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Q12866

- MERTK_HUMAN

UniProt

Q12866 - MERTK_HUMAN

Protein

Tyrosine-protein kinase Mer

Gene

MERTK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.1 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 sitei615 – 6151ATPPROSITE-ProRule annotation
    Active sitei723 – 7231Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi593 – 6019ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic cell clearance Source: Ensembl
    2. blood coagulation Source: Reactome
    3. cell-cell signaling Source: ProtInc
    4. cell surface receptor signaling pathway Source: ProtInc
    5. leukocyte migration Source: Reactome
    6. natural killer cell differentiation Source: Ensembl
    7. negative regulation of lymphocyte activation Source: Ensembl
    8. peptidyl-tyrosine phosphorylation Source: GOC
    9. phagocytosis Source: BHF-UCL
    10. platelet activation Source: Ensembl
    11. positive regulation of phagocytosis Source: UniProtKB
    12. protein kinase B signaling Source: Ensembl
    13. protein phosphorylation Source: ProtInc
    14. retina development in camera-type eye Source: Ensembl
    15. secretion by cell Source: Ensembl
    16. spermatogenesis Source: Ensembl
    17. substrate adhesion-dependent cell spreading Source: Ensembl
    18. vagina development Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
    SignaLinkiQ12866.

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Mer (EC:2.7.10.1)
    Alternative name(s):
    Proto-oncogene c-Mer
    Receptor tyrosine kinase MerTK
    Gene namesi
    Name:MERTK
    Synonyms:MER
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7027. MERTK.

    Subcellular locationi

    Membrane By similarity; Single-pass type I membrane protein By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular space Source: UniProtKB
    3. integral component of plasma membrane Source: ProtInc
    4. photoreceptor outer segment Source: Ensembl
    5. plasma membrane Source: Reactome
    6. rhabdomere Source: BHF-UCL

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Retinitis pigmentosa 38 (RP38) [MIM:613862]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti540 – 5401E → K in RP38. 1 Publication
    Corresponds to variant rs113485015 [ dbSNP | Ensembl ].
    VAR_021046
    Natural varianti661 – 6611S → C in RP38. 1 Publication
    VAR_021047
    Natural varianti871 – 8711I → T in RP38. 1 Publication
    VAR_021048

    Keywords - Diseasei

    Disease mutation, Proto-oncogene, Retinitis pigmentosa

    Organism-specific databases

    MIMi613862. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA30759.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 999979Tyrosine-protein kinase MerPRO_0000024443Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi115 ↔ 175PROSITE-ProRule annotation
    Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi218 ↔ 262PROSITE-ProRule annotation
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi442 – 4421N-linked (GlcNAc...)1 Publication
    Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence Analysis
    Modified residuei543 – 5431Phosphoserine1 Publication
    Modified residuei749 – 7491Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei753 – 7531Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei754 – 7541Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei872 – 8721Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei935 – 9351Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated on Tyr-749, Tyr-753 and Tyr-754 in the activation loop allowing full activity. Autophosphorylated on Tyr-872 leading to recruitment of downstream partners of the signaling cascade such as PLCG2 By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ12866.
    PaxDbiQ12866.
    PRIDEiQ12866.

    PTM databases

    PhosphoSiteiQ12866.

    Expressioni

    Tissue specificityi

    Not expressed in normal B- and T-lymphocytes but is expressed in numerous neoplastic B- and T-cell lines. Highly expressed in testis, ovary, prostate, lung, and kidney, with lower expression in spleen, small intestine, colon, and liver.

    Gene expression databases

    ArrayExpressiQ12866.
    BgeeiQ12866.
    CleanExiHS_MERTK.
    GenevestigatoriQ12866.

    Organism-specific databases

    HPAiHPA036196.

    Interactioni

    Subunit structurei

    Interacts (upon activation) with TNK2; stimulates TNK2 autophosphorylation. Interacts (via N-terminus) with extracellular ligands LGALS3, TUB, TULP1 and GAS6 By similarity. Interacts with VAV1 in a phosphotyrosine-independent manner.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi115724. 8 interactions.
    IntActiQ12866. 4 interactions.
    STRINGi9606.ENSP00000295408.

