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Q12866 (MERTK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Mer

EC=2.7.10.1
Alternative name(s):
Proto-oncogene c-Mer
Receptor tyrosine kinase MerTK
Gene names
Name:MERTK
Synonyms:MER
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length999 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Catalytic activity

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

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.14

Subcellular location

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

Tissue specificity

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.

Post-translational modification

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. Ref.5

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.

Contains 2 fibronectin type-III domains.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Proto-oncogene
Retinitis pigmentosa
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic cell clearance

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cell surface receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

leukocyte migration

Traceable author statement. Source: Reactome

natural killer cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of lymphocyte activation

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Traceable author statement Ref.1. Source: GOC

phagocytosis

Inferred from mutant phenotype PubMed 19204785. Source: BHF-UCL

platelet activation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phagocytosis

Inferred from direct assay PubMed 18395422. Source: UniProtKB

protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

secretion by cell

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

substrate adhesion-dependent cell spreading

Inferred from electronic annotation. Source: Ensembl

vagina development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18395422. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 18395422. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

photoreceptor outer segment

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

rhabdomere

Inferred from direct assay PubMed 19204785. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 20103767. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 999979Tyrosine-protein kinase Mer
PRO_0000024443

Regions

Topological domain21 – 505485Extracellular Potential
Transmembrane506 – 52621Helical; Potential
Topological domain527 – 999473Cytoplasmic Potential
Domain81 – 186106Ig-like C2-type 1
Domain197 – 27377Ig-like C2-type 2
Domain286 – 38196Fibronectin type-III 1
Domain386 – 48499Fibronectin type-III 2
Domain587 – 858272Protein kinase
Nucleotide binding593 – 6019ATP By similarity

Sites

Active site7231Proton acceptor By similarity
Binding site6151ATP By similarity

Amino acid modifications

Modified residue5431Phosphoserine Ref.13
Modified residue7491Phosphotyrosine; by autocatalysis Ref.5
Modified residue7531Phosphotyrosine; by autocatalysis Ref.5
Modified residue7541Phosphotyrosine; by autocatalysis Ref.5
Modified residue8721Phosphotyrosine; by autocatalysis By similarity
Modified residue9351Phosphoserine Ref.13
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation3891N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4421N-linked (GlcNAc...) Ref.9
Glycosylation4541N-linked (GlcNAc...) Potential
Disulfide bond115 ↔ 175 By similarity
Disulfide bond218 ↔ 262 By similarity

Natural variations

Natural variant201R → S. Ref.3 Ref.16
Corresponds to variant rs35898499 [ dbSNP | Ensembl ].
VAR_021039
Natural variant1181S → N. Ref.1 Ref.3 Ref.16
Corresponds to variant rs13027171 [ dbSNP | Ensembl ].
VAR_021040
Natural variant1851V → M. Ref.16
Corresponds to variant rs56205303 [ dbSNP | Ensembl ].
VAR_041741
Natural variant2141F → V Found in a patient with Leber congenital amaurosis. Ref.17
VAR_067194
Natural variant2821A → T. Ref.3 Ref.16
Corresponds to variant rs7588635 [ dbSNP | Ensembl ].
VAR_021041
Natural variant2891E → K. Ref.16
VAR_041742
Natural variant2931R → H. Ref.3 Ref.16
Corresponds to variant rs34072093 [ dbSNP | Ensembl ].
VAR_021042
Natural variant3291N → S.
Corresponds to variant rs34943572 [ dbSNP | Ensembl ].
VAR_051698
Natural variant4461A → G in a renal clear cell carcinoma sample; somatic mutation. Ref.16
VAR_041743
Natural variant4521V → L. Ref.16
Corresponds to variant rs34010621 [ dbSNP | Ensembl ].
VAR_041744
Natural variant4661R → K. Ref.3 Ref.16
Corresponds to variant rs7604639 [ dbSNP | Ensembl ].
VAR_021043
Natural variant4981N → S. Ref.3 Ref.16
Corresponds to variant rs35858762 [ dbSNP | Ensembl ].
VAR_021044
Natural variant5181I → V. Ref.3 Ref.16
Corresponds to variant rs2230515 [ dbSNP | Ensembl ].
VAR_021045
Natural variant5401E → K in RP38. Ref.3
Corresponds to variant rs113485015 [ dbSNP | Ensembl ].
VAR_021046
Natural variant6611S → C in RP38. Ref.3
VAR_021047
Natural variant6621Q → E. Ref.16
Corresponds to variant rs56209758 [ dbSNP | Ensembl ].
VAR_041745
Natural variant7081A → S in a head & Neck squamous cell carcinoma sample; somatic mutation. Ref.16
VAR_041746
Natural variant8231E → Q. Ref.16
Corresponds to variant rs55924349 [ dbSNP | Ensembl ].
VAR_041747
Natural variant8651R → W. Ref.16
Corresponds to variant rs2230516 [ dbSNP | Ensembl ].
VAR_020285
Natural variant8701V → I. Ref.16
Corresponds to variant rs2230517 [ dbSNP | Ensembl ].
VAR_029237
Natural variant8711I → T in RP38. Ref.3
VAR_021048
Natural variant8711I → V. Ref.3
VAR_021049
Natural variant9581P → L Found in a patient with Leber congenital amaurosis. Ref.17
Corresponds to variant rs201460398 [ dbSNP | Ensembl ].
VAR_067195

