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Protein

Tyrosine-protein kinase Mer

Gene

MERTK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 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)DescriptionActionsGraphical viewLength
Binding sitei615ATPPROSITE-ProRule annotation1
Active sitei723Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi593 – 601ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • transmembrane receptor protein tyrosine kinase activity Source: ProtInc

GO - Biological processi

  • apoptotic cell clearance Source: Ensembl
  • cell-cell signaling Source: ProtInc
  • cell surface receptor signaling pathway Source: ProtInc
  • leukocyte migration Source: Reactome
  • natural killer cell differentiation Source: Ensembl
  • negative regulation of leukocyte apoptotic process Source: CACAO
  • negative regulation of lymphocyte activation Source: Ensembl
  • phagocytosis Source: BHF-UCL
  • platelet activation Source: Ensembl
  • positive regulation of phagocytosis Source: UniProtKB
  • protein kinase B signaling Source: Ensembl
  • protein phosphorylation Source: ProtInc
  • retina development in camera-type eye Source: Ensembl
  • secretion by cell Source: Ensembl
  • spermatogenesis Source: Ensembl
  • substrate adhesion-dependent cell spreading Source: Ensembl
  • vagina development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07891-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-202733. Cell surface interactions at the vascular wall.
SignaLinkiQ12866.
SIGNORiQ12866.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:7027. MERTK.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 505ExtracellularSequence analysisAdd BLAST485
Transmembranei506 – 526HelicalSequence analysisAdd BLAST21
Topological domaini527 – 999CytoplasmicSequence analysisAdd BLAST473

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular space Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • photoreceptor outer segment Source: Ensembl
  • plasma membrane Source: Reactome
  • rhabdomere Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 38 (RP38)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613862
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021046540E → K in RP38. 1 PublicationCorresponds to variant rs113485015dbSNPEnsembl.1
Natural variantiVAR_021047661S → C in RP38. 1 Publication1
Natural variantiVAR_021048871I → T in RP38. 1 PublicationCorresponds to variant rs377341255dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Proto-oncogene, Retinitis pigmentosa

Organism-specific databases

DisGeNETi10461.
MalaCardsiMERTK.
MIMi613862. phenotype.
OpenTargetsiENSG00000153208.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA30759.

Chemistry databases

ChEMBLiCHEMBL5331.
GuidetoPHARMACOLOGYi1837.

Polymorphism and mutation databases

BioMutaiMERTK.
DMDMi160332297.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000002444321 – 999Tyrosine-protein kinase MerAdd BLAST979

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi114N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi115 ↔ 175PROSITE-ProRule annotation
Glycosylationi170N-linked (GlcNAc...)Sequence analysis1
Glycosylationi207N-linked (GlcNAc...)Sequence analysis1
Glycosylationi215N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi218 ↔ 262PROSITE-ProRule annotation
Glycosylationi234N-linked (GlcNAc...)Sequence analysis1
Glycosylationi294N-linked (GlcNAc...)Sequence analysis1
Glycosylationi316N-linked (GlcNAc...)Sequence analysis1
Glycosylationi329N-linked (GlcNAc...)Sequence analysis1
Glycosylationi336N-linked (GlcNAc...)Sequence analysis1
Glycosylationi354N-linked (GlcNAc...)Sequence analysis1
Glycosylationi389N-linked (GlcNAc...)Sequence analysis1
Glycosylationi395N-linked (GlcNAc...)Sequence analysis1
Glycosylationi442N-linked (GlcNAc...)1 Publication1
Glycosylationi454N-linked (GlcNAc...)Sequence analysis1
Modified residuei543PhosphoserineCombined sources1
Modified residuei749Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei753Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei754Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei872Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei935PhosphoserineCombined sources1

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

EPDiQ12866.
MaxQBiQ12866.
PaxDbiQ12866.
PeptideAtlasiQ12866.
PRIDEiQ12866.

PTM databases

iPTMnetiQ12866.
PhosphoSitePlusiQ12866.

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

BgeeiENSG00000153208.
CleanExiHS_MERTK.
ExpressionAtlasiQ12866. baseline and differential.
GenevisibleiQ12866. HS.

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 interactors.
IntActiQ12866. 4 interactors.
STRINGi9606.ENSP00000295408.

Chemistry databases

BindingDBiQ12866.

