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Q00993

- UFO_MOUSE

UniProt

Q00993 - UFO_MOUSE

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Protein

Tyrosine-protein kinase receptor UFO

Gene

Axl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TENC1. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response.2 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by GAS6-binding and subsequent autophosphorylation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei561 – 5611ATPPROSITE-ProRule annotation
Active sitei666 – 6661Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi536 – 5449ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphatidylserine binding Source: Ensembl
  3. protein heterodimerization activity Source: MGI
  4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. apoptotic cell clearance Source: UniProtKB
  2. blood vessel remodeling Source: MGI
  3. cell maturation Source: Ensembl
  4. cellular response to extracellular stimulus Source: MGI
  5. cellular response to hydrogen peroxide Source: Ensembl
  6. cellular response to interferon-alpha Source: Ensembl
  7. cellular response to lipopolysaccharide Source: Ensembl
  8. dendritic cell differentiation Source: Ensembl
  9. enzyme linked receptor protein signaling pathway Source: MGI
  10. erythrocyte homeostasis Source: MGI
  11. forebrain cell migration Source: MGI
  12. inflammatory response Source: MGI
  13. innate immune response Source: UniProtKB-KW
  14. natural killer cell differentiation Source: MGI
  15. negative regulation of apoptotic process Source: UniProtKB
  16. negative regulation of dendritic cell apoptotic process Source: Ensembl
  17. negative regulation of interferon-gamma production Source: Ensembl
  18. negative regulation of lymphocyte activation Source: MGI
  19. negative regulation of neuron apoptotic process Source: MGI
  20. negative regulation of tumor necrosis factor production Source: MGI
  21. neuron migration Source: MGI
  22. organ regeneration Source: Ensembl
  23. ovulation cycle Source: MGI
  24. phagocytosis Source: MGI
  25. platelet activation Source: MGI
  26. positive regulation of cytokine-mediated signaling pathway Source: Ensembl
  27. positive regulation of natural killer cell differentiation Source: Ensembl
  28. positive regulation of protein kinase B signaling Source: UniProtKB
  29. protein kinase B signaling Source: MGI
  30. secretion by cell Source: MGI
  31. spermatogenesis Source: MGI
  32. substrate adhesion-dependent cell spreading Source: MGI
  33. vagina development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Differentiation, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase receptor UFO (EC:2.7.10.1)
Alternative name(s):
Adhesion-related kinase
Gene namesi
Name:Axl
Synonyms:Ark, Ufo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1347244. Axl.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Keywords - Diseasei

Oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 888870Tyrosine-protein kinase receptor UFOPRO_0000024482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi50 ↔ 111PROSITE-ProRule annotation
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi154 ↔ 199PROSITE-ProRule annotation
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
Modified residuei697 – 6971Phosphotyrosine; by autocatalysisBy similarity
Modified residuei773 – 7731Phosphotyrosine; by autocatalysisBy similarity
Modified residuei815 – 8151Phosphotyrosine; by autocatalysisBy similarity
Modified residuei860 – 8601Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Monoubiquitinated upon GAS6-binding. A very small proportion of the receptor could be subjected to polyubiquitination in a very transient fashion (By similarity).By similarity
Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ00993.
PaxDbiQ00993.
PRIDEiQ00993.

PTM databases

PhosphoSiteiQ00993.

Miscellaneous databases

PMAP-CutDBQ80YQ3.

Expressioni

Tissue specificityi

In distinct substructures of a broad spectrum of developing tissues (in the late embryogenesis). In cells forming organ capsules as well as in connective tissue structures (in adult).

Gene expression databases

BgeeiQ00993.
CleanExiMM_AXL.
ExpressionAtlasiQ00993. baseline and differential.
GenevestigatoriQ00993.

Interactioni

Subunit structurei

Heterodimer and heterotetramer with ligand GAS6 (By similarity). Interacts with CBL, GRB2, LCK, NCK2, PIK3R1, PIK3R2, PIK3R3, PLCG1, SOCS1 and TENC1. Part of a complex including AXL, TNK2 and GRB2, in which GRB2 promotes AXL recruitment by TNK2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi204922. 1 interaction.
IntActiQ00993. 2 interactions.
STRINGi10090.ENSMUSP00000002677.