    Structurei

    Secondary structure

    1
    999
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi388 – 3947
    Beta strandi396 – 40611
    Beta strandi417 – 42812
    Beta strandi431 – 44111
    Beta strandi446 – 4494
    Beta strandi453 – 4597
    Beta strandi461 – 4677
    Beta strandi476 – 4794
    Turni577 – 5804
    Helixi584 – 5863
    Beta strandi587 – 5948
    Beta strandi601 – 6077
    Beta strandi613 – 6208
    Helixi628 – 64215
    Beta strandi654 – 6574
    Beta strandi667 – 6726
    Helixi679 – 6857
    Beta strandi688 – 6925
    Helixi697 – 71519
    Turni716 – 7183
    Helixi726 – 7283
    Beta strandi729 – 7313
    Beta strandi737 – 7393
    Helixi764 – 7663
    Helixi769 – 7735
    Helixi779 – 79416
    Helixi806 – 8083
    Helixi809 – 8146
    Beta strandi822 – 8243
    Helixi827 – 8359
    Helixi841 – 8433
    Helixi847 – 86014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DBJNMR-A373-483[»]
    2P0CX-ray2.40A/B570-864[»]
    3BPRX-ray2.80A/B/C/D570-864[»]
    3BRBX-ray1.90A/B570-864[»]
    3TCPX-ray2.69A/B570-864[»]
    4M3QX-ray2.72A/B570-864[»]
    4MH7X-ray2.51A/B570-864[»]
    4MHAX-ray2.59A/B570-864[»]
    ProteinModelPortaliQ12866.
    SMRiQ12866. Positions 103-281, 283-492, 575-900.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12866.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 505485ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini527 – 999473CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei506 – 52621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 186106Ig-like C2-type 1Add
    BLAST
    Domaini197 – 27377Ig-like C2-type 2Add
    BLAST
    Domaini286 – 38196Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini386 – 48499Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini587 – 858272Protein kinasePROSITE-ProRule annotationAdd
    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.
    HOGENOMiHOG000231685.
    HOVERGENiHBG006346.
    InParanoidiQ12866.
    KOiK05117.
    OMAiNEIGWSA.
    OrthoDBiEOG77DJ5C.
    PhylomeDBiQ12866.
    TreeFamiTF317402.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    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. 1 hit.
    PF07679. I-set. 1 hit.
    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.