Structurei

Secondary structure

1999
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi388 – 394Combined sources7
Beta strandi396 – 406Combined sources11
Beta strandi417 – 428Combined sources12
Beta strandi431 – 441Combined sources11
Beta strandi446 – 449Combined sources4
Beta strandi453 – 459Combined sources7
Beta strandi461 – 467Combined sources7
Beta strandi476 – 479Combined sources4
Turni577 – 580Combined sources4
Helixi584 – 586Combined sources3
Beta strandi587 – 594Combined sources8
Beta strandi601 – 607Combined sources7
Beta strandi613 – 620Combined sources8
Helixi628 – 642Combined sources15
Beta strandi654 – 657Combined sources4
Beta strandi661 – 663Combined sources3
Beta strandi667 – 672Combined sources6
Helixi679 – 685Combined sources7
Beta strandi688 – 692Combined sources5
Helixi697 – 715Combined sources19
Turni716 – 718Combined sources3
Helixi726 – 728Combined sources3
Beta strandi729 – 731Combined sources3
Beta strandi737 – 739Combined sources3
Helixi764 – 766Combined sources3
Helixi769 – 773Combined sources5
Helixi779 – 794Combined sources16
Helixi806 – 808Combined sources3
Helixi809 – 814Combined sources6
Beta strandi822 – 824Combined sources3
Helixi827 – 835Combined sources9
Helixi841 – 843Combined sources3
Helixi847 – 860Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12866.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini81 – 186Ig-like C2-type 1Add BLAST106
Domaini197 – 273Ig-like C2-type 2Add BLAST77
Domaini286 – 381Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST96
Domaini386 – 484Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST99
Domaini587 – 858Protein kinasePROSITE-ProRule annotationAdd BLAST272

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

eggNOGiENOG410IG6I. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00810000125384.
HOGENOMiHOG000231685.
HOVERGENiHBG006346.
InParanoidiQ12866.
KOiK05117.
OMAiKHIPLQT.
OrthoDBiEOG091G016X.
PhylomeDBiQ12866.
TreeFamiTF317402.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
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.
PF00047. ig. 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]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF49265. 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

        10         20         30         40         50
MGPAPLPLLL GLFLPALWRR AITEAREEAK PYPLFPGPFP GSLQTDHTPL
60 70 80 90 100
LSLPHASGYQ PALMFSPTQP GRPHTGNVAI PQVTSVESKP LPPLAFKHTV
110 120 130 140 150
GHIILSEHKG VKFNCSISVP NIYQDTTISW WKDGKELLGA HHAITQFYPD
160 170 180 190 200
DEVTAIIASF SITSVQRSDN GSYICKMKIN NEEIVSDPIY IEVQGLPHFT
210 220 230 240 250
KQPESMNVTR NTAFNLTCQA VGPPEPVNIF WVQNSSRVNE QPEKSPSVLT
260 270 280 290 300
VPGLTEMAVF SCEAHNDKGL TVSKGVQINI KAIPSPPTEV SIRNSTAHSI
310 320 330 340 350
LISWVPGFDG YSPFRNCSIQ VKEADPLSNG SVMIFNTSAL PHLYQIKQLQ
360 370 380 390 400
ALANYSIGVS CMNEIGWSAV SPWILASTTE GAPSVAPLNV TVFLNESSDN
410 420 430 440 450
VDIRWMKPPT KQQDGELVGY RISHVWQSAG ISKELLEEVG QNGSRARISV
460 470 480 490 500
QVHNATCTVR IAAVTRGGVG PFSDPVKIFI PAHGWVDYAP SSTPAPGNAD
510 520 530 540 550
PVLIIFGCFC GFILIGLILY ISLAIRKRVQ ETKFGNAFTE EDSELVVNYI
560 570 580 590 600
AKKSFCRRAI ELTLHSLGVS EELQNKLEDV VIDRNLLILG KILGEGEFGS
610 620 630 640 650
VMEGNLKQED GTSLKVAVKT MKLDNSSQRE IEEFLSEAAC MKDFSHPNVI
660 670 680 690 700
RLLGVCIEMS SQGIPKPMVI LPFMKYGDLH TYLLYSRLET GPKHIPLQTL
710 720 730 740 750
LKFMVDIALG MEYLSNRNFL HRDLAARNCM LRDDMTVCVA DFGLSKKIYS
760 770 780 790 800
GDYYRQGRIA KMPVKWIAIE SLADRVYTSK SDVWAFGVTM WEIATRGMTP
810 820 830 840 850
YPGVQNHEMY DYLLHGHRLK QPEDCLDELY EIMYSCWRTD PLDRPTFSVL
860 870 880 890 900
RLQLEKLLES LPDVRNQADV IYVNTQLLES SEGLAQGSTL APLDLNIDPD
910 920 930 940 950
SIIASCTPRA AISVVTAEVH DSKPHEGRYI LNGGSEEWED LTSAPSAAVT
960 970 980 990
AEKNSVLPGE RLVRNGVSWS HSSMLPLGSS LPDELLFADD SSEGSEVLM
Length:999
Mass (Da):110,249
Last modified:November 13, 2007 - v2
Checksum:i05BC339F05DFD355
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti140A → G in AAB60430 (PubMed:8086340).Curated1
Sequence conflicti143A → R in AAB60430 (PubMed:8086340).Curated1
Sequence conflicti247S → G in AAB60430 (PubMed:8086340).Curated1
Sequence conflicti274K → Q in AAB60430 (PubMed:8086340).Curated1
Sequence conflicti328S → G in AAB60430 (PubMed:8086340).Curated1
Sequence conflicti628Q → H in AAB60430 (PubMed:8086340).Curated1
Sequence conflicti794A → R in AAB60430 (PubMed:8086340).Curated1
Sequence conflicti888S → P in AAB60430 (PubMed:8086340).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02103920R → S.2 PublicationsCorresponds to variant rs35898499dbSNPEnsembl.1
Natural variantiVAR_021040118S → N.3 PublicationsCorresponds to variant rs13027171dbSNPEnsembl.1
Natural variantiVAR_041741185V → M.1 PublicationCorresponds to variant rs56205303dbSNPEnsembl.1
Natural variantiVAR_067194214F → V Found in a patient with Leber congenital amaurosis. 1 Publication1
Natural variantiVAR_021041282A → T.2 PublicationsCorresponds to variant rs7588635dbSNPEnsembl.1
Natural variantiVAR_041742289E → K.1 PublicationCorresponds to variant rs766215580dbSNPEnsembl.1
Natural variantiVAR_021042293R → H.2 PublicationsCorresponds to variant rs34072093dbSNPEnsembl.1
Natural variantiVAR_051698329N → S.Corresponds to variant rs34943572dbSNPEnsembl.1
Natural variantiVAR_041743446A → G in a renal clear cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041744452V → L.1 PublicationCorresponds to variant rs34010621dbSNPEnsembl.1
Natural variantiVAR_021043466R → K.2 PublicationsCorresponds to variant rs7604639dbSNPEnsembl.1
Natural variantiVAR_021044498N → S.2 PublicationsCorresponds to variant rs35858762dbSNPEnsembl.1
Natural variantiVAR_021045518I → V.2 PublicationsCorresponds to variant rs2230515dbSNPEnsembl.1
Natural variantiVAR_021046540E → K in RP38. 1 PublicationCorresponds to variant rs113485015dbSNPEnsembl.1
Natural variantiVAR_021047661S → C in RP38. 1 Publication1
Natural variantiVAR_041745662Q → E.1 PublicationCorresponds to variant rs56209758dbSNPEnsembl.1
Natural variantiVAR_041746708A → S in a head & Neck squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041747823E → Q.1 PublicationCorresponds to variant rs55924349dbSNPEnsembl.1
Natural variantiVAR_020285865R → W.1 PublicationCorresponds to variant rs2230516dbSNPEnsembl.1
Natural variantiVAR_029237870V → I.1 PublicationCorresponds to variant rs2230517dbSNPEnsembl.1
Natural variantiVAR_021048871I → T in RP38. 1 PublicationCorresponds to variant rs377341255dbSNPEnsembl.1
Natural variantiVAR_021049871I → V.1 Publication1
Natural variantiVAR_067195958P → L Found in a patient with Leber congenital amaurosis. 1 PublicationCorresponds to variant rs201460398dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2. human.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115724. 8 interactors.
IntActiQ12866. 4 interactors.
STRINGi9606.ENSP00000295408.