Experimental info

Sequence conflict1401A → G in AAB60430. Ref.1
Sequence conflict1431A → R in AAB60430. Ref.1
Sequence conflict2471S → G in AAB60430. Ref.1
Sequence conflict2741K → Q in AAB60430. Ref.1
Sequence conflict3281S → G in AAB60430. Ref.1
Sequence conflict6281Q → H in AAB60430. Ref.1
Sequence conflict7941A → R in AAB60430. Ref.1
Sequence conflict8881S → P in AAB60430. Ref.1

Secondary structure

........................................................... 999
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12866 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 05BC339F05DFD355

FASTA999110,249
        10         20         30         40         50         60 
MGPAPLPLLL GLFLPALWRR AITEAREEAK PYPLFPGPFP GSLQTDHTPL LSLPHASGYQ 

        70         80         90        100        110        120 
PALMFSPTQP GRPHTGNVAI PQVTSVESKP LPPLAFKHTV GHIILSEHKG VKFNCSISVP 

       130        140        150        160        170        180 
NIYQDTTISW WKDGKELLGA HHAITQFYPD DEVTAIIASF SITSVQRSDN GSYICKMKIN 

       190        200        210        220        230        240 
NEEIVSDPIY IEVQGLPHFT KQPESMNVTR NTAFNLTCQA VGPPEPVNIF WVQNSSRVNE 

       250        260        270        280        290        300 
QPEKSPSVLT VPGLTEMAVF SCEAHNDKGL TVSKGVQINI KAIPSPPTEV SIRNSTAHSI 

       310        320        330        340        350        360 
LISWVPGFDG YSPFRNCSIQ VKEADPLSNG SVMIFNTSAL PHLYQIKQLQ ALANYSIGVS 

       370        380        390        400        410        420 
CMNEIGWSAV SPWILASTTE GAPSVAPLNV TVFLNESSDN VDIRWMKPPT KQQDGELVGY 

       430        440        450        460        470        480 
RISHVWQSAG ISKELLEEVG QNGSRARISV QVHNATCTVR IAAVTRGGVG PFSDPVKIFI 

       490        500        510        520        530        540 
PAHGWVDYAP SSTPAPGNAD PVLIIFGCFC GFILIGLILY ISLAIRKRVQ ETKFGNAFTE 

       550        560        570        580        590        600 
EDSELVVNYI AKKSFCRRAI ELTLHSLGVS EELQNKLEDV VIDRNLLILG KILGEGEFGS 

