Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P54761

- EPHB4_MOUSE

UniProt

P54761 - EPHB4_MOUSE

Protein

Ephrin type-B receptor 4

Gene

Ephb4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei647 – 6471ATPPROSITE-ProRule annotation
    Active sitei740 – 7401Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi621 – 6299ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ephrin receptor activity Source: UniProtKB
    3. protein binding Source: MGI
    4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. cell adhesion Source: UniProtKB
    3. cell migration involved in sprouting angiogenesis Source: UniProtKB
    4. ephrin receptor signaling pathway Source: UniProtKB
    5. heart morphogenesis Source: UniProtKB
    6. peptidyl-tyrosine phosphorylation Source: GOC
    7. protein autophosphorylation Source: UniProtKB

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-B receptor 4 (EC:2.7.10.1)
    Alternative name(s):
    Developmental kinase 2
    Short name:
    mDK-2
    Hepatoma transmembrane kinase
    Tyrosine kinase MYK-1
    Gene namesi
    Name:Ephb4
    Synonyms:Htk, Mdk2, Myk1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:104757. Ephb4.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Embryo display cardiovascular defects and lethality with very high penetrance. Growth retardation is observed at E9.5 with arrested heart development and lack of blood flow. By E10.5 degeneration and necrosis are apparent throughout the embryo.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 987972Ephrin type-B receptor 4PRO_0000016835Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi61 ↔ 184By similarity
    Disulfide bondi97 ↔ 107By similarity
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi335 – 3351N-linked (GlcNAc...)2 Publications
    Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence Analysis
    Modified residuei911 – 9111PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated; autophosphorylation is stimulated by EFNB2.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP54761.
    PRIDEiP54761.

    PTM databases

    PhosphoSiteiP54761.

    Expressioni

    Tissue specificityi

    Expressed in various organ systems, including lung, liver, kidney, intestine, muscle and heart.1 Publication

    Developmental stagei

    Specifically expressed in the developing cardiovascular system with higher expression in veins. First detected in the developing anterior cardinal vein at E8.75. Abundant expression at E16.5 in various organ systems, including thymus, heart, lung and kidney, where it is associated with cells of endothelial origin.1 Publication

    Gene expression databases

    ArrayExpressiP54761.
    BgeeiP54761.
    CleanExiMM_EPHB4.
    GenevestigatoriP54761.

    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

    STRINGi10090.ENSMUSP00000106684.

    Structurei

    3D structure databases

    ProteinModelPortaliP54761.
    SMRiP54761. Positions 15-533, 564-973.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini16 – 539524ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini561 – 987427CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei540 – 56021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 202186Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini323 – 432110Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini436 – 52994Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 899285Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini907 – 97165SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi985 – 9873PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi184 – 320137Cys-richAdd
    BLAST

    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

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115081.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    KOiK05113.
    OrthoDBiEOG7VTDM6.

    Family and domain databases

    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. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    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.
    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.
    PF00041. fn3. 2 hits.
    PF07699. GCC2_GCC3. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00615. EPH_lbd. 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.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS01186. EGF_2. 1 hit.
    PS51550. 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.

    P54761-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELRALLCWA SLATALEETL LNTKLETADL KWVTYPQAEG QWEELSGLDE    50
    EQHSVRTYEV CDMKRPGGQA HWLRTGWVPR RGAVHVYATI RFTMMECLSL 100
    PRASRSCKET FTVFYYESEA DTATAHTPAW MENPYIKVDT VAAEHLTRKR 150
    PGAEATGKVN IKTLRLGPLS KAGFYLAFQD QGACMALLSL HLFYKKCSWL 200
    ITNLTYFPET VPRELVVPVA GSCVANAVPT ANPSPSLYCR EDGQWAEQQV 250
    TGCSCAPGYE AAESNKVCRA CGQGTFKPQI GDESCLPCPA NSHSNNIGSP 300
    VCLCRIGYYR ARSDPRSSPC TTPPSAPRSV VHHLNGSTLR LEWSAPLESG 350
    GREDLTYAVR CRECRPGGSC LPCGGDMTFD PGPRDLVEPW VAIRGLRPDV 400
    TYTFEVAALN GVSTLATGPP PFEPVNVTTD REVPPAVSDI RVTRSSPSSL 450
    ILSWAIPRAP SGAVLDYEVK YHEKGAEGPS SVRFLKTSEN RAELRGLKRG 500
    ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE SESWREQLAL IAGTAVVGVV 550
    LVLVVVIIAV LCLRKQSNGR EVEYSDKHGQ YLIGHGTKVY IDPFTYEDPN 600
    EAVREFAKEI DVSYVKIEEV IGAGEFGEVC RGRLKAPGKK ESCVAIKTLK 650
    GGYTERQRRE FLSEASIMGQ FEHPNIIRLE GVVTNSVPVM ILTEFMENGA 700
    LDSFLRLNDG QFTVIQLVGM LRGIASGMRY LAEMSYVHRD LAARNILVNS 750
    NLVCKVSDFG LSRFLEENSS DPTYTSSLGG KIPIRWTAPE AIAFRKFTSA 800
    SDAWSYGIVM WEVMSFGERP YWDMSNQDVI NAIEQDYRLP PPPDCPTSLH 850
    QLMLDCWQKD RNARPRFPQV VSALDKMIRN PASLKIVARE NGGASHPLLD 900
    QRQPHYSAFG SVGEWLRAIK MGRYEESFAA AGFGSFEVVS QISAEDLLRI 950
    GVTLAGHQKK ILASVQHMKS QAKPGAPGGT GGPAQQF 987
    Length:987
    Mass (Da):108,848
    Last modified:July 27, 2011 - v2
    Checksum:iE4FC5B2210723974
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201A → R in CAA88909. (PubMed:7478528)Curated
    Sequence conflicti120 – 1201A → R in AAA18591. (PubMed:8152808)Curated
    Sequence conflicti351 – 3533GRE → RPR in AAA18591. (PubMed:8152808)Curated
    Sequence conflicti389 – 3891P → R in AAA18591. (PubMed:8152808)Curated
    Sequence conflicti659 – 6591R → A in AAA18591. (PubMed:8152808)Curated
    Sequence conflicti783 – 7831P → S in CAA88909. (PubMed:7478528)Curated
    Sequence conflicti805 – 8051S → R in AAA18591. (PubMed:8152808)Curated
    Sequence conflicti913 – 9131G → V in AAA18591. (PubMed:8152808)Curated
    Sequence conflicti938 – 9381V → M in AAA18591. (PubMed:8152808)Curated
    Sequence conflicti970 – 9712SQ → WE in AAA18591. (PubMed:8152808)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49085 mRNA. Translation: CAA88909.1.
    U06834 mRNA. Translation: AAA18591.1.
    AF312033 Genomic DNA. Translation: AAK28823.1.
    CH466529 Genomic DNA. Translation: EDL19273.1.
    CH466529 Genomic DNA. Translation: EDL19275.1.
    CCDSiCCDS19767.1.
    PIRiI48652.
    I48953.
    RefSeqiNP_034274.4. NM_010144.6.
    UniGeneiMm.34533.