Structurei

3D structure databases

ProteinModelPortaliQ00993.
SMRiQ00993. Positions 29-417, 485-805.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 445427ExtracellularSequence AnalysisAdd
BLAST
Topological domaini467 – 888422CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei446 – 46621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 12293Ig-like C2-type 1Add
BLAST
Domaini133 – 21684Ig-like C2-type 2Add
BLAST
Domaini221 – 325105Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini330 – 42293Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini530 – 801272Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 8668Interaction with GAS6By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119065.
HOGENOMiHOG000231685.
HOVERGENiHBG006346.
InParanoidiQ00993.
KOiK05115.
OMAiQVQGEPP.
OrthoDBiEOG77DJ5C.
TreeFamiTF317402.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
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.
[Graphical view]
PfamiPF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 2 hits.
SM00409. IG. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50853. FN3. 2 hits.
PS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q00993-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRVPLAWWL ALCCWGCAAH KDTQTEAGSP FVGNPGNITG ARGLTGTLRC
60 70 80 90 100
ELQVQGEPPE VVWLRDGQIL ELADNTQTQV PLGEDWQDEW KVVSQLRISA
110 120 130 140 150
LQLSDAGEYQ CMVHLEGRTF VSQPGFVGLE GLPYFLEEPE DKAVPANTPF
160 170 180 190 200
NLSCQAQGPP EPVTLLWLQD AVPLAPVTGH SSQHSLQTPG LNKTSSFSCE
210 220 230 240 250
AHNAKGVTTS RTATITVLPQ RPHHLHVVSR QPTELEVAWT PGLSGIYPLT
260 270 280 290 300
HCNLQAVLSD DGVGIWLGKS DPPEDPLTLQ VSVPPHQLRL EKLLPHTPYH
310 320 330 340 350
IRISCSSSQG PSPWTHWLPV ETTEGVPLGP PENVSAMRNG SQVLVRWQEP
360 370 380 390 400
RVPLQGTLLG YRLAYRGQDT PEVLMDIGLT REVTLELRGD RPVANLTVSV
410 420 430 440 450
TAYTSAGDGP WSLPVPLEPW RPGQGQPLHH LVSEPPPRAF SWPWWYVLLG
460 470 480 490 500
ALVAAACVLI LALFLVHRRK KETRYGEVFE PTVERGELVV RYRVRKSYSR
510 520 530 540 550
RTTEATLNSL GISEELKEKL RDVMVDRHKV ALGKTLGEGE FGAVMEGQLN
560 570 580 590 600
QDDSILKVAV KTMKIAICTR SELEDFLSEA VCMKEFDHPN VMRLIGVCFQ
610 620 630 640 650
GSDREGFPEP VVILPFMKHG DLHSFLLYSR LGDQPVFLPT QMLVKFMADI
660 670 680 690 700
ASGMEYLSTK RFIHRDLAAR NCMLNENMSV CVADFGLSKK IYNGDYYRQG
710 720 730 740 750
RIAKMPVKWI AIESLADRVY TSKSDVWSFG VTMWEIATRG QTPYPGVENS
760 770 780 790 800
EIYDYLRQGN RLKQPVDCLD GLYALMSRCW ELNPRDRPSF AELREDLENT
810 820 830 840 850
LKALPPAQEP DEILYVNMDE GGSHLEPRGA AGGADPPTQP DPKDSCSCLT
860 870 880
AADVHSAGRY VLCPSTAPGP TLSADRGCPA PPGQEDGA
Length:888
Mass (Da):98,191
Last modified:July 27, 2011 - v2
Checksum:iC5350E3A8995E975
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti394 – 3941A → R in CAA42158. (PubMed:1840679)Curated
Sequence conflicti486 – 4861G → P in CAA42158. (PubMed:1840679)Curated
Sequence conflicti566 – 5661A → V in CAA42158. (PubMed:1840679)Curated
Sequence conflicti768 – 7681C → F in CAA45097. (PubMed:1320243)Curated
Sequence conflicti774 – 7741A → S in CAA45097. (PubMed:1320243)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X63535 mRNA. Translation: CAA45097.1.
X59560 Genomic DNA. Translation: CAA42158.1.
AK155567 mRNA. Translation: BAE33327.1.
CH466593 Genomic DNA. Translation: EDL24236.1.
BC046618 mRNA. Translation: AAH46618.1.
BC050914 mRNA. Translation: AAH50914.1.
CCDSiCCDS20996.1.
PIRiS23065.
S23251.
RefSeqiNP_033491.2. NM_009465.4.
XP_006540052.1. XM_006539989.1.
XP_006540053.1. XM_006539990.1.
UniGeneiMm.4128.