Chemistry databases

BindingDBiQ12866.
ChEMBLiCHEMBL5331.
GuidetoPHARMACOLOGYi1837.

PTM databases

iPTMnetiQ12866.
PhosphoSitePlusiQ12866.

Polymorphism and mutation databases

BioMutaiMERTK.
DMDMi160332297.

Proteomic databases

EPDiQ12866.
MaxQBiQ12866.
PaxDbiQ12866.
PeptideAtlasiQ12866.
PRIDEiQ12866.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295408; ENSP00000295408; ENSG00000153208.
ENST00000421804; ENSP00000389152; ENSG00000153208.
GeneIDi10461.
KEGGihsa:10461.
UCSCiuc002thk.2. human.

Organism-specific databases

CTDi10461.
DisGeNETi10461.
GeneCardsiMERTK.
GeneReviewsiMERTK.
H-InvDBHIX0002374.
HGNCiHGNC:7027. MERTK.
HPAiHPA036196.
MalaCardsiMERTK.
MIMi604705. gene.
613862. phenotype.
neXtProtiNX_Q12866.
OpenTargetsiENSG00000153208.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA30759.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG6I. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00810000125384.
HOGENOMiHOG000231685.
HOVERGENiHBG006346.
InParanoidiQ12866.
KOiK05117.
OMAiKHIPLQT.
OrthoDBiEOG091G016X.
PhylomeDBiQ12866.
TreeFamiTF317402.

Enzyme and pathway databases

BioCyciZFISH:HS07891-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-202733. Cell surface interactions at the vascular wall.
SignaLinkiQ12866.
SIGNORiQ12866.

Miscellaneous databases

ChiTaRSiMERTK. human.
EvolutionaryTraceiQ12866.
GeneWikiiMERTK.
GenomeRNAii10461.
PROiQ12866.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000153208.
CleanExiHS_MERTK.
ExpressionAtlasiQ12866. baseline and differential.
GenevisibleiQ12866. HS.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
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.
PF00047. ig. 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]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF49265. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 186 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.