene namesi
Name:Kdr
Synonyms:Flk1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2965. Kdr.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cytoplasmic vesicle By similarity
  • Early endosome By similarity
  • Cell junction By similarity
  • Endoplasmic reticulum By similarity

  • Note: Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus. Localized with RAP1A at cell-cell junctions. Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (By similarity).By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 760ExtracellularSequence analysisAdd BLAST741
Transmembranei761 – 781HelicalSequence analysisAdd BLAST21
Topological domaini782 – 1343CytoplasmicSequence analysisAdd BLAST562

GO - Cellular componenti

  • cell junction Source: UniProtKB
  • cytoplasm Source: RGD
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • early endosome Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001677320 – 1343Vascular endothelial growth factor receptor 2Add BLAST1324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi46N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi53 ↔ 103PROSITE-ProRule annotation
Glycosylationi96N-linked (GlcNAc...)Sequence analysis1
Glycosylationi143N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi150 ↔ 200PROSITE-ProRule annotation
Glycosylationi158N-linked (GlcNAc...)Sequence analysis1
Glycosylationi245N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi246 ↔ 307PROSITE-ProRule annotation
Glycosylationi318N-linked (GlcNAc...)Sequence analysis1
Glycosylationi374N-linked (GlcNAc...)Sequence analysis1
Glycosylationi395N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi445 ↔ 526PROSITE-ProRule annotation
Glycosylationi507N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi567 ↔ 638PROSITE-ProRule annotation
Glycosylationi576N-linked (GlcNAc...)Sequence analysis1
Glycosylationi609N-linked (GlcNAc...)Sequence analysis1
Glycosylationi615N-linked (GlcNAc...)Sequence analysis1
Glycosylationi627N-linked (GlcNAc...)Sequence analysis1
Glycosylationi671N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi684 ↔ 733PROSITE-ProRule annotation
Glycosylationi700N-linked (GlcNAc...)Sequence analysis1
Glycosylationi717N-linked (GlcNAc...)Sequence analysis1
Modified residuei797PhosphotyrosineBy similarity1
Modified residuei947Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei978PhosphoserineCombined sources1
Modified residuei980PhosphoserineCombined sources1
Modified residuei992Phosphotyrosine; by autocatalysisBy similarity1
Disulfide bondi1020 ↔ 1041Redox-activePROSITE-ProRule annotation
Modified residuei1050Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1055Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1171Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1210Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1227PhosphoserineBy similarity1
Modified residuei1231PhosphoserineBy similarity1
Modified residuei1234PhosphothreonineBy similarity1
Modified residuei1301Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1305Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1315Phosphotyrosine; by autocatalysisBy similarity1

Post-translational modificationi

N-glycosylated.By similarity
Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases (By similarity).By similarity
Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-947 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1171 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1210 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRB. Dephosphorylated by PTPRJ at Tyr-797, Tyr-947, Tyr-992, Tyr-1050, Tyr-1055, Tyr-1171 and Tyr-1210 (By similarity).By similarity
The inhibitory disulfide bond between Cys-1020 and Cys-1041 may serve as a specific molecular switch for H2S-induced modification that regulates VEGFR2 function.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO08775.
PRIDEiO08775.

PTM databases

iPTMnetiO08775.
PhosphoSitePlusiO08775.

Expressioni

Tissue specificityi

Expressed in the post-pubertal mammary glands.1 Publication

Developmental stagei

Increases during pregnancy (1.6-fold at 4 days) and lactation (3.8-fold at 7 days). Decreases in the early phases of involution (45%, 50% and 34% on days 1, 2, and 3 respectively).1 Publication

Interactioni

Subunit structurei

Homodimer in the presence of bound dimeric VEGFA, VEGFC or VEGFD ligands; monomeric in the absence of bound ligands. Can also form heterodimers with FLT1/VEGFR1 and FLT4/VEGFR2. Interacts (tyrosine phosphorylated) with LFYN, NCK1, PLCG1. Interacts (tyrosine-phosphorylated active form preferentially) with DAB2IP (via C2 domain and active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts with SHBSH2D2A/TSAD, GRB2, MYOF, CBL and PDCD6. Interacts (via C-terminus domain) with ERN1 (via kinase domain); the interaction is facilitated in a XBP1- and vascular endothelial growth factor (VEGF)-dependent manner in endothelial cells (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1171Interaction with SHBBy similarity1

GO - Molecular functioni

  • growth factor binding Source: RGD

Protein-protein interaction databases

IntActiO08775. 1 interactor.
MINTiMINT-7138598.
STRINGi10116.ENSRNOP00000066886.

Chemistry databases

BindingDBiO08775.

Structurei

3D structure databases

ProteinModelPortaliO08775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 109Ig-like C2-type 1Add BLAST64
Domaini141 – 207Ig-like C2-type 2Add BLAST67
Domaini224 – 320Ig-like C2-type 3Add BLAST97
Domaini328 – 414Ig-like C2-type 4Add BLAST87
Domaini421 – 540Ig-like C2-type 5Add BLAST120
Domaini547 – 654Ig-like C2-type 6Add BLAST108
Domaini663 – 749Ig-like C2-type 7Add BLAST87
Domaini830 – 1158Protein kinasePROSITE-ProRule annotationAdd BLAST329