    Q12866-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPAPLPLLL GLFLPALWRR AITEAREEAK PYPLFPGPFP GSLQTDHTPL    50
    LSLPHASGYQ PALMFSPTQP GRPHTGNVAI PQVTSVESKP LPPLAFKHTV 100
    GHIILSEHKG VKFNCSISVP NIYQDTTISW WKDGKELLGA HHAITQFYPD 150
    DEVTAIIASF SITSVQRSDN GSYICKMKIN NEEIVSDPIY IEVQGLPHFT 200
    KQPESMNVTR NTAFNLTCQA VGPPEPVNIF WVQNSSRVNE QPEKSPSVLT 250
    VPGLTEMAVF SCEAHNDKGL TVSKGVQINI KAIPSPPTEV SIRNSTAHSI 300
    LISWVPGFDG YSPFRNCSIQ VKEADPLSNG SVMIFNTSAL PHLYQIKQLQ 350
    ALANYSIGVS CMNEIGWSAV SPWILASTTE GAPSVAPLNV TVFLNESSDN 400
    VDIRWMKPPT KQQDGELVGY RISHVWQSAG ISKELLEEVG QNGSRARISV 450
    QVHNATCTVR IAAVTRGGVG PFSDPVKIFI PAHGWVDYAP SSTPAPGNAD 500
    PVLIIFGCFC GFILIGLILY ISLAIRKRVQ ETKFGNAFTE EDSELVVNYI 550
    AKKSFCRRAI ELTLHSLGVS EELQNKLEDV VIDRNLLILG KILGEGEFGS 600
    VMEGNLKQED GTSLKVAVKT MKLDNSSQRE IEEFLSEAAC MKDFSHPNVI 650
    RLLGVCIEMS SQGIPKPMVI LPFMKYGDLH TYLLYSRLET GPKHIPLQTL 700
    LKFMVDIALG MEYLSNRNFL HRDLAARNCM LRDDMTVCVA DFGLSKKIYS 750
    GDYYRQGRIA KMPVKWIAIE SLADRVYTSK SDVWAFGVTM WEIATRGMTP 800
    YPGVQNHEMY DYLLHGHRLK QPEDCLDELY EIMYSCWRTD PLDRPTFSVL 850
    RLQLEKLLES LPDVRNQADV IYVNTQLLES SEGLAQGSTL APLDLNIDPD 900
    SIIASCTPRA AISVVTAEVH DSKPHEGRYI LNGGSEEWED LTSAPSAAVT 950
    AEKNSVLPGE RLVRNGVSWS HSSMLPLGSS LPDELLFADD SSEGSEVLM 999
    Length:999
    Mass (Da):110,249
    Last modified:November 13, 2007 - v2
    Checksum:i05BC339F05DFD355
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401A → G in AAB60430. (PubMed:8086340)Curated
    Sequence conflicti143 – 1431A → R in AAB60430. (PubMed:8086340)Curated
    Sequence conflicti247 – 2471S → G in AAB60430. (PubMed:8086340)Curated
    Sequence conflicti274 – 2741K → Q in AAB60430. (PubMed:8086340)Curated
    Sequence conflicti328 – 3281S → G in AAB60430. (PubMed:8086340)Curated
    Sequence conflicti628 – 6281Q → H in AAB60430. (PubMed:8086340)Curated
    Sequence conflicti794 – 7941A → R in AAB60430. (PubMed:8086340)Curated
    Sequence conflicti888 – 8881S → P in AAB60430. (PubMed:8086340)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201R → S.2 Publications
    Corresponds to variant rs35898499 [ dbSNP | Ensembl ].
    VAR_021039
    Natural varianti118 – 1181S → N.3 Publications
    Corresponds to variant rs13027171 [ dbSNP | Ensembl ].
    VAR_021040
    Natural varianti185 – 1851V → M.1 Publication
    Corresponds to variant rs56205303 [ dbSNP | Ensembl ].
    VAR_041741
    Natural varianti214 – 2141F → V Found in a patient with Leber congenital amaurosis. 1 Publication
    VAR_067194
    Natural varianti282 – 2821A → T.2 Publications
    Corresponds to variant rs7588635 [ dbSNP | Ensembl ].
    VAR_021041
    Natural varianti289 – 2891E → K.1 Publication
    VAR_041742
    Natural varianti293 – 2931R → H.2 Publications
    Corresponds to variant rs34072093 [ dbSNP | Ensembl ].
    VAR_021042
    Natural varianti329 – 3291N → S.
    Corresponds to variant rs34943572 [ dbSNP | Ensembl ].
    VAR_051698
    Natural varianti446 – 4461A → G in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041743
    Natural varianti452 – 4521V → L.1 Publication
    Corresponds to variant rs34010621 [ dbSNP | Ensembl ].
    VAR_041744
    Natural varianti466 – 4661R → K.2 Publications
    Corresponds to variant rs7604639 [ dbSNP | Ensembl ].
    VAR_021043
    Natural varianti498 – 4981N → S.2 Publications
    Corresponds to variant rs35858762 [ dbSNP | Ensembl ].
    VAR_021044
    Natural varianti518 – 5181I → V.2 Publications
    Corresponds to variant rs2230515 [ dbSNP | Ensembl ].
    VAR_021045
    Natural varianti540 – 5401E → K in RP38. 1 Publication
    Corresponds to variant rs113485015 [ dbSNP | Ensembl ].
    VAR_021046
    Natural varianti661 – 6611S → C in RP38. 1 Publication
    VAR_021047
    Natural varianti662 – 6621Q → E.1 Publication
    Corresponds to variant rs56209758 [ dbSNP | Ensembl ].
    VAR_041745
    Natural varianti708 – 7081A → S in a head & Neck squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041746
    Natural varianti823 – 8231E → Q.1 Publication
    Corresponds to variant rs55924349 [ dbSNP | Ensembl ].
    VAR_041747
    Natural varianti865 – 8651R → W.1 Publication
    Corresponds to variant rs2230516 [ dbSNP | Ensembl ].
    VAR_020285
    Natural varianti870 – 8701V → I.1 Publication
    Corresponds to variant rs2230517 [ dbSNP | Ensembl ].
    VAR_029237
    Natural varianti871 – 8711I → T in RP38. 1 Publication
    VAR_021048
    Natural varianti871 – 8711I → V.1 Publication
    VAR_021049
    Natural varianti958 – 9581P → L Found in a patient with Leber congenital amaurosis. 1 Publication
    Corresponds to variant rs201460398 [ dbSNP | Ensembl ].
    VAR_067195