    Genome annotation databases

    EnsembliENSMUST00000061244; ENSMUSP00000051622; ENSMUSG00000029710.
    ENSMUST00000144296; ENSMUSP00000115731; ENSMUSG00000029710.
    ENSMUST00000166239; ENSMUSP00000130275; ENSMUSG00000029710.
    GeneIDi13846.
    KEGGimmu:13846.
    UCSCiuc009aci.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49085 mRNA. Translation: CAA88909.1 .
    U06834 mRNA. Translation: AAA18591.1 .
    AF312033 Genomic DNA. Translation: AAK28823.1 .
    CH466529 Genomic DNA. Translation: EDL19273.1 .
    CH466529 Genomic DNA. Translation: EDL19275.1 .
    CCDSi CCDS19767.1.
    PIRi I48652.
    I48953.
    RefSeqi NP_034274.4. NM_010144.6.
    UniGenei Mm.34533.

    3D structure databases

    ProteinModelPortali P54761.
    SMRi P54761. Positions 15-533, 564-973.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000106684.

    PTM databases

    PhosphoSitei P54761.

    Proteomic databases

    PaxDbi P54761.
    PRIDEi P54761.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000061244 ; ENSMUSP00000051622 ; ENSMUSG00000029710 .
    ENSMUST00000144296 ; ENSMUSP00000115731 ; ENSMUSG00000029710 .
    ENSMUST00000166239 ; ENSMUSP00000130275 ; ENSMUSG00000029710 .
    GeneIDi 13846.
    KEGGi mmu:13846.
    UCSCi uc009aci.2. mouse.

    Organism-specific databases

    CTDi 2050.
    MGIi MGI:104757. Ephb4.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115081.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    KOi K05113.
    OrthoDBi EOG7VTDM6.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    ChiTaRSi EPHB4. mouse.
    NextBioi 284692.
    PROi P54761.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54761.
    Bgeei P54761.
    CleanExi MM_EPHB4.
    Genevestigatori P54761.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 2 hits.
    InterProi IPR027936. Eph_TM.
    IPR001090. Ephrin_rcpt_lig-bd_dom.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR009030. Growth_fac_rcpt_N_dom.
    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.
    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 ]
    Pfami PF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07699. GCC2_GCC3. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00615. EPH_lbd. 1 hit.
    SM00060. FN3. 2 hits.
    SM00454. SAM. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS01186. EGF_2. 1 hit.
    PS51550. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization, and differential expression of MDK2 and MDK5, two novel receptor tyrosine kinases of the eck/eph family."
      Ciossek T., Lerch M.M., Ullrich A.
      Oncogene 11:2085-2095(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Kidney.
    2. "Expression of two novel eph-related receptor protein tyrosine kinases in mammary gland development and carcinogenesis."
      Andres A.-C., Reid H.H., Zurcher G., Blaschke R.J., Albrecht D., Ziemiecki A.
      Oncogene 9:1461-1467(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Lung.
    3. "Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5."
      Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F.
      Nucleic Acids Res. 29:1352-1365(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development."
      Gerety S.S., Wang H.U., Chen Z.F., Anderson D.J.
      Mol. Cell 4:403-414(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN ANGIOGENESIS, DEVELOPMENTAL STAGE.
    6. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-335.
      Tissue: Myoblast.
    7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-335.

    Entry informationi

    Entry nameiEPHB4_MOUSE
    AccessioniPrimary (citable) accession number: P54761
    Secondary accession number(s): Q60627, Q99MR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3