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P54764 (EPHA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-A receptor 4

EC=2.7.10.1
Alternative name(s):
EPH-like kinase 8
Short name=EK8
Short name=hEK8
Tyrosine-protein kinase TYRO1
Tyrosine-protein kinase receptor SEK
Gene names
Name:EPHA4
Synonyms:HEK8, SEK, TYRO1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length986 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor tyrosine kinase which binds membrane-bound ephrin 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. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. Beside its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, plays also a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. Ref.5

Catalytic activity

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

Subunit structure

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. Interacts (phosphorylated at position Tyr-602) with FYN. Interacts with CDK5, CDK5R1 and NGEF; upon activation by EFNA1 induces NGEF phosphorylation by the kinase CDK5. Interacts with CHN1; effector of EPHA4 in axon guidance linking EPHA4 activation to RAC1 regulation By similarity. Interacts (via PDZ motif) with SIPA1L1 (via PDZ domain); controls neuronal morphology through regulation of the RAP1 (RAP1A or RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases. Ref.4

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Cell projectionaxon By similarity. Cell projectiondendrite By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Early endosome By similarity. Note: Clustered upon activation and targeted to early endosome By similarity.

Tissue specificity

Ubiquitous.

Domain

The protein kinase domain mediates interaction with NGEF By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 1 Eph LBD (Eph ligand-binding) domain.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processCell adhesion
Neurogenesis
   Cellular componentCell junction
Cell membrane
Cell projection
Endosome
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

corticospinal tract morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

fasciculation of motor neuron axon

Inferred from sequence or structural similarity. Source: UniProtKB

fasciculation of sensory neuron axon

Inferred from sequence or structural similarity. Source: UniProtKB

glial cell migration

Inferred from electronic annotation. Source: Ensembl

motor neuron axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of axon regeneration

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 12775584. Source: UniProtKB

positive regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rho guanyl-nucleotide exchange factor activity

Inferred from direct assay PubMed 12775584. Source: UniProtKB

positive regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from direct assay PubMed 12775584. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rap GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of astrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

axon

Inferred from sequence or structural similarity. Source: UniProtKB

axon terminus

Inferred from electronic annotation. Source: Ensembl

axonal growth cone

Inferred from electronic annotation. Source: Ensembl

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

early endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

filopodium

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

perikaryon

Inferred from electronic annotation. Source: Ensembl

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DH domain binding

Inferred from direct assay PubMed 12775584. Source: UniProtKB

GPI-linked ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

PH domain binding

Inferred from physical interaction PubMed 12775584. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 12775584. Source: UniProtKB

transmembrane-ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 986967Ephrin type-A receptor 4
PRO_0000016807

Regions

Topological domain20 – 547528Extracellular Potential
Transmembrane548 – 56922Helical; Potential
Topological domain570 – 986417Cytoplasmic Potential
Domain30 – 209180Eph LBD
Domain328 – 439112Fibronectin type-III 1
Domain440 – 53798Fibronectin type-III 2
Domain621 – 882262Protein kinase
Domain911 – 97565SAM
Nucleotide binding627 – 6359ATP By similarity
Motif984 – 9863PDZ-binding Potential
Compositional bias191 – 325135Cys-rich

Sites

Active site7461Proton acceptor By similarity
Binding site6531ATP By similarity

Amino acid modifications

Modified residue5961Phosphotyrosine; by autocatalysis By similarity
Modified residue6021Phosphotyrosine; by autocatalysis By similarity
Modified residue7791Phosphotyrosine; by autocatalysis Potential
Modified residue9281Phosphotyrosine; by autocatalysis Potential
Glycosylation2351N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation4081N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential

Natural variations

Natural variant2691R → Q. Ref.10
Corresponds to variant rs35084379 [ dbSNP | Ensembl ].
VAR_042135
Natural variant3701G → E in a bladder carcinoma NOS sample; somatic mutation. Ref.10
VAR_042136
Natural variant3991S → F in a metastatic melanoma sample; somatic mutation. Ref.10
VAR_042137
Natural variant9531R → K.
Corresponds to variant rs35341687 [ dbSNP | Ensembl ].
VAR_049721

Experimental info

Mutagenesis401Q → A: 10-fold reduced affinity for EFNB2; when associated with A-42. Ref.9
Mutagenesis421E → A: 10-fold reduced affinity for EFNB2; when associated with A-40. Ref.9

Secondary structure

......................................................................................... 986
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54764 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0C39C1152EDDD46F

FASTA986109,860
        10         20         30         40         50         60 
MAGIFYFALF SCLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL EGGWEEVSIM 

        70         80         90        100        110        120 
DEKNTPIRTY QVCNVMEPSQ NNWLRTDWIT REGAQRVYIE IKFTLRDCNS LPGVMGTCKE 

       130        140        150        160        170        180 
TFNLYYYESD NDKERFIREN QFVKIDTIAA DESFTQVDIG DRIMKLNTEI RDVGPLSKKG 

       190        200        210        220        230        240 
FYLAFQDVGA CIALVSVRVF YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK 

       250        260        270        280        290        300 
DVPKMYCGAD GEWLVPIGNC LCNAGHEERS GECQACKIGY YKALSTDATC AKCPPHSYSV 

       310        320        330        340        350        360 
WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS PQNTGGRQDI 

       370        380        390        400        410        420 
SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTKVSI TDLLAHTNYT FEIWAVNGVS 

       430        440        450        460        470        480 
KYNPNPDQSV SVTVTTNQAA PSSIALVQAK EVTRYSVALA WLEPDRPNGV ILEYEVKYYE 

       490        500        510        520        530        540 
KDQNERSYRI VRTAARNTDI KGLNPLTSYV FHVRARTAAG YGDFSEPLEV TTNTVPSRII 