       610        620        630        640        650        660 
VMEGNLKQED GTSLKVAVKT MKLDNSSQRE IEEFLSEAAC MKDFSHPNVI RLLGVCIEMS 

       670        680        690        700        710        720 
SQGIPKPMVI LPFMKYGDLH TYLLYSRLET GPKHIPLQTL LKFMVDIALG MEYLSNRNFL 

       730        740        750        760        770        780 
HRDLAARNCM LRDDMTVCVA DFGLSKKIYS GDYYRQGRIA KMPVKWIAIE SLADRVYTSK 

       790        800        810        820        830        840 
SDVWAFGVTM WEIATRGMTP YPGVQNHEMY DYLLHGHRLK QPEDCLDELY EIMYSCWRTD 

       850        860        870        880        890        900 
PLDRPTFSVL RLQLEKLLES LPDVRNQADV IYVNTQLLES SEGLAQGSTL APLDLNIDPD 

       910        920        930        940        950        960 
SIIASCTPRA AISVVTAEVH DSKPHEGRYI LNGGSEEWED LTSAPSAAVT AEKNSVLPGE 

       970        980        990 
RLVRNGVSWS HSSMLPLGSS LPDELLFADD SSEGSEVLM 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: AUTOPHOSPHORYLATION 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]"Tyro3 family-mediated cell entry of Ebola and Marburg viruses."
Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K., Irimura T., Jones S., Feldmann H., Kawaoka Y.
J. Virol. 80:10109-10116(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CELL ENTRY FACTOR IN FILOVIRUS INFECTION.
[12]"Immunobiology of the TAM receptors."
Lemke G., Rothlin C.V.
Nat. Rev. Immunol. 8:327-336(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08023 mRNA. Translation: AAB60430.1.
AH010001 Genomic DNA. Translation: AAG33129.1.
AC093675 Genomic DNA. No translation available.
AC104651 Genomic DNA. No translation available.
CCDSCCDS2094.1.
PIRI38547.
RefSeqNP_006334.2. NM_006343.2.
UniGeneHs.306178.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ12866.
SMRQ12866. Positions 103-281, 283-492, 575-900.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115724. 8 interactions.
IntActQ12866. 3 interactions.
STRING9606.ENSP00000295408.

Chemistry

BindingDBQ12866.
ChEMBLCHEMBL5331.
GuidetoPHARMACOLOGY1837.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ12866.

Polymorphism databases

DMDM160332297.

Proteomic databases

MaxQBQ12866.
PaxDbQ12866.
PRIDEQ12866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295408; ENSP00000295408; ENSG00000153208.
ENST00000421804; ENSP00000389152; ENSG00000153208.
GeneID10461.
KEGGhsa:10461.
UCSCuc002thk.1. human.

Organism-specific databases

CTD10461.
GeneCardsGC02P112656.
GeneReviewsMERTK.
H-InvDBHIX0002374.
HGNCHGNC:7027. MERTK.
HPAHPA036196.
MIM604705. gene.
613862. phenotype.
neXtProtNX_Q12866.
Orphanet791. Retinitis pigmentosa.
PharmGKBPA30759.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231685.
HOVERGENHBG006346.
InParanoidQ12866.
KOK05117.
OMANEIGWSA.
OrthoDBEOG77DJ5C.
PhylomeDBQ12866.
TreeFamTF317402.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_604. Hemostasis.
SignaLinkQ12866.

Gene expression databases

ArrayExpressQ12866.
BgeeQ12866.
CleanExHS_MERTK.
GenevestigatorQ12866.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR003961. 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]
PfamPF00041. fn3. 1 hit.
PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00060. FN3. 2 hits.
SM00409. IG. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50853. 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]
ProtoNetSearch...

Other

ChiTaRSMERTK. human.
EvolutionaryTraceQ12866.
GeneWikiMERTK.
GenomeRNAi10461.
NextBio39667.
PROQ12866.
SOURCESearch...

Entry information

Entry nameMERTK_HUMAN
AccessionPrimary (citable) accession number: Q12866
Secondary accession number(s): Q9HBB4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM