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Protein

Ephrin type-B receptor 3

Gene

EPHB3

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

Functioni

Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei665ATPPROSITE-ProRule annotation1
Active sitei758Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi639 – 647ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • axon guidance receptor activity Source: Ensembl
  • ephrin receptor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Angiogenesis, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS00011-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP54753.
SIGNORiP54753.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-B receptor 3 (EC:2.7.10.1)
Alternative name(s):
EPH-like tyrosine kinase 2
Short name:
EPH-like kinase 2
Embryonic kinase 2
Short name:
EK2
Short name:
hEK2
Tyrosine-protein kinase TYRO6
Gene namesi
Name:EPHB3
Synonyms:ETK2, HEK2, TYRO6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3394. EPHB3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini34 – 559ExtracellularSequence analysisAdd BLAST526
Transmembranei560 – 580HelicalSequence analysisAdd BLAST21
Topological domaini581 – 998CytoplasmicSequence analysisAdd BLAST418

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi614Y → F: Partial loss of phosphorylation and loss of interaction with SH2-containing proteins. 1 Publication1
Mutagenesisi665K → R: Kinase-dead. Loss of autophosphorylation. 1 Publication1

Organism-specific databases

DisGeNETi2049.
OpenTargetsiENSG00000182580.
PharmGKBiPA27826.

Chemistry databases

ChEMBLiCHEMBL4901.
GuidetoPHARMACOLOGYi1832.

Polymorphism and mutation databases

BioMutaiEPHB3.
DMDMi76803655.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000001683134 – 998Ephrin type-B receptor 3Add BLAST965

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi81 ↔ 1991 Publication
Glycosylationi351N-linked (GlcNAc...)Sequence analysis1
Glycosylationi445N-linked (GlcNAc...)Sequence analysis1
Modified residuei614Phosphotyrosine; by autocatalysis1 Publication1

Post-translational modificationi

Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-614 is required for interaction with SH2 domain-containing proteins.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP54753.
MaxQBiP54753.
PaxDbiP54753.
PeptideAtlasiP54753.
PRIDEiP54753.

PTM databases

iPTMnetiP54753.
PhosphoSitePlusiP54753.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000182580.
CleanExiHS_EPHB3.
GenevisibleiP54753. HS.

Organism-specific databases

HPAiHPA007698.
HPA008184.

Interactioni

Subunit structurei

Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity).By similarity

Protein-protein interaction databases

BioGridi108363. 12 interactors.
IntActiP54753. 5 interactors.
MINTiMINT-1538099.
STRINGi9606.ENSP00000332118.

Chemistry databases

BindingDBiP54753.

Structurei

Secondary structure

1998
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 44Combined sources6
Helixi45 – 47Combined sources3
Beta strandi55 – 58Combined sources4
Beta strandi63 – 68Combined sources6
Beta strandi74 – 80Combined sources7
Beta strandi85 – 87Combined sources3
Beta strandi90 – 93Combined sources4
Beta strandi103 – 114Combined sources12
Helixi116 – 118Combined sources3
Beta strandi130 – 139Combined sources10
Beta strandi155 – 160Combined sources6
Beta strandi175 – 181Combined sources7
Beta strandi186 – 198Combined sources13
Beta strandi200 – 210Combined sources11
Beta strandi633 – 640Combined sources8
Beta strandi646 – 652Combined sources7
Beta strandi655 – 657Combined sources3
Beta strandi660 – 666Combined sources7
Helixi673 – 687Combined sources15
Beta strandi697 – 701Combined sources5
Beta strandi703 – 706Combined sources4
Beta strandi708 – 712Combined sources5
Helixi719 – 725Combined sources7
Turni726 – 728Combined sources3
Helixi732 – 751Combined sources20
Helixi761 – 763Combined sources3
Beta strandi764 – 766Combined sources3
Beta strandi772 – 774Combined sources3
Beta strandi791 – 793Combined sources3
Beta strandi796 – 798Combined sources3
Helixi802 – 804Combined sources3
Helixi807 – 812Combined sources6
Helixi817 – 832Combined sources16
Turni838 – 841Combined sources4
Helixi844 – 852Combined sources9
Helixi865 – 874Combined sources10
Turni879 – 881Combined sources3
Helixi885 – 897Combined sources13
Helixi899 – 902Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P1IX-ray2.10A/B/C39-211[»]
3ZFYX-ray2.20A/B616-910[»]
5L6OX-ray1.88A616-910[»]
5L6PX-ray2.26A616-910[»]
ProteinModelPortaliP54753.
SMRiP54753.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54753.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 217Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini339 – 451Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST113
Domaini452 – 545Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST94
Domaini633 – 896Protein kinasePROSITE-ProRule annotationAdd BLAST264
Domaini925 – 989SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi996 – 998PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi199 – 336Cys-richAdd BLAST138