       550        560        570        580        590        600 
GDGANSTVLL VSVSGSVVLV VILIAAFVIS RRRSKYSKAK QEADEEKHLN QGVRTYVDPF 

       610        620        630        640        650        660 
TYEDPNQAVR EFAKEIDASC IKIEKVIGVG EFGEVCSGRL KVPGKREICV AIKTLKAGYT 

       670        680        690        700        710        720 
DKQRRDFLSE ASIMGQFDHP NIIHLEGVVT KCKPVMIITE YMENGSLDAF LRKNDGRFTV 

       730        740        750        760        770        780 
IQLVGMLRGI GSGMKYLSDM SYVHRDLAAR NILVNSNLVC KVSDFGMSRV LEDDPEAAYT 

       790        800        810        820        830        840 
TRGGKIPIRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVIKAIEEG 

       850        860        870        880        890        900 
YRLPPPMDCP IALHQLMLDC WQKERSDRPK FGQIVNMLDK LIRNPNSLKR TGTESSRPNT 

       910        920        930        940        950        960 
ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHVNQED LARIGITAIT 

       970        980 
HQNKILSSVQ AMRTQMQQMH GRMVPV 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases."
Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R., Welcher A.A.
Oncogene 10:897-905(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Unified nomenclature for Eph family receptors and their ligands, the ephrins."
Eph nomenclature committee
Cell 90:403-404(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[4]"The EphA4 receptor regulates neuronal morphology through SPAR-mediated inactivation of Rap GTPases."
Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.
J. Neurosci. 27:14205-14215(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIPA1L1.
[5]"Cdk5 regulates EphA4-mediated dendritic spine retraction through an ephexin1-dependent mechanism."
Fu W.Y., Chen Y., Sahin M., Zhao X.S., Shi L., Bikoff J.B., Lai K.O., Yung W.H., Fu A.K., Greenberg M.E., Ip N.Y.
Nat. Neurosci. 10:67-76(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CDK5, AUTOPHOSPHORYLATION.
[6]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Crystal structure and NMR binding reveal that two small molecule antagonists target the high affinity ephrin-binding channel of the EphA4 receptor."
Qin H., Shi J., Noberini R., Pasquale E.B., Song J.
J. Biol. Chem. 283:29473-29484(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 29-209.
[8]"Structural plasticity of EPH receptor A4 facilitates cross-class ephrin signaling."
Bowden T.A., Aricescu A.R., Nettleship J.E., Siebold C., Rahman-Huq N., Owens R.J., Stuart D.I., Jones E.Y.
Structure 17:1386-1397(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 30-202 IN COMPLEX WITH EFNA2 OR EFNB2, LIGAND-BINDING.
[9]"Structural characterization of the EphA4-Ephrin-B2 complex reveals new features enabling Eph-ephrin binding promiscuity."
Qin H., Noberini R., Huan X., Shi J., Pasquale E.B., Song J.
J. Biol. Chem. 285:644-654(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-203 IN COMPLEX WITH EFNB2, MUTAGENESIS OF GLN-40 AND GLU-42.
[10]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-269; GLU-370 AND PHE-399.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36645 mRNA. Translation: AAA74246.1.
BC105000 mRNA. Translation: AAI05001.1.
BC105002 mRNA. Translation: AAI05003.1.
PIRI78844.
RefSeqNP_004429.1. NM_004438.3.
UniGeneHs.371218.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LW8NMR-A29-209[»]
2WO1X-ray1.85A/B30-202[»]
2WO2X-ray2.45A30-202[»]
2WO3X-ray2.35A30-202[»]
3CKHX-ray2.80A/B29-209[»]
3GXUX-ray2.50A29-203[»]
4BK4X-ray3.65A/B20-547[»]
4BK5X-ray4.00A20-547[»]
4BKAX-ray5.30A20-547[»]
4BKFX-ray4.65A/B20-547[»]
4M4PX-ray2.08A27-543[»]
4M4RX-ray3.13A/C/E/G27-543[»]
ProteinModelPortalP54764.
SMRP54764. Positions 27-981.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108357. 13 interactions.
DIPDIP-48294N.
IntActP54764. 2 interactions.
STRING9606.ENSP00000281821.

Chemistry

BindingDBP54764.
ChEMBLCHEMBL3988.
GuidetoPHARMACOLOGY1824.

PTM databases

PhosphoSiteP54764.

Polymorphism databases

DMDM1711371.

Proteomic databases

PaxDbP54764.
PeptideAtlasP54764.
PRIDEP54764.

Protocols and materials databases

DNASU2043.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000281821; ENSP00000281821; ENSG00000116106.
ENST00000409938; ENSP00000386829; ENSG00000116106.
GeneID2043.
KEGGhsa:2043.
UCSCuc002vmq.3. human.

Organism-specific databases

CTD2043.
GeneCardsGC02M222248.
HGNCHGNC:3388. EPHA4.
HPACAB004654.
MIM602188. gene.
neXtProtNX_P54764.
PharmGKBPA27820.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP54764.
KOK05105.
OMAVTHQNKI.
PhylomeDBP54764.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP54764.

Gene expression databases

ArrayExpressP54764.
BgeeP54764.
CleanExHS_EPHA4.
GenevestigatorP54764.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
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.
IPR011510. SAM_2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51550. 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]
ProtoNetSearch...

Other

ChiTaRSEPHA4. human.
EvolutionaryTraceP54764.
GeneWikiEPH_receptor_A4.
GenomeRNAi2043.
NextBio8301.
PROP54764.
SOURCESearch...

Entry information

Entry nameEPHA4_HUMAN
AccessionPrimary (citable) accession number: P54764
Secondary accession number(s): Q2M380
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM