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P54761

- EPHB4_MOUSE

UniProt

P54761 - EPHB4_MOUSE

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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

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. 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
Complete GO annotation...

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.
ReactomeiREACT_241951. Ephrin signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 539524ExtracellularSequence AnalysisAdd
BLAST
Transmembranei540 – 56021HelicalSequence AnalysisAdd
BLAST
Topological domaini561 – 987427CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

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

MaxQBiP54761.
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

BgeeiP54761.
CleanExiMM_EPHB4.
ExpressionAtlasiP54761. baseline and differential.
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

BioGridi199478. 2 interactions.
STRINGi10090.ENSMUSP00000106684.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54761.
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

        10         20         30         40         50
MELRALLCWA SLATALEETL LNTKLETADL KWVTYPQAEG QWEELSGLDE
60 70 80 90 100
EQHSVRTYEV CDMKRPGGQA HWLRTGWVPR RGAVHVYATI RFTMMECLSL
110 120 130 140 150
PRASRSCKET FTVFYYESEA DTATAHTPAW MENPYIKVDT VAAEHLTRKR
160 170 180 190 200
PGAEATGKVN IKTLRLGPLS KAGFYLAFQD QGACMALLSL HLFYKKCSWL
210 220 230 240 250
ITNLTYFPET VPRELVVPVA GSCVANAVPT ANPSPSLYCR EDGQWAEQQV
260 270 280 290 300
TGCSCAPGYE AAESNKVCRA CGQGTFKPQI GDESCLPCPA NSHSNNIGSP
310 320 330 340 350
VCLCRIGYYR ARSDPRSSPC TTPPSAPRSV VHHLNGSTLR LEWSAPLESG
360 370 380 390 400
GREDLTYAVR CRECRPGGSC LPCGGDMTFD PGPRDLVEPW VAIRGLRPDV
410 420 430 440 450
TYTFEVAALN GVSTLATGPP PFEPVNVTTD REVPPAVSDI RVTRSSPSSL
460 470 480 490 500
ILSWAIPRAP SGAVLDYEVK YHEKGAEGPS SVRFLKTSEN RAELRGLKRG
510 520 530 540 550
ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE SESWREQLAL IAGTAVVGVV
560 570 580 590 600
LVLVVVIIAV LCLRKQSNGR EVEYSDKHGQ YLIGHGTKVY IDPFTYEDPN
610 620 630 640 650
EAVREFAKEI DVSYVKIEEV IGAGEFGEVC RGRLKAPGKK ESCVAIKTLK
660 670 680 690 700
GGYTERQRRE FLSEASIMGQ FEHPNIIRLE GVVTNSVPVM ILTEFMENGA
710 720 730 740 750
LDSFLRLNDG QFTVIQLVGM LRGIASGMRY LAEMSYVHRD LAARNILVNS
760 770 780 790 800
NLVCKVSDFG LSRFLEENSS DPTYTSSLGG KIPIRWTAPE AIAFRKFTSA
810 820 830 840 850
SDAWSYGIVM WEVMSFGERP YWDMSNQDVI NAIEQDYRLP PPPDCPTSLH
860 870 880 890 900
QLMLDCWQKD RNARPRFPQV VSALDKMIRN PASLKIVARE NGGASHPLLD
910 920 930 940 950
QRQPHYSAFG SVGEWLRAIK MGRYEESFAA AGFGSFEVVS QISAEDLLRI
960 970 980
GVTLAGHQKK ILASVQHMKS QAKPGAPGGT GGPAQQF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

BioGridi 199478. 2 interactions.
STRINGi 10090.ENSMUSP00000106684.

PTM databases

PhosphoSitei P54761.

Proteomic databases

MaxQBi P54761.
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 ENSGT00760000118975.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi P54761.
KOi K05113.
OrthoDBi EOG7VTDM6.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_241951. Ephrin signaling.
REACT_243590. EPH-ephrin mediated repulsion of cells.
REACT_257656. EPHB-mediated forward signaling.
REACT_258158. EPH-Ephrin signaling.

Miscellaneous databases

ChiTaRSi Ephb4. mouse.
NextBioi 284692.
PROi P54761.
SOURCEi Search...

Gene expression databases

Bgeei P54761.
CleanExi MM_EPHB4.
ExpressionAtlasi P54761. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 145 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