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54753.
KOiK05112.
OMAiELAWTAH.
OrthoDBiEOG091G00W0.
PhylomeDBiP54753.
TreeFamiTF315608.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P54753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARARPPPPP SPPPGLLPLL PPLLLLPLLL LPAGCRALEE TLMDTKWVTS
60 70 80 90 100
ELAWTSHPES GWEEVSGYDE AMNPIRTYQV CNVRESSQNN WLRTGFIWRR
110 120 130 140 150
DVQRVYVELK FTVRDCNSIP NIPGSCKETF NLFYYEADSD VASASSPFWM
160 170 180 190 200
ENPYVKVDTI APDESFSRLD AGRVNTKVRS FGPLSKAGFY LAFQDQGACM
210 220 230 240 250
SLISVRAFYK KCASTTAGFA LFPETLTGAE PTSLVIAPGT CIPNAVEVSV
260 270 280 290 300
PLKLYCNGDG EWMVPVGACT CATGHEPAAK ESQCRPCPPG SYKAKQGEGP
310 320 330 340 350
CLPCPPNSRT TSPAASICTC HNNFYRADSD SADSACTTVP SPPRGVISNV
360 370 380 390 400
NETSLILEWS EPRDLGGRDD LLYNVICKKC HGAGGASACS RCDDNVEFVP
410 420 430 440 450
RQLGLTERRV HISHLLAHTR YTFEVQAVNG VSGKSPLPPR YAAVNITTNQ
460 470 480 490 500
AAPSEVPTLR LHSSSGSSLT LSWAPPERPN GVILDYEMKY FEKSEGIAST
510 520 530 540 550
VTSQMNSVQL DGLRPDARYV VQVRARTVAG YGQYSRPAEF ETTSERGSGA
560 570 580 590 600
QQLQEQLPLI VGSATAGLVF VVAVVVIAIV CLRKQRHGSD SEYTEKLQQY
610 620 630 640 650
IAPGMKVYID PFTYEDPNEA VREFAKEIDV SCVKIEEVIG AGEFGEVCRG
660 670 680 690 700
RLKQPGRREV FVAIKTLKVG YTERQRRDFL SEASIMGQFD HPNIIRLEGV
710 720 730 740 750
VTKSRPVMIL TEFMENCALD SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS
760 770 780 790 800
EMNYVHRDLA ARNILVNSNL VCKVSDFGLS RFLEDDPSDP TYTSSLGGKI
810 820 830 840 850
PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW DMSNQDVINA
860 870 880 890 900
VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFSQIVN TLDKLIRNAA
910 920 930 940 950
SLKVIASAQS GMSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKESFVSAG
960 970 980 990
FASFDLVAQM TAEDLLRIGV TLAGHQKKIL SSIQDMRLQM NQTLPVQV
Length:998
Mass (Da):110,330
Last modified:September 27, 2005 - v2
Checksum:i9B65A4EF58B27407
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti367G → V in CAA53021 (PubMed:8397371).Curated1
Sequence conflicti406 – 408TER → SEP in CAA53021 (PubMed:8397371).Curated3
Sequence conflicti412I → T in CAA53021 (PubMed:8397371).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042176168R → L in a lung small cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042177440R → C.1 PublicationCorresponds to variant rs56029711dbSNPEnsembl.1
Natural variantiVAR_042178579I → V.1 PublicationCorresponds to variant rs56103851dbSNPEnsembl.1
Natural variantiVAR_042179601I → L.1 PublicationCorresponds to variant rs56129875dbSNPEnsembl.1
Natural variantiVAR_042180724R → W in a lung neuroendocrine carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs371378866dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75208 mRNA. Translation: CAA53021.1.
BC052968 mRNA. Translation: AAH52968.1.
CCDSiCCDS3268.1.
PIRiS37627.
RefSeqiNP_004434.2. NM_004443.3.
UniGeneiHs.2913.

Genome annotation databases

EnsembliENST00000330394; ENSP00000332118; ENSG00000182580.
GeneIDi2049.
KEGGihsa:2049.
UCSCiuc003foz.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75208 mRNA. Translation: CAA53021.1.
BC052968 mRNA. Translation: AAH52968.1.
CCDSiCCDS3268.1.
PIRiS37627.
RefSeqiNP_004434.2. NM_004443.3.
UniGeneiHs.2913.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P1IX-ray2.10A/B/C39-211[»]
3ZFYX-ray2.20A/B616-910[»]
5L6OX-ray1.88A616-910[»]
5L6PX-ray2.26A616-910[»]
ProteinModelPortaliP54753.
SMRiP54753.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108363. 12 interactors.
IntActiP54753. 5 interactors.
MINTiMINT-1538099.
STRINGi9606.ENSP00000332118.

Chemistry databases

BindingDBiP54753.
ChEMBLiCHEMBL4901.
GuidetoPHARMACOLOGYi1832.

PTM databases

iPTMnetiP54753.
PhosphoSitePlusiP54753.

Polymorphism and mutation databases

BioMutaiEPHB3.
DMDMi76803655.

Proteomic databases

EPDiP54753.
MaxQBiP54753.
PaxDbiP54753.
PeptideAtlasiP54753.
PRIDEiP54753.

Protocols and materials databases

DNASUi2049.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330394; ENSP00000332118; ENSG00000182580.
GeneIDi2049.
KEGGihsa:2049.
UCSCiuc003foz.4. human.

Organism-specific databases

CTDi2049.
DisGeNETi2049.
GeneCardsiEPHB3.
HGNCiHGNC:3394. EPHB3.
HPAiHPA007698.
HPA008184.
MIMi601839. gene.
neXtProtiNX_P54753.
OpenTargetsiENSG00000182580.
PharmGKBiPA27826.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54753.
KOiK05112.
OMAiELAWTAH.
OrthoDBiEOG091G00W0.
PhylomeDBiP54753.
TreeFamiTF315608.

Enzyme and pathway databases

BioCyciZFISH:HS00011-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-2682334. EPH-Ephrin signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP54753.
SIGNORiP54753.

Miscellaneous databases

EvolutionaryTraceiP54753.
GeneWikiiEPHB3.
GenomeRNAii2049.
PROiP54753.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000182580.
CleanExiHS_EPHB3.
GenevisibleiP54753. HS.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. FN3_dom.
IPR008979. Galactose-bd-like.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF07699. Ephrin_rec_like. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEPHB3_HUMAN
AccessioniPrimary (citable) accession number: P54753
Secondary accession number(s): Q7Z740
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 27, 2005
Last modified: November 30, 2016
This is version 171 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 3
    Human chromosome 3: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.