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08023 mRNA. Translation: AAB60430.1.
    AH010001 Genomic DNA. Translation: AAG33129.1.
    AC093675 Genomic DNA. No translation available.
    AC104651 Genomic DNA. No translation available.
    CCDSiCCDS2094.1.
    PIRiI38547.
    RefSeqiNP_006334.2. NM_006343.2.
    UniGeneiHs.306178.

    Genome annotation databases

    EnsembliENST00000295408; ENSP00000295408; ENSG00000153208.
    ENST00000421804; ENSP00000389152; ENSG00000153208.
    GeneIDi10461.
    KEGGihsa:10461.
    UCSCiuc002thk.1. human.

    Polymorphism databases

    DMDMi160332297.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Mutations of the MERTK gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08023 mRNA. Translation: AAB60430.1 .
    AH010001 Genomic DNA. Translation: AAG33129.1 .
    AC093675 Genomic DNA. No translation available.
    AC104651 Genomic DNA. No translation available.
    CCDSi CCDS2094.1.
    PIRi I38547.
    RefSeqi NP_006334.2. NM_006343.2.
    UniGenei Hs.306178.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DBJ NMR - A 373-483 [» ]
    2P0C X-ray 2.40 A/B 570-864 [» ]
    3BPR X-ray 2.80 A/B/C/D 570-864 [» ]
    3BRB X-ray 1.90 A/B 570-864 [» ]
    3TCP X-ray 2.69 A/B 570-864 [» ]
    4M3Q X-ray 2.72 A/B 570-864 [» ]
    4MH7 X-ray 2.51 A/B 570-864 [» ]
    4MHA X-ray 2.59 A/B 570-864 [» ]
    ProteinModelPortali Q12866.
    SMRi Q12866. Positions 103-281, 283-492, 575-900.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115724. 8 interactions.
    IntActi Q12866. 4 interactions.
    STRINGi 9606.ENSP00000295408.

    Chemistry

    BindingDBi Q12866.
    ChEMBLi CHEMBL5331.
    GuidetoPHARMACOLOGYi 1837.

    Protein family/group databases

    MEROPSi I43.001.

    PTM databases

    PhosphoSitei Q12866.

    Polymorphism databases

    DMDMi 160332297.

    Proteomic databases

    MaxQBi Q12866.
    PaxDbi Q12866.
    PRIDEi Q12866.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295408 ; ENSP00000295408 ; ENSG00000153208 .
    ENST00000421804 ; ENSP00000389152 ; ENSG00000153208 .
    GeneIDi 10461.
    KEGGi hsa:10461.
    UCSCi uc002thk.1. human.

    Organism-specific databases

    CTDi 10461.
    GeneCardsi GC02P112656.
    GeneReviewsi MERTK.
    H-InvDB HIX0002374.
    HGNCi HGNC:7027. MERTK.
    HPAi HPA036196.
    MIMi 604705. gene.
    613862. phenotype.
    neXtProti NX_Q12866.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA30759.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231685.
    HOVERGENi HBG006346.
    InParanoidi Q12866.
    KOi K05117.
    OMAi NEIGWSA.
    OrthoDBi EOG77DJ5C.
    PhylomeDBi Q12866.
    TreeFami TF317402.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_12051. Cell surface interactions at the vascular wall.
    SignaLinki Q12866.