Genome annotation databases

EnsembliENSMUST00000002677; ENSMUSP00000002677; ENSMUSG00000002602.
GeneIDi26362.
KEGGimmu:26362.
UCSCiuc009ftx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X63535 mRNA. Translation: CAA45097.1 .
X59560 Genomic DNA. Translation: CAA42158.1 .
AK155567 mRNA. Translation: BAE33327.1 .
CH466593 Genomic DNA. Translation: EDL24236.1 .
BC046618 mRNA. Translation: AAH46618.1 .
BC050914 mRNA. Translation: AAH50914.1 .
CCDSi CCDS20996.1.
PIRi S23065.
S23251.
RefSeqi NP_033491.2. NM_009465.4.
XP_006540052.1. XM_006539989.1.
XP_006540053.1. XM_006539990.1.
UniGenei Mm.4128.

3D structure databases

ProteinModelPortali Q00993.
SMRi Q00993. Positions 29-417, 485-805.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204922. 1 interaction.
IntActi Q00993. 2 interactions.
STRINGi 10090.ENSMUSP00000002677.

Protein family/group databases

MEROPSi I43.001.

PTM databases

PhosphoSitei Q00993.

Proteomic databases

MaxQBi Q00993.
PaxDbi Q00993.
PRIDEi Q00993.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002677 ; ENSMUSP00000002677 ; ENSMUSG00000002602 .
GeneIDi 26362.
KEGGi mmu:26362.
UCSCi uc009ftx.2. mouse.

Organism-specific databases

CTDi 558.
MGIi MGI:1347244. Axl.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119065.
HOGENOMi HOG000231685.
HOVERGENi HBG006346.
InParanoidi Q00993.
KOi K05115.
OMAi QVQGEPP.
OrthoDBi EOG77DJ5C.
TreeFami TF317402.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.

Miscellaneous databases

ChiTaRSi AXL. mouse.
NextBioi 304223.
PMAP-CutDB Q80YQ3.
PROi Q00993.
SOURCEi Search...

Gene expression databases

Bgeei Q00993.
CleanExi MM_AXL.
ExpressionAtlasi Q00993. baseline and differential.
Genevestigatori Q00993.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
InterProi IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
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.
[Graphical view ]
Pfami PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00060. FN3. 2 hits.
SM00409. IG. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50853. FN3. 2 hits.
PS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The murine ufo receptor: molecular cloning, chromosomal localization and in situ expression analysis."
    Faust M., Ebensperger C., Schulz A.S., Schleithoff L., Hameister H., Bartram C.R., Janssen J.W.G.
    Oncogene 7:1287-1293(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Heart.
  2. "A putative receptor tyrosine kinase with unique structural topology."
    Rescigno J., Mansukhani A., Basilico C.
    Oncogene 6:1909-1913(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Dendritic cell.
  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. "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].
    Strain: C57BL/6.
    Tissue: Brain and Eye.
  6. "The anticoagulation factor protein S and its relative, Gas6, are ligands for the Tyro 3/Axl family of receptor tyrosine kinases."
    Stitt T.N., Conn G., Gore M., Lai C., Bruno J., Radziejewski C., Mattsson K., Fisher J., Gies D.R., Jones P.F., Masiakowski P., Ryan T.E., Tobkes N.J., Chen D.H., DiStefano P.S., Long G.L., Basilico C., Goldfarb M.P.
    , Lemke G., Glass D.J., Yancopoulos G.D.
    Cell 80:661-670(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIGAND GAS6.
  7. "TAM receptors are pleiotropic inhibitors of the innate immune response."
    Rothlin C.V., Ghosh S., Zuniga E.I., Oldstone M.B., Lemke G.
    Cell 131:1124-1136(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INNATE IMMUNE RESPONSE INHIBITION.
  8. "Sertoli cell-initiated testicular innate immune response through toll-like receptor-3 activation is negatively regulated by Tyro3, Axl, and mer receptors."
    Sun B., Qi N., Shang T., Wu H., Deng T., Han D.
    Endocrinology 151:2886-2897(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INNATE IMMUNE RESPONSE INHIBITION.

Entry informationi

Entry nameiUFO_MOUSE
AccessioniPrimary (citable) accession number: Q00993
Secondary accession number(s): Q80YQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 148 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