Domaini

The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOVERGENiHBG053432.
InParanoidiO08775.
KOiK05098.
PhylomeDBiO08775.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009136. VEGFR2_rcpt.
[Graphical view]
PANTHERiPTHR24416:SF45. PTHR24416:SF45. 3 hits.
PfamiPF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01834. VEGFRECEPTR2.
SMARTiSM00409. IG. 7 hits.
SM00408. IGc2. 5 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O08775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESRALLAVA LWFCVETRAA SVGLPGDSLH PPKLSTQKDI LTILANTTLQ
60 70 80 90 100
ITCRGQRDLD WLWPNTPRDS EERVLVTECG DSIFCKTLTV PRVVGNDTGA
110 120 130 140 150
YKCFYRDTDV SSIVYVYVQD HRSPFIASVS DEHGIVYITE NKNKTVVIPC
160 170 180 190 200
RGSISNLNVS LCARYPEKRF VPDGNRISWD SEKGFTIPSY MISYAGMVFC
210 220 230 240 250
EAKINDETYQ SIMYIVLVVG YRIYDVVLSP PHEIELSAGE KLVLNCTART
260 270 280 290 300
ELNVGLDFSW QFPSSKHQHK KIVNRDVKSL PGTVAKMFLS TLTIDSVTKS
310 320 330 340 350
DQGEYTCTAY SGLMTKKNKT FVRVHTKPFI AFGSGMKSLV EATVGSQVRI
360 370 380 390 400
PVKYLSYPAP DIKWYRNGRP IESNYTMIVG DELTIMEVSE RDAGNYTVIL
410 420 430 440 450
TNPISMEKQS HMVSLVVNVP PQIGEKALIS PMDSYQYGTM QTLTCTVYAN
460 470 480 490 500
PPLHHIQWYW QLEEACSYRP SQTNPYTCKE WRHVKDFQGG NKIEVTKNQY
510 520 530 540 550
ALIEGKNKTV STLVIQAAYV SALYKCEAIN KAGRGERVIS FHVIRGPEIT
560 570 580 590 600
VQPATQPTER ESMSLLCTAD RNTFENLTWY KLGSQATSVH MGESLTPVCK
610 620 630 640 650
NLDALWKLNG TVFSNSTNDI LIVAFQNASL QDQGNYVCSA QDKKTKKRHC
660 670 680 690 700
LVKQLVILER MAPMITGNLE NQTTTIGETI EVVCPTSGNP TPLITWFKDN
710 720 730 740 750
ETLVEDSGIV LKDGNRNLTI RRVRKEDGGL YTCQACNVLG CARAETLFII
760 770 780 790 800
EGVQEKTNLE VIILVGTAVI AMFFWLLLVI LVRTVKRANE GELKTGYLSI
810 820 830 840 850
VMDPDELPLD ERCERLPYDA SKWEFPRDRL KLGKPLGRGA FGQVIEADAF
860 870 880 890 900
GIDKTATCKT VAVKMLKEGA THSEHRALMS ELKILIHIGH HLNVVNLLGA
910 920 930 940 950
CTKPGGPLMV IVEFCKFGNL STYLRGKRNE FVPYKSKGAR FRSGKDYVGE
960 970 980 990 1000
LSVDLKRRLD SITSSQSSAS SGFVEEKSLS DVEEEEASEE LYKDFLTLEH
1010 1020 1030 1040 1050
LICYSFQVAK GMEFLASRKC IHRDLAARNI LLSEKNVVKI CDFGLARDIY
1060 1070 1080 1090 1100
KDPDYVRKGD PRLPLKWMAP ETIFDRIYTI QSGVWSFGVL LWEIFSLGAS
1110 1120 1130 1140 1150
PYPGVKIDEK FCRRLKEGTR MRAPDYTTPE MYQTMLDCWH EDPNQRPAFS
1160 1170 1180 1190 1200
ELVEHLGNLL QANAQQDGKD YIVLPMSETL SMEEDSGLSL PTSPVSCMEE
1210 1220 1230 1240 1250
EEVCDPKFHY DNTAGISHYL QNSKRKSRPV SVKTFEDIPL EEPEVKVIPD
1260 1270 1280 1290 1300
DSQTDSGMVL ASEELKTLED RNKLSPSFGG MMPSKSRESV ASEGSNQTSG
1310 1320 1330 1340
YQSGYHSDDT DTTVYSSDEA GLLKLVDVAG HVDSGTTLRS SPV
Length:1,343
Mass (Da):150,394
Last modified:July 1, 1997 - v1
Checksum:iAD7E509EB62D3FF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93306 mRNA. Translation: AAB97508.1.
U93307 mRNA. Translation: AAB97509.1.
RefSeqiNP_037194.1. NM_013062.1.
UniGeneiRn.88869.

Genome annotation databases

GeneIDi25589.
KEGGirno:25589.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93306 mRNA. Translation: AAB97508.1.
U93307 mRNA. Translation: AAB97509.1.
RefSeqiNP_037194.1. NM_013062.1.
UniGeneiRn.88869.

3D structure databases

ProteinModelPortaliO08775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08775. 1 interactor.
MINTiMINT-7138598.
STRINGi10116.ENSRNOP00000066886.

Chemistry databases

BindingDBiO08775.

PTM databases

iPTMnetiO08775.
PhosphoSitePlusiO08775.

Proteomic databases

PaxDbiO08775.
PRIDEiO08775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25589.
KEGGirno:25589.

Organism-specific databases

CTDi3791.
RGDi2965. Kdr.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
HOVERGENiHBG053432.
InParanoidiO08775.
KOiK05098.
PhylomeDBiO08775.

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Miscellaneous databases

PROiO08775.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009136. VEGFR2_rcpt.
[Graphical view]
PANTHERiPTHR24416:SF45. PTHR24416:SF45. 3 hits.
PfamiPF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01834. VEGFRECEPTR2.
SMARTiSM00409. IG. 7 hits.
SM00408. IGc2. 5 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVGFR2_RAT
AccessioniPrimary (citable) accession number: O08775
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.