    Miscellaneous databases

    ChiTaRSi MERTK. human.
    EvolutionaryTracei Q12866.
    GeneWikii MERTK.
    GenomeRNAii 10461.
    NextBioi 39667.
    PROi Q12866.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12866.
    Bgeei Q12866.
    CleanExi HS_MERTK.
    Genevestigatori Q12866.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    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. 1 hit.
    PF07679. I-set. 1 hit.
    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

    1. "Cloning and mRNA expression analysis of a novel human protooncogene, c-mer."
      Graham D.K., Dawson T.L., Mullaney D.L., Snodgrass H.R., Earp H.S.
      Cell Growth Differ. 5:647-657(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-118.
      Tissue: Peripheral blood leukocyte.
    2. Erratum
      Graham D.K., Dawson T.L., Mullaney D.L., Snodgrass H.R., Earp H.S.
      Cell Growth Differ. 5:1022-1022(1994)
    3. "Mutations in MERTK, the human orthologue of the RCS rat retinal dystrophy gene, cause retinitis pigmentosa."
      Gal A., Li Y., Thompson D.A., Weir J., Orth U., Jacobson S.G., Apfelstedt-Sylla E., Vollrath D.
      Nat. Genet. 26:270-271(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-999, VARIANTS RP38 LYS-540; CYS-661 AND THR-871, VARIANTS SER-20; ASN-118; THR-282; HIS-293; LYS-466; SER-498; VAL-518 AND VAL-871.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Identification of the major autophosphorylation sites of Nyk/Mer, an NCAM-related receptor tyrosine kinase."
      Ling L., Templeton D., Kung H.J.
      J. Biol. Chem. 271:18355-18362(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-749; TYR-753 AND TYR-754.
    6. "Identification of Gas6 as a ligand for Mer, a neural cell adhesion molecule related receptor tyrosine kinase implicated in cellular transformation."
      Chen J., Carey K., Godowski P.J.
      Oncogene 14:2033-2039(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAS6.
    7. "An SH2 domain-dependent, phosphotyrosine-independent interaction between Vav1 and the Mer receptor tyrosine kinase: a mechanism for localizing guanine nucleotide-exchange factor action."
      Mahajan N.P., Earp H.S.
      J. Biol. Chem. 278:42596-42603(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VAV1.
    8. "Activated tyrosine kinase Ack1 promotes prostate tumorigenesis: role of Ack1 in polyubiquitination of tumor suppressor Wwox."
      Mahajan N.P., Whang Y.E., Mohler J.L., Earp H.S.
      Cancer Res. 65:10514-10523(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNK2.
    9. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-442.
      Tissue: Plasma.
    10. "Signalling and functional diversity within the Axl subfamily of receptor tyrosine kinases."
      Hafizi S., Dahlback B.
      Cytokine Growth Factor Rev. 17:295-304(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    11. Cited for: FUNCTION AS CELL ENTRY FACTOR IN FILOVIRUS INFECTION.
    12. Cited for: REVIEW ON FUNCTION.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-935, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Galectin-3 is a new MerTK-specific eat-me signal."
      Caberoy N.B., Alvarado G., Bigcas J.L., Li W.
      J. Cell. Physiol. 227:401-407(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LGALS3.
    15. "Solution structures of the FN3 domain of human proto-oncogene tyrosine-protein kinase MER precursor."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 366-483.
    16. "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.
      , 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] SER-20; ASN-118; MET-185; THR-282; LYS-289; HIS-293; GLY-446; LEU-452; LYS-466; SER-498; VAL-518; GLU-662; SER-708; GLN-823; TRP-865 AND ILE-870.
    17. "Detection of variants in 15 genes in 87 unrelated Chinese patients with Leber congenital amaurosis."
      Li L., Xiao X., Li S., Jia X., Wang P., Guo X., Jiao X., Zhang Q., Hejtmancik J.F.
      PLoS ONE 6:E19458-E19458(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-214 AND LEU-958.

    Entry informationi

    Entry nameiMERTK_HUMAN
    AccessioniPrimary (citable) accession number: Q12866
    Secondary accession number(s): Q9HBB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 166 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 2
      Human chromosome 2: 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

    External Data

    Dasty 3